ID A0A1Y2WGQ9_9PEZI Unreviewed; 848 AA.
AC A0A1Y2WGQ9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Origin recognition complex subunit 4 {ECO:0000256|ARBA:ARBA00019083};
GN ORFNames=M426DRAFT_19424 {ECO:0000313|EMBL:OTB08279.1};
OS Hypoxylon sp. CI-4A.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX NCBI_TaxID=1001833 {ECO:0000313|EMBL:OTB08279.1, ECO:0000313|Proteomes:UP000242955};
RN [1] {ECO:0000313|EMBL:OTB08279.1, ECO:0000313|Proteomes:UP000242955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CI-4A {ECO:0000313|EMBL:OTB08279.1,
RC ECO:0000313|Proteomes:UP000242955};
RX PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA Henrissat B., Gladden J.M.;
RT "Characterization of four endophytic fungi as potential consolidated
RT bioprocessing hosts for conversion of lignocellulose into advanced
RT biofuels.";
RL Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the ORC4 family.
CC {ECO:0000256|ARBA:ARBA00005334}.
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DR EMBL; KZ111527; OTB08279.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2WGQ9; -.
DR STRING; 1001833.A0A1Y2WGQ9; -.
DR InParanoid; A0A1Y2WGQ9; -.
DR OrthoDB; 230201at2759; -.
DR Proteomes; UP000242955; 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:0005524; F:ATP binding; 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 CDD; cd15492; PHD_BRPF_JADE_like; 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; IPR003959; ATPase_AAA_core.
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; PF00004; AAA; 1.
DR Pfam; PF14629; ORC4_C; 1.
DR Pfam; PF13831; PHD_2; 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:UP000242955};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 320..370
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..320
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 848 AA; 93290 MW; 57F7F57575E5DF2D CRC64;
MATAQTPTGR RKRALPDDEP DSSPAVTPNI TSAVKRRRLN TLANASPSTP KGFSAITSAI
GGALGWGRKG DAKSTTKANQ TNSANPTVYD VPDSPEETKA SEATRSVASK QKHPSLAPSD
KSQRHSSNVY EIPESEEEVD HSRERTDELQ DEVQSTPSGR KGINGISSTS SKKSVSTRLL
ESRKKKPASP APAKVGRDTP KRRGRPPKAQ DKIDEPARSP KSTAKARLTK YDIDALPAVQ
LPAIKGILSP QKKRMGRPRK SVAFNDADRG KENEIYFEDI GSKPTKPTRA KPQKKPVDII
IEEKPASEDE ENESQDDEDD EVCAICSKPD SEPPNEIIFC ENCDLAVHQK CYNVPVIPEG
DWICKNCSQD DVIPVPKVTP KKQIRVAKAS KAPVIPNFEQ HLQHMQRVLL DRCSGNRRIK
LCGQDEAYDK AFQLVEQTVL AGEGNSMMVI GARGCGKTTL MEEIISNLRA EHEEEFHVVR
LNGFIHTDDK LALKEIWRQL GKEMNLEDDL INKTNNYADT MASLLALLSH PAEITGADDG
VTSKSVIFII DEFDLFATHA RQTLLYNLFD IAQARKAPIA VLGLTTRVDV VESLEKRVKS
RFSHRYVYMS LPKSLPAYWD VCRQGLAVDE EDLSNEGFDT NLPGLYEFRD YWDKKIETLR
KTPNFEDHLE YHYYTAKSIP ALLTSCILPL SAVSTSSLDL TIPSNAPGCI SLEPSESKLH
LLSTLSDLEL ALLISAARLD IVAHTDTVNF AMAYDEYSSQ MGKQRVQSAS SGMMALGAGA
RTWGRGIAAV SWERLVSLGI LIPAGIGGRS NAAHGGLEGK MWKLDVALDE IPAACELPGF
LARWCSQI
//
