ID A0A0V1PH05_9BILA Unreviewed; 2415 AA.
AC A0A0V1PH05;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 03-MAY-2023, entry version 31.
DE RecName: Full=Spectrin beta chain {ECO:0000256|PIRNR:PIRNR002297};
GN Name=beta-Spec {ECO:0000313|EMBL:KRZ95488.1};
GN ORFNames=T08_9470 {ECO:0000313|EMBL:KRZ95488.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ95488.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ95488.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ95488.1};
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:KRZ95488.1}.
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DR EMBL; JYDM01000012; KRZ95488.1; -; Genomic_DNA.
DR Proteomes; UP000054924; 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; 3.
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:UP000054924};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 71..175
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 229..334
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 2268..2378
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 2185..2243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1051..1092
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1376..1435
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1620..1654
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 2199..2214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2227..2242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2415 AA; 281370 MW; 42987F8F5E0B31A0 CRC64;
MTTDIAIRPD YVDEHIFEDY DENSSARLFE RSRIKALAGD DSSSLLLLSE EDLDLYTMDK
IVKILKDERE NVQKKTFTKW VNSHLERAQC RIQDLYTDLR DGKMLIKLLE ILSGERLPKP
TKGKMRIHCL ENVDKALQFL RLQHVHLENM GSHDIVDGNP RLSLGLIWTI ILRFQTVSSA
ILVRISLSVV LLNLGESVVS VCDNCDRFFM ACVQIQGIEL FDTESQETRS AREALLLWCQ
MKTAGYPNVN VRNFTTSWRD GLAFNALIHK HRPDLISFEK LQRSNALHNL KNAFEVAENQ
LGITSLLDAE DVNVEMPDEK SIITYLVSYY HYFNKLRQET IQGRRIGKVV SELMENDVMI
EEYERLSSDL LQWIKKTIEK LNDRVFVNSL VGVQKQLTTF NNYRTEEKPP KFVSKGNLEV
LLFTLQSRMR ANNQKPYLPR EGRMISDINK AWENLEKAEH ERELALKEEL IRQEKLEQLA
ARFDRKAGMR ETWLAENQRL VSQDNFGSDL PSVEAATKKH EAIETDIYAY EERVQAVVAV
AQDLEAENYN DIDRINARKD NVLQLWNFLL ELLMARRVRL ELSMVIQKIF QDMIHVLGWM
EELKARMLSD DYGKHLMGVE DLIQKHQLVE ADVNIVGDRL KLVCQQAEKF THPDGPDGSG
YQPVEPALVQ ERIQMLEAAY KELLAMVEQR RQRLEDSKRL CQFFLDAEEL EQGFKELEQV
LSSPDVGHDV VSVNLLLAKH KSVEDQIASL QRNKNAVIDI GRGLIGENLP GSSDIQAQID
HIEEMWQALQ TLANLRKQRL VGAVDYYQLF SDIDDNEAWL LDSLRILSSE DVGKDEPSVQ
HLIKQHDGVT EELQNGRNSL DQLYAQAEQL PEAARAGPDV ADRLGQIEKR YAEVMELGSM
RKQRLLDALT LYKLFNDTDN LEAWIDEKAK LLESLKPADD LEEVEIMRHR FETLEQDLNN
QSAKVLTVNK LSRQLLHVEH PNSDAILQRQ NRLNARWAQL QDMVRRKRLE LDQAHRLQTF
RIDCQETVTW IQDKTRVLED TEELKDDLSG IMKLQRRLSM MERDLGAIQA KLDNLEQQAV
RLQQERPEEV EAIRENIARI QYVWDRLTGK VREYEAKLDE AGDLQRFLRD LDHFQGWLSS
VMRQVASEDE PQSLAEAEQL LSQHSVIREE IDGYAEDYAK MRMMGDRVTQ DQTDPQYLLL
RQRLDGLQEG WQELHRMWDN RQAMLSQALN LQMFLRDAKQ AELLLNQQEN YLAKDEAPTS
LEQAETMLKR HGDFLTTMEA GDEKIRAVVV FGNQLCEDGH FAADRIHKKV SNVHERRELN
REKANSMTER LREHVALQQF LSDCEELRRW IEEKMIRAQD ETYRDAKTVH SKFMRHQAFE
AEIQSNKERL QRLQEACVRL IAEKPQLDSF VDPHVAELTA QFDELESKTK EKGQRLFDAN
REAIYVQACE DMTEWVEAME KQMGTEDVAQ DLATVNVEIQ KQQLIESEML KRVQQVCQLQ
AMEPQLEELR PEEFDAIKTH RLTVQEKFSK LQAPLEQRRQ LLERKKEAFQ FLRDVEDEKL
WIADRRPMAR SPMLGDTLFD CHRLQKQNQS LKNEIENHQP WIQRICDNGR KLIASGHENA
PEFEAKIKEL LEALEELKKD VEKRRERLAE SEKAHQYIYD ANEAEVWMSE QELYMMTDDR
GRDEFTTENL IKKHERQRQD VEQFADTIRD LADRAQKLIA EHAPMSDTIA IRQAQIDKSY
AGLQDLSRER RHRLGETLQL FNLHRQIEDI LQWIAEREVV AASQDAGQDY EHVQMLQERF
RQFAKDTETI GTERVSNANE ECDQLMAVHH PDAPTVALWK DNLNEAWENL LELMQTRAQM
LDASCQLHKF FHDCRDTLSR ILEKSHSMPE DLGRDASSVS ALQRKHQNFL TDLLSLESQV
KQVQADARSL QASYAGDRAL EIQAREGEVL NAWRLLQANC EGRRTKLLDT SDLFRFMQMV
RDLLLWMEEV KREMNTQERP KDVSGVELLM NNHQSLKAEI DAREENFSSC IALGRDLLAR
KHYASSEIEK KLIKLTTERA EMMRRWEDRW EYLQLILEVY QFARDAAVAD AWLLAQEPYL
LSKEYGRTLE EVVKLIKKHE AFEKSTIAQE ERFQALEKLT TLELRAQEYL MWLRMGNRLA
LADMAQCGLR FMEAMESEMF ELKELQRRQD EQERLRRTGS PRTSTPTRSP EKLETTFPAE
SGGRTETTLG VDEERRRQLH SSESPGWRIS LSRSKYFDAN DSVGTESAEG FEGHLIRKHT
WETLDRKASI RSWDKLYCVI RGSQLEFYKD HKHREDGELY RGETPINLVG WNVEIASSYT
KRRNVLSLRS PAGFEYLLQA RDEDDMLRWL HQLRTAVGIL ETSTSSSGKA STLPAAQQPS
AKKRFFGTLK KKQAL
//
