ID A8PGI1_COPC7 Unreviewed; 1620 AA.
AC A8PGI1;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 2.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=Kinesin {ECO:0000313|EMBL:EAU80586.2};
GN ORFNames=CC1G_11386 {ECO:0000313|EMBL:EAU80586.2};
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176 {ECO:0000313|EMBL:EAU80586.2, ECO:0000313|Proteomes:UP000001861};
RN [1] {ECO:0000313|EMBL:EAU80586.2, ECO:0000313|Proteomes:UP000001861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003
RC {ECO:0000313|Proteomes:UP000001861};
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canback B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kues U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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}.
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:EAU80586.2}.
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DR EMBL; AACS02000005; EAU80586.2; -; Genomic_DNA.
DR RefSeq; XP_001841223.2; XM_001841171.2.
DR STRING; 240176.A8PGI1; -.
DR GeneID; 6017900; -.
DR KEGG; cci:CC1G_11386; -.
DR VEuPathDB; FungiDB:CC1G_11386; -.
DR eggNOG; KOG0245; Eukaryota.
DR HOGENOM; CLU_001485_20_3_1; -.
DR InParanoid; A8PGI1; -.
DR OMA; RIDKPKR; -.
DR OrthoDB; 126886at2759; -.
DR Proteomes; UP000001861; 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: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; 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; 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};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001861}.
FT DOMAIN 9..361
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 1518..1617
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 36..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1146..1173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 775..802
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 308..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1620 AA; 180697 MW; EBD9A3B41420474E CRC64;
MAPEAGEGNI KVVVRCRPLN SRELARGAKP LIRMQGNQTF LDPPEPGSSQ DTKRATERKT
MAFSFDKSYW SAGPRDEPGY CSQQTLFDDL GKELLDHGFA GFNACILAYW SMQILTRFLH
SMMGYGPDKG IIPLTCSELF ARVAQKTAED PNLTFTVEVS YIEIYNEKVR DLLNPKNTGN
LRVREHPIYG PYVEDLSKLV VSTYEEMMNL MDEGNKARTV AATNMNETSS RSHAVFTLLL
TMKRHDVETK MDTEKVSRIS LVDLAGSERA NSTGATGQRL KEGANINKSL TTLGKVISQL
AITSQSDGKK GKKGKGEEFI PYRDSDSLGG NSKTAMIAAI SPADYEETLS TLRYADQAKK
IKNKAVVNED PNAKLVRELK EELEMLRARV QAASGEDTFD PKVPPEKQKV TYQTKDGRIK
TVTKAELQDQ LEASEKLMQG LNETWEQKLA KTQEVQRERE KALEELGITV EKNLVGVHTP
KKMPHLVNLV SGACSLEKQR AKPKHPYFSL SLASPSLERR SPYERMLNLS TQARENHHSD
VPAAIRLSGE NILPEHCCFE NNEGKVTLTA FPDSVTFLNG KQLPPDEPRR LRSGYRLILG
DHHVFRFNNP EEVRKQRDRA TMKSNLQNSI SAADLEAASE SPRPDSPTSS AGELDHVDWT
FAKREAALAR LGLDPALDSL PDEDLNKLFE KITKVKTMRD HNLKSRPESS LSHAGDDVWS
ETGRPLPSDA TTDDTSLYAA PWGSPFTDEP LKETQTTLET RLHELDESSA EEEVAEDLRV
EKEHMEHQLR LVKAQMRRLI DARARGETDT EAMQFEPVIY TGKQLRLIRK VLDRWRAHRS
FSMAEQILIN AVAMKEANVI CKELGKQVTY NFTIASGGSL AAPSSAVDTI AGLDQFGDVA
DPILTSATQP SAAVKVIDKR NNAIYVWSLD RMQQQLQRMR NLTTYIDRPS YTQHFSSDEP
FFESPPPEYS FIGNALISLA PLSRRLSSSS TVPIFCRYTA EAIGSCRIDI KVMNVVLPAK
YLNGSSPSTR SSSPAPGAVP PGSKLSFSLT IDSVKGLSSY DFSAVHLQVR LSSFVGPTVA
AEEVFPSSAI NIDDSSLSEV KFRRNFTIAT TSKVLNHIRQ GYAPIEFFAA LKPTYLERME
RWDEMREQKQ YRPSPSSPSP QPESRPASAT LPPMRRSETD FVVEQVHDVV AWLQVCELGP
DGSYVPVPVI SQGSLDPGVF SLHQGLQRRI SISLSSNSGQ QLPWTEFTKI RIGNVRLLDP
HGRIHDSTSK ALVTLPLLKE QTLEFKPDGS GALAAEALWD SSVHNSVLLN RVTASNQRIL
LQLQFSVAVD TCADPVQFSM DLAITMHSRD ASPPSKLLSF FGSSKILSKT STLFSVKLSP
PLTRSAKDLW RLDTSEKYVR GEETLATWKP RGISVVEDYN RLITTERRAA DVQAIRVILA
NSPPKPLPQE TLAWRADDLV KRSLHLWQKQ FGHKGKIVLS QEPEEPVETV TSPKRKRESP
LETLKFISET KLISRSDSAT KKGHLMILTD AGQGLWERRW FVLKRPYLHM YAHSNEVEEV
GIITLSGVNV ESDPLKESLL GKPFSFMLFT SSNSHGLAAP NQKEMLSWVT KLDPTRLPST
//
