ID A0A094HZA7_9PEZI Unreviewed; 771 AA.
AC A0A094HZA7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=V502_03939 {ECO:0000313|EMBL:KFZ18789.1};
OS Pseudogymnoascus sp. VKM F-4520 (FW-2644).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420915 {ECO:0000313|EMBL:KFZ18789.1, ECO:0000313|Proteomes:UP000029308};
RN [1] {ECO:0000313|EMBL:KFZ18789.1, ECO:0000313|Proteomes:UP000029308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4520 (FW-2644) {ECO:0000313|Proteomes:UP000029308};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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}.
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:KFZ18789.1}.
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DR EMBL; JPKE01001527; KFZ18789.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094HZA7; -.
DR STRING; 1420915.A0A094HZA7; -.
DR HOGENOM; CLU_375577_0_0_1; -.
DR OrthoDB; 38671at2759; -.
DR Proteomes; UP000029308; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15737; FYVE2_Vac1p_like; 1.
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:UP000029308};
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 295..384
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 723..764
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 771 AA; 83484 MW; 92D2AA849D224A8A CRC64;
MTSEAELRAR YQTSRFRETG RQVSPTEADE GSAEPPQAPI IDTAEPNILG EEEPRGLMAD
PAGEEDPAAA NTDTEPIRVD EEDPVIANAD IQPSSVDIEA GSIADAQSDD GPALHRLSLA
DESLGNPTDL ALPESQPSTP DVPLSTPSLS NQEEIEAQTV TYDDSGSGLP SGPRSPVEPN
ISTFPLNQSG DIPAQSLISA EAETSETRDT EDDIGRSAPA ENVDTGQLDG TTCSTRHRRH
LQGNDSDSEQ GPALTSQRDE HDDTVAGTEV TAATAATGGE EATINTVGPP RWQPDAEVTY
CPICRTQFNF FIRKHHCRKC GRVVCASCSP HRITIPYQFI VQPPVSGPAA ALPIVPLAGR
DTDNISQFGG TKVRLCNPCV PDPNTLPPQP QRTAADERWR DAPPTYYLSS SSRPYSFGEQ
DMEHLERQAS ASSVRSRAVS STGATHRHQL SQNPYPPRSS SQTSYLGGTS YTGPHHLNQG
SSSYQRRYPN RNLQGPRHQS HQSLSMSSTG SPSNVQPHYR SLLDPFSSQQ SQSSASGVDT
SRPLPPIPRI REEDECPVCH RELPSRALPD FEALRSNHIT ECIEEQIAIH SGRPRQQSPA
SIPARHQRPS PVAMVSSSSS PSQVRSNSPN SATSSSSSQG EINLAQAINL QPPVPDISSF
PNTPEGRTAF REAQHAAVVL GHTRSSSHSP LAHPSASFSP EPRRTGMFPY KATEKDCVDD
AECTICLEEF EVGVHMARLE CLCRFHEKCI RSWWEGKPGR CPVHGHDAWG L
//
