ID A0A2N5SGJ6_9BASI Unreviewed; 570 AA.
AC A0A2N5SGJ6;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Postreplication repair E3 ubiquitin-protein ligase RAD18 {ECO:0000256|ARBA:ARBA00015551};
GN ORFNames=PCANC_23433 {ECO:0000313|EMBL:PLW12353.1}, PCASD_20327
GN {ECO:0000313|EMBL:PLW32156.1};
OS Puccinia coronata f. sp. avenae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=200324 {ECO:0000313|EMBL:PLW12353.1, ECO:0000313|Proteomes:UP000235388};
RN [1] {ECO:0000313|Proteomes:UP000235388, ECO:0000313|Proteomes:UP000235392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12NC29 {ECO:0000313|EMBL:PLW12353.1}, and 12SD80
RC {ECO:0000313|EMBL:PLW32156.1};
RA Miller M.E., Zhang Y., Omidvar V., Sperschneider J., Schwessinger B.,
RA Raley C., Palmer J.M., Garnica D., Upadhyaya N., Rathjen J., Taylor J.M.,
RA Park R.F., Dodds P.N., Hirsch C.D., Kianian S.F., Figueroa M.;
RT "De novo assembly and phasing of dikaryotic genomes from two isolates of
RT Puccinia coronata f. sp. avenae, the causal agent of oat crown rust.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
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:PLW12353.1}.
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DR EMBL; PGCJ01000985; PLW12353.1; -; Genomic_DNA.
DR EMBL; PGCI01000250; PLW32156.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N5SGJ6; -.
DR STRING; 200324.A0A2N5SGJ6; -.
DR OrthoDB; 6177at2759; -.
DR Proteomes; UP000235388; Unassembled WGS sequence.
DR Proteomes; UP000235392; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0006301; P:postreplication repair; IEA:InterPro.
DR GO; GO:0006513; P:protein monoubiquitination; IEA:InterPro.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR039577; Rad18.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR14134; E3 UBIQUITIN-PROTEIN LIGASE RAD18; 1.
DR PANTHER; PTHR14134:SF2; E3 UBIQUITIN-PROTEIN LIGASE RAD18; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50800; SAP; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000235388};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 38..96
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 293..327
FT /note="SAP"
FT /evidence="ECO:0000259|PROSITE:PS50800"
FT REGION 136..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 570 AA; 62424 MW; 45FC4F4FD9C095A1 CRC64;
MSSKTNKNSL QYQLSLVAPQ DFPPELRALS TLDSTLRCPV CKELYQAPVI IHIQKCCHTF
CSSCIRTCFN NNSNNHKIGA TGLGGVGNSQ RCPICKVEAQ EEKIKPVPTL ESAVICWEDA
REEIFKLIAR AQASESQLKQ IQSTSVNPFS RNTTKNRTPL EDATRKSKEN SHAHSKQKAE
ETRSLPEPKT RAQKKAQLAA PPKRKPQRQS TKGDESDHEI EMLSYNPTDP AAPVRCPVCS
TQMLNSKMDE HITACLSGKK KNQAPSSGPA KKIKTSHRGG TKPPQTRIPL PHFASLKTKD
IKAELSKHGL SSNGTTSMQT RRLSKYITLF NANLDANPLH QKSLESLREE LEQWESLQES
ENLRLDKNRE KIFSNQARYL KANHHQFASL IQQASKSLQS TQKLVAPHVS DSVFEPTTTD
GRDPAPDAST SKLVPSELDH TSEVAPSTDH TSEVTPSTTR VSSPKIGERQ SSHPPLTQLK
PATGNENHPD LNPSTSGAVR DHSDNQATDH LGEPASHLVP LKASNPPPLE SAASDPPPLE
SAARDVNHLQ ADTSTSNTLS ADSDTTIAVT
//
