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Database: UniProt
Entry: A0A135SJP3_9PEZI
LinkDB: A0A135SJP3_9PEZI
Original site: A0A135SJP3_9PEZI 
ID   A0A135SJP3_9PEZI        Unreviewed;       725 AA.
AC   A0A135SJP3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Kinesin motor domain-containing protein {ECO:0000313|EMBL:KXH36101.1};
GN   ORFNames=CSIM01_10610 {ECO:0000313|EMBL:KXH36101.1};
OS   Colletotrichum simmondsii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=703756 {ECO:0000313|EMBL:KXH36101.1, ECO:0000313|Proteomes:UP000070328};
RN   [1] {ECO:0000313|EMBL:KXH36101.1, ECO:0000313|Proteomes:UP000070328}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS122122 {ECO:0000313|EMBL:KXH36101.1,
RC   ECO:0000313|Proteomes:UP000070328};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum simmondsii CBS122122.";
RL   Submitted (FEB-2014) 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: 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:KXH36101.1}.
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DR   EMBL; JFBX01000544; KXH36101.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135SJP3; -.
DR   OrthoDB; 129693at2759; -.
DR   Proteomes; UP000070328; Unassembled WGS sequence.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
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; cd00106; KISc; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   InterPro; IPR027640; Kinesin-like_fam.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010994; RuvA_2-like.
DR   PANTHER; PTHR24115:SF1000; KINESIN-LIKE PROTEIN KIF22; 1.
DR   PANTHER; PTHR24115; KINESIN-RELATED; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF47781; RuvA domain 2-like; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          2..333
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          403..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          578..650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          498..525
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        433..458
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        613..628
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         90..97
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   725 AA;  79987 MW;  C6ED43D3D6B2AC6C CRC64;
     MSVRVVARIR PLLEKELDKD VIVRADSTEP GKPATLVKIP SPKNESEEFS FAFTSVYDQS
     TTQDALFTSE VAPHIKALFQ GLDVTIFAYG VTGTGKTHTM RGGLKLADRG VIPRLLSGVY
     RRGKKITKDT SGQTTVDVVL SYYEIYNDKV FDLFEPPEKR QPSGLPLREK DGKTMVVGLS
     ERACEDLQDF SRLYIEANNN RVTASTKLNA HSSRSHAIMR IKVTQTTGDQ VRESVASAID
     LAGSEDNRRT DNGKERLVES AAINKSLFVL SQCIDAISRG DKRIPYRESK MTRILSLGQN
     NGITVMILNL APIRSYHLDT LSSLNVSSRA KRIEVREIEN EVVFKQVPRT NSGSSTSTLR
     QPLRPLSNAH NIHSGTIAAK ANEKAADPTR PVKLFNVYTD RSKSAVPVRP TANMTQTRKP
     LVERELPAKA SKLARPSQSS LIAQPTQPAQ QAQPAEQKLS ISAEQLEAIV EKKVSEILAS
     RENKTAEPAP APAHPDINDA VRRRLEALER RIANEERERD DGRSEGLRFL LAARQAKETG
     NDVVALQMYE EALPFFPGQA KLLGKIEKLR VKLGNMLPTE SLPVSSSPRN GHEKKRRRIA
     ADDSDEEYQQ DRGDEDMSFV DVAAKTKSRK AKPAKPPKMV LPDPAGPASP RTQNLLSIVN
     SRDLAQIKGL HGFGSKKAQD LVDYLENLAD EEDAEIETLA QLKTIPGMGG RTVERAYDGL
     VGLAI
//
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