ID A0A0V1CUB8_TRIBR Unreviewed; 2090 AA.
AC A0A0V1CUB8;
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=Myosin-VIIa {ECO:0000313|EMBL:KRY52686.1};
GN Name=ck {ECO:0000313|EMBL:KRY52686.1};
GN ORFNames=T03_17574 {ECO:0000313|EMBL:KRY52686.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY52686.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY52686.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY52686.1};
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 TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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:KRY52686.1}.
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DR EMBL; JYDI01000100; KRY52686.1; -; Genomic_DNA.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR CDD; cd17092; FERM1_F1_Myosin-VII; 1.
DR CDD; cd17093; FERM2_F1_Myosin-VII; 1.
DR CDD; cd14473; FERM_B-lobe; 2.
DR CDD; cd13198; FERM_C1_MyoVII; 1.
DR CDD; cd13199; FERM_C2_MyoVII; 1.
DR CDD; cd01381; MYSc_Myo7; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 1.20.80.10; -; 2.
DR Gene3D; 6.20.240.20; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR Gene3D; 1.25.40.530; MyTH4 domain; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR041793; MyoVII_FERM_C1.
DR InterPro; IPR041794; MyoVII_FERM_C2.
DR InterPro; IPR036106; MYSc_Myo7.
DR InterPro; IPR000857; MyTH4_dom.
DR InterPro; IPR038185; MyTH4_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR22692:SF33; MYOSIN; 1.
DR PANTHER; PTHR22692; MYOSIN VII, XV; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF00612; IQ; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF00784; MyTH4; 2.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00295; B41; 2.
DR SMART; SM00015; IQ; 3.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00139; MyTH4; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF47031; Second domain of FERM; 2.
DR SUPFAM; SSF54236; Ubiquitin-like; 2.
DR PROSITE; PS50057; FERM_3; 2.
DR PROSITE; PS50096; IQ; 3.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51016; MYTH4; 2.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 64..755
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 939..1177
FT /note="MyTH4"
FT /evidence="ECO:0000259|PROSITE:PS51016"
FT DOMAIN 1182..1494
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT DOMAIN 1630..1780
FT /note="MyTH4"
FT /evidence="ECO:0000259|PROSITE:PS51016"
FT DOMAIN 1786..2084
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 611..633
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT BINDING 150..157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2090 AA; 241430 MW; 1EEE65F935DB6C33 CRC64;
MVHFEKDDYV WIPFFSNQTG FSCPIGARIV DIDNGRVFLR DDDGNETWLE GSVSMPIMHP
SSVQGVEDMI ELTDFHDASV LRNLQIRYKQ KLIYATINPY QQLPIYSAEM LEMYRGKRIG
ELAPHVFAVA ENAYMQMMND NQSYCIIISG ESGAGKTETA KLVLQHLAVV SSRCDRHSWI
EQQILEANPI LEAFGNAKTV RNDNSSRFGR YIDMLYNDHG MIESARIEQY LLEKSRLVSQ
SKNERNFHIF YCMLAGMNSQ EKAMFELEDS STYFYLSQGK NFQIEGREDE SIIFRDVRAA
MKVLFFSDIE IMSIFKLLAA ILHIGNIRYT ATLINNLEAT EITTAASVLK VAKLLQVDQM
KLINALTTRT ISLKEETVVS SMTAEQSLDV RDALAKAIYG RLFTWIVDKI NFVIKKVREE
NGQQNSIGIL DIYGFEQFQR NSFEQFCINY ANESLQQFFI RHSFKLEQEE YAREQIKWTT
LEYIDNQPIL DLIAYRSINL FGLLDEESRI PKGTDQSFLT KAHQAFGRNR NYIKPKSDLN
PSFGVVHYAG SVMYHNKGFV EKNRDALSKE LLMLLQESNF PFVAHLFSKE FQDDNARQLK
VTTSFKFRKS LETLMAQIDR RKPYFIRCIK PNDMKKPMLF DRELCYDQLK YLGLMDTIQI
RKSGYPIRYK FQDFAARYKT LLPSLSKPNF CNSALMFTEN QHLISHSDSK NAKNNQWVCE
RICFNAFGPP GEYQIGTSRV FLKDSQLLFL EQRRDEMLHI RATLIQKTIR GWLMRSKYQR
TRQACIMIQK HWRRYQQETR YRKIVRGFSR LQALVRAKKL TMEYQKLKIL ITSFQALCRG
MLMRTKLRHS IATGQPKIYL SEMALESVYE RDELIHENTN DSKMIDEFFD FLLADVDPIT
DYKHGIQAKG KLSSVEDVSQ YQFTKFAAAY FVGNATPNFT KTILRTPLLN HTNPANRIAA
VGIWITILRF MGDLSRQRKM TTHLNGFNCP SVMTQLFSTL ARGMHRKDRS QQADESILDY
SPAGLVGENV RYKMTGWSPQ RKAKSSTVEP MFKDLESQAD DYENMLEKAT ANPLDQLHFI
IGHGILRPEL RDEILCQICK QLSNNPNSQS TLRGWILLSL CVSCFPPSSK FIKYLRCFIR
HQAPKEYIVY CEQRLNRTLE NGARTQPPSH YEVQATKQRK PLVFPVTFMN GTTQTLVGDA
ATNAHELCEA LAKSINLRDK FGFSLYIALQ DKVCSLGSTD EHVLDAISQC EQYAKEIGAK
EQAVQWRLFF RKEIFTPWHN PAEDPVATDL IYQQVTRGVK FGEYRCNRDE DLAQLIAYQY
FLDYGFHFQA EQLKSVIQNY IPDHVLDGVE NMKHAIERWV QIVLHTSRKC LPLEEKTSSQ
HVQENVVAYC RLKWPLLFSR FYEAYKFAGP KLPKNEVIVA VNWTGIYVVD DQDQVLLEIG
FIEMANATCT HSKNKMPTVT IETIQTDEYS FQAPNAEDIV NLVCYFLHGL RMRSRFVIAL
TDTTADQSGQ WLKMRKGDLI KLDSSVNGEL LIRNRSAQGE HTLTGEVGHV ECESVYILPT
LSKPSQEILE EFVQCREVGG VNSRALVNRY RADGPHTLES FSAEHFRAPL AIVTVNTLPR
QRITEELWRH SYEPLTQPLL KKVQTVEDAC QSALATYEAI VAYMGDSAQR HRQRFSTLEQ
TDLIFSAPLK QALLRDEIYC QIIKQLTGNP GRMSVEKGWE LMWLCVGLFP PSQTLHKEVA
LFLRSQHHPV AADCFNRLQR IKRVGSRKYP PHVVEVEAIQ RKTTQIFHKF YFPNDTYENI
EVDSCNKAKD LSVRIAKHIQ LKSVKGFAFF VKIQDKILSL PENEFFFDFI RHLSELTSKT
KSGQSGRNLN YQVYFMKKLW VDTVPGQDRQ ADIVFHYSQE LPKYIRGYHQ CTRDEAAELA
ALIYRSRYGD NASNISSSLA DLLPKVFLKM ASSVDWKRHI LSYYHKGSFM SREEAKVQFL
KVIYKWPTFG SAFFEVKQTG DNKIPEKLII AINKNGIILI EPERKDIIAS YSFPEISNWN
SGNTYFHLTI GNVVNGSRLL CETSMGYKMD DLLTSYITPA IRKQPACRRH
//
