ID A0A420HP87_9PEZI Unreviewed; 865 AA.
AC A0A420HP87;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 08-NOV-2023, entry version 16.
DE RecName: Full=Origin recognition complex subunit 4 {ECO:0000256|ARBA:ARBA00019083};
GN ORFNames=OnM2_061058 {ECO:0000313|EMBL:RKF59258.1};
OS Erysiphe neolycopersici.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Erysiphe.
OX NCBI_TaxID=212602 {ECO:0000313|EMBL:RKF59258.1, ECO:0000313|Proteomes:UP000286134};
RN [1] {ECO:0000313|EMBL:RKF59258.1, ECO:0000313|Proteomes:UP000286134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMSG2 {ECO:0000313|EMBL:RKF59258.1};
RX PubMed=30253736; DOI=10.1186/s12864-018-5069-z;
RA Wu Y., Ma X., Pan Z., Kale S.D., Song Y., King H., Zhang Q., Presley C.,
RA Deng X., Wei C.I., Xiao S.;
RT "Comparative genome analyses reveal sequence features reflecting distinct
RT modes of host-adaptation between dicot and monocot powdery mildew.";
RL BMC Genomics 19:705-705(2018).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the ORC4 family.
CC {ECO:0000256|ARBA:ARBA00005334}.
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:RKF59258.1}.
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DR EMBL; MCFK01006171; RKF59258.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A420HP87; -.
DR STRING; 212602.A0A420HP87; -.
DR Proteomes; UP000286134; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000808; C:origin recognition complex; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd00009; AAA; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041664; AAA_16.
DR InterPro; IPR016527; ORC4.
DR InterPro; IPR032705; ORC4_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12087; ORIGIN RECOGNITION COMPLEX SUBUNIT 4; 1.
DR PANTHER; PTHR12087:SF0; ORIGIN RECOGNITION COMPLEX SUBUNIT 4; 1.
DR Pfam; PF13191; AAA_16; 1.
DR Pfam; PF14629; ORC4_C; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 3: Inferred from homology;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000286134};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 329..380
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 865 AA; 96946 MW; E59B327B52C52B65 CRC64;
MSLSRKRNRA QFNHDQDEVS VENDRRAKKG KGNTWETTNL PPKKSAPCRS GTLATPELEL
KKLKVREKDI YDFTSSDSED HRQYARRKSA ISSIKKTTLT DKTINDDSKI SVGIDSSIKE
RGDLKAASKE LTASKSSQKE FNSQINAKTE RQRGSDVTPL FSKKSMPVVE IISSGLSKNS
GTQKSRKKRP KVDTTTQSIK VAGNLDLDCR PSSSLGKRKK GSTESISKKS ALAISLPSSR
PRELSSEPKK RRIRNASPEQ AKGSNYITRS IFTSDIKLLS SKKKVDANAN EKFDLGFKDL
PVTVVAKKQQ GKKHSSSGGK ASPAHPDDDT ACEVCRRYDS KKNNPMLLCD GCDNGYHIKC
VGLVEEPDTD LWFCEKCKPD VTYVQKDGPP LESLDMPQNI SNFEHHLKNM QRTVLDKLTG
RIPLKLTNLE DEMQKVYQIV HQTVLSGEGN SMLIIGSRGT GKSTLVDHVI SDISNNHRDD
FHVVRLNGFI HTDDRLALRE IWRQLGREMR VDDDDPMMKS GHHADILVTL LALLSDPSHI
SETEPNQTAT SVIFILDEFD HFTTHHRQTL LYNLFDIAQS KKAPILVLGL TTKVDVAEML
EKRVKSRFSH RYVHLSLPRS LPAFWQTCKE SLTMNEFEAK IESKELMFAA GYQEFMSYWQ
AMIENLYTKD VTFIYHLESI FYRTKSVPTF LNSCILPISN LSAQRPILRG TSFQHGEMLL
TEPDSKLHIL QGLSELELAL LISAARLDVI LDTDTCNFAM AYEEYSSLTS RHKIQTSNSG
IKAIGASGAK VWGRQVSLDA WEKLARYELL IPVTASGASL FGAAAGHGRD CSITGRMWKV
DVALEEIPGS VETLSKVMVK WCKEI
//
