ID A0A0J8RHX7_COCIT Unreviewed; 960 AA.
AC A0A0J8RHX7;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Beta-Ala-His dipeptidase {ECO:0000313|EMBL:KMU83614.1};
GN ORFNames=CIHG_01397 {ECO:0000313|EMBL:KMU83614.1};
OS Coccidioides immitis H538.4.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=396776 {ECO:0000313|EMBL:KMU83614.1, ECO:0000313|Proteomes:UP000054563};
RN [1] {ECO:0000313|Proteomes:UP000054563}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H538.4 {ECO:0000313|Proteomes:UP000054563};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
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DR EMBL; DS016983; KMU83614.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J8RHX7; -.
DR STRING; 396776.A0A0J8RHX7; -.
DR VEuPathDB; FungiDB:CIHG_01397; -.
DR eggNOG; KOG2276; Eukaryota.
DR Proteomes; UP000054563; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006751; P:glutathione catabolic process; IEA:InterPro.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR Gene3D; 3.40.630.10; Zn peptidases; 2.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR017149; GSH_degradosome_Dug2.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR43270; BETA-ALA-HIS DIPEPTIDASE; 1.
DR PANTHER; PTHR43270:SF8; DI- AND TRIPEPTIDASE DUG2-RELATED; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR Pfam; PF00400; WD40; 2.
DR PIRSF; PIRSF037237; Peptidase_WD_repeats_DUG2; 1.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000054563};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT REPEAT 86..127
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 245..270
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..840
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..870
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 960 AA; 104787 MW; 5B0F2355EA85A7C8 CRC64;
MDSSQCHEPA VGVSTDGDDG IATTQPRQSI SSNTANLKNE CAIGHRVHAV RSVLALVVDE
ECVFAGLQGG DIVAWSLDTY ELVLSVKAHE ESVLGLYLSD DRNLLFSSGG DSVVNVWSTS
TFERLYSIYT HHDVGDIFTV AYSSELKTVY CGGQNTSLQW YNLLRDAHPP PQIATHPSCR
THKFFDSRGP GGIAPPARTD NQSLNALYDG QTLTFKRDQH KLFAHNGYVY CMLLVRGILE
CQSGGEVLFT GSGDGSVKLW ELNQGTNVAP TEIASLQNGS ESVLSIAVDG PFLYCGLTGG
AINIWNLDSR QIIKTITSHT GDLWAIDIIK GIIVSGDGDG IVKKFNSRFE EIGSWAAHDG
TMLASAAGVV KDRWIYATGG NDNSVAIWDL TEHPVDSHEI PATSNDELVN ALAKFVGFKT
ISARPKFSGE CNQGAAFLRR HCIYLGAQTN ILTTGQNTNP IVFAKFPATS QNALDRTVLF
YGHYDVVGAE ANQAKWNTDP FQLTSLNGFL YGRGVSDNKG PILAALYAAA ELTQRKELTC
NVVFLIEGEE ESGSQGFAET IKENKDLIGP VDWILLANSY WLDDHIPCLT YGLRGVIHAN
LIVASHHPDL HSGIDGSSLL DEPLKDLTML LSTIVGPKGK INLPGFQDPV LPLTPIEKQR
YDAIAEALLP HHPEIEDVES FTASLMHRWR EPSLTIHSVE IPGCKSSTTT ISRKAKATLS
IRLVPNQNAD KVAEDLIDYA QTQFADLDSQ NILTVEITGK ADPWLGDPGN ELFETLSRAV
TAVWSASTES RKYNNYPPPI PTRHLSNSGL PRTNSSDSLA STSKIERILA SSSSVPNHKS
GRKAKSSHLS PIPTSSTLTT DPTDPNQPSH SQEHETSENH RKTAPQLIKP IYIREGGSIP
TIRFLEKEFN APAAHLPCGQ ASDNAHLSNE RLRVENLYRS REIFRRVFRE LGGSLPAHEE
//
