DPEP2_UNCRE
ID DPEP2_UNCRE Reviewed; 453 AA.
AC C4JQN7;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Putative dipeptidase UREG_03382;
DE EC=3.4.13.19 {ECO:0000255|PROSITE-ProRule:PRU10073};
GN ORFNames=UREG_03382;
OS Uncinocarpus reesii (strain UAMH 1704).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Uncinocarpus.
OX NCBI_TaxID=336963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 1704;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
CC -!- FUNCTION: Hydrolyzes a wide range of dipeptides. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid;
CC Xref=Rhea:RHEA:48940, ChEBI:CHEBI:15377, ChEBI:CHEBI:59869,
CC ChEBI:CHEBI:77460; EC=3.4.13.19; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10073};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10073};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Peptidase M19 family. {ECO:0000255|PROSITE-ProRule:PRU10073}.
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DR EMBL; CH476616; EEP78536.1; -; Genomic_DNA.
DR RefSeq; XP_002543865.1; XM_002543819.1.
DR AlphaFoldDB; C4JQN7; -.
DR SMR; C4JQN7; -.
DR STRING; 336963.C4JQN7; -.
DR EnsemblFungi; EEP78536; EEP78536; UREG_03382.
DR GeneID; 8440221; -.
DR KEGG; ure:UREG_03382; -.
DR VEuPathDB; FungiDB:UREG_03382; -.
DR eggNOG; KOG4127; Eukaryota.
DR HOGENOM; CLU_031404_4_2_1; -.
DR InParanoid; C4JQN7; -.
DR OrthoDB; 1272387at2759; -.
DR Proteomes; UP000002058; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070573; F:metallodipeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd01301; rDP_like; 1.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR008257; Pept_M19.
DR PANTHER; PTHR10443; PTHR10443; 1.
DR Pfam; PF01244; Peptidase_M19; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR PROSITE; PS51365; RENAL_DIPEPTIDASE_2; 1.
PE 3: Inferred from homology;
KW Dipeptidase; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
KW Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..453
FT /note="Putative dipeptidase UREG_03382"
FT /id="PRO_0000411220"
FT TRANSMEM 41..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT BINDING 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT BINDING 286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT BINDING 297
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT BINDING 357
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 147..223
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
SQ SEQUENCE 453 AA; 50043 MW; 6E5A7FB4C93CD013 CRC64;
MSTRDHVKQS PMPVQEGYPR SSKEFSPPSS RSRKRTWVRN LTMSLLIAAG AATFSKYIFP
LGSILGAGSL QPIDPHDYAA RADRILSTTP LIDGHNDLPY LIRLETKNKI YDHEKLPFEA
GLLSHTDAKK IRQGKLGGQF WSVYVECPAD PSAGIDDPSW AVRDTLEQID VAKRLVDEYP
DLLEYCETAS CARSAFKKGR VGSFLGIEVH DLGVRYITVT HNCDNAFATA ASTVAAGKPD
HGLTDFGREF VKEMNRLGML IDLSHVSHQT MRDVLSVTNA PVIFSHSSSY ALSKHLRNVP
DDVLRTVTKN GGVVMVTFVP LFLKVNDPAS VTIHDAVDHI LHVAKVAGWD HVGIGSDFDG
TAVVPKGLEN VSKYPRLVEL LLERGVTDEQ ARKLVGENLL RVWSKAEDIA YAIQASGQKP
NEETWSGRKW TAAADIPMPS MFNDSAERRK QLE
