ID A0A024G3U8_9STRA Unreviewed; 2601 AA.
AC A0A024G3U8;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Myosin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BN9_021890 {ECO:0000313|EMBL:CCI41405.1};
OS Albugo candida.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI41405.1, ECO:0000313|Proteomes:UP000053237};
RN [1] {ECO:0000313|EMBL:CCI41405.1, ECO:0000313|Proteomes:UP000053237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI41405.1,
RC ECO:0000313|Proteomes:UP000053237};
RA Gardiner A., Kemen E., Schultz-Larsen T., MacLean D., Van Oosterhout C.,
RA Jones J.D.G.;
RT "Recombination and specialization in a pathogen metapopulation.";
RL Submitted (MAY-2012) 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:CCI41405.1}.
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DR EMBL; CAIX01000018; CCI41405.1; -; Genomic_DNA.
DR STRING; 65357.A0A024G3U8; -.
DR InParanoid; A0A024G3U8; -.
DR OrthoDB; 90944at2759; -.
DR Proteomes; UP000053237; 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 Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.58.530; -; 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 Gene3D; 1.25.40.530; MyTH4 domain; 1.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR000857; MyTH4_dom.
DR InterPro; IPR038185; MyTH4_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR13140:SF856; HEAVY CHAIN, UNCONVENTIONAL MYOSIN; 1.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF00063; Myosin_head; 2.
DR Pfam; PF00784; MyTH4; 1.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00139; MyTH4; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51016; MYTH4; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW 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|PROSITE-ProRule:PRU00782};
KW Reference proteome {ECO:0000313|Proteomes:UP000053237}.
FT DOMAIN 187..1106
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1964..2127
FT /note="MyTH4"
FT /evidence="ECO:0000259|PROSITE:PS51016"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 971..993
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1169..1193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1858..1901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2410..2494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1272..1300
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1609..1643
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..964
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2464..2494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 326..333
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2601 AA; 289409 MW; 11313C00CB5942B0 CRC64;
MEQGGGNTLL AGSSSQSLNI SSSLPGHNND LGTISPSISQ RKTPMGQSPL TNKARKNSRT
KGSVDHSTTA NGYADSRSGM IDEGDHIWVP ESSGNTENTH LLVDCDVGGT QRKEGVIPAS
VVRVGYIYDP VTDHEKPVIT VHTEDGEERE IRNSDYVRIP LCHHPKTAPS RNIQDLSSIP
LMATNGDSGK NEVFSQKQLE NIVLYTLRAR YRIDQIYTWM DRVLISINPV VSLPIYTPLV
MQDMMQQQQQ LDLTMTAAGS LASSAVGFST QSLASSHASS SSGTYFMGAP KTINYNSIPP
HLFAMAHNAF RFMQDTGEDQ AIILVGVMGS GKSDAAKLLV QYLCEYCEET ETADLLVEGR
ELADVPTSTP KAPQSAQQNT SSASLQSDSL NANSTAHSVG QQILHAFSVL ESFGNATTRQ
NRNSSRFAKM ISVEFNKHRH LIGGGFTIHY FEKSRVIETR YDERNFHVFY QVLAGVQHDP
GLREQLELSN KCANDFALLK NQSDSVGSFP PFTTAPGGDE TIDARDYRDL MSSFSVLRIR
KSQRLEIIRI IAGLLHLGNV EFVPETSGEG STRDQTYDAT GNPGRRDSVL NAASCVLKDP
AQITLVAHLL DVEPVVLDNY FRTRQFFSRD ENNKAVSSLK VVTVAQANKA RDTFIRSVYE
SLFHFMVETL NGFLGGVFDR YANSNLVIQS QGIHILDTIG HEDITSEIVL PSGTASALRN
SSTDINARTS GAPYHSQSTS VRFNGFEQLC ANYWSEKVHH FYLINTLSPL EAFATTKSRS
SSMKGGSFST RLSENTMSSS HVENKCLDFM EHPTLGLFVL LRDHSKMRLP DEEELISNLL
AVNDGSRALA RPTNTEYLES RINNPRDWNL LFTIEHYHGK ILYSGKSFCP KNMLTVSATC
AAIMHSSKNG ILRAVGAAQI ATNQAAAGAL STEDNKKADS RKRTTSGKTA SKKRQNTNST
QGTALEMQTQ SDALLQALNH TGKNFLVCLK PNSTLEQGHF DSGYVAEQLR MMHIVDLMRA
SRSVFSVQLS FSHFIRRYKN ICGHRGTIES LLRSLSAIGV LEDDSYRIST APQRLSDSSN
VLDASMKANK IFCTSHQYKK LEQARDIYLN ACATMIQRSL LHGVFRKKAL EIRVNMQRLR
TAIQKRDGNE LFISIQKCQQ LLAPSLSTPS ARSKRVNQQQ DHASSAHGSL NYRDQQEPPQ
YIRVLNEASA LVTVLEEEEY VQSLANDLTQ TSELHEPAET ITSKGSHIHP VLVDYVIRIA
ETYHPSMDTG HLRKLRLRCA SLLDEKHAQQ ERSHKNLQAQ QEIRKQLWDG ILSKDVESLM
GTLALLDEST KDIKEQKLAT VLVIRALEEK GAVEALMNTL EAVNKAIPVV SKQSAHEAIR
TLHSPLKNVL QKGLESQCPE IETFLRSAID AAKDTSTQPS PQPMATCIND KSTDAITLST
EKLSLLRAAL ERSMEEGNWI ATKKILERLA SLGDQVITQL GIELVQNARD NLAHGLSALS
FHAERNQSIK FLAIARTCGD LTLLNSAIST AIEGGIATWD FNLKNALKQR DELQNVEDSE
DTDNTMLDVA PLMDQEQAAS PLQMLLQLWT ACNEDDMTYL IDLAQGDPIE ELITAKVEHQ
NEVKKVTQDL EHALNAIENN EADLTVIDKL IQRALTCGCD VDAYGRIIEF YHDSMLLTMS
ESTEQSDRTE ETFNLDKWIQ DPDDALATTV LFFESRLARR AEIREDAIEF LTTQYEEFTS
ANGDNEPWQR FRTTEREELL RRIARLQRAL GKAVTARSRL ETQLHIPIET LSVGTLTSAL
ETARSAGVQS RLIDLAVAKL DAVIMYRRAD QRHGHRRDSF PGTSSAECCG LHIDEDDEKD
LSRSCGPSTE GSDTIARGND EEDETTDPSE PIATNLNEEQ ATNHLTDYVK KERDAFAFFH
FPRLQRLILS NRTGQDERPQ VVKLYWSLTP LQRSLLILDE DSSHSNWALR TPNMAVSTND
SSGAQSPGKL SELAIGINRC ILGYMRDRVV LYRDMLAQFI LQLGVEEVGG LVDEIYIQLM
KQLTKNPKRD SSLRGWALLA MCATSFLPSD ALQEYVFRFL NASRPSSNSF WRILNGIASY
CSKRLETLIS NGATGFIPSM DEIQAYDSRP PFLASSIELL DGTVLAEGFP VTPEMTVEHL
IEICAHFLGL DDRLAQFLGI VTISASAKLT EQNASSSSNS FQRFVALPSF LEPNEFLGDI
FEREALRGRE FKFVLKIRIL IPPRYALHQT GATFLFEDEL FNRLTYIQAV DDVLSGLVPV
EEEEVVARLA AYAIAIDRGG LVVCECSSNT DDEFVCMAFH NCDDVLHEVS ISEYVALAWW
ITKTESEWLS VIFDALQEIL NHSNGDVEAG SLQSMFVDEI QLSRLYGAVT FPCKLALEYF
DPAIVLTNSS RSSSTRTRTK SRSRVRNESV SRDNFQNVKM AGEDEETGED GETSQDDDQE
INRVTRTQSI SQRFTTRPSQ LPLSGTGRKV QKASASSSRL RTRHWLGTDL PGYFALALNI
HGIHFLGRDG SILATCSIAD VVAAYGTAHR FVLSIMRTTI TKEPEHLYIT TRYVDVIRRF
LFEFRELEGV LTAAAATTTM D
//
