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Database: UniProt
Entry: A0A0V0U100_9BILA
LinkDB: A0A0V0U100_9BILA
Original site: A0A0V0U100_9BILA 
ID   A0A0V0U100_9BILA        Unreviewed;      2421 AA.
AC   A0A0V0U100;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   03-MAY-2023, entry version 30.
DE   RecName: Full=Spectrin beta chain {ECO:0000256|PIRNR:PIRNR002297};
GN   Name=beta-Spec {ECO:0000313|EMBL:KRX44567.1};
GN   ORFNames=T05_5492 {ECO:0000313|EMBL:KRX44567.1};
OS   Trichinella murrelli.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX44567.1, ECO:0000313|Proteomes:UP000055048};
RN   [1] {ECO:0000313|EMBL:KRX44567.1, ECO:0000313|Proteomes:UP000055048}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS417 {ECO:0000313|EMBL:KRX44567.1};
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   -!- SIMILARITY: Belongs to the spectrin family.
CC       {ECO:0000256|ARBA:ARBA00006826, ECO:0000256|PIRNR:PIRNR002297}.
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:KRX44567.1}.
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DR   EMBL; JYDJ01000093; KRX44567.1; -; Genomic_DNA.
DR   STRING; 144512.A0A0V0U100; -.
DR   Proteomes; UP000055048; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProt.
DR   GO; GO:0008091; C:spectrin; IEA:InterPro.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:UniProtKB-UniRule.
DR   GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-UniRule.
DR   CDD; cd21246; CH_SPTB-like_rpt1; 1.
DR   CDD; cd21248; CH_SPTB_like_rpt2; 1.
DR   CDD; cd10571; PH_beta_spectrin; 1.
DR   CDD; cd00176; SPEC; 9.
DR   Gene3D; 1.20.58.60; -; 12.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 2.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR001589; Actinin_actin-bd_CS.
DR   InterPro; IPR001715; CH_dom.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001605; PH_dom-spectrin-type.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR016343; Spectrin_bsu.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   PANTHER; PTHR11915:SF447; SPECTRIN BETA CHAIN; 1.
DR   PANTHER; PTHR11915; SPECTRIN/FILAMIN RELATED CYTOSKELETAL PROTEIN; 1.
DR   Pfam; PF00307; CH; 2.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00435; Spectrin; 17.
DR   PIRSF; PIRSF002297; Spectrin_beta_subunit; 2.
DR   PRINTS; PR00683; SPECTRINPH.
DR   SMART; SM00033; CH; 2.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00150; SPEC; 17.
DR   SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF46966; Spectrin repeat; 13.
DR   PROSITE; PS00019; ACTININ_1; 1.
DR   PROSITE; PS00020; ACTININ_2; 1.
DR   PROSITE; PS50021; CH; 2.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   3: Inferred from homology;
KW   Actin capping {ECO:0000256|ARBA:ARBA00022467,
KW   ECO:0000256|PIRNR:PIRNR002297};
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203,
KW   ECO:0000256|PIRNR:PIRNR002297}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR002297};
KW   Cytoskeleton {ECO:0000256|PIRNR:PIRNR002297};
KW   Reference proteome {ECO:0000313|Proteomes:UP000055048};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          56..160
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          214..319
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          2274..2384
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          2175..2211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1036..1077
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1361..1420
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1605..1639
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        2184..2199
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2421 AA;  282121 MW;  7A9F6B79F2DC990B CRC64;
     MNKSCEYLHA NNAHDSRSTT DSRGDDSSSL LLLSEEDLDL YTMDKIVKIL KDERENVQKK
     TFTKWVNSHL ERAQCRIQDL YTDLRDGKML IKLLEILSGE RLPKPTKGKM RIHCLENVDK
     ALQFLRLQHV HLENMGSHDI VDGNPRLSLG LIWTIILRFQ TVSSSILVRI SLSVVLLNLG
     ESVVSVCDNC DRFFMACVQI QGIELFDTES QETRSAREAL LLWCQMKTAG YPNVNVRNFT
     TSWRDGLAFN ALIHKHRPDL ISFEKLQRSN ALHNLKNAFE VAENQLGITS LLDAEDVNVE
     MPDEKSIITY LVSYYHYFNK LRQETIQGRR IGKVVSELME NDVMIEEYER LSSDLLQWIK
     KTIEKLNDRV FVNSLVGVQK QLTTFNNYRT EEKPPKFVSK GNLEVLLFTL QSRMRANNQK
     PYLPREGRMI SDINKAWENL EKAEHERELA LKEELIRQEK LEQLAARFDR KAGMRETWLA
     ENQRLVSQDN FGSDLPSVEA ATKKHEAIET DIYAYEERVQ AVVAVAQDLE AENYNDIDRI
     NARKDNVLQL WNFLLELLMA RRVRLELSMV IQKIFQDMIH VLGWMEELKA RMLSDDYGKH
     LMGVEDLIQK HQLVEADVNI VGDRLKLVCQ QAEKFTHPDG PDGSGYQPVE PALVQERIQM
     LEAAYKELLA MVEQRRQRLE DSKRLCQFFL DAEELEQGFK ELEQVLSSPD VGHDVVSVNL
     LLAKHKSVED QIASLQRNKN AVIDIGRGLI GENLPGSSDI QAQIDHIEEM WQALRTLANL
     RKQRLVGAVD YYQLFSDIDD NEAWLLDSLR ILSSEDVGKD EPSVQHLIKQ HDGVTEELQN
     GRNSLDQLYA QAEQLPEAAR AGPDVADRLG QIEKRYAEVM ELGSMRKQRL LDALTLYKLF
     NDTDNLEAWI DEKAKLLESL KPADDLEEVE IMRHRFETLE QDLNNQSAKV LTVNKLSRQL
     LHVEHPNSDA ILQRQNRLNA RWAQLQDMVR RKRLELDQAH RLQTFRIDCQ ETVTWIQDKT
     RVLEDTEELK DDLSGIMKLQ RRLSMMERDL GAIQAKLDNL EQQAVRLQQE RPEEVEAIRE
     NIARIQYVWD RLTGKVREYE AKLDEAGDLQ RFLRDLDHFQ GWLSSVMRQV ASEDEPQSLA
     EAEQLLSQHS VIREEIDGYA EDYAKMRMMG DRVTQDQTDP QYLLLRQRLD GLQEGWQELH
     RMWDNRQAML SQALNLQMFL RDAKQAELLL NQQENYLAKD EAPTSLEQAE TMLKRHGDFL
     TTMEAGDEKI RAVVVFGNQL CEDGHFAADR IHKKVSNVHE RRELNREKAN SMTERLREHV
     ALQQFLSDCE ELRRWIEEKM IRAQDETYRD AKTVHSKFMR HQAFEAEIQS NKERLQRLQE
     ACVRLIAEKP QLDSFVDPHV AELTAQFDEL ESKTKEKGQR LFDANREAIY VQACEDMTEW
     VEAMEKQMGT EDVAQDLATV NVEIQKQQLI ESEMLKRVQQ VCQLQAMEPQ LEELRPEEFD
     AIKTHRLTVQ EKFSKLQAPL EQRRQLLERK KEAFQFLRDV EDEKLWIADR RPMARSPMLG
     DTLFDCHRLQ KQNQSLKNEI ENHQPWIQRI CDNGRKLIAS GHENAPEFEA KIKELLEALE
     ELKKDVEKRR ERLAESEKAH QYIYDANEAE VWMSEQELYM MTDDRGRDEF TTENLIKKHE
     RQRQDVEQFA DTIRDLADRA QKLIAEHAPM SDTIAIRQAQ IDKSYAGLQD LSRERRHRLG
     ETLQLFNLHR QIEDILQWIA EREVVAASQD AGQDYEHVQM LQERFRQFAK DTETIGTERV
     SNANEECDQL MAVHHPDAPT VALWKDNLNE AWENLLELMQ TRAQMLDASC QLHKFFHDCR
     DTLSRILEKS HSMPEDLGRD ASSVSALQRK HQNFLTDLLS LESQVKQVQA DARSLQASYA
     GDRALEIQAR EGEVLNAWRL LQANCEGRRT KLLDTSDLFR FMQMVRDLLL WMEEVKREMN
     TQERPKDVSG VELLMNNHQS LKAEIDAREE NFSSCIALGR DLLARKHYAS SEIEKKLIKL
     TTERAEMMRR WEDRWEYLQL ILEVYQFARD AAVADAWLLA QEPYLLSKEY GRTLEEVVKL
     IKKHEAFEKS TIAQEERFQA LEKLTTLELR AQEYLMWLRM GNRLALADMA QCGLRFMEAM
     ESEMFELKEL QRRQDEQERL RRTGSPRTST PTRSPEKLET TFPAESGGRT ETTLGVDEGK
     LFSYFLLVQD IFTRCCHERE RRRQLHSSES PGWRISLSRS KYFDANDSVG TESAEGFEGH
     LIRKHTWETL DRKASIRSWD KLYCVIRGSQ LEFYKDHKHR EDGELYRGET PINLVGWNVE
     IASSYTKRRN VLSLRSPAGF EYLLQARDED DMLRWLHQLR TAVGILETST SSSGKASTLP
     AAQQPSAKKR FFGTLKKKQA L
//
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