ID A0A177C4Q5_9PLEO Unreviewed; 596 AA.
AC A0A177C4Q5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=CC84DRAFT_1252530 {ECO:0000313|EMBL:OAG02151.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG02151.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAG02151.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG02151.1,
RC ECO:0000313|Proteomes:UP000077069};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-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 -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
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DR EMBL; KV441556; OAG02151.1; -; Genomic_DNA.
DR RefSeq; XP_018032516.1; XM_018184359.1.
DR AlphaFoldDB; A0A177C4Q5; -.
DR STRING; 1460663.A0A177C4Q5; -.
DR GeneID; 28767845; -.
DR InParanoid; A0A177C4Q5; -.
DR OrthoDB; 38671at2759; -.
DR Proteomes; UP000077069; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd16489; mRING-CH-C4HC2H_ZNRF; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46661; E3 UBIQUITIN-PROTEIN LIGASE ZNRF1-LIKE PROTEIN; 1.
DR PANTHER; PTHR46661:SF4; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Myristate {ECO:0000256|ARBA:ARBA00022707};
KW Reference proteome {ECO:0000313|Proteomes:UP000077069};
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 196..291
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 550..593
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..99
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..312
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 596 AA; 64844 MW; B1AB933DA9920ECF CRC64;
MAGRAAFSHS SPNLGRQLDG ANSGAPQDAA GMHPPRTHSY GAVASHFLAQ PNGAYGGQTW
VDFLRDAGAD PSASAQQPRA PPQPNLHAPL PPLPVDSFPH RPSPHYSLPA HPSAHTEARP
SRSSSERKRR LTTADSPFRR PSSIRMHSED QPGSSHNPIV LGSSPAAAPA QRPSLQSHTS
TGRRDSDFAL PRWQPDSEVT HCFVCGSHFT FFYRKHHCRK CGRVVCSACS PHRITIPRQY
IVHPPYDNPN IIDPTSEDDD HPMSRFGPFG NPALGGGEEV RVCNPCVPDP NYSPPPQHGQ
TSPFPPFSPT AHSPHLAPSN ALPRGPRPSH RSTQSVNDSA RTVSHGQAPR SRDLFTDRRT
SYHGASRVAD LWPPTQANPH DYAQPPAYDH RTRPHSRSVL SANPQPTSSD FAGQHSMPGS
RRSFFAHGHP VPGPPPQPQP TPRRQIAEED ECPVCGNELP AKGPDGDETA RTQHVEECIA
LYSGSPPPAP TTPADLSSNS LPSQRTRGMS SAAGNGEGSS NRMSMMARGM VPYVATEKDC
VDEEGNEAEC VICFEEFEAG DKMARLVCWC KFHESCIKEW WDKKGRGACP THQLQY
//
