ID A0A0K0FKM8_STRVS Unreviewed; 1770 AA.
AC A0A0K0FKM8;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Dilute class unconventional myosin (inferred by orthology to a D. melanogaster protein) {ECO:0000313|WBParaSite:SVE_0959200.2};
OS Strongyloides venezuelensis (Threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=75913 {ECO:0000313|Proteomes:UP000035680, ECO:0000313|WBParaSite:SVE_0959200.2};
RN [1] {ECO:0000313|Proteomes:UP000035680}
RP NUCLEOTIDE SEQUENCE.
RA Martin A.A, De Silva N.;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:SVE_0959200.2}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (AUG-2015) to UniProtKB.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR STRING; 75913.A0A0K0FKM8; -.
DR WBParaSite; SVE_0959200.2; SVE_0959200.2; SVE_0959200.
DR Proteomes; UP000035680; Unassembled WGS sequence.
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; cd01380; MYSc_Myo5; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 3.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.30.70.1590; -; 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 InterPro; IPR002710; Dilute_dom.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR036103; MYSc_Myo5.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR13140:SF860; DILUTE CLASS UNCONVENTIONAL MYOSIN, ISOFORM C; 1.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR Pfam; PF01843; DIL; 1.
DR Pfam; PF00612; IQ; 5.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM01132; DIL; 1.
DR SMART; SM00015; IQ; 6.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF50084; Myosin S1 fragment, N-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50096; IQ; 5.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Coiled coil {ECO:0000256|SAM:Coils};
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:UP000035680}.
FT DOMAIN 80..767
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1458..1722
FT /note="Dilute"
FT /evidence="ECO:0000259|PROSITE:PS51126"
FT REGION 646..668
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1103..1130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1374..1395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 919..1053
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1143..1177
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1103..1118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 177..184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1770 AA; 206056 MW; 0097477D01A23377 CRC64;
MDSMCTLGRQ EKFPLESYTK GTSVWIRDNE LVWKCYILQD NIKFSQSTIL LQNTDDEDDI
IKYDILKNNL PFLKNPDILR GKNDLTSLSY LHEPAVLSNL QYRFETLSSI YTYCGIVLVA
INPYCDCSNL YSDEVIKVYS GVGKQVRGLD PHIYAISEEA YYDLCEYGKN QSIIVSGESG
AGKTVSAKFV MRYLATVASN WKENLKNEIG IEKKVLASNP IMEAIGNAKT IRNDNSSRFG
KFIKINFNER RTISGAQMKT YLLETSRVVF QTTYERNYHI FYQMCAAKNH PILKDLDLMD
CIKYNYLYGG ECDVIDGVDD EKEFYETLEA LTRLGIYGDL KNNIFKLLAA ILIMGNINYV
EISENVAQVT DDNSLNICGS LLSVDPSTLK LWLTAREIRC GKELMRKPLS KNEALVNRDA
LSKLLYSSLF NWIVEQINIS LSVEKNAIKY QKGKKCEPKF IGVLDIYGFE TFTINSFEQF
CINYANEKLQ QQFNQHVFKL EQEEYVKEGI EWVRIDFYDN QSCIDLIENR PGIIDYLDEQ
CKVGRGTDDD WLRTMSTCKN VSKNPNFLLP KISDPSFIVK HFAADVQYKI EGFLEKNKNT
VNEQLLEVVL NSQSDFIKNV MVDTVGMSTS GNERKKTVSF KFRESLKELI LVLSSTTPHY
VRCIKPNDVK ESFFMEPKRS IQQLRACGIL ETVRLSAAGY PSRMEYEDFG RRYRVLYTVD
SKLWKNNCKK FAEITCAEYL ENEKFALGKT KMFFRTGQIA LLERLRFDKF SSAALTIQCF
WRKCQAVKLF NSRKGALLLI QRSLKGFLAY RRIKYLQMYR AAIEIQSKWR GYYHRQNYKK
VCKAVLVIQT YYRRNVAKKE YMRQRYEHAA LTIQRYARGW LVRKEQIERT RKIIKVQCLV
RRWLARRKLR ELKIEAKSVG HLQKLNKGLE NKIISLQQKL DIAVSNIEVV NEKEKKIELL
SKEIERFEIE RLSLLEIKKN YEKMKEEMTF LKNQINEKDK HIDDLNKKIK DEERLENLHK
KREQKVVELK EELNKASLEN MKLTEECSKL RKELGIECDM RLDAQSRLEE MKNQLMENAC
LLAPESSPEV SDDKSVLNDI INTPSKKNRS NGSEIGVTST EREIDGKSSH EDVSVINKQM
TMLLSQQKII QNLRHREDEL KRKVDDLLSS VEELSASHIC CNSYDNLKYI SLENSYNKLK
LEMSLLLGEK ISNKSFLSNI PVFGNSGDKN FKDIFNRLIN ENEKLIMESN ELKFLLTKCL
KTSDLASSKD SNINYMEYDN EEEDSIIGSD SYNPLETELS LLREITCLKN KLLFKEQQLE
EKTINIEKLH QRIENLTPFI KVEDNQSYLE CAGQIINLVD ENLSLQEKIN KQSEKIEQMR
KNSSNENTEY DKDNSVSEHN KGLIKVTNIP EFANSLVIGL RAKIIKVIPP LLPAKIIFGA
LRLFDKENDE IGFTNCFTNI HDNIKEVFNE SSDFDVVLIW FVNSWKLLNL LRQYSMNDET
CKGIWYEKNT EQQKMMILQN IHTESFRRQL ETRIESGYNI ILKKHIEIVL TPKIVPAILM
HDETKGQNKN DKSLYNLLDF LASIYTKLKR MNADDTIMQQ FFSQLTQWVS SLSLNHMLFR
KDLCSFERAF IIKHNVTELG DWLKKNNLSK FCEYLEPLIQ ATHLIQSQKT VQNVETLCGS
MTSSLKPRQI ISILQHYTPS IDFEDDKPTP EFLRMVKEHL AKREKENDES LVRGTYIEPF
NIENFVYSDD NLEDISIPPC LRLISYCKLI
//
