ID A0A0N5AM27_9BILA Unreviewed; 2088 AA.
AC A0A0N5AM27;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Spectrin beta chain {ECO:0000313|WBParaSite:SMUV_0000561801-mRNA-1};
OS Syphacia muris.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Syphacia.
OX NCBI_TaxID=451379 {ECO:0000313|Proteomes:UP000046393, ECO:0000313|WBParaSite:SMUV_0000561801-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SMUV_0000561801-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
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DR STRING; 451379.A0A0N5AM27; -.
DR WBParaSite; SMUV_0000561801-mRNA-1; SMUV_0000561801-mRNA-1; SMUV_0000561801.
DR Proteomes; UP000046393; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR CDD; cd21193; CH_beta_spectrin_rpt1; 1.
DR CDD; cd21194; CH_beta_spectrin_rpt2; 1.
DR CDD; cd00174; SH3; 1.
DR CDD; cd00176; SPEC; 8.
DR Gene3D; 1.20.58.60; -; 11.
DR Gene3D; 1.10.418.10; Calponin-like domain; 2.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
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:SF435; SPECTRIN BETA CHAIN, NON-ERYTHROCYTIC 5; 1.
DR PANTHER; PTHR11915; SPECTRIN/FILAMIN RELATED CYTOSKELETAL PROTEIN; 1.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF00435; Spectrin; 11.
DR SMART; SM00033; CH; 2.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00150; SPEC; 14.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR SUPFAM; SSF46966; Spectrin repeat; 14.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 66..170
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 188..293
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 863..934
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT COILED 633..660
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1178..1205
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2007..2034
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 2088 AA; 243909 MW; AC70E4D8557414FD CRC64;
MLLGNEEIEF MQRFSKCEMV QVPQVNRNGY AYTPSAPHPE DYDELADATL FFERTRIKQL
QDERVHIQKK TFTKWCNSFL SRIRMEIDDL FVDVGDGVIL MKLLEIISGE KLGKPNRGQM
RVQKIENLNK SLDFLKAKKI QLENIGAEDI LDRNERLILG LIWTIILRYQ IDNISIPVDD
EEETGERKHA KDALLLWCQR KTAGYPNVKV ENFTTSWKNG LAFNALIHAH RPDLINYEAL
SPQDPVSNLN NAFDVAEREF EVARLLDAED VNVAHPDEKS IITYVSLYYH YFAKQKSEMT
GARRVAKIIG GLMAVDRMQD EYESLCSDLL YWIHHTVAEL TDRSFPNSLK GIQELLIQFK
NYRTVEKPPK YKEKGDLEAL FFTIQTKRKA MHRKPYVPPQ GLFMHDIETA WALLDHSESD
RQLALMAELQ HQERLELKAR KFDRKAKLRE TWLREMYGVL QDFEFGKTAA QVEAALKKQQ
AIAADILPRV FNLWLFSVLS CNISVTSGFS TLEVRFKTLT SMAAELKKEN YHDADRIRTH
EREIWDKWTQ LLTALEARRV ALMSLNDLME LLRDIDALTS EMRLLEPQFL NRDVGKHLLG
VEDLLQKQEI LEAQLNSQGE LLKNMSFRAR SYIRQEGEQY DILQRKLDDA KALHERLIDL
CRQRRTTLFR ARDLYRFIQD HEEEMSWLKE KEDLCIAVLS SRDLSSTPQL SRIFKNLETE
MHSHWQQSKA VIAQGEKLMS SGFNKDDIQS RINKLQNKWE KLRKSASAVE KWLQEAEQAH
QYFQDANEAE SWIREKFPLV KSDDFGRDEQ SSENLLSRHI RLEEEIHAYR SDINRLDQMV
RELANSEFIN APVLHIQEET DELVVPQVRM LYPYSGNNMT VKKDEVRLMH CSNKALCVIM
LALMEKTNND WWMVLKQDGR EGYVPANYCR EIEGEVIKVT QKTTTQKARH EPQDSKKEIL
ERQETINADY RKLNSTAQVR RRLLSDMVKL YRFLRECDQF EAWAKITEAA LSEQVSSENV
AATRMKFDKI DSEIKAQGQT QLKRINDMAN DLINEGHSQS EEIQRRQELA NRLWDHLINS
RKGKGLKVEA AEKVDSFNKI CEETRAWMGD KSLLLDQEID INDPNAVRAI QKRYQNIGKD
LRPLEEKIAE LSRLAEEVTY EVFFLVRVMV KKEHPEEAEK IESLVRDLQK MHSDLQKKAT
EKLQEAEQTQ GHQMFDDGYR KLKAWIENIK TVLAEFPRPV DIASAEELLK KHQELKDDID
SKKYEFDYVR DLAQRLLQKN HDLPEVRRML SELDSDQAEI YKKWNDKERY LNEMLELQLF
NTEAERIDAA TKGHEAFLEI TNLGDSVESV ENLLKRHSDF EAKLKAQDDR LKVFSKTADD
MIKVGHRETP FIKQRRDEVL ARRASVHERA AERRKQLEAS LVYQNLRRNA VELMQWISDK
KKIANDEAYK DTASLPMKKL KHDAFMAEIK ANMPRIEQIN KDGNALIAQQ HQKSAAIKQL
LGDLNKNWRE LCTAADEKSE RLMQADKQKA LNAAFDDVHG RLNEIEEALC SEDLGADLRG
VKDLLLKQGF TEQELVAFEK RINELRTRGD EMIKEGHPDA AKIKADIDKL VQRCFVFCLS
NTAKFNGMKR PADQRRFALE ESLKWHKLSF DIDCELQWIS EKEPIAASKE SGRSLTEVTN
MLKKQDQLIA EVNSHSPIIE ATINRGEQLI KENHYASEEI RNKCHQCKMF LSHSWDSLNH
LLEERKVLLD WALKEEQYLF DALEVVESWI NEKKPLVSSL DYGKDEDAAS KLLAKHKALQ
ADMGTYRKWL SKLTLKCEEL KDSKRSGAER FEARQAELEA QFESLKELVE DRRYQLENAM
FLYQYKRESQ ELESWINDQL QVAMSEEYGQ DYEHLIELKT RFEEFKQSVK TGSERFVHCE
ATAKSLLKRN PPFVRDILMR QEKLRSVWTL LLDYIESRER RLDAAEELHR FNRDVAESHE
RIAEKRAEIP SELGKDIKQV HSLWLKHEAF ENQLSAMETQ LQELLEESAR LKAAYPGGNA
EHITAQQGAL AEAWQDLQDA TVERRDLLKA SYDLHRFNVN LLYFQCIL
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