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Database: UniProt
Entry: A0A367L3B8_9HYPO
LinkDB: A0A367L3B8_9HYPO
Original site: A0A367L3B8_9HYPO 
ID   A0A367L3B8_9HYPO        Unreviewed;      1674 AA.
AC   A0A367L3B8;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Kinesin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=L249_5116 {ECO:0000313|EMBL:RCI08925.1};
OS   Ophiocordyceps polyrhachis-furcata BCC 54312.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX   NCBI_TaxID=1330021 {ECO:0000313|EMBL:RCI08925.1, ECO:0000313|Proteomes:UP000253664};
RN   [1] {ECO:0000313|EMBL:RCI08925.1, ECO:0000313|Proteomes:UP000253664}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCC 54312 {ECO:0000313|EMBL:RCI08925.1,
RC   ECO:0000313|Proteomes:UP000253664};
RX   PubMed=26511477; DOI=10.1186/s12864-015-2101-4;
RA   Wichadakul D., Kobmoo N., Ingsriswang S., Tangphatsornruang S.,
RA   Chantasingh D., Luangsa-ard J.J., Eurwilaichitr L.;
RT   "Insights from the genome of Ophiocordyceps polyrhachis-furcata to
RT   pathogenicity and host specificity in insect fungi.";
RL   BMC Genomics 16:881-881(2015).
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:RCI08925.1}.
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DR   EMBL; LKCN02000017; RCI08925.1; -; Genomic_DNA.
DR   STRING; 1330021.A0A367L3B8; -.
DR   Proteomes; UP000253664; 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   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; IPR008984; SMAD_FHA_dom_sf.
DR   PANTHER; PTHR47117:SF3; KINESIN FAMILY MEMBER 14-LIKE; 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   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:UP000253664}.
FT   DOMAIN          8..350
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   DOMAIN          1540..1663
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          609..650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1089..1123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1205..1232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1406..1471
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1604..1623
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          742..787
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        618..632
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1097..1123
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1412..1426
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1450..1467
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         97..104
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1674 AA;  185429 MW;  FEC4A15223C86F5D CRC64;
     MPPAGGGNIK VVVRIDRGSK CIVSMKDNQT ILTPPDSPAG RAAKETAAKT FAFDRSYWSF
     SKDDASYAGQ SNLFGDLGKP LLDNAFQGYN NCIFAYGQTG SGKSYSMMGY GKEVGIIPNI
     CQEMFRRIQA IQTLDHSTKC TVEVSYLEIY NERVRDLLNP STKGNLKVRE HPSTGPYVED
     LAKLVVGSFQ EIEHLMDEGN KARTVAATNM NETSSRSHAV FTLMLTQRKH DAETNMDMEK
     VAKISLVDLA GSERATSTGA TGARLKEGAE INRSLSTLGR VIAALADLST GKKKKNSGQV
     PYRDSVLTWL LKDSLGGNSM TAMIAAISPA DINYDETLST LRYADSAKRI KNHAVINEDA
     NARMIRELKE ELALLRSKLG GSGAASSPAS GEVYADDTPL EQQMVTITGA DGAVKKVSKA
     DIAEQLSQSE KLLTDLNQTW EQKLQKTEEI HKEREAALEE LGISIEKGFV GLHTPKKMPH
     LVNLSDDPLL AECLVYNLKP GTTTVGNGQN ADHHHQAYIR LNGSRILHDH CAFENAPDGT
     VTVIPRENAP VMVNGKRIEE PIQLHSGYRV ILGDFHIFRF NHPMEARAER AEVVGHSLLR
     QSLTASQISA LDRSSPCHSP RLGHDRSFSK SSEPSIDYRP DSPRNGRDSD WSLARREAAG
     AILGTDQNLA SLTDEELNAL FEDVQRARAE RVNVRDDGED TESVTSYQLR DKYMSTGTID
     NFSLDTALTM PSTPKHTEPE TREEVADEVE EMRREKARME AELQELKADL LKQLDLQREQ
     YEEKMDKLDP LKRPRPNPRL SEKEAARARA AVRVWRGRRF VKMAESVLQE AATLKEAQIM
     SNELNESVVF QFTVVDIGHV LCSSYDMVLN GLTGEGEDGA LEETAKPCIG IRVMDYRNSV
     VRLWSLEKLQ DRLRQMRQMH QYLDQPEYAQ HLSLDNAFAE TCMPSYTLIG EVDVPLAAVF
     ESRVHDLGLD VLSPHTSHTV GIVRLSLEPS HARAPSSRLK FNVVMRELLG FAEREGTEVH
     AQLFIPGVPE EEGITTTQMI RDFDEGPIRF ESVHNMSVPL SAPRDVTLRV ALFARVSSMH
     LDKLASWDDM RDSSGKGLLP SKSSSCASSS SSSSSSSSRL NESQFLTQEK HDLLSRVQML
     ELSEEGEYRP VEVTQTSELD TGTFQLHQGL QRRISISLSH SSGDALPWGG VTAVRVGKVR
     LVDSAGKTPD MGGEEPDVTL TTGTPPVFRD RSNGTRSVTL TAQWDSSLHN SLLLDRVTAE
     RYRVQMTISW EMSSEKLAEP MRFAQKVCVQ VLPRTFVRQQ SMFSGLFQQV RFVRSSTGIF
     TLTLRPVPIK RVGDLWRASS RHDYVKGEEK LVRWAPRGVS LVTDFMAARK KRRRMAEIGA
     MQTRLLALGF RESGKKTGAE SAAAAIVTRQ DDDNSNHNKG VVDDDDADVL NDTPDTSQAP
     SINEEERDEG NEEGRGEEGE EEVEEEEEKT VKVLQADKDG STRLLSKCVA LWTKYPDPLS
     RILSPANTAS PRNGIAPDLP PASTAPRLAA TVVRVPKNPT LLRGGYLLVP SDVSSSSQRW
     VKRFVELRRP YLHIHSASDG DEVALVSLRN ARVDSQPEVC GLLQGGGADT GEEEEEEEGG
     GSNARRFHTA VFAIYGTDNT WLFAARSERD KMDWIFRIDQ TYLTPMNGGS PAGW
//
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