ID A0A0F4ZJF2_9PEZI Unreviewed; 825 AA.
AC A0A0F4ZJF2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=PHD-type domain-containing protein {ECO:0000259|PROSITE:PS50016};
GN ORFNames=TD95_002257 {ECO:0000313|EMBL:KKA30340.1};
OS Thielaviopsis punctulata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Ceratocystidaceae; Thielaviopsis.
OX NCBI_TaxID=72032 {ECO:0000313|EMBL:KKA30340.1, ECO:0000313|Proteomes:UP000033483};
RN [1] {ECO:0000313|EMBL:KKA30340.1, ECO:0000313|Proteomes:UP000033483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR-DP1 {ECO:0000313|EMBL:KKA30340.1};
RA Radwan O., Al-Naeli F.A., Rendon G.A., Fields C.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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:KKA30340.1}.
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DR EMBL; LAEV01000407; KKA30340.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4ZJF2; -.
DR OrthoDB; 230201at2759; -.
DR Proteomes; UP000033483; 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 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; 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; PF00628; PHD; 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:UP000033483};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 278..325
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..272
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 825 AA; 90822 MW; 05EC40BC8C21A26F CRC64;
MDHPRTPSKS GHKRVRSETT TPTSDTKSPS KRRRLDPAND GATKPATASP MLLSNEVADP
LEAHPETYRG GSELPSPSKQ PKPRGRPPKA AKAAAALQPQ TQLHHPSQTQ QPGSPHATAS
FPDMSPRKAA PASPSKSPSR SPAKSPLKSI LTPSRKNRGP ASERARKSVV FDVAPVSKAP
VEVVFEDLPD PVPASTRRGT KSNTPKLTQA GKGRMSLSEK LRRASTKKQP EQVEEPQRES
EVETEPEDET QEEADEEAQE EVEEELAEEA STEETYQDQV CEICRRSAPN QVLFCDVCDL
GYHQKCLGIS DIPQGDWLCP NCAQEDVTKT PSTKRYAHVS SEQLTSGVTP AQQNLKIPPI
PNFELHMRSF QRVVVDRCTG RRRMRLVGQS DQMLKTQELI KQTVVAGEGN SMLIIGARGS
GKTTMVESTI DDMITTYGDM FHTVRLNGFV HTDDKLALKE IWRQLGVEME VDDDLMKRTS
YADTLASILA LLSHPTEIAG AEAEGFTSKS VVFIIDEFDM FAYHPRQTLL YNLFDIAQAR
KAPIAVIGCT TRLDVVDMLE KRVKSRFSHR YVYMTPARSL KGFWDMCRQG LVISDEDALH
EGIDMEADGY FEFQDYWTDM VNKLYEQEDF QKLLKHHYYT SKSVPGFLAT CVLPLSLLRP
ATLPLVIPAP VPATMSSSKY SLEEPNDCVA TQSLSAPPSK AHVLSSLSDL DLSLLIAAAR
LEIVAHTDTV NFAMAYDEYV SLISRQRMQA GLLAIGGGAR VWGRGVAGVA WEKLVNSGLL
VPASIGGRGQ MGGLEGKMWK VDMALEDIPA GAKLSGAMAK WCREI
//
