ID A0A2N3NGY8_9PEZI Unreviewed; 874 AA.
AC A0A2N3NGY8;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=jhhlp_001828 {ECO:0000313|EMBL:PKS11677.1};
OS Lomentospora prolificans.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Microascaceae; Lomentospora.
OX NCBI_TaxID=41688 {ECO:0000313|EMBL:PKS11677.1, ECO:0000313|Proteomes:UP000233524};
RN [1] {ECO:0000313|EMBL:PKS11677.1, ECO:0000313|Proteomes:UP000233524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHH-5317 {ECO:0000313|EMBL:PKS11677.1,
RC ECO:0000313|Proteomes:UP000233524};
RX PubMed=28963165; DOI=10.1534/g3.117.300107;
RA Luo R., Zimin A., Workman R., Fan Y., Pertea G., Grossman N., Wear M.P.,
RA Jia B., Miller H., Casadevall A., Timp W., Zhang S.X., Salzberg S.L.;
RT "First Draft Genome Sequence of the Pathogenic Fungus Lomentospora
RT prolificans (Formerly Scedosporium prolificans).";
RL G3 (Bethesda) 7:3831-3836(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:PKS11677.1}.
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DR EMBL; NLAX01000006; PKS11677.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N3NGY8; -.
DR STRING; 41688.A0A2N3NGY8; -.
DR VEuPathDB; FungiDB:jhhlp_001828; -.
DR InParanoid; A0A2N3NGY8; -.
DR OrthoDB; 2912447at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000233524; 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 InterPro; IPR024766; Znf_RING_H2.
DR PANTHER; PTHR22763:SF184; E3 UBIQUITIN-PROTEIN LIGASE SYNOVIOLIN; 1.
DR PANTHER; PTHR22763; RING ZINC FINGER PROTEIN; 1.
DR Pfam; PF12678; zf-rbx1; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000233524};
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 36..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 138..159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 278..297
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 346..398
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 400..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 204..235
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 401..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..807
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..822
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 874 AA; 96414 MW; BC902E49F7DCFED0 CRC64;
MRLAWYAGAS TALAVSVVIS AFHQRANFYS AMVYLAQSNF CLLALINFIY IVYGAFMFGL
QRLCFGRLRA VEVDQLSDRA WVAITETCLA MTIFREEIGA WFLVMFTALV TGKVWGWIGD
GRLEILEQQP PANPRLFHTR LTVSLLMSTF YDMWLLRYCV NTVIQQARPN MMVMFLFEFA
VLTASSLRTN SRYALALVDA RIVAHQTQKR LVERRKEVQE QRDQMLRERE AAEAEGREHT
ISEADIPNPD DIDEMDIEVP GWEAKGQWIL TLELFTDFIK LSIYIAFFTV LLMFYGLPVH
IMREVYITAS AFFKRLSALL KYRRAIQSMS KYPDATAEDL GREDTCIICR EEMKPWDPET
NPGAVERTRP KKLPCGHILH FGCLRSWLER QQVCPTCRSP VVLDGQSTNR DQNRRPRVVP
GVQPQQQQAQ GQPDEQQRQL PGPFQRPGQG DQGTGQNNDA GAHDNEPQPA PPRHRMFNFG
PFRLEFIRQE LRNPQQLDAF LGGELGGAAE NAAPPPPTNV QASSPTSILS SGFDNIVNRE
LTSLQNLQHM QHELQTASLL LAELVRLRQL RATTENAPHN PTASSTPHHT QPNTPSSQVP
PQIQHSRTPP PPGALPHHPS TFSHLAPPYP YRPSSSVLSR YAAPPNTTAI PAGSSELPEG
VVLPPGWSLL PLQRMDNSSG VPLTATPPPQ PTEVTAGPST QPTTSSAAAP AHSGINGSTV
HTRHTEAPRP GMAFPRPQPP EAAAAAALAA SAAAAASAAS VPPRPSQDDD DRPTPVLAPN
PVMPNWGGSS QLFSNQARLS SNSTPDIPEA EEESDESEEE SDQEASNQRH PPPVPNRDDA
GESSNGPLNG KGKAVTMEDA SSSEEEEDED SDEE
//