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Database: UniProt
Entry: A0A0H2S5I7_9AGAM
LinkDB: A0A0H2S5I7_9AGAM
Original site: A0A0H2S5I7_9AGAM 
ID   A0A0H2S5I7_9AGAM        Unreviewed;      1921 AA.
AC   A0A0H2S5I7;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   28-JUN-2023, entry version 37.
DE   SubName: Full=Kinesin {ECO:0000313|EMBL:KLO19229.1};
GN   ORFNames=SCHPADRAFT_843904 {ECO:0000313|EMBL:KLO19229.1};
OS   Schizopora paradoxa.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Hymenochaetales; Schizoporaceae; Schizopora.
OX   NCBI_TaxID=27342 {ECO:0000313|EMBL:KLO19229.1, ECO:0000313|Proteomes:UP000053477};
RN   [1] {ECO:0000313|EMBL:KLO19229.1, ECO:0000313|Proteomes:UP000053477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KUC8140 {ECO:0000313|EMBL:KLO19229.1,
RC   ECO:0000313|Proteomes:UP000053477};
RG   DOE Joint Genome Institute;
RA   Min B., Park H., Jang Y., Kim J.-J., Kim K.H., Pangilinan J., Lipzen A.,
RA   Riley R., Grigoriev I.V., Spatafora J.W., Choi I.-G.;
RT   "Complete genome sequence of Schizopora paradoxa KUC8140, a cosmopolitan
RT   wood degrader in East Asia.";
RL   Submitted (APR-2015) 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}.
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DR   EMBL; KQ085888; KLO19229.1; -; Genomic_DNA.
DR   STRING; 27342.A0A0H2S5I7; -.
DR   InParanoid; A0A0H2S5I7; -.
DR   OrthoDB; 1430657at2759; -.
DR   Proteomes; UP000053477; 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; 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; KINESIN-LIKE PROTEIN KIN-4A; 1.
DR   Pfam; PF00225; Kinesin; 2.
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:UP000053477}.
FT   DOMAIN          11..462
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          45..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          235..254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          266..333
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          860..900
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          943..965
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1691..1782
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          518..552
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          579..620
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          698..774
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          980..1007
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1081..1248
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1477..1516
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1599..1671
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1788..1903
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        266..284
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        291..313
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1715..1735
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1742..1782
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         120..127
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1921 AA;  214150 MW;  81061A877382BBC0 CRC64;
     MPPSSAAATT SVQVALRIRP TTPQDATSIP SRFQRTVIHA VSSNTVSVDS TPSNQASGSL
     VPSSPAPAAA SSASPAKKQS FTFDQVHGQD ATQHEIFAST AEPLIHRFVE GFNCTVLAYG
     QTSSGKTYSM TGVDLDADPN DPSNGMGIIP RSIATIFNKA NALKEERGGA WTYSIKGSFI
     ELYNEDLIDL LSMDDGVGGR REVQIREDKH GHIIWDGLRE ITVKSTNEVM SLIKQGSSIR
     RTNETDMNAQ SSRSHAIFSL TLTQRKYSGS GAPPRSSTPV QAGRSPSRLA RPASTYASTG
     ANRVSSPTFG RPPTPSFASA MGRGGGLRPS SALGMHSETK KIVDDDSGEW VTIVSKFHFV
     DLAGSERLKR TAAVGERVKE GISINSGLLA LGNVISALGD PSRAKSHTAT HIPYRDSKLT
     RLLQDSLGGN AHTLMIACVS PAEWNAGETV NTLKYANRAR NIKNRAVVTE KEEGWDDMEW
     LQNMVTRLRK DMKALKEGGG IVASGRSDGD AVEVEGASKK VLAQMTELQN NYEDLRGKFV
     ERTEELTRLR RELGEQHRNS SSGATSGTAK YEEIVGPVIE EYEKTISAME AELSLNRAAL
     RHTNDLVEEK EEELSTLTER HSATELYVEE LKSRVGKLTE REASTEAYIR DLEEKIKLHE
     DTSMSSSESV SDLKREIARH KDAEERNAHY IGELEARLTK ADESVLSLRE TIEKLEHDCD
     SRREEVEILQ ERLNNVLTDG EAWRSDLEER ESRVRELEAK MEQWEAKRLA ADEERTRLKG
     INTEVQRQRL SLEVDMADHA PPSVTDVNGV TSTESESLQE QFDALRETQA ATLADLDSLT
     AKYRDALKEI SDLAEQIKEM QLGSPSSDRS ESPDFHDVPA TPRRRHKMRS RENSDVQIAI
     NNRRPFFRHA ASVESLHSRS LSQSQSLSQE LFSARSRMLS SPDLNGMPNG HAGRLGHSPT
     GSRTNLSISL PYGTNHERSA ASLEKEIMRL QEVLKEREAE IQTLETSLKE KHTLQVAVPE
     KQVPNGHVPN QSELSPQILD QIAAIRRSME IRHPPSDIPT GDEDEPLVRL NDLMLSMAQK
     EARHREVVDE LNEQIEHIQQ ERDELTTHAT SYSTEYDTLR DQHEEQSAQL AELRVREQSL
     IAEREAAVDQ FNSSISTLKR EHEEALHSKQ AEVDSLLQRL SAEHDTALVD LQKQLLNASD
     ELAASQKAHE EAFGKLKAEH DDELKKQREE VEAALAKAKE EHEAELSSLK TSHEAELAAK
     EQEHAGVLQR TEEEYYVALS KLRSGHAETL AKKEADFSSS IERLKEEHAG ALKMADLARE
     GSLTESHSHQ AELIGQLQAE HASAIEKKET QFADDLRKLH EEHASILAKK VEDHSAVVER
     LKTKHSAKLS ELEESKDREA DALKQTLQST VQQHGEALTA LRTEHEAALQ AAKQQHDSLI
     ETLQGTHEKA FSVLKTEHAL ALENAESSAR EALEPLLREK TEEVVRLKKE HEEALLEAES
     SKVAIQEQHL QELEAARLRG ESMLKEEGER LQKSLSDMQI EQAQEMETLQ KDNALLHDEL
     ASYKASHDEF LIAQEDARQA HDRELQERDR LIMDLRQGHD SSLAEKAELA AELDRLRSEL
     AQVASEKSRL AQEAADKATF EDQVSQQRVA MDDLHAELQK TKEHRDALLS ERTKQETIVR
     DLQVQLSRAI NIPDAIPPRP SDRNPSFSRT NGSKLPPLTP PPSIPPPPAP RSIPPVPMDV
     AHSISSQAST LRSSGSSRES NPDSPSTSVA GSAPNPPSPM DSKLTVQIED QARHIEEQEV
     IIKTLNKQLS HCESDLQAHM DLVSTLETSL GDSEKNLRKA RMQATEIARE RDTLNAQIER
     LRGELEEARR EVTTVRRSVV EQKQSLEKEL DEERRARERV RQQLDMRVDE LQKRKSKFVC
     L
//
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