ID M5GFC2_DACPD Unreviewed; 1585 AA.
AC M5GFC2;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Kinesin-like protein {ECO:0000313|EMBL:EJU06137.1};
GN ORFNames=DACRYDRAFT_92267 {ECO:0000313|EMBL:EJU06137.1};
OS Dacryopinax primogenitus (strain DJM 731) (Brown rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Dacryopinax.
OX NCBI_TaxID=1858805 {ECO:0000313|EMBL:EJU06137.1, ECO:0000313|Proteomes:UP000030653};
RN [1] {ECO:0000313|EMBL:EJU06137.1, ECO:0000313|Proteomes:UP000030653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJM-731 SS1 {ECO:0000313|EMBL:EJU06137.1,
RC ECO:0000313|Proteomes:UP000030653};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
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; JH795855; EJU06137.1; -; Genomic_DNA.
DR STRING; 1858805.M5GFC2; -.
DR HOGENOM; CLU_001485_20_3_1; -.
DR OMA; IKITICH; -.
DR OrthoDB; 126886at2759; -.
DR Proteomes; UP000030653; 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: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:UP000030653}.
FT DOMAIN 6..361
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 1484..1583
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 676..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 424..466
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 753..780
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 676..690
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 105..112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1585 AA; 177151 MW; 6F9577689ABF8AC6 CRC64;
MSADTNIKVV VRCRPLNSRE HARGAKELIR MMGNQTFLDP PEHVGNAAKA IEKKTMAFSF
DKSYWSAGPR DAPEYCSQQT LYDDLGKELL DHAFEGFNAC ILAYGQTGSG KSYSMMGYGL
DKGIIPLTCE ELFRRVVSKT SGNPNLSFTV EVSYMEIYNE KVRDLLNPKN SGNLKVREHP
VMGPYVEDLA KLVVGSYDEM MTLMDEGNKA RTVAATNMNE TSSRSHAVFT LILTQKIHDE
ALNLDAEKAS RISLVDLAGS ERANSTGATG QRLKEGANIN KSLTTLGKVI ASLAVASEAT
GKGGKKKKVE EHIPYRDSVL TWLLKDSIGG NSKTAMIAAI SPADYDETLS TLRYADQAKK
IKNKAVVNED PNAKLVRELK EELDLLRARV ASSSAESTYD PTVPATQQMV TYQTATGEVK
TISKADLQEQ LEASEKLMKE VNETWEEKLE RTKAIQQERE QALEELGITV ERDMVGVHTP
KRMPHLVNLN EDPLMSECLI YQLKPGKTMV GRLDSDKPAV IRLSGSGILN EHCLFENNEG
KVTLLAMPDS MTMLNGNRIS SDKPYRLRSG YRIILGDNHF FRFNNPEEVR KRRDRTKMHQ
SISAADLAAE GINGSPRPET PDSAAGDDVA EVDWTYAKRE AALVHLNGQG EGFESLPDDD
LNKLYHEISK VKNLREYAKS RPESSLSHVE EIWSDGRPPP SEITDDTSVE PNGGTSHGSP
SMEDQPRDAQ VHLEHQRAEF EERLNAMADT TQTEDLEIER DHMQLQLKLV QNQMKRLMEL
RKTGASTVDF VPMEPVLYSA RQLRLIRKVL DKWRSHKSFS MAESVLSNAV IVKEANVLSK
ELDKAVSYNF TVLSGGSLSA PTSALEDIGA LGEFGDVADP VLLSTKEPTV GIKVLDKRHT
AVYIWSLDRL QQQLQRMRNL TSFIDRPSYS RHFSSEEPFY DRSPPHYSFI GNALVSLAPL
SRRMSPAATI PIFCRYTAEA IGSCRVDARV LTVNTPARGA VNGSAMTSRS SSPLPEALPQ
GSKLSFTLTI DSVKGLSSLD FGSVHMQVRL SAFMGPSVAA EDVFPSTVID MDNAPLYNLK
LRRTFSFVLN AKVTAYMRQG YAPIEFFAEV KPSYIERLER WDEMREQHMQ KELRSTRPAQ
MRRAETDFVV EERHDVVAWV QVRELTSSGE YQAVPVLSQG QLDSGVFLLR QGLQRRLALT
LTCHSGKQMP WKQITRINAG KIRLLDAKGR LHDPSTADDR VDLKLLKPQT VDLKPDGSAT
LHAEASWDSS AHDSLLLNRV TGIRQRVLLQ LDWMVEIDTC AEPALFTTDI AVDIQERDAR
PPSMLTGLFS STKVLTKCSA IFSLRLTPQL SRSAKDMWRL DTSEKYVRGE EVLASWKPRG
VSVVEDYIRL DNVERRAADV QAIKILLDAS PTCGAMERTL SDEEATDLLR KTMDLWTRRS
VPRPELQFKL VQEPSSPMEE SEDIDQAPKP KLVAHTKLIA RSDTATKKGH LSMLIDPAGN
SWKRRWFVLR RPYLYIYAHS NELEELSVIA LNGVNVEHSS QLAVLFDKPF TFTLFTASNS
HALAAPNAKE LQSWMIKLDP TRLPS
//
