ID   A0A177C930_9PLEO        Unreviewed;       580 AA.
AC   A0A177C930;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN   ORFNames=CC84DRAFT_1098234 {ECO:0000313|EMBL:OAG03362.1};
OS   Paraphaeosphaeria sporulosa.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC   Paraphaeosphaeria.
OX   NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG03362.1, ECO:0000313|Proteomes:UP000077069};
RN   [1] {ECO:0000313|EMBL:OAG03362.1, ECO:0000313|Proteomes:UP000077069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG03362.1,
RC   ECO:0000313|Proteomes:UP000077069};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) 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,
CC       ECO:0000256|RuleBase:RU000394}.
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DR   EMBL; KV441555; OAG03362.1; -; Genomic_DNA.
DR   RefSeq; XP_018033727.1; XM_018174757.1.
DR   AlphaFoldDB; A0A177C930; -.
DR   STRING; 1460663.A0A177C930; -.
DR   GeneID; 28758243; -.
DR   InParanoid; A0A177C930; -.
DR   OrthoDB; 126886at2759; -.
DR   Proteomes; UP000077069; Unassembled WGS sequence.
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   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
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   PANTHER; PTHR47117:SF3; KINESIN FAMILY MEMBER 14-LIKE; 1.
DR   PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 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   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00283,
KW   ECO:0000256|RuleBase:RU000394}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Microtubule {ECO:0000256|RuleBase:RU000394};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283,
KW   ECO:0000256|RuleBase:RU000394};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283,
KW   ECO:0000256|RuleBase:RU000394};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077069}.
FT   DOMAIN          13..366
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          504..536
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          400..427
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        504..524
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         113..120
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   580 AA;  65369 MW;  1223696FE4BA3AD4 CRC64;
     MLAPPPMLDD AGNVKVVVRC RAFVRREKEK GTQCLIRMDP ATNKTTLLAP VEDTESSTRR
     AYEDKEFVFD KSFWSHDEAD PYYAHQEDVY RSFGEEFLDH NFNGYHTCIF AYGQTGSGKS
     YTMMGSPDNP GLIPRTCEEL FERIRDEPTP NTSYHVQVSY FEVYNEHVRD LLAARTSPSM
     YLKIRESPKD GVYVQGLTET EVKSYADVER LMRIGDSSRT TASTKMNDTS SRSHAVFTIR
     LKQITHSLLS DETIERTARM RLVDLAGSER AKSTEATGQR LKEGGQINKS LTTLGRVIAA
     LADPKRQNSK GRRPKEVVPF RDSVLTWLLK DSLGGNSKTA MVACIAPSDY DETLSTLRYA
     DQAKRIRTRA SVNQDCMSAA QRDAQISEMA EQIRSLQVSV NAATIRKREE ATELEEYQRQ
     VAMMQRLEEE NRMVADSRIK ALTAEVEELR PMNIALRSEI DALRRHLALA LGELKNPIVL
     PPPIPGSPEI EQDGFIRVDK RGVDLGEDGK ENSIPIHSDD EMSGDDSDSG YDEGDHDELA
     QELQIEAQDF LKDLGLFRRK VGGDVERFGV RQALHEIIGN
//