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Database: UniProt
Entry: A0A225ACA6_9EURO
LinkDB: A0A225ACA6_9EURO
Original site: A0A225ACA6_9EURO 
ID   A0A225ACA6_9EURO        Unreviewed;      1629 AA.
AC   A0A225ACA6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Kinesin-like protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=UA08_06040 {ECO:0000313|EMBL:OKL58712.1};
OS   Talaromyces atroroseus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Trachyspermi.
OX   NCBI_TaxID=1441469 {ECO:0000313|EMBL:OKL58712.1, ECO:0000313|Proteomes:UP000214365};
RN   [1] {ECO:0000313|EMBL:OKL58712.1, ECO:0000313|Proteomes:UP000214365}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 11181 {ECO:0000313|EMBL:OKL58712.1,
RC   ECO:0000313|Proteomes:UP000214365};
RA   Rasmussen K.B., Rasmussen S., Petersen B., Sicheritz-Ponten T.,
RA   Mortensen U.H., Thrane U.;
RT   "Talaromyces atroroseus IBT 11181 draft genome.";
RL   Submitted (JUN-2015) 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   -!- 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:OKL58712.1}.
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DR   EMBL; LFMY01000009; OKL58712.1; -; Genomic_DNA.
DR   RefSeq; XP_020118833.1; XM_020268729.1.
DR   STRING; 1441469.A0A225ACA6; -.
DR   GeneID; 31005796; -.
DR   OrthoDB; 126886at2759; -.
DR   Proteomes; UP000214365; 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: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; cd22705; FHA_KIF1; 1.
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:SF6; KINESIN-LIKE PROTEIN KIF1C ISOFORM X1; 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, ECO:0000256|PROSITE-
KW   ProRule:PRU00283};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00283}; Reference proteome {ECO:0000313|Proteomes:UP000214365};
KW   Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT   DOMAIN          8..361
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   DOMAIN          1508..1617
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          36..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          394..418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          612..651
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          756..821
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        612..629
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         110..117
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1629 AA;  182004 MW;  8E2DF57A2CCB29C7 CRC64;
     MAPAGGGNIK VVLTSTASSL ENERNAKCIV QMKGNQTVLT PPPGAEEKMR KGGMKGTPDG
     PKTFAFDRSY WSFDKSAPNY AGQENLFADL GVPLLDNAFQ GYNNCIFAYG QTGSGKSYSM
     MGYGKEHGVI PKICQDMFKR IATIQEDKNL NCTVEVSYLE IYNERVRDLL NPATKGNLKV
     REHPSTGPYV EDLAKLVVRS FQEIENLMDE GNKARTVAAT NMNETSSRSH AVFTLTLTQK
     RHDAETTMDT EKVAKISLVD LAGSERATST GATGARLKEG AEINRSLSTL GRVIAALADL
     SSGKGKKGTL VPYRDSVLTW LLKDSLGGNS MTAMIAAISP ADINFEETLS TLRYADSAKR
     IKNHAVVNED PNARMIRELK EELAQLRSKL GGGAGSIASG GGSGVPMEES YPPDTPLDQQ
     MVSIAQPDGT IKKVSKAEIV EQLNQSEKLY KDLNETWEEK LAKTEEIQKE REAALEELGI
     SIEKGFVGLS TPKKMPHLVN LSDDPLLTEC LVYNIKPGQT RVGNIDQENA AEIRLNGSKI
     RQQHCIFENV DNVVTLIPSE GAAIMVNGLR VEKPTRLRSA CRIILGDFHI FRFNHPEEAR
     AERVEQSLLR HSVTTSQLGS PAPSRTHDRT MSKAGSEVEG EMSPTPTPYR GGRDADWFYA
     RREAASAILG PDQKISDLND DELNALFDDV QKARAVRRGL LENDEDTDSL SSFPVRDKYM
     SNGTIDNFSL DTAITMPGTP RQIDEEEGEF SLQAARDDMQ RQLDRQKGEF QEKLKAEAPH
     ADVEEVRQQR TRMEEALRTA KADFEKQLQK QKEQYENHIK EMGHPVPKIY ENGFAKLEPE
     EIEVAKTVVR HWSKRNYVRM AESILQHASL LKEAQVMSQI MDKNVVFQFA IIDDGHNMVS
     SYDLVLNGIS GEDDSALDEV KKPCVCVRVI DFKHCAIHLW SMEKLQKRVQ AMRQMHQYID
     RPDYIQHFKL ENPFSETCPA QYSLVGDADI PLTAVFETRV QDFSVEVVSP YTQSVIGIIR
     LSLEPSSAQG PSSTLKFNVV MRDMAGFAER EGTEVHAQLF VPGVSEEGGA TTTQMISGFD
     ENPVRFESVH SMSLPLSSLR TVSLKVCIYA KVTPMHLDKL LSWDDMRDSS ETPAPSKRKA
     PRIAETEFFS EERHDVFARI QILELAESGD YLPVEVVQNS SMDAGTYQLH QGLQRRVAVH
     LTHSSTENFP WEDITNLRVG SVRLLDPWGK IPDQDLQTPD VPLRLIQEPM IKDNADGTSN
     VTIIGQWDSS LHGSLLLDRT TAEKYRVQIS LRWDLVSSRV HEPIVFQLDQ TLVILGRTYV
     RQQSILRQIW NSTRVVHSTV GMFSVVIRPV SAKRAADLWR MNTQSDYVKG EELLTSWSPR
     KVSLVRDFIA SRKRRQRAAE LEAARGALGA DSLVASPLKG SGRSTPMRNQ DFTERQMKLV
     QRYLSLWSTR KDPTETILVK TNTEQPTNGD VVSTTNKNNN KALLDASDSH GSAPRYVAAV
     QTLSKNATVA KSSYLMMPDD DNSTRWVRRF VELRGSYLHI YSAPEGDEIN TINLRHARVD
     HDPDFARLFD NRADGMASSR GRPNIFAVYG PQNTFLFAAR TEAQKVEWIL KIDQSYFSNN
     APVNGNGRR
//
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