ID U7PQ44_SPOS1 Unreviewed; 1076 AA.
AC U7PQ44;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Origin recognition complex subunit 4 {ECO:0000256|ARBA:ARBA00019083};
GN ORFNames=HMPREF1624_05883 {ECO:0000313|EMBL:ERS97712.1};
OS Sporothrix schenckii (strain ATCC 58251 / de Perez 2211183) (Rose-picker's
OS disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX NCBI_TaxID=1391915 {ECO:0000313|EMBL:ERS97712.1, ECO:0000313|Proteomes:UP000018087};
RN [1] {ECO:0000313|Proteomes:UP000018087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58251 / de Perez 2211183
RC {ECO:0000313|Proteomes:UP000018087};
RX PubMed=24855299; DOI=10.1128/genomea.00446-14;
RA Cuomo C.A., Rodriguez-Del Valle N., Perez-Sanchez L., Abouelleil A.,
RA Goldberg J., Young S., Zeng Q., Birren B.W.;
RT "Genome sequence of the pathogenic fungus Sporothrix schenckii (ATCC
RT 58251).";
RL Genome Announc. 2:E0044614-E0044614(2014).
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; KI440847; ERS97712.1; -; Genomic_DNA.
DR AlphaFoldDB; U7PQ44; -.
DR STRING; 1391915.U7PQ44; -.
DR eggNOG; KOG0955; Eukaryota.
DR eggNOG; KOG2228; Eukaryota.
DR HOGENOM; CLU_007115_1_2_1; -.
DR OrthoDB; 230201at2759; -.
DR Proteomes; UP000018087; 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; 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; 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; 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:UP000018087};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 425..475
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 125..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 965..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1076 AA; 113491 MW; C77F16C86E0AE30E CRC64;
MSGAIGRKRA RSEDGNNDAV DENVPLTGTV EATGTVKRQR LAHSHSTASV ANRTSASDDA
ALFPGANIAT TPQTPRTVHA VASAITGALA YGVGSLVGAS KDAGKARGQA RDRLLARPFA
SLLHERNTRT TQQDDLDKLY EFPDDDGGDA NASNRPTRAA LESDVEENTL VGSASPTPDT
PSKKQPQTPS AMKTASAATK TATDKNKKKR RDLLEDLAID GTDKMAAGLE GGRLSRRDRV
RTTPKNVDRE IGNASTPNSA SKSRSRGKAV NGGAPAAASP ALAVEPDVAP GVALTTTEAS
SAPTSTRRRA RSTTAAKVSS TADTPPKPLA SPREKTNRTA MTDTEKGDEA TPASTRRSRA
KATPAKTTEK LVPKRASRAK STSKEAAGTA TKDTSTKPLD QVVQNIPQTD SAPAEGGDSS
DDTDGDVCAI CSKPDSEPPN EIIFCETCDL AVHQQCYNVP VIPEGDWFCK KCLRQQNDDT
LETAAGNQPT DSVGEESAAD LTDKDDAAAA AAARDLAPDI ANFEHHLARM KRVLLGRCTG
RQRVRLQGQD DAYDKVYQVV KQTVVAGEGN SMMVIGARGT GKTTMVESIL GALAAEHGGA
FHVVRLNGFI HTDDKLALRE IWRQLGKEMA VEDDVVNKTN NYADTLASLL ALLSHPSEIQ
GAAIGTGAVE KDGDGAPDVT STAVVFVMDE FDRFATHARQ TLLYNLFDIA QARKAPIAVL
GLTTKIDVVE SLEKRVKSRF SHRYVYLPLA RSLPAFWDIC RHGLVIEDDD DKDGAGPKAV
DIAMDVDETE GHAEFRQWWK HMIDSVKDDD HFQEQLAFHF YSTKSVAAFW TTCIMPLAAV
SSTAPRLKLP PVGEAALSGG AAAAGSASST DGPRSVGRPS LAALAASSTR KITKTTSLND
IDPLPLAPPD SKLHLLAALS ELELSLLIAA ARLDIVLSTD TVNFAMAYDE YVSLMGRQRV
QSSLAGSGVG SGRGVGRPPG GSSSTVGGTV VGGGARVWGR GVASRAWESL AALSLLIPAG
MGASARARGP GRPSNALVTS GLEGRSMWRT EVALEEIAAA PGVRLSAVMA RWCKEI
//
