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Database: UniProt
Entry: A0A0V1MM99_9BILA
LinkDB: A0A0V1MM99_9BILA
Original site: A0A0V1MM99_9BILA 
ID   A0A0V1MM99_9BILA        Unreviewed;      2284 AA.
AC   A0A0V1MM99;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   03-MAY-2023, entry version 29.
DE   SubName: Full=Spectrin beta chain {ECO:0000313|EMBL:KRZ72966.1};
DE   Flags: Fragment;
GN   Name=beta-Spec {ECO:0000313|EMBL:KRZ72966.1};
GN   ORFNames=T10_12095 {ECO:0000313|EMBL:KRZ72966.1};
OS   Trichinella papuae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ72966.1, ECO:0000313|Proteomes:UP000054843};
RN   [1] {ECO:0000313|EMBL:KRZ72966.1, ECO:0000313|Proteomes:UP000054843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ72966.1};
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}.
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:KRZ72966.1}.
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DR   EMBL; JYDO01000070; KRZ72966.1; -; Genomic_DNA.
DR   Proteomes; UP000054843; 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:InterPro.
DR   GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
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; 8.
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; 15.
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   Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054843};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          47..151
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          166..271
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          2137..2247
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          2087..2136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          988..1029
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1313..1372
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1557..1591
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1631..1658
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        2098..2131
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRZ72966.1"
SQ   SEQUENCE   2284 AA;  266752 MW;  453FF97D157566F0 CRC64;
     LKSNMTTDIA IRPDYVDEHI FEDYDENSSA RLFERSRIKA LADERENVQK KTFTKWVNSH
     LERAQCRIQD LYTDLRDGKM LIKLLEILSG ERLPKPTKGK MRIHCLENVD KALQFLRLQH
     VHLENMGSHD IVDGNPRLSL GLIWTIILRF QIQGIELFDT ESQETRSARE ALLLWCQMKT
     AGYPNVNVRN FTTSWRDGLA FNALIHKHRP DLISFEKLQR SNALHNLKNA FEVAENQLGI
     TSLLDAEDVN VEMPDEKSII TYLVSYYHYF NKLRQETIQG RRIGKVVSEL MENDVMIEEY
     ERLSSDLLQW IKKTIEKLND RVFVNSLVGV QKQLTTFNNY RTEEKPPKFV SKGNLEVLLF
     TLQSRMRANN QKPYLPREGR MISDINKAWE NLEKAEHERE LALKEELIRQ EKLEQLAARF
     DRKAGMRETW LAENQRLVSQ DNFGADLPSV EAATKKHEAI ETDIYAYEER VQAVIAVAQD
     LEAENYNDIA RINARKDNVL QLWNFLLELL MARRVRLELS MVIQKIFQDM IHVLGWMEEL
     KARMLSDDYG KHLMGVEDLI QKHQLVEADV NIVGDRLKLV CQQAEKFTHP DGPDGSGYQP
     VEPALVQERI QMLETAYKEL LAMVEQRRRR LEDSKRLCQF FLDAEELEQG FKELEQVLSS
     PDVGHDVVSV NLLLAKHKSV EDQIASLERN KNVVIDTGRG LIGENLPGSS DIQAQIDHIE
     EMWQALQTLA NLRKQRLVGA VDYYQLFSDI DDNEAWLLDS LRILSSEDVG KDEPSVQHLI
     KQHDGVTEEL QNGRNLLDQL YTQADQLPEA ARAGPDVVDR LKQIETRYAE VIELGTMRKQ
     RLLDALTLYK LFNDTDNLEA WIDEKAKLLE SLKPADDLEE VEIMRHRFET LEQDLNNQSA
     KVLTVNKLSR QLLHVEHPNS DAILQRQNRL NARWAQLQDM VRRKKLELDQ AHRLQTFRID
     CQETVTWIQD KTRVLEDTEE LKDDLSGIMK LQRRLSMMER DLGAIQAKLD NLEQQAVRLQ
     QERPEEVEAI RDNIARIQYV WDRLTGKVRE YEAKLDEAGD LQRFLRDLDH FQGWLSSVMR
     QVASEDEPQS LAEAEQLLSQ HSVIREEIDG YAEDYAKMRM MGDRVTQDQT DPQYLLLRQR
     LDGLQEGWQE LHRMWDNRQA MLSQALNLQM FLRDAKQAEL LLNQQENYLA KDEAPTSLEQ
     AETMLKRHGD FLTTMEAGDE KIRAVVVFGN QLCEDGHFAA DRIHKKVSNV HERRELNREK
     ANSMTERLRE HVALQQFLSD CEELRRWIEE KMIRAQDETY RDAKTVHSKF MRHQAFEAEI
     QSNKERLQRL QEACVRLIAE KPQLDSFVDP HVAELTAQFD ELESKTKEKG QRLFDANREA
     IYVQACEDMT EWVEAMEKQM GTEDVAQDLA TVNVEIQKQQ LIESEMLKRV QQVCQLQAME
     PQLEELRPEE FDAIKTHRLT VQEKFSKLQA PLEQRRQLLE RKKEAFQFLR DVEDEKLWIA
     DRRPMARSPM LGDTLFDCHR LQKQNQSLKN EIENHQPWIQ RICDNGRKLI ASGHENAPEF
     EVKIKELLEA LEELKKDVEK RRQRLAESEK AHRYIYDANE AEVWMSEQEL YMMTDDRGRD
     EFTTENLIKK HERQRQDVEQ FADTIRDLAE RAQKLIAEHA PMSDTIAIRQ AQIDKSYAGL
     QDLSRERRHR LGETLQLFNL HRQIEDILQW IAEREVVAGS QDAGQDYEHV QMLQERFRQF
     AKDTETIGTE RVSNANEECD QLMAVHHPDA PTVALWKDNL NEAWENLLEL MQTRAQMLDA
     SCQLHKFFHD CRDTLSRILE KSHSMPEDLG RDASSVSALQ RKHQNFLTDL LSLESQVKQV
     QADARSLQAS YAGDRALEIQ AREGEVLNAW RMLQANCEGR RTKLLDTSDL FRFMQMVRDL
     LLWMEEVKRE MNTQERPKDV SGVELLMNNH QSLKAEIDAR EENFSSCIAL GRDLLSRKHY
     ASSEIEKKLI KLTTERAEMM RRWEDRWEYL QLILEVYQFA RDAAVADAWL LAQEPYLLSK
     EYGRTLEEVV KLIKKHEAFE KSTIAQEERF QALEKLTTFE LKELQRRQDE QERLRRTGSP
     RTSTPTRSPE KLETTFPAES GARTETTLGV DEGTESAEGF EGHLIRKHTW ETLDRKASIR
     SWDKLYCVIR GNQLEFYKDH KHREDGELYR GETPINLIGW NVEIASSYTK RRNVLSLRSP
     TGFEYLLQAR DEDDMLRWLH QLRTAIGILE TSTSSSGKAS TLPAAQQPSA KKRFFGTLKK
     KQAL
//
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