ID A0A024TV27_9STRA Unreviewed; 960 AA.
AC A0A024TV27;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=H310_09205 {ECO:0000313|EMBL:ETV97883.1};
OS Aphanomyces invadans.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=157072 {ECO:0000313|EMBL:ETV97883.1};
RN [1] {ECO:0000313|EMBL:ETV97883.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJM9701 {ECO:0000313|EMBL:ETV97883.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL Submitted (DEC-2013) 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:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; KI913971; ETV97883.1; -; Genomic_DNA.
DR RefSeq; XP_008873444.1; XM_008875222.1.
DR AlphaFoldDB; A0A024TV27; -.
DR STRING; 157072.A0A024TV27; -.
DR EnsemblFungi; H310_09205-t26_1; H310_09205-t26_1-p1; H310_09205.
DR EnsemblProtists; ETV97883; ETV97883; H310_09205.
DR GeneID; 20086255; -.
DR VEuPathDB; FungiDB:H310_09205; -.
DR eggNOG; KOG1609; Eukaryota.
DR OrthoDB; 1342875at2759; -.
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; 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; PS51292; ZF_RING_CH; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 102..124
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 153..174
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 296..321
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 381..403
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 410..433
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 453..473
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 508..528
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 548..568
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 675..699
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 719..745
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 766..792
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 798..820
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 869..891
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 903..922
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 10..71
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT REGION 240..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 960 AA; 107427 MW; 23829B338AFDD52A CRC64;
MDRTDSMDFD EHLDAAECRV CREEADSRRR LFAPCKCNGS IRHIHSDCLI QWLNFSKRET
CDLCSHAFTF RQVYAHGCPE VLPFRDILTS SVKLISRHAL EYIRMGAILV MWAAVTPYCL
SWIYRLWFLR SPSMASVHFF DRVHSLERVV DDIFFGLILM MVVVLAGFYV ICIAEDVQTE
SNRYHRDALI ASGWHIDEEA EPEGESDDDQ DDFDDVGPFV AEVGAPRRRI RLREADNLPF
AAEPPQDPAN PPPAPHEPHH DQDHQHHDHA QGPDEVDWMW EVMGFQAPWP VVLRNVLFFL
VLASGFLVVF VFAPHAFGAL YNGRGLHLPL PSSLLATAQE AFDAAKARGD CLQFLDVVRC
LSTYVSWGSG LLLWRAVRPS IISPHLGPFF GPIFWAMSCM CAAAKVTSHL VLKVFVLPVV
IGTAVDAATL PLFQAAAMHR LTFALHNMLA AYVMHWVLGM SFIHFVSVAV LQLREVLHPD
ILTGILHPHD PYQYRVKNIL AGSMPRQYCA MAFATLKYIA FVPVLVYLPV VTATTLLPSG
WFPLELRFRY IFALVQVPLE LAIVHINVQD SLDHFAPNIG DLQTLWMATM CRHLGLVEFL
LPRVPALVHG DPDVVLTLPD LVFDPLDDNH PHHGHEPVVY GYRRKEWPKN GAADALKMEY
TLLPRTTPPF VAGRLAVLAV LWWGTMFAAI AAVTIGPLVV GRCASALLDR YFGGGHDSFS
FAAGVVIYFI VLYAAEACAA LSIPHNEIDP ELRQRGYEVR GMSRHGLILA VGLYMVGLPY
LIGVLVSMLL PASPWPSLLE STCFGVIVMQ FCLYWACCLV RWDEGSVLDS LTLAMNQIHF
HVMANCAGVV DEGDLTHKCL DLATFKANVV WPLVHVVSAG LVVPLVCSSV YRHAFDGMLH
VTHVHVFRAA FATQVIVGLV VVGQTSKATA RWLQDLHDAI RDDLYLIGRE LTDYEHPKQC
//
