ID A0A1V9Z4M0_9STRA Unreviewed; 452 AA.
AC A0A1V9Z4M0;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=RanBP-type and C3HC4-type zinc finger-containing protein 1 {ECO:0000256|ARBA:ARBA00017887};
GN ORFNames=ACHHYP_03082 {ECO:0000313|EMBL:OQR92926.1};
OS Achlya hypogyna.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Achlya.
OX NCBI_TaxID=1202772 {ECO:0000313|EMBL:OQR92926.1, ECO:0000313|Proteomes:UP000243579};
RN [1] {ECO:0000313|EMBL:OQR92926.1, ECO:0000313|Proteomes:UP000243579}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 48635 {ECO:0000313|EMBL:OQR92926.1,
RC ECO:0000313|Proteomes:UP000243579};
RX PubMed=25527045; DOI=10.1093/gbe/evu276;
RA Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT identify the ancestral oomycete secretome and reveal gene acquisitions by
RT horizontal gene transfer.";
RL Genome Biol. Evol. 7:120-135(2014).
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:OQR92926.1}.
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DR EMBL; JNBR01000435; OQR92926.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9Z4M0; -.
DR STRING; 1202772.A0A1V9Z4M0; -.
DR OrthoDB; 2951736at2759; -.
DR Proteomes; UP000243579; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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; 4.10.1060.10; Zinc finger, RanBP2-type; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR039577; Rad18.
DR InterPro; IPR001876; Znf_RanBP2.
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; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00547; ZnF_RBZ; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:OQR92926.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000243579};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00322}.
FT DOMAIN 29..71
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 413..438
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT REGION 246..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 452 AA; 50107 MW; 788D284FF2176EBC CRC64;
MDGLDPVDDE WAWPTSLMEG RQLEGFLRCQ VCGEFMNGPV LLRNCRHCFC SECVRKHLLA
RGTNGNCPEC KQACSSGDLV PNRPLEMIID HFRGLKGKVL ALANGATVPI TTPIKTHAQP
KAKDGECATK RMPVVSYNLM KDKKIQELLD SVGLREIRGN RDTLIATHKE YTMLWNAQLD
TLHPKSPNEI RQQILRNYRL RTNEKYEMAS TKRSLGLRHD EPIEKAITAS STMNDNFRKL
AEQIRAQKRA KTQGASSTDP SPAKPQAPSS SKLLVPSPLR PATSSTPPKI PSHKHPQALE
TPPPKANFDS LHPNASASPE FEDEEKPAHP DLLPDGDLRY LPRETVAPKV AFGQPVPVAA
AGTWRRVILN STQQQVYVHS GTTEVRTEPP PGLFAQTTIT KRVVEAPPCT TTWACPRCTL
LNEYHVDECV ACGGPNAKKR PKRVIQKKLS LG
//
