ID A0A1V6SZ29_9EURO Unreviewed; 659 AA.
AC A0A1V6SZ29;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PENFLA_c019G02419 {ECO:0000313|EMBL:OQE19216.1};
OS Penicillium flavigenum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=254877 {ECO:0000313|EMBL:OQE19216.1, ECO:0000313|Proteomes:UP000191342};
RN [1] {ECO:0000313|Proteomes:UP000191342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 14082 {ECO:0000313|Proteomes:UP000191342};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQE19216.1}.
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DR EMBL; MLQL01000019; OQE19216.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6SZ29; -.
DR STRING; 254877.A0A1V6SZ29; -.
DR OrthoDB; 3084186at2759; -.
DR Proteomes; UP000191342; Unassembled WGS sequence.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd20354; Rcat_RBR_RNF14; 1.
DR CDD; cd23134; RING-HC_ITT1-like; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR047548; Rcat_RBR_RNF14.
DR InterPro; IPR006575; RWD_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR11685:SF457; TRANSLATION TERMINATION INHIBITOR PROTEIN ITT1; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF05773; RWD; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR SUPFAM; SSF54495; UBC-like; 1.
DR PROSITE; PS50908; RWD; 1.
DR PROSITE; PS51873; TRIAD; 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 Reference proteome {ECO:0000313|Proteomes:UP000191342};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 13..157
FT /note="RWD"
FT /evidence="ECO:0000259|PROSITE:PS50908"
FT DOMAIN 192..462
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 196..230
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 252..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 659 AA; 74487 MW; D1196FCDF8000E89 CRC64;
MTELDFLEDD RSVELSSIAA IFPEIQIDPF SPFKAVLDLP VAPSTPTSIC FQQPLDTAAA
ITPPTSLDES KGELDQPPVK DVHLLSHLPP LNLEVELPEG YPTEKSPIIH LRTIPSWLPP
SVIDRLSSDC HRLWEECGKD LVVFTYIDHL QQLAETIFNI QDPSGEVCLP RDLKIGLLDY
NKKAEREKFE QGTFECGVCL EPKKGTVCYR LLRCSHVFCI QCLQDFYNSC ITEGDVDSVK
CMAPDCEYNK RPAAVPGDGQ TPRKKRDRTL GPSELLQIPL ATETVQRYAF LKRKKKIEAD
KTTVYCPRQW CQGAARSKRH PKPEDPMSDD LNSSDEEDGS EPCSEVKDGE LPPMAERVSI
CEDCNYAFCC VCKKGWHGEL VRCYPRRDGE PTEEEKATEE YLRLYTTPCP TCNVPCQKQM
GCNHMRCFQC DTHFCYLCSA WLCADNPYKH FNDEKGQCFN RLWDLEGGDG INPDGAEALH
RIPDALLNFD DDPHVVAIHE ATDESDDDHP AFEFDNDEDD LHRHPPPPAP VPPQVNRGAG
RPGQRDHAAA RAAAAERQAQ ARAMAEVRNR NARRQARHPV RWADAPQRLP PQAGDPRRPV
RWAEVPAEPL ADEDGPIRWE AIAIRPGRAQ AHPGLQRFLH LVQNDREDEW DSDEMDDDF
//
