ID E3QHV8_COLGM Unreviewed; 506 AA.
AC E3QHV8;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Kelch domain-containing protein {ECO:0000313|EMBL:EFQ30446.1};
GN ORFNames=GLRG_05590 {ECO:0000313|EMBL:EFQ30446.1};
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|EMBL:EFQ30446.1, 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).
RN [2] {ECO:0007829|PDB:5C86, ECO:0007829|PDB:5C92}
RP X-RAY CRYSTALLOGRAPHY (1.51 ANGSTROMS) OF 25-506, AND DISULFIDE BONDS.
RX PubMed=26680532; DOI=10.1038/ncomms10197;
RA Yin D.T., Urresti S., Lafond M., Johnston E.M., Derikvand F., Ciano L.,
RA Berrin J.G., Henrissat B., Walton P.H., Davies G.J., Brumer H.;
RT "Structure-function characterization reveals new catalytic diversity in the
RT galactose oxidase and glyoxal oxidase family.";
RL Nat. Commun. 6:10197-10197(2015).
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DR EMBL; GG697349; EFQ30446.1; -; Genomic_DNA.
DR RefSeq; XP_008094466.1; XM_008096275.1.
DR PDB; 5C86; X-ray; 1.51 A; A=25-506.
DR PDB; 5C92; X-ray; 2.10 A; A=25-506.
DR PDBsum; 5C86; -.
DR PDBsum; 5C92; -.
DR AlphaFoldDB; E3QHV8; -.
DR SMR; E3QHV8; -.
DR STRING; 645133.E3QHV8; -.
DR EnsemblFungi; EFQ30446; EFQ30446; GLRG_05590.
DR GeneID; 24410955; -.
DR VEuPathDB; FungiDB:GLRG_05590; -.
DR eggNOG; ENOG502SCD5; Eukaryota.
DR HOGENOM; CLU_013444_1_0_1; -.
DR OrthoDB; 2433441at2759; -.
DR Proteomes; UP000008782; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd02851; E_set_GO_C; 1.
DR Gene3D; 2.130.10.80; Galactose oxidase/kelch, beta-propeller; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
DR InterPro; IPR037293; Gal_Oxidase_central_sf.
DR InterPro; IPR015202; GO-like_E_set.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR006652; Kelch_1.
DR PANTHER; PTHR32208:SF68; GALACTOSE OXIDASE; 1.
DR PANTHER; PTHR32208; SECRETED PROTEIN-RELATED; 1.
DR Pfam; PF09118; GO-like_E_set; 1.
DR Pfam; PF01344; Kelch_1; 1.
DR SMART; SM00612; Kelch; 3.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF50965; Galactose oxidase, central domain; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:5C86, ECO:0007829|PDB:5C92};
KW Metal-binding {ECO:0007829|PDB:5C92};
KW Reference proteome {ECO:0000313|Proteomes:UP000008782};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..506
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003180429"
FT DOMAIN 408..504
FT /note="Galactose oxidase-like Early set"
FT /evidence="ECO:0000259|Pfam:PF09118"
FT BINDING 144
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /evidence="ECO:0007829|PDB:5C92"
FT BINDING 359
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /evidence="ECO:0007829|PDB:5C92"
FT BINDING 447
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /evidence="ECO:0007829|PDB:5C92"
FT CARBOHYD 80
FT /note="N-acetyl-D-glucosamine 1"
FT /evidence="ECO:0007829|PDB:5C92"
FT CARBOHYD 82
FT /note="N-acetyl-D-glucosamine 1"
FT /evidence="ECO:0007829|PDB:5C92"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007829|PDB:5C92"
FT CARBOHYD 210
FT /note="N-acetyl-D-glucosamine 2"
FT /evidence="ECO:0007829|PDB:5C92"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007829|PDB:5C92"
FT CARBOHYD 226
FT /note="N-acetyl-D-glucosamine 2"
FT /evidence="ECO:0007829|PDB:5C92"
FT CARBOHYD 228
FT /note="N-acetyl-D-glucosamine 2"
FT /evidence="ECO:0007829|PDB:5C92"
FT DISULFID 378..382
FT /evidence="ECO:0007829|PDB:5C86, ECO:0007829|PDB:5C92"
SQ SEQUENCE 506 AA; 53934 MW; D5BBF2449D09408D CRC64;
MPTLRSALRN LPAALLALAA ACEAQNVGKW GPMVKFPVVP VAVALVPETG NLLVWSSGWP
NRWTTAGNGK TYTSLYNVNT GNISDAIVQN TQHDMFCPGT SLDADGRIIV TGGSSAAKTS
VLDFKKGESS PWTPLSNMQI SRGYQSSCTT SEGKIFVIGG SFSGAGTRNG EVYDPKANTW
TKLAGCPVKP LVMQRGMFPD SHAWLWSWKN GSVLQAGPSK KMNWYDTKGT GSNTPAGLRG
TDEDSMCGVS VMYDAVAGKI FTYGGGKGYT GYDSTSNAHI LTLGEPGQAV QVQKLANGKY
NRGFANAVVM PDGKIWVVGG MQKMWLFSDT TPQLTPELFD PATGSFTPTT PHTVPRNYHS
TALLMADATI WSGGGGLCGA NCKENHFDGQ FWSPPYLFEA DGVTPAKRPV IQSLSDTAVR
AGAPITITMQ DAGAYTFSMI RVSATTHTVN TDQRRIPLDG QDGGDGKSFT VNVPNDYGVA
IPGYYMLFAM NEAGVPCVAQ FFKVTL
//
