ID A0A423WBK0_9PEZI Unreviewed; 1805 AA.
AC A0A423WBK0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Kinesin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=VMCG_06461 {ECO:0000313|EMBL:ROW00746.1};
OS Valsa malicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=356882 {ECO:0000313|EMBL:ROW00746.1, ECO:0000313|Proteomes:UP000283895};
RN [1] {ECO:0000313|EMBL:ROW00746.1, ECO:0000313|Proteomes:UP000283895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03-1 {ECO:0000313|EMBL:ROW00746.1,
RC ECO:0000313|Proteomes:UP000283895};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-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:ROW00746.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LKEA01000020; ROW00746.1; -; Genomic_DNA.
DR STRING; 356882.A0A423WBK0; -.
DR Proteomes; UP000283895; 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 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; 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 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:UP000283895}.
FT DOMAIN 1..353
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 1613..1786
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 601..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1469..1554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1578..1599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1676..1713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 770..825
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 610..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1469..1508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1509..1539
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 98..105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1805 AA; 200052 MW; E33874511E5E0E48 CRC64;
MAGAGLTWHL PAIEIDRGAK CIVEMKGNQT VLTPPPDAPQ GKNAKDGGQK VFAFDRSYWS
FNKEDSNYAG QNCLHEDLGT PLLDNAFQGY NNCIFAYGQT GSGKSYSMMG YGKEHGIIPS
ICQDMFERIG RIQQAEPNTR CTVEVSYLEI YNERVKDLLN PGTKGNLKVR EHPSTGPYVE
DLAKLVVGSF QEIEHLMDEG NKARTVAATN MNATSSRSHA VFTLMLTQKS VDTDTKMEME
KVAKISLVDL AGSERATSTG ATGARLKEGA EINRSLSTLG RVIAALAEMS TGAKKKKGAA
SQVPYRDSVL TWLLKDSLGG NSMTAMIAAI SPADINYDET LSTLRYADSA KRIKNHAVVN
EDANARMIRE LKEELSLLRS KLGGGGGGAV GGGAGGVAVP ADEVYAEGTP LEKQLVTITG
SDGSTKKVSK AEIAEQLSQS EKLLSDLNQT WEQKLAKTEE IHKERESALE ELGISIEKGF
IGLSTPKRMP HLVNLSDDPL LAECLVYNLK PGITTVGNVE SEVDNNLGIR LKGSRILPEH
CQFENGADST VTLIPMEGAA VMINGKRITE PQQLHSGYRV ILGDFHIFRF NHPTEALAER
AERTETQRHS LLRQSVTASQ LHALERTSPT PSPSPRLGPH ERSWSKGGSE LGSDSRSESP
APRGRETDWS FARREAAGAI LGSDQNFSSL TDEELNALFE EVQRARAERV TTGKEGDDDL
ESLASYPVRE KYMSTGTIDN FSLDTALTMP STPKQGDADD KIRDARDEMQ AHLEKQKGEF
QDQLKSAEAA NVEVEEIKKE KAQMEETLKK MKEDMQKQLA IQKRDFEAKI EKMDPLRRRK
ASPRLSEAEI ELAKKAVKHW RGRRYVQMAE SVLQHAATLK EAQIMSQELD ESVVFQFCVV
DYGHNLCSSY DMILNGGESD DIALEQAIKP CIGVRVVDYK HNIVHLWSLH KLHDRVRQMR
QMHQYLDQPE YAQHLSLDNP FIETCMPQYT LIGEADVPLK AVFESRVQDF HLDVLSPHTS
HAIGIIKLSL EPSLARAPSN SLKFNVVMHE MVGFAEREGT EVHAQLFIPG ISEEDGITTT
QFVKDFDEDP IRFESVHSMN VPLSSPSDVV LRVAIFAKVS TMHLDKLLSW DDMRDAVPSS
RTKPMTARIN ESHFYTEEKH DILSRVQILE MDENGEYVPV EVAQTSDLDS GTFQLHQGLQ
RRITINLTHS SGDVLPWDDV VSVRVGKVQL VDHAGKNPDM GSVSPDIALK LAAKPVFRHN
ANGTRSITIT GQWDSSLHNS LLLDRTTGDK YRVQMTISWE ISSPKLAEPM RFSTKACCQI
LSRSFVRQTS MFSALWQNVR FVHSSTSIFT LKMRPAPIKR VGDLWRMNSQ HDYVKGEENL
TTWTPRGVSL IGDYIGARKK RRRIAEIGAM QNFLRKVGLP EPRIVVSDES HDVYGIPPPK
AKEDDVDSID ELLQYTPDVT QVVDPLDAQT STGEQSGDQQ QEQQPEQESE QQVEQSSGQQ
SEQQSDQESG PESEQEGDQE EAQEPEQANQ DEEGAEEPQP PEEPSPPEPP MSEYTERETL
VLERCLKLWR SYPDPLNQIL SEGNTKPPAD GDPETPTPPD LVASIIRVPK NPTVLRGGYL
LVPSSDATRW IKRFVELRRP YLHVHNVTDG EEVAIVSLRN SRVDSQPGIL GLLNGDEDED
GGMDMNGALT TSPPQLSPQY DDDRNGHRRT SSGRVISSIV GTMNGNGSGS AAQTRTRRVT
SGLAKLSSRL QAGVFAIYGT DNTWLFAARS ERDKLDWIFK IDQSYFSSSS VSPDETGADS
PGLGY
//
