ID R1EPE2_BOTPV Unreviewed; 432 AA.
AC R1EPE2;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=UCRNP2_3845 {ECO:0000313|EMBL:EOD49412.1};
OS Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS (Neofusicoccum parvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Neofusicoccum.
OX NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD49412.1, ECO:0000313|Proteomes:UP000013521};
RN [1] {ECO:0000313|Proteomes:UP000013521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX PubMed=23766404; DOI=10.1128/genomea.00339-13;
RA Blanco-Ulate B., Rolshausen P., Cantu D.;
RT "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a fungal
RT vascular pathogen associated with grapevine cankers.";
RL Genome Announc. 1:E0033913-E0033913(2013).
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:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; KB916082; EOD49412.1; -; Genomic_DNA.
DR RefSeq; XP_007583136.1; XM_007583074.1.
DR AlphaFoldDB; R1EPE2; -.
DR STRING; 1287680.R1EPE2; -.
DR KEGG; npa:UCRNP2_3845; -.
DR eggNOG; KOG1609; Eukaryota.
DR HOGENOM; CLU_634577_0_0_1; -.
DR OrthoDB; 1342875at2759; -.
DR Proteomes; UP000013521; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd16702; RING_CH-C4HC3_MARCH6; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13145:SF0; E3 UBIQUITIN-PROTEIN LIGASE MARCHF6; 1.
DR PANTHER; PTHR13145; SSM4 PROTEIN; 1.
DR Pfam; PF12906; RINGv; 1.
DR SMART; SM00744; RINGv; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS51292; ZF_RING_CH; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000013521};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT TRANSMEM 249..273
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 34..95
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT DOMAIN 42..89
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..334
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 432 AA; 48301 MW; B666974F29935563 CRC64;
MASADDMSAA APQSSVPDIM NDPAYDPNSA ASDKASDDPD TCRICRGEGT KEEPLFYPCK
CSGSIKFVHQ DCLMEWLSHS QKKHCELCKT PFRFTKLYHP QMPSSLPTTV FLRRAVVHVL
KYLMTWCRGL LVGSVWLLWL PWCMRVIWRA LFCAAGTNAT SLANLTGIPA VLAPFSQTLN
MSAGEPTAYI LIKKFLFGLG PFPDFFNASF TNSTDNATVA HTISLRQASL LSDVSFLKSL
TSHPSVNRLI LDIIEGQIIT VLVVIAFILI FLIREWVVQQ QPVINVAAMQ PINNPAPPAH
QARQDAAPNA VEEQEMPDVP DADDSADDED RFSDVSDDSL GPEADVLPAR HDTPEENPEL
PDIVRINLDR ISDSDIRKAV ARSQFEKVAE IIDQRGSLAE KVIRKDLFVW IEMVSDRQRK
WSYVEWRYLH AS
//