ID E3QAX3_COLGM Unreviewed; 848 AA.
AC E3QAX3;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN ORFNames=GLRG_03155 {ECO:0000313|EMBL:EFQ28011.1};
OS Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS anthracnose fungus) (Glomerella graminicola).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=645133 {ECO:0000313|Proteomes:UP000008782};
RN [1] {ECO:0000313|Proteomes:UP000008782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1.001 / M2 / FGSC 10212 {ECO:0000313|Proteomes:UP000008782};
RX PubMed=22885923; DOI=10.1038/ng.2372;
RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA Ma L.-J., Vaillancourt L.J.;
RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT by genome and transcriptome analyses.";
RL Nat. Genet. 44:1060-1065(2012).
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; GG697339; EFQ28011.1; -; Genomic_DNA.
DR RefSeq; XP_008092031.1; XM_008093840.1.
DR AlphaFoldDB; E3QAX3; -.
DR STRING; 645133.E3QAX3; -.
DR EnsemblFungi; EFQ28011; EFQ28011; GLRG_03155.
DR GeneID; 24408520; -.
DR VEuPathDB; FungiDB:GLRG_03155; -.
DR eggNOG; KOG0828; Eukaryota.
DR HOGENOM; CLU_010475_0_0_1; -.
DR OrthoDB; 51730at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008782; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProt.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR024766; Znf_RING_H2.
DR PANTHER; PTHR22763; RING ZINC FINGER PROTEIN; 1.
DR PANTHER; PTHR22763:SF165; TRANSMEMBRANE E3 UBIQUITIN-PROTEIN LIGASE 1; 1.
DR Pfam; PF12678; zf-rbx1; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000008782};
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 416..434
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 455..474
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 486..505
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 604..626
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 661..683
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 695..717
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 781..842
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 510..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..524
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 848 AA; 94350 MW; D65E295E4024FEEA CRC64;
MPSYPFENPR PVVLGLAIVG ILWILLAPGN GGASLFSASD LAVQRLERHR HALDLLNTSK
WGDFAPRQNG SSTGPLPRSL NLTGFRAQDG FAWDDLERFR ERCLEWSHNA IPPVGGVNLW
DIGEGEAVWQ NATGAVKGTW VRKEAMFKRE WTSYNLSTIT PSLHWSGLQS EWARNITGDE
GKILMDLVDT GRHGREIAYQ GVVDDGVASS GGKVRSAKAS VTIEDVKGSG VNWEMRLHGV
QWPRQGAILL TTTSEKFDGI FGLPHLTPSS DFFQSSQRLL NATLAEVLRR KEKEVFNDGV
MPWTSDLTNP PDTLNPAPHC EYIMYAQVHP PDRSYLNMKG FRPTREGMEK IISDIEQELR
FPEGAPIRGV PELQLSAIIW SPDCAFFLET KGPPDFAPMD GQHLRGMKTE IIYHKIRIWI
LLFAVVILSQ ALLLKQQMKE SATPSTMGRI SYSTISMMVM VDGGIFAAAS MWALDASITY
LESLSLLFAA FLSMSLGGFF LAEIHKVQEP ENRRRAEREQ HASNDTSART PATPAATAEP
DSLPQPVTAG ARRRAPSPPV IVPSDQDMDA EIADAASGAA AVLTAGTGAG GGHRMGPEVT
FQAVIFRFAM IVSLVLLVSI ASTSWYPRVR NLFVNSVAMV YFSFWVPQIH RNILRNCRRA
LTWQFMIGQS VLRLLPFAYF YVYENNFLFA ETDRRAFLVF CAWLWIQLWV LAFQYVLGPR
FGIPKSWTPD AWDYHPVLRE DGVEAGGLPI GLLSEPGSPS LDRVRSGEDR KSGSNLRAID
CAICREVLEV PVMRAGEEDP AAGGVVGVFT RRNYMVTPCR HIFHSACLEG WMRFRLQCPI
CREELPPL
//
