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Database: UniProt
Entry: A0A0J8URV0_COCIT
LinkDB: A0A0J8URV0_COCIT
Original site: A0A0J8URV0_COCIT 
ID   A0A0J8URV0_COCIT        Unreviewed;       412 AA.
AC   A0A0J8URV0;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=dipeptidyl-peptidase IV {ECO:0000256|ARBA:ARBA00012062};
DE            EC=3.4.14.5 {ECO:0000256|ARBA:ARBA00012062};
DE   AltName: Full=Dipeptidyl peptidase IV {ECO:0000256|ARBA:ARBA00030567};
GN   ORFNames=CIHG_08193 {ECO:0000313|EMBL:KMU90383.1};
OS   Coccidioides immitis H538.4.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=396776 {ECO:0000313|EMBL:KMU90383.1, 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   -!- FUNCTION: Extracellular dipeptidyl-peptidase which removes N-terminal
CC       dipeptides sequentially from polypeptides having unsubstituted N-
CC       termini provided that the penultimate residue is proline. Contributes
CC       to pathogenicity. {ECO:0000256|ARBA:ARBA00037607}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a
CC         polypeptide, preferentially when Yaa is Pro, provided Zaa is neither
CC         Pro nor hydroxyproline.; EC=3.4.14.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00001257};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the peptidase S9B family.
CC       {ECO:0000256|ARBA:ARBA00006150}.
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DR   EMBL; DS017021; KMU90383.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J8URV0; -.
DR   STRING; 396776.A0A0J8URV0; -.
DR   VEuPathDB; FungiDB:CIHG_08193; -.
DR   eggNOG; KOG2100; Eukaryota.
DR   Proteomes; UP000054563; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 2.140.10.30; Dipeptidylpeptidase IV, N-terminal domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002471; Pept_S9_AS.
DR   InterPro; IPR001375; Peptidase_S9.
DR   InterPro; IPR002469; Peptidase_S9B_N.
DR   PANTHER; PTHR11731:SF162; DIPEPTIDYL PEPTIDASE 4-RELATED; 1.
DR   PANTHER; PTHR11731; PROTEASE FAMILY S9B,C DIPEPTIDYL-PEPTIDASE IV-RELATED; 1.
DR   Pfam; PF00930; DPPIV_N; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
DR   PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW   ECO:0000313|EMBL:KMU90383.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022438, ECO:0000313|EMBL:KMU90383.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054563};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW   Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT   DOMAIN          2..98
FT                   /note="Dipeptidylpeptidase IV N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00930"
FT   DOMAIN          181..374
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   412 AA;  46996 MW;  3F6CD8C80FB36486 CRC64;
     MDGWSHLYLF PVGEGEPIQL TRGRWEVTAL NHVDTERQLI YFVATKRHST QRHLYSVSYR
     DMKIKALVND REAGHYTANF SARGGYYVLH YQGPDVPYQE LFATRTGKAI RTINSNADVV
     NKLKEYKLPR IDYLDIRLPS GETLNVMQRL PANFSPSKKY PVLFTPYGGP NSQQVHVGFQ
     SFGWTAYIAS DPELEYITWT VDNRGTGFKG RKFRSTVAKR LGALEAEDQV YAAKVLSKFP
     YVDKERIGIW GTSYGGYLTA KTLETDSGRF SFGISSAPVS DWRFYDSMYT ERYMKTYEMN
     EAGYNASAVR KTEGFKNVRG SFLLQHGTGD DNVHFQHSAA LSDLLMGAGV SPNKMAGTWF
     TDSDHGIRYN GGHAFQYKEL TMKLYEEKNR KFDEEKHQWS KKDLEFAASI GI
//
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