ID A0A1Q5UKR5_9EURO Unreviewed; 442 AA.
AC A0A1Q5UKR5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=PENSUB_1160 {ECO:0000313|EMBL:OKP13060.1};
OS Penicillium subrubescens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1316194 {ECO:0000313|EMBL:OKP13060.1, ECO:0000313|Proteomes:UP000186955};
RN [1] {ECO:0000313|EMBL:OKP13060.1, ECO:0000313|Proteomes:UP000186955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 132785 {ECO:0000313|EMBL:OKP13060.1,
RC ECO:0000313|Proteomes:UP000186955};
RA De Vries R.P., Peng M., Dilokpimol A., Hilden K., Makela M.R.,
RA Grigoriev I., Riley R., Granchi Z.;
RT "Genome sequence of the ascomycete fungus Penicillium subrubescens.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
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:OKP13060.1}.
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DR EMBL; MNBE01000157; OKP13060.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q5UKR5; -.
DR STRING; 1316194.A0A1Q5UKR5; -.
DR OrthoDB; 5474929at2759; -.
DR Proteomes; UP000186955; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR15710; E3 UBIQUITIN-PROTEIN LIGASE PRAJA; 1.
DR PANTHER; PTHR15710:SF228; FINGER DOMAIN PROTEIN, PUTATIVE-RELATED; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000186955};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 300..341
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 71..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 442 AA; 48033 MW; 9360C1E490E7D899 CRC64;
MADQGDRVFC HACGGVWLLD TGEDGHDNSQ TCPHCESDFT EIIEIPPDSP QPEPAAEPHL
PSVNPWADHN PWAQQESTRP QTSGWMESGS PGYSHRSYRS PDGRFTFSST TIGGGYSSRQ
DAQPNPMLPF MVQSLDTLFQ GLAGTHDGHQ TQRGPGMNVH PYPHAAGMRE PDVMHDPFQA
EDEHARRHEG LYPHDTNGPQ DMTAPLQTLA DLLEAFQGIS GAQRGTARNP AENPFAMLSA
LMRNNDAVYS QEELDRVISQ LIDHTQQGTA PPPASDTAIQ SLPKKKMTPQ MMGSDGKAEC
SICMDPVELD TEVTVLPCTH WFHFDCIKAW LSQHNTCPHC RRSIDLPGVT STNTGAGTSE
NPVVIPDSPP ASPQRQRRRS SPFTSRSIRS ARSSISRSSH NSTSPEMGGE SGTRRGSRSE
SSRGGITGWV WSRFGGGGGA SS
//
