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Database: UniProt
Entry: A0A0D1WQR2_9EURO
LinkDB: A0A0D1WQR2_9EURO
Original site: A0A0D1WQR2_9EURO 
ID   A0A0D1WQR2_9EURO        Unreviewed;      1643 AA.
AC   A0A0D1WQR2;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=Kinesin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PV11_09218 {ECO:0000313|EMBL:KIV77421.1};
OS   Exophiala sideris.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV77421.1, ECO:0000313|Proteomes:UP000053599};
RN   [1] {ECO:0000313|EMBL:KIV77421.1, ECO:0000313|Proteomes:UP000053599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV77421.1,
RC   ECO:0000313|Proteomes:UP000053599};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala sideris CBS121828.";
RL   Submitted (JAN-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; KN846954; KIV77421.1; -; Genomic_DNA.
DR   STRING; 1016849.A0A0D1WQR2; -.
DR   HOGENOM; CLU_001485_20_2_1; -.
DR   OrthoDB; 126886at2759; -.
DR   Proteomes; UP000053599; 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; cd22705; FHA_KIF1; 1.
DR   CDD; cd01365; KISc_KIF1A_KIF1B; 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; 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   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; 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};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
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:UP000053599};
KW   Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT   DOMAIN          16..367
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   DOMAIN          1506..1634
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          612..652
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          693..712
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          732..754
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1459..1486
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          796..831
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        634..652
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         118..125
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1643 AA;  183151 MW;  0DDB10DEE603A7CF CRC64;
     MAPTGGGTAG GGGGGNIKVV VRVRPFNNRE IDRNAKCIVQ MQGAQTVLQP PPEADERLRK
     GGKAGSEAQR TFKFDQSYWS FNKGDSHYAG QDNLFNDLGT PLLDNAFQGY NNCIFAYGQT
     GSGKSYSMMG YGEEVGVIPR ICRDMFERIN AVQSDVNLTC TVEVSYLEIY NERVRDLLNP
     ATKGNLRVRE HPSTGPYVED LAKLAVRSFN EIENLMDEGN KARTVAATNM NETSSRSHAV
     FTLTLTQKRH DVETSMDTEK VAKISLVDLA GSERATSTGA TGARLKEGAE INRSLSTLGR
     VIAALADLSS GKKGMKVPYR DSVLTWLLKD SLGGNSMTAM IAAISPADIN FEETLSTLRY
     ADSAKRIKNH AVVNEDPNAR MIRELKEELA KLRSQLGGAG APGMAEETYP PDTPLDKQMV
     SITQVDGSIK RVSKAEIMDQ LSQSEKLYGD LNQTWEEKLQ KTEEIHKERE AALEELGISI
     EKGNVGMSTP KKMPHLVNLS DDPLLAECLV YNLKPGVTTV GNVDSSEASE IRLNGSRILD
     HHCKLENVDN VVTVIPEEGA AVMVNGVRVD KATRLKSGNR IILGDFHIFR FNNPLEAKAE
     RAERSLLRHS VTASQLNSPT PFRPAHERSW SAAGSEFDGS SSRAQSPGMN NKDSDWLLAR
     REAAGALLGS DPKIMQLTDE ELDNLFANVQ RAREERRGRP ENRIYEHDED SDDLSSFLVR
     DKYMSNGTAD NFSVDTALTQ PGTPSQHGDS QEDGDVTLTQ DQFEEQGEQQ VKPEIEVNRT
     PSVAHAGQDD EQEVQAIQMQ KELELAKKQF QEELQKQKDA FEAQIKKMDL DVRTREATRS
     PSGFLPLDAN ELAIARNVVE KWQQRNYVLI AEAVLQNASL LKEAQVMAKL LDPDCNFQYV
     ILDLGQDRSS SYDLILHDIS GDEDDALANA RKPCLAVRVV DNQLKCIHLW SVEKLRSRVN
     KMRQMHQYKN EPEYLQHFRM DNPFRDSDQP LFSLVGDGSI PLTAVFETRV QDFVVEICSP
     STQQIIGRVR MSLEPSLTES PPHTIKFNII LRDLVGFSEH EGTQVHAQMT VLGTSDESVA
     TTQPIHGFGD GPIRFESIHN LSVRRASEKS ATMKIAIFAQ VSSTHLDKLL SWDELREMNE
     QGPDQDIAHR LPESEYNVEE RHDVFVKVQM LELAENGQYM PIEVLQTSAD DNGAFQLHQG
     LQRRISITLT HSLTESLPWD DLKGLRVGEV HLIDSSGRIA DIGSVTPDIP LKQIQEPMIK
     DNADGTSNIS LLGQWDSSLH KSLLLDRATN EQCRIQIALR WDVVSSRLEQ SMTFSIEQQL
     QILPRSFVRP QSMFKSLWTQ TRITHATDGL FSIVVRPISA QRAADLWRLD TSRNYIKGEE
     LLGSWKARGI SMVKDYLVTR RKKRQLQDIE SAKAAFGLKK LSLSKSRTRA ASPSNIDARE
     EALLRKFLTI WEKPSIEMSN PVFNNDDGSD SPQADTRSTN TPDLNAVSGR KTRYLATVTS
     VPKNVTSLKS GYLLMPSENH EPGHSQSMQW KRRFVDLRPP YLYIHSVPDG EGINAINLTH
     ARIDHDPDFK RLLGSGSSIS SGDGVSGHKR SGSAELHGLA HVFAVYGEQN TFLFAARSES
     QKMEWILKID QSYFEGEDEG EEA
//
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