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Database: UniProt
Entry: A0A1V8TVG8_9PEZI
LinkDB: A0A1V8TVG8_9PEZI
Original site: A0A1V8TVG8_9PEZI 
ID   A0A1V8TVG8_9PEZI        Unreviewed;       751 AA.
AC   A0A1V8TVG8;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Kinesin motor domain-containing protein {ECO:0000259|PROSITE:PS50067};
GN   ORFNames=B0A51_17708 {ECO:0000313|EMBL:OQO15358.1};
OS   Rachicladosporium sp. CCFEE 5018.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX   NCBI_TaxID=1974281 {ECO:0000313|EMBL:OQO15358.1, ECO:0000313|Proteomes:UP000192386};
RN   [1] {ECO:0000313|Proteomes:UP000192386}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCFEE 5018 {ECO:0000313|Proteomes:UP000192386};
RA   Coleine C., Masonjones S., Stajich J.E.;
RT   "Genomes of endolithic fungi from Antarctica.";
RL   Submitted (MAR-2017) 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:OQO15358.1}.
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DR   EMBL; NAEU01001453; OQO15358.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V8TVG8; -.
DR   STRING; 1974281.A0A1V8TVG8; -.
DR   Proteomes; UP000192386; 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   Gene3D; 1.10.150.320; Photosystem II 12 kDa extrinsic protein; 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   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192386};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          2..337
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          402..461
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          568..662
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        402..431
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        568..588
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         93..100
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   751 AA;  82602 MW;  72FA1DFFBEAB93FE CRC64;
     MSVRVVARIR PLLKAEIEKD IIVHADKTAS ATEKDTATVV RIPNPKNHGE NFSFNFNSVY
     DQSATQSQIF DNEVSSTVKH LFKGFDVTIF AYGVTGTGKT HTMRGGKSLA ERGVIPRLLS
     GIYRRARKAE KDSAGESTVE VSMSYFEIYN DKVYDLFEPP EKRTPAGLPI RDNQQGKAVV
     VGLTERPCTS LKEFEGLYDH ANINRSTSAT KLNAHSSRSH AILCVKISQR TGDQTRISTV
     SAIDLAGSED NRRTDNNKER LVESAAINKS LFVLAQCVEA ISKGQARIPY RESKMTRILS
     LGQNKAHTVM VLNIAPVKSY HLDTLSSLNF ANRTKKIETN EIENQPFYRE LPGKGKLDAP
     TTSILPATSS LNRQPLRPKI LSHNAIIKDA TTAIAKPTKQ FSVYSDKPVR PSNQANTSHP
     RTTTRPSIRS PKRPSTDALP TLARPAKIPR TTASLPKPGM SQSDIEALIE RKVTEALAER
     ADNTSISNPE PISDEVQKRL EALEKRVEGQ ETERAEGLQY LLMAKQHQVR GEEASALKMY
     MLAQPSFKGN EKLERKIEGL RHRIEGKKRV EVETRRSPAR DAPPRTRDSP KKPAAAAAAK
     DFDADSSYHA APSLHAASDS DSDSDTPVPR RPLTKIRRRP HGPTRSITAP SPATHTPFDT
     EDPLIRDLCL PTPRTTRLLE IINTRDVAQI RLLRGVGAKR AEAIVGALCD MEIGEEDGGR
     GVGSLQELGR LRGVGAKLVE GMRGGCGEAV S
//
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