ID A0A0D2K9P2_9EURO Unreviewed; 1665 AA.
AC A0A0D2K9P2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Kinesin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=Z520_11170 {ECO:0000313|EMBL:KIX93113.1};
OS Fonsecaea multimorphosa CBS 102226.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIX93113.1, ECO:0000313|Proteomes:UP000053411};
RN [1] {ECO:0000313|EMBL:KIX93113.1, ECO:0000313|Proteomes:UP000053411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 102226 {ECO:0000313|EMBL:KIX93113.1,
RC ECO:0000313|Proteomes:UP000053411};
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 Fonsecaea multimorphosa CBS 102226.";
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; KN848097; KIX93113.1; -; Genomic_DNA.
DR RefSeq; XP_016627236.1; XM_016781659.1.
DR STRING; 1442371.A0A0D2K9P2; -.
DR GeneID; 27716916; -.
DR VEuPathDB; FungiDB:Z520_11170; -.
DR OrthoDB; 126886at2759; -.
DR Proteomes; UP000053411; 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; SM00240; FHA; 1.
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}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
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:UP000053411};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 21..372
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 1512..1653
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 614..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 698..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1470..1499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1579..1611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..656
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..804
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1482..1499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1585..1599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 123..130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1665 AA; 185176 MW; FC90067F109C7461 CRC64;
MAPTGGGGGG AAGGGLGGGG NIKVVVRVRP FNNREIDRNA KCIVQMQDAQ TILQPPPEAE
DRLRKGGKDG ASAQRTFKFD KSYWSFNKAD PNYAGQDNLF DDLGVPLLDN AFQGYNNCIF
AYGQTGSGKS YSMMGYGEEA GVIPRICREM FERINGLQSD PHLTCTVEVS YLEIYNERVR
DLLNPATKGN LRVREHPSTG PYVEDLAKLA VRSFSEIENL MDEGNKARTV AATNMNETSS
RSHAVFTLTL TQKRHDAETN MDTEKVAKIS LVDLAGSERA TSTGATGARL KEGAEINRSL
STLGRVIAAL ADLSSGKKGL KVPYRDSVLT WLLKDSLGGN SMTAMIAAIS PADINFEETL
STLRYADSAK RIKNHAVINE DPNARMIREL KEELAKLRSQ LGGTTAAGAE ETYPEGTPLD
KQMVSIVQTD GSVKRVSKAE IMDQLSQSEK LYQDLNQTWE EKLQKTEQIH KEREAALEEL
GISIEKGNVG MSTPKKMPHL VNLSDDPLLA ECLVYNLKPG VTTVGNVDSS EASEIRLNGS
KILDHHCKLE HVDNVVTIIP HEGAAVMVNG VRVDKPKRLK SGNRIILGDF HIFRFNNPLE
AKAERAERSL LRQSVTASQL SSPTPFRPGH ERTWSAAGSE FDGESSRAQS PGLGSNKDSD
WFFARREAAG ALLGSDPKIM QLTDEELDNL LENIQRAREE RRGRSDNKHF EHDEDSDDLS
SFLVRDKYMS NGTIDNFSLD TALTLPGTPS VHGSSQEDGE PTLTPSQFGH QVQNPTHKTG
EGDKQGVAED ASKDAEREAQ AARMQQELEL ARQEFEEELR KQKEEYEAQI KKMDRDVRIR
EAARTPAGFL PLEAPEKAIA RNVVEKWQQR NYILIAEAIL QNAGLLKEAQ VMSKLLDHDT
NFQFVILDNG QEGGSSYDLI LQDISGDDDD ALAAAHKPCL AVRVIDNQLS CIHLWSLEKL
RLRVAKMRQM RQYKNQPEYL QHFRIDNPFR DSDQPLFSLI GDGSIPLTAV FETRVQDFVV
EITSPSTRQI VGKVRMSLEP SLAESPPSTI KFNIVMRDFV GFAEHEGTQV HAQMTVLGTD
DESVATTQPI HGFGDGPVRF ESIHNLSIRR SGEKSATLKI AIFAQVSSTH LDKLISWDEL
REMNEQPPDQ QPAHRLPESE YMVEERHDVF AKVQILELAE NGQYMPVEVL QSNPNDCGAF
QLHQGLQRRI SVNLTHVLTE GLPWDDLKSL RVGEVHQLDS SGRVTDIASI TPDIPLKQIQ
EPMIKDNADG TSNITIVGQW DSSLHKTLLL DRATNENSRV QISLRWDVIS SRLGRDQPMT
FSIDQQLQIL PRSYVRPQSM FKSFWNQTRV THSTDGLFSI VVRPVSAKRA ADLWRLDTSK
NYINGEELLG NWQPRGISLV KDYLIARRKR RQLEDIESAK AALGLRKLSV TAHKARGRAA
SPSSKLDSRE ENLLRKYLAI WMKPSAEMKN PIFDEGDEST RSRPSPTPVP ETSRSSSTRY
QATIAHVPKN AVSLKSGYLL MPSETYEPSP SGNHGSTMQW KRRFVDLRPP YLHIQSVPDG
EGINAVNLTH ARIDHDPDFK RLLGGGSSIS SQDGADSSSA EQRGGHRRTG SNAELHGLAH
VFAVYGEQNT FLFAARSESQ KVEWILKIDQ SYFASEGEQQ DQIEV
//
