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Database: UniProt
Entry: R0KZP8_ANAPL
LinkDB: R0KZP8_ANAPL
Original site: R0KZP8_ANAPL 
ID   R0KZP8_ANAPL            Unreviewed;      1766 AA.
AC   R0KZP8;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Myosin-Va {ECO:0000313|EMBL:EOA93467.1};
DE   Flags: Fragment;
GN   ORFNames=Anapl_16740 {ECO:0000313|EMBL:EOA93467.1};
OS   Anas platyrhynchos (Mallard) (Anas boschas).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Anatinae; Anas.
OX   NCBI_TaxID=8839 {ECO:0000313|EMBL:EOA93467.1, ECO:0000313|Proteomes:UP000296049};
RN   [1] {ECO:0000313|Proteomes:UP000296049}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23749191; DOI=10.1038/ng.2657;
RA   Huang Y., Li Y., Burt D.W., Chen H., Zhang Y., Qian W., Kim H., Gan S.,
RA   Zhao Y., Li J., Yi K., Feng H., Zhu P., Li B., Liu Q., Fairley S.,
RA   Magor K.E., Du Z., Hu X., Goodman L., Tafer H., Vignal A., Lee T.,
RA   Kim K.W., Sheng Z., An Y., Searle S., Herrero J., Groenen M.A.,
RA   Crooijmans R.P., Faraut T., Cai Q., Webster R.G., Aldridge J.R.,
RA   Warren W.C., Bartschat S., Kehr S., Marz M., Stadler P.F., Smith J.,
RA   Kraus R.H., Zhao Y., Ren L., Fei J., Morisson M., Kaiser P., Griffin D.K.,
RA   Rao M., Pitel F., Wang J., Li N.;
RT   "The duck genome and transcriptome provide insight into an avian influenza
RT   virus reservoir species.";
RL   Nat. Genet. 45:776-783(2013).
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; KB746221; EOA93467.1; -; Genomic_DNA.
DR   Proteomes; UP000296049; 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; cd15478; Myo5a_CBD; 1.
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; 2.
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; IPR037988; Myo5a_CBD.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR036103; MYSc_Myo5.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR13140; MYOSIN; 1.
DR   PANTHER; PTHR13140:SF273; UNCONVENTIONAL MYOSIN-VA; 1.
DR   Pfam; PF01843; DIL; 1.
DR   Pfam; PF00612; IQ; 6.
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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR   PROSITE; PS51126; DILUTE; 1.
DR   PROSITE; PS50096; IQ; 6.
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:UP000296049}.
FT   DOMAIN          1..649
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          1445..1721
FT                   /note="Dilute"
FT                   /evidence="ECO:0000259|PROSITE:PS51126"
FT   REGION          485..520
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          529..551
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          994..1036
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1058..1089
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          801..987
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1225..1277
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1323..1350
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         60..67
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EOA93467.1"
FT   NON_TER         1766
FT                   /evidence="ECO:0000313|EMBL:EOA93467.1"
SQ   SEQUENCE   1766 AA;  205470 MW;  B595A1090D7E767B CRC64;
     GIVLVAINPY EQLPIYGEDI INAYSGQNMG DMDPHIFAVA EEAYKQMARD ERNQSIIVSG
     ESGAGKTVSA KYAMRYFATV SGSASEANVE EKVLASNPIM ESVYCKCRNS QVLKHIFIRN
     FLPLFLCYPV LLYKVYSLLE EERNYHIFYQ LCASAALPEF KTLRLGNANY FHYTKQGGSP
     VIDGVDDAKE MVNTRQACTL LGISDSYQMG IFRILAGILH LGNVEFASRD SDSCAIPPKH
     DPLTIFCDLM GVEYEEMAHW LCHRKLATAT ETYIKPISKL HAINARDALA KHIYANLFNW
     IVDHVNKALH STVKQHSFIG VLDIYGFETF EINSFEQFCI NYANEKLQQQ FNMHVFKLEQ
     EEYMKEQIPW TLIDFYDNQP CINLIEAKMG ILDLLDEECK MPKGSDDTWA QKLYNTHLNK
     CALFEKPRLS NKAFIIKHFA DKVEYQCEGF LEKNKDTVYE EQIKVLKSSK FKLLPELFQD
     EEKVLSPTSA TPSGRVPLSR TAVKPAKARP GQTSKEHKKT VGHQFRNSLH LLMETLNATT
     PHYVRCIKPN DFKFPFTFDE KRAVQQLRAC GVLETIRISA AGFPSRWTYQ EFFSRYRVLM
     KQRDVLGDRK QTCKNVLEKL ILDKDKYQFG KTKIFFRAGQ VAYLEKIRAD KLRAACIRIQ
     KTIRGWLMRK KYVRMRKAAI TIQRYVRGYQ ARCYATFLRR TRAAITIQKF QRMYVVRKRY
     QCMRDATIAL QALLRGYMAR NKYQMMLREH KSIIIQKHVR GWLARVHYRR TLKAIVYLQC
     CYRRMMAKRE LKKLKIEARS VERYKKLHIG LENKIMQLQR KIDEQNKEYK SLLEKLNSLE
     ITYSTETERL RSDVERLRMS EEEAKNATNR VLSLQEEIAK LRKELHQTQS EKKTIEEWAD
     KYKHETEQAS MQSPELKDQN TLLKTEKEEL NRRIHDQAKE ITEAMEKKLV EETKQLELDL
     NDERLRYQNL LNEFSRLEER YDDLKDEMNL MVSIPKPGHK RTDSTHSSNE SEYTFSSEIT
     EAEDLPLRME EPSEKKAPLD MSLFLKLQKR VTELEQEKQS LQDELDRKEE QALRAKAKEE
     ERPPIRGAEL EYESLKRQEL ESENKKLKNE LNELQKALTE TRSPEVTAPG APAYRVLLDQ
     LTSVSEELEV RKEEVLILRS QLVSQKEAIQ PKNTMTDSTI LLEDVQKMKD KGEIAQAYIG
     LKETNRQSPQ DYHMLNEDGE LWLVYEGLKQ ANRLLESQLQ SQKKSHENEL ESLRGEIQSL
     KEENNRQQQL LAQNLQLPPE ARIEASLQHE ITRLTNENLF YEELYADDPK KYQSYRISLY
     KRMIDLMEQL EKQDKTVRKL KKQLKVFAKK IGELEVGQME NISPGQIIDE PIRPVNIPRK
     EKDFQGMLEY KKEDEQKLVK NLILELKPRG VAVNLIPGLP AYILFMCVRH ADYLNDDQKV
     RSLLTSTING IKKVLKKRGD DFETVSFWLS NTCRFLHCLK QYSGEEGFMK HNTPRQNEHC
     LTNFDLAEYR QVLSDLAIQI YQQLVRVLEN ILQPMIVSGM LEHETIQGVS GVKPTGLRKR
     TSSIADEGTY TLDSIIRQLN SFHSVMCQHG MDPELIKQVV KQMFYIIGAV TLNNLLLRKD
     MCSWSKGMQI RYNVSQLEEW LRDKNLMNSG AKETLEPLIQ AAQLLQVKKK TDEDAEAICS
     MCNALTTAQI VKVLNLYTPV NEFEERVLVS FIRTIQLRLR DRKDSPQLLM DAKHIFPVTF
     PFNPSSLALE TIQIPASLGL GFISRV
//
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