ID B6Q7S2_TALMQ Unreviewed; 1741 AA.
AC B6Q7S2;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Kinesin family protein {ECO:0000313|EMBL:EEA28807.1};
GN ORFNames=PMAA_036000 {ECO:0000313|EMBL:EEA28807.1};
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA28807.1, ECO:0000313|Proteomes:UP000001294};
RN [1] {ECO:0000313|Proteomes:UP000001294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000313|Proteomes:UP000001294};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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}.
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DR EMBL; DS995899; EEA28807.1; -; Genomic_DNA.
DR RefSeq; XP_002145322.1; XM_002145286.1.
DR STRING; 441960.B6Q7S2; -.
DR VEuPathDB; FungiDB:PMAA_036000; -.
DR HOGENOM; CLU_241013_0_0_1; -.
DR OrthoDB; 1430657at2759; -.
DR PhylomeDB; B6Q7S2; -.
DR Proteomes; UP000001294; 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 Gene3D; 1.10.287.1490; -; 2.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
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; PTHR47969; CHROMOSOME-ASSOCIATED KINESIN KIF4A-RELATED; 1.
DR PANTHER; PTHR47969:SF15; ZGC:66125; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Reference proteome {ECO:0000313|Proteomes:UP000001294}.
FT DOMAIN 51..439
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 869..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 990..1011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1565..1626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 557..703
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 819..860
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 956..990
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1111..1250
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1304..1331
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1660..1739
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 182..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..918
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1011
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1565..1588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1604..1626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 138..145
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1741 AA; 194371 MW; D75D4D0366F1EF71 CRC64;
MTISPPGSPA APTPTTRPMS AIIRPPRSMS RMSTGSRPGD SRASDEESKT AVKVAVRVRP
PLRPTDPGYE LIPQRFQRSM VHVTSPTSLA VDVPQGRKLF VFDRVFPEST DQEGIWEYLS
DSVNSFTQGY NVSILAYGQS GAGKSYTMGT SGPGEQNDTR AMGIIPRAAQ LLFERLDGPK
HSRTQSSGLR TPARYSMSSP QSFNRSPVEK TWQLKATYVE IYNEQLRDLL LPDTTPVGDR
STVTIREDAK GRIILTGLHQ VDINSFDDLI GALNFGSSIR QTDATAINAK SSRSHAVFSL
NLVQRKSPAQ TMTAKEKRMS VPVEALTSSD AIVTVDSKLH FVDLAGSERL KNTGAIGERA
KEGISINAGL ASLGKVISQL SSRQSGAHVS YRDSKLTRLL QDSLGGTAIT YMVACVTPAE
FHLSETLNTV QYAQRARAIQ SKPRIQQITD ESDKQAVIER LKAEIAFLRQ QIRNSETGDR
KSVVQPERSE RSSDREMELQ NHLLDMQESY TSLSQRHAKL ISELSKASDL QTEDPDELAA
AIENSSIERL KRSHSFAESV EQVVLEYEKT IQSLESSLSN TRSSLSNTES SLLERESKCA
FMETLNAQLQ TRVQKLMERE NSTEHYLHDL ESRLDGHSTG EEKNSALVNE LRKEIARARE
NEAGCEDYIS TLEERLAEAD QDMELMQREI NRLEHVIDRQ RNLGKLDNLL YELDHIQQNG
NKSQVLESKP PAVKDIRTNR ARGNTLDILT EAVETAIPED DDEDLGEDSA GNVFSEETRE
LDISSGDDVD VVEEEASEAK EIDEHSHSPA QSKFVAEKLE NVTQELLDLR VQHETTQNEY
DLLAAKYEEA LRAMAEMQDQ IDFSRHPVGP MNVDTPVDSS SRPQSFLESV KTEETKTGGQ
HSSSRSLSSE LSSVEQSGIS QDTFDTTIMS TQEDVPISNG TSPQSEEEVK TLRQLLREHE
EGMNLVAQKY AQLEAEHDET LILVEQLKTD LHKSRRPQSP TASSPGGASV IRRMTSQNLT
STVDRAHRSL AALRNIASEE FEQRPDTMQN FEQNLNAAMH ELHIRMERIQ ALEAENTNVK
KEMEMKATII SGLTRERSSL QGAKPMDMAM VSQMRDQIFQ QESQMREMQE AHESREQELR
AEIEKLTSEL SSHTKNDPSE TTVANGTVLS GESLARIAQL ETELDEWKAR HQTAIEALEA
SEQKLRETSA ELSAALATVD ALRAEHADSL ESVTNEKAAL LQGREEERKQ QESYVAHLQS
EIDEHKFTIS THLAAISELE ASHSTIQDQL THLASTKEAN DANSAVYQSR IAELEDELDS
HRALVGTHDR ELATLRETHA QQLSELESRS AAVDSAKADH DSFIAQLNAQ HDETLTALRS
EIAGSKHDLT GLLNSISRVL ETEVTPVTVG DQLEDLVSEK RSLESKYADL IDAHEDLQSQ
LETQGATAEE PKISNEEHEA KITKLATLVA TLEDKLKEKE ELVKKKDATI EEISAEKQKS
VRLVEELEEQ ITNTFDQHHN RLSVMQNERL QALEEANVKV ANLERDVETY QVRIEQLELQ
LKNSGTEMTM DRTNSLSSVR KSTSTTSLPS PPPAIPLPPL PNIASATAGN TNSMSPPSSR
HASRELVSTQ LMEDQEARIK TIEKHLYAEK QLTATLEEAL GDLETQSNKI KADMEAWKKK
AWQYEDELQT LRKERNSARL SLQAVEEERS ARREAEAARA QLEERMNAIN KKKKKSTLNC
F
//
