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Database: UniProt
Entry: A0A125PHK6_9BASI
LinkDB: A0A125PHK6_9BASI
Original site: A0A125PHK6_9BASI 
ID   A0A125PHK6_9BASI        Unreviewed;      1624 AA.
AC   A0A125PHK6;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Kinesin-domain-containing protein {ECO:0000313|EMBL:KWU41614.1};
DE   Flags: Fragment;
GN   ORFNames=RHOSPDRAFT_6029 {ECO:0000313|EMBL:KWU41614.1};
OS   Rhodotorula sp. JG-1b.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU41614.1, ECO:0000313|Proteomes:UP000062823};
RN   [1] {ECO:0000313|EMBL:KWU41614.1, ECO:0000313|Proteomes:UP000062823}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JG-1b {ECO:0000313|EMBL:KWU41614.1,
RC   ECO:0000313|Proteomes:UP000062823};
RG   DOE Joint Genome Institute;
RA   Goordial J., Raymond-Bouchard I., Riley R., Ronholm J., Shapiro N.,
RA   Woyke T., Grigoriev I.V., Labutti K.M., Greer C., Whyte L., Bakermans C.;
RT   "Draft genome of eurypsychrophile Rhodotorula sp. JG1b isolated from
RT   permafrost in the hyper-arid Upper Elevation McMurdo Dry Valleys,
RT   Antarctica.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR   EMBL; KQ954531; KWU41614.1; -; Genomic_DNA.
DR   STRING; 1305733.A0A125PHK6; -.
DR   OrthoDB; 126886at2759; -.
DR   Proteomes; UP000062823; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; cd01365; KISc_KIF1A_KIF1B; 1.
DR   CDD; cd01233; PH_KIFIA_KIFIB; 1.
DR   Gene3D; 2.60.200.20; -; 1.
DR   Gene3D; 6.10.250.2520; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR022164; Kinesin-like.
DR   InterPro; IPR022140; Kinesin-like_KIF1-typ.
DR   InterPro; IPR032405; Kinesin_assoc.
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; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR049780; PH_KIFIA_KIFIB.
DR   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   PANTHER; PTHR47117:SF3; KINESIN FAMILY MEMBER 14-LIKE; 1.
DR   PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR   Pfam; PF12473; DUF3694; 1.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF12423; KIF1B; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   Pfam; PF16183; Kinesin_assoc; 1.
DR   Pfam; PF00169; PH; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00283}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00283}; Reference proteome {ECO:0000313|Proteomes:UP000062823}.
FT   DOMAIN          4..366
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   DOMAIN          524..582
FT                   /note="FHA"
FT                   /evidence="ECO:0000259|PROSITE:PS50006"
FT   DOMAIN          1533..1624
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          629..651
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          702..759
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          785..806
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1495..1523
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        632..646
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        740..759
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         108..115
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KWU41614.1"
FT   NON_TER         1624
FT                   /evidence="ECO:0000313|EMBL:KWU41614.1"
SQ   SEQUENCE   1624 AA;  179831 MW;  8CA62BF5E90F5B58 CRC64;
     GGGNIKVVVR CRPLNQREIA RGAKCLVRME GNHTFLDPPD AILQVANMTS GRATEKETKS
     FAFDKSYWSA CPKDDPAYAS QQTLFNDLGR DLLDHAFEGY NTTVFAYGQT GSGKSYSMMG
     YGSDRGIIPL ICEALFERIE NRTAESGGDV SFTVEVSYTE IYQEKVRDLL NPSNNNKGSL
     KVREHPTLGP YVENLSKCAV QNFEDVERLM DEGTKARTVA ATNMNETSSR SHAVFTLLLT
     QKRLDPTTSM VGEKVSRISL VDLAGSERAN STGATGTRLK EGALINKSLT TLGRVIAALA
     QASSAPAGKA AKAAADKVPY RDSVLTWLLK DSLGGNSKTA MIAAISPADY EETLSTLRYA
     DQAKKIQNKA VVNEDPNAKL IRELKEELET LRARMAGPAT FGGGSPSMLT MNGFHDESTF
     DDSVPPERQM VQYKTASGEI KTISKAELQD QLEASEKLMA SVTETWEQKL EKTKEVQLER
     ERALESLGIT IEKNLLGVHT PKKMPHLVNL NEDPLMSECL IYQIKRGRTT VGNMDSDRPA
     DIKLSGPSIQ DDHCYFECTD DDNKVTLHAG PKGTTMVNGQ RLAPGSVKEL RSGFRVILGD
     FHIFRFNHPE EVRRARLTKS RQEVRSPLAA LVDESSATSS PSGTRPDSPM GFAAEDAAVD
     WSYARREAVV ARLNSRDVNL DQLNDVDLNQ LYSNILRVRH SRTSSSMAGS DRPESRMSFL
     DSVTEDGDGD DDEGEGTASS SRRGSRVRPP SAATWSTDAT SLADSPLTLR HLPDLEEKGF
     TFDDVPTRSA LLPPSVTSST ADEEALREKR VMEEKLRKLE TRMAVQRRRL ARLRTTGSSG
     SGSSVSDPDA WLDEWPSLTP EEEPLARRVA RVWRRQRRVQ MAEDALSQAV LLKEANVMSR
     ELQKGVTFQF ANVERPPPIS ACDHVAGIDE LDNVEDPALH DCIKPCVGVK VLDRRHQAIS
     IWSVSKLQRR VQQMREQYRW LDKPEYRQHL VSQDPFYELP PPPGGFSHVA TGLVSLLPLV
     RRTTSVQIIQ LYSPYIADPI GTCRIRLQPV EAARTPKMGR VSLPDDDASE FLLVDLAIDE
     VCGFDKSEFA ALHLQTSLAD LIDYEDSTGG LAISETVHLD EASAGNLTLE HRFCVPITPA
     IEDSLRNKLG AIHVFARPRL SHFDKIDRWD EAREGPRIAS AGVRGGDPSH TDVTRRPETE
     LISAQQHDVI AHVEIRELGE KGEYDPVQVV SANRLDAGAF FLRQGLQRRL VLGLSHNSGR
     ELAWRRVSKV SLGNVRLLDQ RGLVHASTST IDVELRGIGT PRPEYSKDGM SLLNFAAAWD
     SSAHDSPHLN RPTPSGSRAL VQLSFEVEVA GCVAPIPFSV DLAVTIAGRD ARSPSRFTTL
     FSSSRLATRV AAVFCVSLRP YQTRKAADIW RLDTSETYVR GEEILSGWRP RGLSLIRDYD
     ATTSARRKLA DLEATKAVLA TFWETVPSTT GQDGHTLLSR ALALWQKRFG TNAEVSEPPA
     QTMADSKITA PDSAPRRPVQ KTGSAALVPR TETANKRGLL AMLRDPTSSE WRKHWFVLRR
     PYLYIYNSAS ELDEAAVINV STVRVEQTPE IEQMLERKFA FAIFTQHNSY FFAAPSYREM
     VDWT
//
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