ID A0A1V6TC24_9EURO Unreviewed; 805 AA.
AC A0A1V6TC24;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=PENSTE_c009G09471 {ECO:0000313|EMBL:OQE23123.1};
OS Penicillium steckii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=303698 {ECO:0000313|EMBL:OQE23123.1, ECO:0000313|Proteomes:UP000191285};
RN [1] {ECO:0000313|Proteomes:UP000191285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 24891 {ECO:0000313|Proteomes:UP000191285};
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 -!- 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 -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}.
CC -!- SIMILARITY: Belongs to the HRD1 family.
CC {ECO:0000256|ARBA:ARBA00010089}.
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:OQE23123.1}.
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DR EMBL; MLKD01000009; OQE23123.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6TC24; -.
DR STRING; 303698.A0A1V6TC24; -.
DR OrthoDB; 2912447at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000191285; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProt.
DR CDD; cd16479; RING-H2_synoviolin; 1.
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; PTHR22763:SF184; E3 UBIQUITIN-PROTEIN LIGASE SYNOVIOLIN; 1.
DR PANTHER; PTHR22763; RING ZINC FINGER PROTEIN; 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 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000191285};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
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 TRANSMEM 43..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 172..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 276..297
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 342..407
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 424..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 657..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..700
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..793
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 805 AA; 88344 MW; BFCE5C0F1081768A CRC64;
MRLAVYAGAS VALATGVFLK ALHQRANFYS ACVYLSQSSA NLMILTNLCL LATGFILFWL
QRLLYGRLRP IETEQLYERA WFAVTETCLA MTIFRGELGG WFLVMFISLL VGKVWGWIGE
GRVEYLEQQP PANPRLFHTR LSSSLVLSVL FNAFMLKYCV DTVIRQPRPD MMVMFGFEFA
ILTLLSASTT ARYVIVLTEI YVTRQQLKEK MDERRAEIRE ARLEAIREHA RAGESSPPSD
LPNENDINEL EFDVPGWEGK ARWVFYLDLL TDLVKLIVYL VFFAILLTFY GLPIHILRDV
VVTIRSFVRR ITDFLRYRNA TRDMNERYPD ATAEEVAREE LCIICREEMV SIQPAAGAPE
EGAAQPAAGA RPVPERLRPK KLPCGHILHF SCLMSWLARQ QNCPTCRRPV ILTAAARARE
AAAANANNAG NGHPDRAAGD QLPGQPGVQG NGMPRARVFQ FGPFRFGFGA VRGGDLFNNL
HQQIHQGNAP LQPAVNANPQ GARQIGFGFG FGRRPPLATP QNLPQQGHPQ QGQPQFQTPS
LDDTEAQLQQ IEDQISQQIA GIRRNIDHLT HVRNLQRSLQ QAQQSLQEQA GLQPGMPSLT
TQASGTLPQT GTLGISARQF VAGPASATLT SGDSRLPEGL TLPPGWTMVP LEATDQAGQP
IPQSVNPTPT INPTNGQSPA QTSQPPVTSA TYTPNANDNV GVRENAGAVP SSAPSSSEAQ
PASSTLPNWN TSTGSSSVTQ RPADSLSQEW TDVRSDQVPD TNQSTIPSWG TNHTSTNEVS
EENSISTSKG KGRAATVEET DDTTN
//