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Database: UniProt
Entry: A0A2N3NGY8_9PEZI
LinkDB: A0A2N3NGY8_9PEZI
Original site: A0A2N3NGY8_9PEZI 
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
//
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