ID A0A1X2I464_9FUNG Unreviewed; 1857 AA.
AC A0A1X2I464;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Kinesin-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BCR42DRAFT_359219 {ECO:0000313|EMBL:ORZ08870.1};
OS Absidia repens.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=90262 {ECO:0000313|EMBL:ORZ08870.1, ECO:0000313|Proteomes:UP000193560};
RN [1] {ECO:0000313|EMBL:ORZ08870.1, ECO:0000313|Proteomes:UP000193560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 1336 {ECO:0000313|EMBL:ORZ08870.1,
RC ECO:0000313|Proteomes:UP000193560};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) 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:ORZ08870.1}.
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DR EMBL; MCGE01000029; ORZ08870.1; -; Genomic_DNA.
DR STRING; 90262.A0A1X2I464; -.
DR OrthoDB; 1360435at2759; -.
DR Proteomes; UP000193560; 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; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR PANTHER; PTHR47117:SF1; 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; PS50006; 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}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
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:UP000193560}.
FT DOMAIN 3..363
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 562..613
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 1752..1851
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 37..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1145..1164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1311..1336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1311..1334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 109..116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1857 AA; 208448 MW; 4E001E1E90E0CF93 CRC64;
MSNIKVVVRC RPLNSKERAR GAISLVRMEG NQTIISQPAS LSTSLTNDSG NTSNSGGDDA
KAFTFDRSFW SVDPDDTNYA SQETVYNDLG QELLDHAFHG YNCCIFAYGQ TGSGKSYTMM
GYGEDSGIIP RTCSELFNRI DQNVDPAITF CLEVNYLEIY NEKVRDLLNP RNKSNLKVRE
HPSLGPYVED LSRLAVKSFN DIDNLMNEGN KARTVAATNM NETSSRSHAV FTIFLTSRKT
DDTTKLITEK VSRISLVDLA GSERADSTGA TGARLKEGAN INRSLATLGK VIAALAEKSS
ALDSKKTKKS KEHFIPYRDS VLTWLLKDCL GGNSRTAMIA AISPADYEET LSTLRYADQA
KRIKNKPVVN EDPNAKLIRE LKEELQALRD TLMTYAPEEV EKIASQTSPR ILGSKSTPRL
GALSPTSKPL TTTSTLSTAA TSSTPSSNAV PRPPSPTTPA KEISFADAFG TTRKLTMTEL
VDQLKASQKL LDQMNQTWEE KLVKTQEIHC EREKALEAMG ILLQRDNGMG IHTPKQIPHL
VNLNEDPLMS ECLMYQIKPG STHVGRCEND AMDIRLSGPN IMDNHCYFEN DNNGLVTLFP
TPGSMTMVNG MRTTDQKQLH NGYRIILGDY HVFRFNHPEE VRKERKRLSS EQQQQQNGVP
LSSSFGMVSS GRNSGMTDRS ESIFSDRDSA NYSASGPPEI VDWNFAKREA VLNYYYSTNN
KFINGNIIGG GDYSKPASLL DDETMSRTTT SSVRFSNGSL PLSMGIMNDD INVKNAYRFS
GSQLSIDTGI FSSPDGLSSS NIDTMDGTSD DFMDGASGLT KRYNAQLQLR RQKEEYEERI
RLATLYHEQP SYIQDMEMKL QRVIEDMRCM MDNQKQAYES KIKRLSSKLP PEMLHSPLSP
GAQSLASKVI TRWRRVRYVL MAEELLVHAV VLKEANIIAK DLGRDVSYQY IVVHDDAMIS
SRSFWEADAA DLQQSMTSLS GDKNYNSSDS EELQRCDDDL DLRQSIKPCL GVQVIDRKHN
AVYIWSLPEI KHRLKQMQNL YNFSDRPLSR DQFTWSDPFY QASCPRYSLI GLASVSIRNL
LHQVPVESVV NVFDRNSGRV MGKLRLAITP IARSTMASSN SKQRGSGSFM STSIDSNHSS
FSSLSAALQQ QSPTSGKHTP ALSPTFKSDE YSGSLLHVGQ QQVFEIQILE LSGLKETLFT
QVHAQFCLSA FGNVQRHSSE DKLFATEPIS GFGKGPVSFN YTQNMTTTIT ENTLKVIMDG
KLTIEVYGQV RAEHMYGIIE RNIQHQKEDS INENNSTDNK VSHDIISKDK ITTGSTSSGA
INNEPTTSLL SPPQHRKQLK FRPPIRSYTD DGLLFKERHH VVAYVQLCEL GDDGEYSPVN
VLAYSAQDPG CFYLRQGLQR RLKITMVHDS GVQLPWKNVT GVTISNVSLF VDKDDSASTK
PRNENGCLSA IEATDNHQPI AIHLHQDQPL EFYPDGTCTL MAHGLWDSSL HDFAHLNRVT
APQHRLRATM AWQVTCDKST EPLSFSMDLD MKIHNRDLVP PSNASSTSSS SAILNYFSSA
FIQQYHRMSY KLRGIFSVHL SPPLTRQVSQ LWRLNTANRY VRGEELLGPE RGLRDVSLIQ
EYRQAAKQMV RRQQVEATQQ ALDLMDQQQK RQKRRQQQQL HQLETMMSRI GGANGDCESN
TSSRNVDLLN KVIQLWSRRF GTQKEVCITH QPPYSTPQLT TVAALSSLPL NKEDTNDVKL
APKVQCVLPS ATIVKKGYLW HPEHTKTDAW VKHWFVFRRP FIMVYEDQTE IDELAVINVS
SIRVERKTDV EGSLQKPNTF AIYTTNNDYL FQAKNNADML DWITKVDQFY PVDNLES
//
