EOL/seabase

>gnl|Smart|14_3_3 14-3-3 homologues; 14-3-3 homologues mediates signal transduction by binding to phosphoserine-containing proteins. They are involved in growth factor signalling and also interact with MEK kinases
RDEYVYKAKLAEQAERYDEMAEAMKNLVENCLDEQQPKDELSVEERNLLSVAYKNAVGARRASWRIISSVEQKELSKQHM
QNKALAAEYRQKVEEELNKICHDILQLLTDKLIPKTSDSESKVFYYKMKGDYYRYISEFSGEEGKKQAADQAQESYQKAT
ETAEGHSPATHPIRLGLALNYSVFFYEILNLPQQACEMAKRAFDDAITEFDNVSEDSYKDSTLIMQLLRDNLTLWTSDLQ
ADQQQQEGG
>gnl|Smart|35EXOc 3'-5' exonuclease; 3\' -5' exonuclease proofreading domain present in DNA polymerase I, Werner syndrome helicase, RNase D and other enzymes
YVTILDEETLKAWIAKLEKAPVFAFDTETDSLDNISANLVGLSFAIEPGVAAYIPVAHDYLDAPDQISRERALELLKPLL
EDEKALKVGQNLKYDRGILANYGIELRGIAFDTMLESYILNSVAGRHDMDSLAERWLKHKTITFEEIAGKGKNQLTFNQI
ALEEAGRYAAEDADVTLQLHLKMWPDLQ
>gnl|Smart|4.1m putative band 4.1 homologues' binding motif
MYKYRNRDEGSYHVDESRN
>gnl|Smart|53EXOc 5'-3' exonuclease
RNLMIVDGTNLGFRFKHNNSKKPFASSYVSTIQSLAKSYSARTTIVLGDKGKSVFRLEHLPEYKGNRDEKYAQRTEEEKA
LDEQFFEYLKDAFELCKTTFPTFTIRGVEADDMAAYIVKLIGHLYDHVWLISTDGDWDTLLTDKVSRFSFTTRREYHLRD
MYEHHNVDDVEQFISLKAIMGDLGDNIRGVEGIGAKRGYNIIREFGNVLDIIDQLPLPGKQKYIQNLNASEELLFRNLIL
VDLPTYCVDAIAAVG
>gnl|Smart|A1pp Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by reciprocal PSI-BLAST searches (unpublished results, and Pehrson & Fuji)
RFHCFKGHFSHDKILNKKSGAVVISSHSSMDFSTTLGRAFAVTTCLQRSCWEKIKNNIPTPEKHLPIGSCVSGPWDVEEG
AQLYTSHLIVINPPTLETLIKEKMRRAITLKDFSMKEAFTNLVLAYLQCFDICIEHNLESVQLEVFGLNNLSADQEEFTT
WE
>gnl|Smart|A4_EXTRA amyloid A4; amyloid A4 precursor of Alzheimers disease
QAASPRWEPQIAVLCEAGQIYQPQYLSEEGRWVTDLSKKTTGPTCLRDKMDLLDYCKKAYPNRDITNIVESSHYQKIGGW
CRQGALNAAKCKGSHRWIKPFRCLGPFQSDALLVPEGCLFDHIHNASRCWPFVRWNQTGAAACQERGMQMRTFAMLLPCG
ISVFSGVEFVCCP
>gnl|Smart|AAA ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment
TPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEVGYVGKEVDSIIRDLTDAAVKMVRVQAIEKNRYRAEELAE
ERILDVLIPPAKNNWGQTEQQQEPSAARQAFRKKLREGQLDDKEIEIDLAAAPMGVEIMAPPGMEEMTSQLQSMFQNLGG
QKQKARKLKIKDAMKLLIEEEAAKLVNPEELKQDAIDAVEQHGIVFIDEIDKICKRGESSGPDVSREGVQRDLLPLVEGC
TVSTKHGMVKTDHILFIASGAFQIAKPSDLIPELQGRLPIRVEL
>gnl|Smart|AAI Plant lipid transfer protein / seed storage protein / trypsin-alpha amylase inhibitor domain family
CYPGQAFQVPALPACRPLLRLQCNGSQVPEAVLRDCCQQLAHISEWCRCGALYSMLDSMYKEHGAQEGQAGTGAFPRCRR
EVVKLTAASITAVCRLPIVVDASGDGAYVC
>gnl|Smart|acidPPc Acid phosphatase homologues
LGVIVMGISVIATQAAKTGAKALFEEPRPFTVYLAEQTHSTPENFYKNDRTLRAEIAKNFYSMDAITPAWLVHHYENETG
YSFPSGHTIFAATWLMLAVGFTQLLGNRSFKAKLLVVGIAVWGLLMLISRVRLGMHYPIDLLVATLLAWLINSIIF
>gnl|Smart|ACTIN Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
VQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEK
IWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVSHTVP
IYEGYALPHAILRLDLAGRDLTDYMMKILTERGYSFTTTAEREIVRDIKEKLAYVALDFEQEMATAASSSALEKSYELPD
GQVITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMFPGIADRMNKELTALAPST
MKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIVHRKCF
>gnl|Smart|ADF Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin monomers
DESLTAFNDLKLGKKYKFILFGLNDAKTEIVVKETSTDPSYDAFLEKLPENDCLYAIYDFEYEINGNEGKRSKIVFFTWS
PDTAPVRSKMVYASSKDALRRALNGVSTDVQGTDFSEVSYDSVLERVS
>gnl|Smart|ALBUMIN serum albumin
LVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQ
LCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKA
TKEQLKAVMDDFAAFVEKCCKADDKETCFAEE
>gnl|Smart|alkPPc Alkaline phosphatase homologues
KNIILLIGDGMGDSEITAARNYAEGAGGFFKGIDALPLTGQYTHYALNKKTGKPDYVTDGAASATAWSTGVKTYNGALGV
DIHEKDHPTILEMAKAAGLATGNVSTAELQDATPAALVAHVTSRKCYGPSATSEKCPGNALEKGGKGSITEQLLNARADV
TLGGGAKTFAETATAGEWQGKTLREQAQARGYQLVSDAASLNSVTEANQQKPLLGLFADGNMPVRWLGPKATYHGNIDKP
AVTCTPNPQRNDSVPTLAQMTDKAIELLSKNEKGFFLQVEGASIDKQDHAANPCGQIGETVDLDEAVQRALEFAKKEGNT
LVIVTADHAHASQIVAPDTKAPGLTQALNTKDGAVMVMSYGNSEEDSQEHTGSQLRIAAYGPHAANVVGLTDQTDLFYTM
KAALGLK
>gnl|Smart|ANATO Anaphylatoxin homologous domain; C3a, C4a and C5a anaphylatoxins are protein fragments generated enzymatically in serum during activation of complement molecules C3, C4, and C5. They induce smooth muscle contraction. These fragments are homologous to a three-fold repeat in fibulins
CCYDGAYRNDDETCEERAARIKIGPKCVKAFKDCC
>gnl|Smart|ANK ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure
DGDSFLHLAIIHEEKALTMEVIRQVKGDLAFLNF
>gnl|Smart|ANX Annexin repeats
GTDDDTLIRVMVSRSEIDLLDIRHEFRKNFAKSLYQMIQKDTSGDYRKALLLL
>gnl|Smart|AP2 DNA-binding domain in plant proteins such as APETALA2 and EREBPs
HYRGVRQRPWGKFAAEIRDPAKNGARVWLGTFETAEDAALAYDRAAFRMRGSRALLNFPLRVNSG
>gnl|Smart|AP2Ec AP endonuclease family 2; These endonucleases play a role in DNA repair. Cleave phosphodiester bonds at apurinic or apyrimidinic sites
YIGAHVSAAGGLANAAIRAAEIDATAFALFTKNQRQWRAAPLTTQTIDEFKAACEKYHYTSAQILPHDSYLINLGHPVTE
ALEKSRDAFIDEMQRCEQLGLSLLNFHPGSHLMQISEEDCLARIAESINIALDKTQGVTAVIENTAGQGSNLGFKFEHLA
AIIDGVEDKSRVGVCIDTCHAFAAGYDLRTPAECEKTFADFARTVGFKYLRGMHLNDAKSTFGSRVDRHHSLGEGNIGHD
AFRWIMQDDRFDGIPLILETINPDIWAEEIAWLKAQQ
>gnl|Smart|APPLE APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple 3 mediates binding to platelets. Factor XI apple 1 binds high-molecular-mass kininogen. Apple 4 in factor XI mediates dimer formation and binds to factor XIIa. Mutations in apple 4 cause factor XI deficiency, an inherited bleeding disorder
CMTQLYKNTFFRGGDLAAIYTPDAQYCQKMCTFHPRCLLFSFLAVTPPKETNKRFGCFMKESITGTLPRIHRTGAISGHS
LKQC
>gnl|Smart|ARF ARF-like small GTPases; ARF, ADP-ribosylation factor; Ras homologues involved in vesicular transport. Activator of phospholipase D isoforms. Unlike Ras proteins they lack cysteine residues at their C-termini and therefore are unlikely to be prenylated. ARFs are N-terminally myristoylated. Contains ATP/GTP-binding motif (P-loop)
MGNIFANLFKGLFGKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRH
YFQNTQGLIFVVDSNDRERVNEAREELMRMLAEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRHRNWYIQATCA
TSGDGLYEGLDWLSNQLRNQK
>gnl|Smart|ArfGap Putative GTP-ase activating proteins for the small GTPase, ARF; Putative zinc fingers with GTPase activating proteins (GAPs) towards the small GTPase, Arf. The GAP of ARD1 stimulates GTPase hydrolysis for ARD1 but not ARFs
IGDDVSTILRGLPGNNACAECNAPEPDWASLNLGVLLCIQCSGVHRNLGVHISKVRSLSLDVKVWEPTILDLFRNLGNVY
CNSLWEGLLHLDDDCEDGSALSHASVSKPCPEDSFSVKEKYILGKYLEKALVIKDESEA
>gnl|Smart|ARM Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form superhelix of helices that is proposed to mediate interaction of beta-catenin with its ligands. Involved in transducing the Wingless/Wnt signal. In plakoglobin arm repeats bind alpha-catenin and N-cadherin
KEASRHAIMRSPQMVSAIVRTMQNTNDVETARCTAGTLHNLSH
>gnl|Smart|AT_hook DNA binding domain with preference for A/T rich regions; Small DNA-binding motif first described in the high mobility group non-histone chromosomal protein HMG-I(Y)
KRPRGRPKGSKNK
>gnl|Smart|AXH domain in Ataxins and HMG containing proteins; unknown function
TVWHCFLKGTRLCFHKGSNKEWQDVEDFARAEGCDNEEDLQMGIHKGYGSDGLKLLSHEESVSFGESVLKLTFDPGTVED
GLLTVECKLDHPFYVKNKGWSSFYPSLTVVQHGIPCCEVHIGDVCLPPGHP
>gnl|Smart|B41 Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs
EEKIFELLRRLPSTSNFFVFDYWTIEDNFETCCRNQLSQFTCYCNSIVSRIGDSLNFACVDNGHYRNVMFSINYLIDQKL
FDKVVKPKTGKNIVIYKVKLLTNLNLSNKILFQFQDQVISGSLPCPKEEAAYLASIQLSVEEQWPSNKRTQTIRRHLLKG
QFGRIRDLAQKIMVTPWEVDQNLYCTPPRFPNESANASRAQSVVEEIQHRSRTPTLLRCITNTDGLMSEEMQAQCLPVDL
RGDRRTIKLVKERKRKLFHSQVYESEIGMKKLYIQTAKKLAAFGCKVF
>gnl|Smart|B_lectin Bulb-type mannose-specific lectin
DNILYSGETLSTGEFLNYGSFVFIMQEDCNLVLYDVDKPIWATNTGGLSRSCFLSMQTDGNLVVYNPSNKPIWASNTGGQ
NGNYVCILQKDRNVVIYGTDRWATGTHT
>gnl|Smart|BAG BAG domains, present in regulator of Hsp70 proteins; BAG domains, present in Bcl-2-associated athanogene 1 and silencer of death domains
QIDNVSLRYGNELEGRSKDLINRFDVEDEKDIYERNYCNEMLLKLLIELDSIDLINVDESLRRPLKEKRKGVIKEIQAML
KSLDSLK
>gnl|Smart|BAH Bromo adjacent homology domain
REMHVNSTVIYLSDSDEPSSIEYLNGDNLTQVESGSALSSGGNEGIVSLDLNNPTKSTKRKGKRVTRTAVQEQNKRSICF
FIGEPLSCEEAQERWRWRYELKMEKATSEFSGFTEQRIQCVYKFFSFIMERQATNHDKRRLFYSTVMNDNPVDCLISKVT
VLQVSPRVGLKPNSIKSDYYFDMEYCVEYSTFQTLR
>gnl|Smart|BASIC Basic domain in HLH proteins of MYOD family
MELLSPPLRDIDLTGPDGSLCSFETADDFYDDPCFDSPDLRFFEDLDPRLVHVGALLKPEEHAHFSTAVHPGPGAREDEH
VRAPSGHHQAGRCLLWACKACKRKTTNADRRKAA
>gnl|Smart|BBC B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
IRASILDMAHCIRTFTEEISDYSRKLVGIVQHIEGGEQIVEDGIGMAHTEHVPGTAENARSCIRAYFYDLHETLCRQEEM
ALSVVDAHVREKLIWLRQQQEDMTILLSEVSAACLHCEKTLQQDDCRVVLAKQEITRLLETLQKQ
>gnl|Smart|BBOX B-Box-type zinc finger
RPLEKCSEHDERLKLYCKDDGTLSCVICRDSLKHASHNFLPI
>gnl|Smart|BCL BCL (B-Cell lymphoma); contains BH1, BH2 regions; (BH1, BH2, (BH3 (one helix only)) and not BH4(one helix only)). Involved in apoptosis regulation
LREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIASW
MATYLNDHLEPWIQENGGW
>gnl|Smart|BH4 BH4 Bcl-2 homology region 4
MSQSNRELVVDFLSYKLSQKGYSWSQF
>gnl|Smart|BHL bacterial (prokaryotic) histone like domain
MTKSELIERLATQQSHIPAKTVEDAVKEMLEHMASTLAQGERIEIRGFGSFSLHYRAPRTGRNPKTGDKVELEGKYVPHF
KPGKELRDRAN
>gnl|Smart|BIR Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis proteins (IAPs) and other proteins. Acts as a direct inhibitor of caspase enzymes
QTHAARMRTFMYWPSSVPVQPEQLASAGFYYVGRNDDVKCFCCDGGLRCWESGDDPWVEHAKWFPRCEFLIR
>gnl|Smart|BowB Bowman-Birk type proteinase inhibitor
CCDQCSCTKSMPPKCRCSDIRLNSCHSACKSCACTYSIPAKCFCTDINDFCYEPC
>gnl|Smart|BPI1 BPI/LBP/CETP N-terminal domain; Bactericidal permeability-increasing protein (BPI) / Lipopolysaccharide-binding protein (LBP) / Cholesteryl ester transfer protein (CETP) N-terminal domain
RISQKGLDYASQQGTAALQKELKRIKIPDYSDSFKIKHLGKGHYSFYSMDIREFQLPSSQISMVPNVGLKFSISNANIKI
SGKWKAQKRFLKMSGNFDLSIEGMSISADLKLGSNPTSGKPTITCSSCSSHINSVHVHISKSKVGWLIQLFHKKIESALR
NKMNSQVCEKVTNSVSSKLQPYFQTLPVMTKIDSVAGINYGLVAPPATTAETLDVQMKGEFYSENH
>gnl|Smart|BPI2 BPI/LBP/CETP C-terminal domain; Bactericidal permeability-increasing protein (BPI) / Lipopolysaccharide-binding protein (LBP) / Cholesteryl ester transfer protein (CETP) C-terminal domain
AAHDRMVYLGLSDYFFNTAGLVYQEAGVLKMTLRDDMIPKESKFRLTTKFFGTFLPEVAKKFPNMKIQIHVSASTPPHLS
VQPTGLTFYPAVDVQAFAVLPNSALASLFLIGMHTTGSMEVSAESNRLVGELKLDRLLLELKHSNIGPFPVELLQDIMNY
IVPILVLPRVNEKLQKGFPLPTPARVQLYNVVLQPHQNFLLFGA
>gnl|Smart|BRCT breast cancer carboxy-terminal domain
PDFFQGKHFFLYGEFPGDERRKLIRYVTAFNGELEDYMSDRVQFVITAQEWDPSFEEALMDNPSLAFVRPRWIYSCNEKQ
>gnl|Smart|BRIGHT BRIGHT, ARID (A/T-rich interaction domain) domain; DNA-binding domain containing a helix-turn-helix structure
PKRKEFLDDLFSFMQKRGTPINRLPIMAKSVLDLYELYNLVIARGGLVDVINKKLWQEIIKGLHLPSS
>gnl|Smart|BRLZ basic region leucin zipper
GRDEALRLKQRRRTLKNRGYAQACRSKRLQQRRGLEAERARLAAQLDALRAEVARLARERDLYKARCDR
>gnl|Smart|BROMO bromo domain
EPRDPDQLYSTLKSILQQVKSHQSAWPFMEPVKRTEAPGYYEVIRSPMDLKTMSERLKNRYYVSKKLFMADLQRVFTNCK
EYNAPESEYYKCANILEKFFFSKIKEAGL
>gnl|Smart|BTB Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. Also known as POZ (poxvirus and zinc finger) domain. Known to be a protein-protein interaction motif found at the N-termini of several C2H2-type transcription factors as well as Shaw-type potassium channels. Known structure reveals a tightly intertwined dimer formed via interactions between N-terminal strand and helix structures. However in a subset of BTB/POZ domains, these two secondary structures appear to be missing. Be aware SMART predicts BTB/POZ domains without the beta1- and alpha1-secondary structures
ADVILVLQERVRIFAHKIYLSTSSSKFYDLFLMDLSEGELGGPSEPGGTHPEDHQGHSDQHHHHHHHHHGRDFLLRAASF
DVCESVDEAGGSGPAGLRASTSDGILRGNGTGYLPGRGRVLSSWSRAFVSIQEEMAEDPLTYKSRLMVVVKMDSSIQPGP
FRAVLKYLYTGELDENERDLMHIAHIAELLEVFDLRMMVANILNNEA
>gnl|Smart|btg1 tob/btg1 family; The tob/btg1 is a family of proteins that inhibit cell proliferation
MKEEIAATVVFLTMLVKKHKQLSKQKIEKFAAKLTTILFAKYKNHWYAENPMKGQAFRCIRINTYQAIDAVFEKACAESN
VDFNDLGLPKEMTIWVDPFEVCCRYGEK
>gnl|Smart|BTK Bruton's tyrosine kinase Cys-rich motif; Zinc-binding motif containing conserved cysteines and a histidine. Always found C-terminal to PH domains (but not all PH domains are followed by BTK motifs). The crystal structure shows this motif packs against the PH domain. The PH+Btk module pair has been called the Tec homology (TH) region
NSDLVQKYHPCFWIDGQYLCCSQTAKNAMGCQILEN
>gnl|Smart|C1 Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains
TTHNFARKTFLKLAFCDICQKFLLNGFRCQTCGYKFHEHCSTKVPTMC
>gnl|Smart|C1Q Complement component C1q domain.; Globular domain found in many collagens and eponymously in complement C1q. When part of full length proteins these domains form a 'bouquet' due to the multimerization of heterotrimers. The C1q fold is similar to that of tumour necrosis factor
VRSGSAKVAFSAIRSTNHEPSEMSNRTMIIYFDQVLVNIGNNFDSERSTFIAPRKGIYSFNFHVVKVYNRQTIQVSLMLN
GWPVISAFAGDQDVTREAASNGVLIQMEKGDRAYLKLERGNLMGGWKYSTFSGFLVFPL
>gnl|Smart|C2 Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotamins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles
LLTVTIIKASNLKAMDLTGFSDPYVKASLISEGRRLKKRKTSIKKNTLNPTYNEALVFDVAPESVENVGLSIAVVDYDCI
GHNEVIGVCRVGPEAADPHGREHWAEMLANPRKPVE
>gnl|Smart|C4 C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome
ANVIAVHSQTIQIPNCPNGWNSLWIGYSFAMHTGAGAEGGGQSLSSPGSCLEDFRATPFIECNGARGTCHYFANKFSFWL
TTIEDDQQFRIPESETLKAGSLRTRVSRCQVCIRS
>gnl|Smart|CA Cadherin repeats.; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium
RIRSDRDKNLSLRYSVTGPGADQPPTGIFIINPISGQLSVTKPLDRELIARFHLRAHAVDINGNQVENPIDIVINVIDMN
DNRP
>gnl|Smart|CAD Domains present in proteins implicated in post-mortem DNA fragmentation
RPFRVCDHKRTIRKGLTAATRQELLAKALETLLLNGVLTLVLEEDGTAVDSEDFFQLLEDDTCLMVLQSGQSW
>gnl|Smart|CALCITONIN calcitonin; This family is formed by calcitonin, the calcitonin gene-related peptide, and amylin. They are short polypeptide hormones
KRACNTATCVTHRLADFLSRSGGVGKNNFVPTNVGSKAFGRRR
>gnl|Smart|Calx_beta Domains in Na-Ca exchangers and integrin-beta4; Domain in Na-Ca exchangers and integrin subunit beta4 (and some cyanobacterial proteins)
VNITIIKEQASGIVSFEQPEYSVSRGDQVARIPVIRHILDNGKSQVSYSTQDNTAHGHRDYVPVEGELLFYPGETWKELQ
VKLLELQEVDSLLRGRQVRRFQVQLS
>gnl|Smart|CARD Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. Mediates homodimerisation. Structure consists of six antiparallel helices arranged in a topology homologue to the DEATH and the DED domain
MDEADRRLLRRCRLRLVEELQVDQLWDVLLSRELFRPHMIEDIQRAGSGSRRDQARQLIIDLETRGSQALPLFISCLEDT
GQDMLASFLRT
>gnl|Smart|CASc Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that mediate programmed cell death (apoptosis). Caspases are synthesised as zymogens and activated by proteolysis of the peptide backbone adjacent to an aspartate. The resulting two subunits associate to form an (alpha)2(beta)2-tetramer which is the active enzyme. Activation of caspases can be mediated by other caspase homologues
SYKMDYPEMGLCIIINNKNFHKSTGMTSRSGTDVDAANLRETFRNLKYEVRNKNDLTREEIVELMRDVSKEDHSKRSSFV
CVLLSHGEEGIIFGTNGPVDLKKITNFFRGDRCRSLTGKPKLFIIQACRGTELDCGIETDSGVDDDMACHKIPVDADFLY
AYSTAPGYYSWRNSKDGSWFIQSLCAMLKQYADKLEFMHILTRVNRKVATEFESFSFDATFHAKKQIPCIVSMLTKELYF
YH
>gnl|Smart|CBF CCAAT-Binding transcription Factor
TEDSTIYVNSKQYHGIIRRRQSRAKAAAVLDQKKLSSRCRKPYMHHSRHLHALRRPRGSGGRFLNT
>gnl|Smart|CBS Domain in cystathionine beta-synthase and other proteins.; Domain present in all 3 forms of cellular life. Present in two copies in inosine monophosphate dehydrogenase, of which one is disordered in the crystal structure [3]. A number of disease states are associated with CBS-containing proteins including homocystinuria, Becker's and Thomsen disease
DLVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKKNRD
>gnl|Smart|CCP Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII
CEEPPTFEAMELIGKPKPYYEIGERVDYKCKKGYFYIPPLATHTICDRNHTWLPVSDDAC
>gnl|Smart|CH Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p
EKYAFVNWINKALENDPDCRHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAINKKKLTPFIIQENLNLALNSA
SAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKI
>gnl|Smart|CheW Two component signalling adaptor domain
VTIRLPLTLAIICALLVKVNNLVYAIPIANIDTILSISKEDIQRVQDRDVIVIRGEVIPVYRLWEVLQIEHKEELEEMEA
VIVRVGNRKYGIVVDDLLGQDDIVIKSLGKVFSEVKEFSGAAILGDGSIALIINVSGIV
>gnl|Smart|CHROMO Chromatin organization modifier domain
GLEPERIIGATDSSGELMFLMKWKNSDEADLVPAKEANVKCPQVVISFYEER
>gnl|Smart|ChSh Chromo Shadow Domain
RGFARGLEPERIIGATDSSGELMFLMKWKNSDEADLVPAKEANVKCPQVVISFYEERLTWH
>gnl|Smart|ChtBD1 Chitin binding domain
PCGKDAGGRVCTNNYCCSKWGSCGIGPGYCGAGCQSGGC
>gnl|Smart|ChtBD2 Chitin-binding domain type 2
EICAPFHNGTINGRDRFPLRNCRYFAFCDTERPYLTLTQCPFNDLFNEATKTCEMHVNCGN
>gnl|Smart|ChtBD3 Chitin-binding domain type 3
SKDWAGGQPTHNEAGQSIVYKGNLYTANWYTASVPGSDSSWTQV