ID A0A0V1C2A7_TRISP Unreviewed; 2785 AA.
AC A0A0V1C2A7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Spectrin alpha chain {ECO:0000313|EMBL:KRY43418.1};
GN Name=alpha-Spec {ECO:0000313|EMBL:KRY43418.1};
GN ORFNames=T01_14998 {ECO:0000313|EMBL:KRY43418.1};
OS Trichinella spiralis (Trichina worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6334 {ECO:0000313|EMBL:KRY43418.1, ECO:0000313|Proteomes:UP000054776};
RN [1] {ECO:0000313|EMBL:KRY43418.1, ECO:0000313|Proteomes:UP000054776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS3 {ECO:0000313|EMBL:KRY43418.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the spectrin family.
CC {ECO:0000256|ARBA:ARBA00006826}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRY43418.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYDH01000001; KRY43418.1; -; Genomic_DNA.
DR Proteomes; UP000054776; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0008534; F:oxidized purine nucleobase lesion DNA N-glycosylase activity; IEA:InterPro.
DR GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR CDD; cd00051; EFh; 1.
DR CDD; cd00056; ENDO3c; 1.
DR CDD; cd11808; SH3_Alpha_Spectrin; 1.
DR CDD; cd00176; SPEC; 13.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 1.20.58.60; -; 18.
DR Gene3D; 3.30.310.40; -; 1.
DR Gene3D; 1.10.238.10; EF-hand; 2.
DR Gene3D; 1.10.1670.10; Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal); 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR035825; Alpha_Spectrin_SH3.
DR InterPro; IPR011257; DNA_glycosylase.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR014837; EF-hand_Ca_insen.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR003265; HhH-GPD_domain.
DR InterPro; IPR023170; HhH_base_excis_C.
DR InterPro; IPR012904; OGG_N.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR PANTHER; PTHR11915:SF422; PH_9 DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR11915; SPECTRIN/FILAMIN RELATED CYTOSKELETAL PROTEIN; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF08726; EFhand_Ca_insen; 1.
DR Pfam; PF00730; HhH-GPD; 1.
DR Pfam; PF07934; OGG_N; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF00435; Spectrin; 20.
DR PRINTS; PR01887; SPECTRNALPHA.
DR SMART; SM00054; EFh; 2.
DR SMART; SM01184; efhand_Ca_insen; 1.
DR SMART; SM00478; ENDO3c; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00150; SPEC; 20.
DR SUPFAM; SSF48150; DNA-glycosylase; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR SUPFAM; SSF46966; Spectrin repeat; 17.
DR SUPFAM; SSF55945; TATA-box binding protein-like; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Actin capping {ECO:0000256|ARBA:ARBA00022467};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000054776};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 1016..1075
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 2308..2343
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 2351..2386
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT COILED 869..928
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1261..1302
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 2785 AA; 321997 MW; 0EA0BD7D3E763AA7 CRC64;
MIGFNIHSSV FKMDDHTPPE PVLEVPPPQE IKILETASDI QQRRSEVLGH YRAFKEMAQN
KRDRLEEARQ FQYFKRDADE LQLWILEKLQ TAQEESYRDP TNLQAKIQKH QAFEAEVQAH
SNAILQLDKT GNDMIMHGHF AHATIKERLD ELHALWEQLL QKLAEKGIRL QQALKLLLFT
RQCDEVMYWI LDKEAFVTTE EFGQDLEHVE VLQKKFDDFL KELANQQYRI AEVNLSAEQL
INEGHPDVEI IKNKRDELLA AWKHLNDLSV TRKERLFGAH EVQRFNRDID ETIAWILEKD
SGLSVDDFGR DLTTVQALQR KHEGTERDLA ALDGKVQSLA IEAERLKSLH PDRVESIESK
KLDALKNWEQ LKRKAAERKA GLERSFLLHR FFADYRDLTS WIADMKALIM ADELAKDVAG
AEALLERHQE QRGEIDARED SFRATEEAGR RLLAEDIPQK NEVAEKVHFF KKEIIATELM
NVNQYTRITF TIKSLAADKE ALLALLEERR ILYEQCMDLQ LFYRDTDQAE TWMTKQEAFL
ANEDLGESLD SVEALIKKHE DFEKSLAAQE EKIKAFDEFA TKLIEGQHYT ADDVALRRQA
LLQRRAGLLE RAARRRTMLE DAYRLQQFER DCDEMMSWIN EKLKTARDEN YLDPTNIQGK
IQKHANFEQE LHANKSRLDD IHKRGSELVS SGHYAADDVS RRLDEVQNSW SDLVVATEQK
GAKLKEAGGQ QQFNRNVEDI EMWLAEVEAQ LMSEDYGKDL ISVQNLQKKH ALLECDVNAH
AERIEGVGQQ AAQFEAAGHF DIGNIRAKEQ KLIGRYNALQ EPMSRRKEKL AESLRGHQLF
RDIEDEFSWI REKEQIADST NRGRDLIGVQ NLIKKHNALM AEIANHEVQI NKVVNAGEEI
MKEDHFLASE IKAKLSALQD NWQLLKEKAN KRGQDLEDSY MAHQYLADAN EAESWMSEKE
PIVGSADYGK DEDSAEALLK KHSALMSDLE AFRSTIEHLR EQVNHCKTDT TIIGSLGREC
VVALYDYSEK SPREVSMKKG DVLTLLNSSN KDWWKVEVND RQGFVPVAYL KKMEPGLSSS
QQQLLQSSSI AAKQSQIENL YQHLLDLGNQ RRKKLEEACK GYQLLREANE LAEWIRSKEQ
LATSHEIGQD LEEVEVLQKK FDEFQADLRA HEVRLAEMNK ISTALAAIGQ TEAAVKIRHQ
IDNLNERWQA LQEVTTQRAQ QLGSAHEVQR FHRDVDEAKD WMKEKDDALD SEDFGRDLRS
VQALQRKHEG LERDLAALGD KIRQLDETAN RLRQTHPEAA EQIYDLQLQL NDRWSALTSK
ANNRKEKLLD SYDYQRFLSD CRDLQRWNNN TMVLVNSDEL ANDVTGAEAL LERHSEYRTE
MDARAGMFQK FDQFGNDLLS MHHYASADVV EQMHKIAEAR ENLEKAWMAR RMKLDQCLEL
QLFYRDCEQA ENWMSSREAF LNQEQVSPDN VESLIKKHED FDKAINSQQE KIAALQSFAN
QLVNRGHYAE EDIIRKRDQV LDRWAKLKQA LIEKRSKLGE SQTLQQFSRD ADEIENWIAE
KLQVALEESY RDPTNIQSKH QKQQAFEAEL GANSDRIQTI MYAGQNLIDS NKCAGSESVV
SQRLTALNDQ WELLVKKTTE KSYRLKEANK QQSFIAAVKD LEFWLGEIET LLASDDFGKD
LASVQNLLKK HQLIEADIAA HAERVRDMNT EASSLLENDQ FDPVTIEERQ KSINDRYKRV
SELAEERKRK LNEALTLHQF FRDIDDEESW IKEKRLLVSS DDFGRDLTGV QNLKKKHKRL
ENEFISHQPN IDSVIEKGEQ LINSGQMGGD EIRGRVDNLR ENWLGLRDIA FGRVKKLNES
EEFQVFIGKV EEEEAWITEK QQVLSVEDFG DTMAAVQSLI KKHGAFEVDL GVHRQRIGEI
MQHGQALIDS GNHHAQTIQA RLHQLQVRLA SLVDLAARRL QNLLDNSAHL LFVWKCDVVD
SWIGEKEAAV RSDDYGRDLS TVQMLLTKQE AFDAGLNAFE HEGIQRITEL KDQLTAAQHR
QSRAILDRHA DVIGRWQRLL NNSAGRRQKL LQTQDQFRQI EELYLAFAKK ASAFNSWFEN
AEEDLTDPVR CNSLDEIKAL RDAHKAFHAS LGSAENDYHQ LQDLDARIKS FNVGPNPYTW
FTMDALDETW KNLQKIIKER EAELIKEHRR QEENDRLRRE FAKQANTFHA WLTDTRTQMM
ETTGTLEEQL DILKRKAVEV RAQRGHLKEI EELGALLEEH LILDNRYTEH STVGLAQAWD
QLDQLAMRMQ HNLEQQIQAR NQSGVSEEAL REFSMMFKHF DKEKTGRLDH QQFKSCLRAL
GYDLPVLEEG QPDPEFQRIL DVVDPNRDGY VTLQEYMAFM ISRETENIQT SEEIESAFRA
LSKDYRPYVT SEELYANLSI EQAEYCIQRM KGYVEPLSGR SVPGALDYEQ FLNESTRENL
SFLAPRHTAA VAFFLPLMDC TWVKIKCSIQ EVNLISLNSG QSFRWTVDKD GIWTGVVHHQ
VLRVRRGDGC IWLQRIGRFS RCQIGKKDCL RDYFQLGTPI ADMHSHWSAL DPRFAEAHRR
HPGVRVLRQD PFECLIAFIC SSNNNIPRIT SMINRLCERF GERIVVGRHS YYDFPTAEAL
SAMHAEGSLR RLGFGYRARF VVEASRIVQD RGRDWLQSLR HCSYEVASGQ LQRLPGVGQK
VADCVCLMAL DKTDAVPVDT HVWRLTRDHY LTNLDDRQHL TPALYKQIGM ICSSSSSSSS
SSSVFYSYAS QTKKMDKSNF VRIYH
//