ID A0A420HPP3_9PEZI Unreviewed; 1326 AA.
AC A0A420HPP3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=OnM2_060016 {ECO:0000313|EMBL:RKF59410.1};
OS Erysiphe neolycopersici.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Erysiphe.
OX NCBI_TaxID=212602 {ECO:0000313|EMBL:RKF59410.1, ECO:0000313|Proteomes:UP000286134};
RN [1] {ECO:0000313|EMBL:RKF59410.1, ECO:0000313|Proteomes:UP000286134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMSG2 {ECO:0000313|EMBL:RKF59410.1};
RX PubMed=30253736; DOI=10.1186/s12864-018-5069-z;
RA Wu Y., Ma X., Pan Z., Kale S.D., Song Y., King H., Zhang Q., Presley C.,
RA Deng X., Wei C.I., Xiao S.;
RT "Comparative genome analyses reveal sequence features reflecting distinct
RT modes of host-adaptation between dicot and monocot powdery mildew.";
RL BMC Genomics 19:705-705(2018).
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}.
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:RKF59410.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MCFK01006048; RKF59410.1; -; Genomic_DNA.
DR STRING; 212602.A0A420HPP3; -.
DR Proteomes; UP000286134; 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:UP000286134};
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 103..125
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 281..298
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 453..479
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 680..698
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 730..757
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 777..795
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 836..859
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 879..897
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1042..1064
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1084..1103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1140..1163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1183..1200
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1229..1248
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1268..1287
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 15..76
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT DOMAIN 23..70
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 1326 AA; 150677 MW; 5E53803B457D9052 CRC64;
MEENKQVINY DKGDEGIGEP DTCRICRGEG DSSESLFYPC KCSGSIKFVH QDCLMEWLSH
SQKKHCELCK TAFRFTKLYS PDMPQSLPFH ILVRHVFKHT FRVLLTTLRF CLVIMVWLGL
LPYTIRQIWR FLFWLSEGGW PPSDLTTIHN GSSNVTLESQ AVRQVEFTAL INDGVAQDTL
ISANITNYMY MRTVVNRLTQ FLTPVSHALR ISGSDDIATS LFKSIFNGLG IQSSTKTERP
LIRSSVFIKS KGSSLLSDVS FFKNLTQNAS FNQLLINITE GYIITVLVVV CFVLVFLIRE
WVVQQQPGIN IGVGFNAEPA PIERPRDDQQ DPGTFADTQG ELQRINEDGE IPVEYAVQRN
LDLQFPNRGE VDERSHEFLE LNDGEAVHDL GTEIHPALAA NHDIINFENN AEIVPRAARV
NNAEGIDFNE PEVIEDAEDF EGIMELLGMR GPLFGLVQNA LFSALLLGLT ITVGVWFPYN
IGRVSLLLLA NPGPTLKVPL KIVFGCAAFT QDIALSILGL SSSVCIQLLA QPYNLWTSYF
GLEKSLIAYQ ASFFASTAMD ISFAAFHRLK NDAANNIMYI TDSEMSAACH ESLITIQSLL
SSSVTKLGAI AVYFYSLNLS NIWESIISSS KVSPTTGVQL FKSLSVSLIK SNLLMINFSE
KKRTAPIDLA LSNWSSIDRF LAITTGYIVL CALGTLYVRK RTPLLSGQVG RELETAIIDL
LRQAGGVLKV ILVISIEMLA FPLYCGLLLD ISLLPLFENT TILSRILFTL RSPLTSIFVH
WFVGTCYMFH FALFVSMCRK IMRKGVLYFI RDPDDPTFHP VRDVLERNVT TQLQKILFSA
LVYGALILIC LGGVVWGISL ALKGVLPVYW SSNEPVLEFP IDLLFYNFLI PFAVKFLRPS
AKLHAMYSWW FRKCARILRL TWFMFDERII DEERHLVRRT WLDFFQRSKA DPNFLVISGN
PKDVFEQNPD LKAYYRRDGC YVRAPASDQV RIPKGSSIFL EVNEWNERID QKPDRKDGIH
GKESDLCKLV YIPPWFRVRI SVFIISIWIF AAITGVGVTI LPLIVGRIVF SNVLPPQVRK
NDAYAFSIGI YILGSIIYCA FNFKTLLECT RKTLVFDANT PRKLLNYIFS ICTRVFRITW
TYTAFLIVLP TLFAFLVEFY LIVPLHTYLA IEEKHVVHFV QSWTLGLLYV KLTARLILWY
EDSRPAQSLR AITRNGFLNP DARLATRNFI LPGALLLSTA LLYPWAIARL TIVTVLQRSP
EKHTLAYRYS YPICLCLCFL ALILWVLTRW IRNWKIKIRN EVYLIGEQLH NYGDRKTLLA
RETIPL
//
