ID A0A0V0X8U3_9BILA Unreviewed; 2719 AA.
AC A0A0V0X8U3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Spectrin alpha chain {ECO:0000313|EMBL:KRX84475.1};
GN Name=alpha-Spec {ECO:0000313|EMBL:KRX84475.1};
GN ORFNames=T06_7463 {ECO:0000313|EMBL:KRX84475.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX84475.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX84475.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX84475.1};
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:KRX84475.1}.
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DR EMBL; JYDK01000006; KRX84475.1; -; Genomic_DNA.
DR Proteomes; UP000054673; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 12.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 1.20.58.60; -; 20.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 2686..2710
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 922..981
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 2206..2241
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 2249..2284
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT COILED 775..834
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1159..1200
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 2719 AA; 314543 MW; 37D1F6D55534C06F CRC64;
MDDHTPPEPV LEVPPPQEIK ILETASDIQQ RRSEVLGHYR AFKEMAQNKR DRLEEARQFQ
YFKRDADELQ LWILEKLQTA QEESYRDPTN LQAKIQKHQA FEAEVQAHSN AILQLDKTGN
DMIMHGHFAH ATIKERLDEL HALWEQLLQK LAEKGIRLQQ ALKLLLFTRQ CDEVMYWILD
KEAFVTTEEF GQDLEHVEVL QKKFDDFLKE LANQQYRIAE ELLAAWKHLN DLSVTRKERL
FGAHEVQRFN RDIDETIAWI LEKDSGLSVD DFGRDLTTVQ ALQRKHEGTE RDLAALDGKV
QSLAIEAERL KSLHPDRVES IESKKLDALT NWEQLKRKAA ERKAGLEHYR DLTSWIADMK
ALIMADELAK DVAGAEALLE RHQEQRGEID AREDSFRATE EAGRRLLAED IPQKNEVAEK
IKSLAADKEA LLALLEERRI LYEQCMDLQL FYRDTDQAET WMTKQEAFLA NEDLGESLDS
VEALIKKHED FEKSLAAQEE KIKAFDEFAT KLIEGQHYTA DDLLQRRAGL LERAARRRTM
LEDAYRLQQF ERDCDEMMSW INEKLKTARD ENYLQELHAN KSRLDDIHKR GSELVSSGHY
AADDVSRRLD EVQNSWSDLV VATEQKGAKL KEAGGQQQFN RNVEDIEMWL AEVEAQLMSE
DYGKDLISVQ NLQKKHALLE CDVNAHAERI EGVGQQAAQF EAAGHFDIGN IRAKEQKLIG
RYNALQEPMS RRKEKLAESL RGHQLFRDIE DEFSWIREKE QIADSTNRGR DLIGVQNLIK
KHNALMAEIA NHEMQINKVV NAGEEIMKED HFLASEIKAK LSALQDNWQL LKEKANKRGQ
DLEDSYMAHQ YLADANEAES WMSEKEPIVG SADYGKDEDS AEALLKKHSA LMSDLEAFRS
TIEHLREQVN HCKTDTTIIG SLGRECVVAL YDYSEKSPRE VSMKKGDVLT LLNSSNKDWW
KVEVNDRQGF VPVAYLKKME PGLSSSQQQL LQSSSIAAKQ SQIENLYQHL LDLGNQRRKK
LEEACKGYQL LREANELAEW IRSKEQLATS HEIGQDLEEV EVLQKKFDEF QADLRAHEVR
LAEMNKISTA LAAIGQTEAA NLNERWQALQ EVTTQRAQQL GSAHEVQRFH RDVDEAKDWM
KEKDDALDSE DFGRDLRSVQ ALQRKHEGLE RDLAALGDKI RQLDETANRL RQTHPEAAEQ
IYDLQLQLND RWSALTSKAN NRKEKLLDSY DYQRFLSDCR DLQRWNNNTM VLVNSDELAN
DVTGAEALLE RHSEYRTEMD ARAGMFQKFD QFGNDLLSMH HYASADVVEQ MHKIAEAREN
LEKAWMARRM KLDQCLELQL FYRDCEQAEN WMSSREAFLN QEQVSPDNVE SLIKKHEDFD
KAINSQQEKI AALQSFANQL VNRGHYAEED IIRKRDQVLD RWAKLKQALI EKRSKLGESQ
TLQQFSRDAD EIENWIAEKL QVALEESYRD PTNIQSKHQK QQAFEAELGA NSDRIQTIMY
AGQNLIDSNK CAGSESVVSQ RLTALNDQWE LLVKKTTEKS YRLKEANKQQ SFIAAVKDLE
FWLGEIETLL ASDDFGKDLA SVQNLLKKHQ LIEADIAAHA ERVRDMNTEA SSLLENDQFD
PVTIEERQKS INDRYKRVSE LAEERKRKLN EALTLHQFFR DIDDEESWIK EKRLLVSSDD
FGRDLTGVQN LKKKHKRLEN EFISHQPNID SVIEKGEQLI NSGQMGGGEI RGRVDNLREN
WLGLRDIAFG RVKKLNESEE FQVFIGKVEE EEAWITEKQQ VLSVEDFGDT MAAVQSLIKK
HGAFEVDLGV HRQRIGEIMQ HGQTLIDSGN HHAQTIESRL HQLQVRLASL VDLAARRLQN
LLDNSAHLLF VWKCDVVDSW IGEKEAAVRL DDYGRDLSTV QMLLTKQEAF DAGLNAFEHE
GIQRITELKD QLTAAQHRQS RAILDRHADV IGRWQRLLNN SAGRRQKLLQ TQDQFRQIEE
LYLAFAKKAS AFNSWFENAE EDLTDPVRCN SLDEIKALRD AHKAFHASLG SAENDYHQLQ
DLDARIKSFN VGPNPYTWFT MDALDETWKN LQKIIKEREA ELIKEHRRQE ENDRLRREFA
KQANTFHAWL TDTRTQMMET TGTLEEQLDI LKRKAVEVRA QRGHLKEIEE LGALLEEHLI
LDNRYTEHST VGLAQAWDQL DQLAMRMQHN LEQQIQARNQ SGVSEEALRE FSMMFKHFDK
EKTGRLDHQQ FKSCLRALGY DLPVLEEGQP DPEFQRILDV VDPNRDGYVT LQEYMAFMIS
RETENIQTSE EIESAFRALS KDYRPYVTSE ELYANLSIEQ AEYCIKRMKG YVEPLSGRSV
PGALDYEQFP QFPGTEAQLR LRCVTLFLPL MDCTWVKIKC SIQEVNLISL NSGQSFRWTV
DKDGIWTGVV HHQVLRVRRG DGCIWLQRIG RFSRCQIGKK DCLRDYFQLG TPIADMHSHW
SAMDPRFAEA HRRHPGVRVL RQDPFECLIA FICSSNNNIP RITSMINRLC ERFGERIVVG
RHSYYDFPTA EALSAMHAEG SLRRLGFGYR ARFVVEASRI VQDRGRDWLQ SLRHCSYEVA
SGQLQRLPGV GQKVADCVCL MALDKTDAVP VDTHVWRLTR DHYLTSLDDR QHLTPALYKQ
IGMICSSSSS SSSSMYHQSV HEQFIAIQVI STAKDLVNML AGHRQFYSAI FSLYLFLLFY
SCFIYCQFFI RMHRRRKNG
//