ID A0A163ERU6_DIDRA Unreviewed; 1404 AA.
AC A0A163ERU6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=ATP binding {ECO:0000313|EMBL:KZM23873.1};
GN ORFNames=ST47_g4992 {ECO:0000313|EMBL:KZM23873.1};
OS Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS rabiei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM23873.1, ECO:0000313|Proteomes:UP000076837};
RN [1] {ECO:0000313|EMBL:KZM23873.1, ECO:0000313|Proteomes:UP000076837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ArDII {ECO:0000313|EMBL:KZM23873.1,
RC ECO:0000313|Proteomes:UP000076837};
RX PubMed=27091329; DOI=10.1038/srep24638;
RA Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D., Verma P.K.;
RT "Draft genome sequencing and secretome analysis of fungal phytopathogen
RT Ascochyta rabiei provides insight into the necrotrophic effector
RT repertoire.";
RL Sci. Rep. 6:24638-24638(2016).
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}.
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:KZM23873.1}.
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DR EMBL; JYNV01000180; KZM23873.1; -; Genomic_DNA.
DR STRING; 5454.A0A163ERU6; -.
DR Proteomes; UP000076837; 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 CDD; cd01366; KISc_C_terminal; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
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; IPR001611; Leu-rich_rpt.
DR InterPro; IPR025875; Leu-rich_rpt_4.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 1.
DR PANTHER; PTHR47972:SF28; PROTEIN CLARET SEGREGATIONAL; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF12799; LRR_4; 2.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SMART; SM00365; LRR_SD22; 10.
DR SMART; SM00369; LRR_TYP; 4.
DR SUPFAM; SSF52058; L domain-like; 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.
DR PROSITE; PS51450; LRR; 7.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Coiled coil {ECO:0000256|SAM:Coils};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
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:UP000076837};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1059..1392
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 783..921
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1018..1059
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..79
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..743
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1150..1157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1404 AA; 157305 MW; EBCB8357DF8D4B87 CRC64;
MTEPNTAPLT KLDPATTGTA ATNKEDRDDH KPRDSRGWDG KLRVDKSVVV KYPADSNADV
QSDAESEEEG PPPDEIQADE DLLDDVPDDE DEIELVHCKV GDMASLRLER FKQIKRLCLR
QNRIQSIEIP TDAAATLTEI DLYDNLISHV KGLEAFTELT SLDLSFNKIK HIKRLDHLKK
LRDLYFVQNK ISVIENLDGL TNLRQIELGA NRVREIQNLE TLTGLEELWL GKNKITEIKG
LDTLTNLKIL SIQSNRLRTI SGLDKLVNLE ELHISHNLLT SLDGLEHNTN LQVIDISSNP
IEHLSGLKTL THLTEFWASN CKLSSFAEVE TELKDKEELE TVYFEGNPLQ RAQPALYRNK
VRLALPQIKQ IDAIPFRRTK YATSTPPSTT HTRDGRPGTF GQSTTPHAPV ELTEDRTQDL
KKASALPKPA SRLPQISSPP RPLAELQNGS MNVRSGIPPP MTGAKHKPSS CKSFLPTYCE
PDRPLTHSVP EPATKIRRTL AERAGDLPSR KPTAPPSSRP LSTSVKGTVA RKERGFSAST
STSRAGTRPA SRSTTAPSFS ASMGPGAKPP RPKSAYGQYA GTHMRSKSHH STARPASSMI
RREEDDDEEE RGVQPFLIST NPGESLLAPR KIRQAPIARP YSISIPAQKM FHLSAARSIS
SPTFRPITPV QEEPADADCE EVCASLEAFT LGDSDADNHN VGFGRGMPCP DEEANPFLKP
LHPSRLPQAT PTKQPPTQTP TRPPSSTPRN THKRYLNRFT NDQCPDFYDD RMEAMERQFS
AFKEKMETDM QKATDQKESI QQLQSRVAEL EAIRARLETV NRDLETDLKD AKSCMKTMEM
EMEMTKRNTA FETDDIRRKF RNEIEDLENK HEKATHRWQT EKEAAEEKVR RSFEAQIDQL
LKEHKEQLDE LNAKLSKETE VERTRQLQKE QEVEAEYASK LRAAGIEADA RQRELQLVQG
DLTNVKSELD RERALRTALQ GQFTEATTKN LTLESANTAM KEKINFLESD SQAQSSAYND
LHRRMQEAIE AAEQAHEKLR QEETLRRKLF NQVQELKGNI RVMCRVRPAH ASESDPAKIT
FPDVDTDSKE VAIQGPEKIS ATGKDITAAY QYSFDRVFGP ASQNLEVFDE ISQLVQSALD
GYNVCIFCYG QTGSGKTYTM SSADGMIPLA TAQIYAEAKR LEEKGWRYKI EGSFIEVYNE
TYNDLLGRSE DLDKKKVEVR HDAAKKQTNL ENTVSIELDG PDRVTELLKT ADKNRTVAAT
KANMRSSRSH SVFILKLVGT NEITGERSEG TLNLVDLAGS ERLEHSKVEG ARLKETQNIN
KSLSCLGDVI NALGSAKEGT HIPYRNSKLT YLLQYSLGGN SKTLMFVMVS PLQAHLQETV
TSLKFATKVH NTHIGTAKKQ TKTA
//
