ID A0A024UL22_9STRA Unreviewed; 1127 AA.
AC A0A024UL22;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Kinesin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=H310_02777 {ECO:0000313|EMBL:ETW06552.1};
OS Aphanomyces invadans.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=157072 {ECO:0000313|EMBL:ETW06552.1};
RN [1] {ECO:0000313|EMBL:ETW06552.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJM9701 {ECO:0000313|EMBL:ETW06552.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR EMBL; KI913955; ETW06552.1; -; Genomic_DNA.
DR RefSeq; XP_008864627.1; XM_008866405.1.
DR AlphaFoldDB; A0A024UL22; -.
DR STRING; 157072.A0A024UL22; -.
DR EnsemblFungi; H310_02777-t26_8; H310_02777-t26_8-p1; H310_02777.
DR EnsemblProtists; ETW06552; ETW06552; H310_02777.
DR GeneID; 20079827; -.
DR VEuPathDB; FungiDB:H310_02777; -.
DR eggNOG; KOG0239; Eukaryota.
DR OrthoDB; 53017at2759; -.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR CDD; cd00201; WW; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 3.30.1470.10; Photosystem I PsaD, reaction center subunit II; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 1.
DR PANTHER; PTHR47972:SF28; PROTEIN CLARET SEGREGATIONAL; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF00397; WW; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF51045; WW domain; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 147..180
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 884..1072
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 816..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1081..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 375..437
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 472..538
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 608..656
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 20..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..834
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1127 AA; 124521 MW; E04B6AE26EBB4F05 CRC64;
MQRTPRGVAA AISPGSPLRR ADSMSPTNHS NPLYASTSPM GSVTSRRESD QRRAQEAGMS
LLGLAFDGGH MTPPTARSPS SYGGSPVTHQ KTSFGIAQAQ YDEHLAPLEG VDPNLFMEGV
KEHAKYLGMD PQRDNDMLWI ARESLVAPMP TGWHQIMTKE GVPYYYNDHT GESRWEHPSD
QDYMALYQEV MRMKLAGEPI DVSRLKYQFV QRQALNTHQH HGAGLHLDDA WARSGSSGSY
HIDTPTDPHD GYNQGQYEAW SQSSAPSRRR RPHSSSHGKL EDVESEYDDE AHECTGEDIP
YSPRDDDDNG SDIQVTTTRR GGAALDDMPD DGHRALVESL YAQLNECKTK LELQQQHQDV
VDALQKSLYD ITGQLEAHVK EVASANEALK AVQDELATAM RDKHTSAQHV IELEDALKQS
RQQLVLAQGE VEIAKAKEAQ DNLALRQEVK TLTMRLHDAE TSAAVDEVQK QLKKETKLRF
QWEQKFKSLE EQHQALMIQV NDANRKHELD RHVAQGDVET YQNELAQSKA KLASEIQTIS
DNHAHELERV KHAMGMRHAQ EIDELTREHD KQLKALQTSE NALLATVRAL EADRLTQSAA
LADSATQLQA VQREAAQSTR RIKQLEASET ANVKQIASLQ AELDALKTSV QAQMDQAKQA
GIAEATAKVR NRTPVDRGCM RFHVIDARGG ARGGRRKGSA GPVVCPGNEG TATIAQPSDG
NGRQHSCVLP HSTRVECRGH ERRLGSSRYV PAQRPARVGP DGRRRPKAHV RIRLCLSAND
RSGGRVRANQ SVGRECDGRI QCVHLCVRPN RVWENAYDGR SRDGPRREFP SDGRTVSRAG
RARAVGKRRM RHEIEHPRSV QRYGFASCVR AAHRGHTIDL GGIETIVDLL DDSPTGERKP
LEVRMGKQGA YVENLMEVEV YSASDVDDLM KLGHSHRSVG SHDVNEHSSR SHLVVSITIT
SSHKLDGRKS LSKLHLIDLA GSERISKTAA SGQRLKEAQH INRSLSALGD VIASLGGHSK
HVPYRNSKLT FLLQESLSGN SKVLMFVNVS PVQWNAWESL CSLNFAQRCR NVALGQAKAN
TSITNGPNAA TSVPKPAKAP SSKQGGTLTA TEKVRVSLAP KSPKKDN
//
