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Database: UniProt
Entry: I4YA00_WALMC
LinkDB: I4YA00_WALMC
Original site: I4YA00_WALMC 
ID   I4YA00_WALMC            Unreviewed;      1583 AA.
AC   I4YA00;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=Myosin 5 {ECO:0000313|EMBL:EIM20792.1};
GN   ORFNames=WALSEDRAFT_33020 {ECO:0000313|EMBL:EIM20792.1};
OS   Wallemia mellicola (strain ATCC MYA-4683 / CBS 633.66) (Wallemia sebi (CBS
OS   633.66)).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC   Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX   NCBI_TaxID=671144 {ECO:0000313|EMBL:EIM20792.1, ECO:0000313|Proteomes:UP000005242};
RN   [1] {ECO:0000313|EMBL:EIM20792.1, ECO:0000313|Proteomes:UP000005242}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4683 / CBS 633.66 {ECO:0000313|Proteomes:UP000005242};
RX   PubMed=22326418; DOI=10.1016/j.fgb.2012.01.007;
RA   Padamsee M., Kumar T.K.A., Riley R., Binder M., Boyd A., Calvo A.M.,
RA   Furukawa K., Hesse C., Hohmann S., James T.Y., LaButti K., Lapidus A.,
RA   Lindquist E., Lucas S., Miller K., Shantappa S., Grigoriev I.V.,
RA   Hibbett D.S., McLaughlin D.J., Spatafora J.W., Aime M.C.;
RT   "The genome of the xerotolerant mold Wallemia sebi reveals adaptations to
RT   osmotic stress and suggests cryptic sexual reproduction.";
RL   Fungal Genet. Biol. 49:217-226(2012).
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR   EMBL; JH668236; EIM20792.1; -; Genomic_DNA.
DR   RefSeq; XP_006959057.1; XM_006958995.1.
DR   STRING; 671144.I4YA00; -.
DR   GeneID; 18471607; -.
DR   KEGG; wse:WALSEDRAFT_33020; -.
DR   eggNOG; KOG0160; Eukaryota.
DR   HOGENOM; CLU_000192_9_0_1; -.
DR   InParanoid; I4YA00; -.
DR   OMA; EIMFDDR; -.
DR   OrthoDB; 1094820at2759; -.
DR   Proteomes; UP000005242; 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   GO; GO:0006996; P:organelle organization; IEA:UniProt.
DR   CDD; cd15480; fMyo2p_CBD; 1.
DR   CDD; cd01380; MYSc_Myo5; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.190; -; 2.
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; IPR046943; Fungal_Myo2/2A_CBD.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR004009; Myosin_N.
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; 2.
DR   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM01132; DIL; 1.
DR   SMART; SM00015; IQ; 5.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF50084; Myosin S1 fragment, N-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51126; DILUTE; 1.
DR   PROSITE; PS50096; IQ; 2.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS51844; SH3_LIKE; 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:UP000005242}.
FT   DOMAIN          5..55
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          61..752
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          1255..1535
FT                   /note="Dilute"
FT                   /evidence="ECO:0000259|PROSITE:PS51126"
FT   REGION          632..654
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   COILED          911..997
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         154..161
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1583 AA;  178941 MW;  CF0EB077AA897C89 CRC64;
     MSEYSIGVRV WIADKTEGWI GAEVTAHSGD EITFKDERGT EIIKKSSAND LPLLRNPVLL
     EGTDDLVNLS YLNEPAVLYS IKRRYAQHSI YTYSGIVLIA VNPFAKLSIY GPAIMQAYST
     RRRGELEPHI YAIAQDAHAS MTRENKNQTM VVSGESGAGK TVSARHIMQY LAFLGQDGTG
     SASTGTDASI LATNPVMEAF GNAKTIRNNN SSRFGRYLKI LFDKQCNIIG AQTSIYLLER
     SRLIFQPEGE RNYHIFHQLC AGVPPKERAE LHLGSSNDFH YLNQGGSASI PGIDDGAEFE
     VTQKALSTLG IGVEKQWNIF KLLASLLHLG NVKIGQTRND AVLNEDDEAF KIATEFLGIN
     PSDFKKWTVK KQITTRGESI VSSLNAAQAS VVRDSVAKYI YACLFDWLVA VLNEALYKES
     DASKFNSFIG VLDIYGFEHF KRNSFEQFCI NYANEKLQQE FNAHVFKLEQ DEYIKEQIRW
     EFISFSDNRP TIDMIEGKLG ILSLLDEESR MPSGTDQNFL EKLHSQLGKP QYKDIYKKPR
     FGNTAFTVAH YAHDVAYEAE GFLEKNRDTV PDEHLQLLGS SSNSFLREVI EIAVASNAAA
     TPASSTASNN VGVGRRQNLK KPTLGSIFKG SLISLMDTIN DTNAHYIRCI KPNEQKKAWD
     IDSQQVLSQL RACGVLETIK ISSAGYPTRW SFAEFTDRYY PLVGSEHWLG DMKELCLQIL
     QVNISDEDKY QIGLSKIFFR AGMLAYLEKL RADRLNTLVT LIQKNILRYL HVKHYKKLRE
     ATVSIQTWWR KILAIRYVEN LRRDTIIFRL QSAGRRKLAV AKFQNIRRSV IMTQAQIRGM
     QARVGFADFK YRSSALNLQR IARGVLARRQ HETSLRGVIH LQACYRRRLA RKEFKQLKSE
     ARSVAHIQEV SYKLENKVVE LTQNLQKTRE EKKELTRRCN QLEKQMGNMQ TRHDDADQRM
     KEMMVELAKP TVALTDFNEL EALKRDLQTQ VSTLKIDIQE RDKQIQQHKD ELGTQAQEIE
     SKSAQAAEAS ARAADETLVN QLKAEIGSLK DQLHRANTLN ALEHGSTKAK QITAPTFSMH
     LGKSNENVAA LVNGAGSPVE GDASDALEAL GLPPNKRRQR RHSANGAFLE QNGLGRDTSD
     EAFAAGKRSE AAPRAVSLAY PTTDNASKLR GLNGRAYFPE VLDDPSEEMI KLLEDEQSID
     DDILTTMIHE LKAPPPSLQN PPSAKEVLFP AHIMSLVTNE MWKYCLIMES ERLLANVMQT
     IQQHVMSFQG EDAIVPGLFW LSNVHEVWSF VCVTEDDMLQ GIVPGGDDPD RPLDWPAYEQ
     LITVVKHDLE SLEYNIYFAF MEETKKKLRK MIVPALIESQ SLPGFITSDT GGRLFNRLLQ
     GNSQPAYNMD DILNLLNKVW KCLKSYRLDE PVVLQVMTEL LRLIGNVGFN DLLMRRNFNS
     WKRAMQIQYN LTRLEEWCKS HDLPEGCLHL EYMMQATKLL QLKKATTQDM EIIFDVCWIL
     SPSQLHKLIT GYMIADYESP LSPHVLQTVS ARLSSDRNDH LLLAEEEGSN FELPQPRQVI
     GLDLYIPGTV SVPHLRRIAG LAA
//
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