ID A0A0F8AZ02_CERFI Unreviewed; 1266 AA.
AC A0A0F8AZ02;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=Origin recognition complex subunit 4 {ECO:0000313|EMBL:KKF93646.1};
GN Name=orc4 {ECO:0000313|EMBL:KKF93646.1};
GN ORFNames=CFO_g4000 {ECO:0000313|EMBL:KKF93646.1};
OS Ceratocystis fimbriata f. sp. platani.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Ceratocystidaceae; Ceratocystis.
OX NCBI_TaxID=88771 {ECO:0000313|EMBL:KKF93646.1, ECO:0000313|Proteomes:UP000034841};
RN [1] {ECO:0000313|EMBL:KKF93646.1, ECO:0000313|Proteomes:UP000034841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFO {ECO:0000313|EMBL:KKF93646.1,
RC ECO:0000313|Proteomes:UP000034841};
RA Belbahri L.;
RT "Genome sequence of Ceratocystis platani, a major pathogen of plane
RT trees.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00004448}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the ORC4 family.
CC {ECO:0000256|ARBA:ARBA00005334}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000256|ARBA:ARBA00006375}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL23 family.
CC {ECO:0000256|ARBA:ARBA00006700}.
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:KKF93646.1}.
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DR EMBL; LBBL01000220; KKF93646.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F8AZ02; -.
DR Proteomes; UP000034841; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000808; C:origin recognition complex; IEA:InterPro.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR CDD; cd15492; PHD_BRPF_JADE_like; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 1.50.40.10; Mitochondrial carrier domain; 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; IPR041664; AAA_16.
DR InterPro; IPR002067; Mit_carrier.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR016527; ORC4.
DR InterPro; IPR032705; ORC4_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013025; Ribosomal_uL23-like.
DR InterPro; IPR012678; Ribosomal_uL23/eL15/eS24_sf.
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; PF00153; Mito_carr; 2.
DR Pfam; PF14629; ORC4_C; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF00276; Ribosomal_L23; 1.
DR PRINTS; PR00926; MITOCARRIER.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54189; Ribosomal proteins S24e, L23 and L15e; 1.
DR PROSITE; PS50920; SOLCAR; 2.
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU00282}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000034841};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW ProRule:PRU00282}; Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|ARBA:ARBA00022448};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT REPEAT 260..360
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 386..474
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT DOMAIN 742..792
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 501..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..552
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..733
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1266 AA; 140508 MW; BEF2F5348811C40F CRC64;
MIHRPNQAPN FATFKVPLRF TKFDLRDYLW NLYNVEVTKV RSFVAPGPVV NTLTENSQQR
VRIHRGQSEK YMTVELAQPF AWPSLPGDLE PWNHRLWEAR KAYSEEITKQ HMVTARNETI
APSKVKPSGD RRLLAKQAAA LLKGDAKWSN GEILDEKWET VLKAAEQDVP LEKVDEQSPV
ASEVTEVKVF TAYSAADRNL DFSFNSGHHN GSSLAETTKQ AQHRLCMEVG SRRRYGGLRS
IKFLAYEQIR AVIITSPEKE THLRRLVSGS LAGVTSVFFT YPLELIRVRL AFETKRDGRY
TLRTICRQIY GESMAGVGTA SSAIFKSGIA NFYRGFAPTL IGMLPYAGVS FLTHDTMGDI
LRSTPLAPYT TLPRPSNAPP ENKPPLRSWA ELLSGGISGM VSQTSAYPLE VIRRRMQVGG
AVGDGHRSSI SETVAVILKE RGFKGFFVGL TIGYVKVVPM VAVSFYTYER FGIATKTVPC
EQAISYNTAL QAKAPLSNAN PLDGQQLVLS PSKPPPAAKR RGRPPKPKAA LQPQPQLQPW
PVLQPPQQSV VPLPQIPHHG ALPLHLDQQR QMQQQHQQQQ QQPSSFSNEL QFVNISPQKY
MAPASPIKSP LKSPLKGILT PSRHRGPLAE RTRKNVVFDM GGGNKTPGEV VFEDLPGTNS
GKRGKPQTPM ALPRAAGDDR TPLSEKLRAA AKQAAQKKMA AEAETEPLPA EEEQDEEEPR
PPTTLRGHDL EGASPEEIDE DEEKCQICGQ HDSEAPNEIL FCDVCDLGYH QQCHGVSTIP
DGDWLCLNCA QEDVTKTPST KRYAKFTGLD VLVSEEPEAT IQEPKFEVPP IPNFEHHLRC
FQRVLVDRCT GRRRIKLIGH EEPWEKTHQL IEQTVAAGEG NSMLVIGARG SGKTTMVESI
VDEMHEQHTD KFHVVRLNGF VHTDDKLALK EIWRQLGVEM EVDEAVMKRT SYSDTLASLL
ALLSHPTEIS GPEAEGVTSK SVIFVIDEFD MFAYHPRQTL LYNLFDIAQS RKAPIGVIGC
TTRLDVVEML EKRVKSRFSH RYVYMTPARS LPAFWDVCRQ GLVVDEDDAV KEGLDPASNG
FAAFQSFWTD MVGQLHEQPE FQKFLKHHFY TAKSVPAFLA TCILPLSLMQ PATLPLRIPT
TAVSTSSSNY TITPNAVVGS VSLSAPPSKA HILESLSDLD LSLLIAAARL DIVAHTDTVN
FAMAYDEYTA LVSKQRVQAG MLALGGGARV WGRGVAGIAW ERLQSGAGRF KGAMWRIKDK
DKLGLY
//
