ID C4JDF6_UNCRE Unreviewed; 426 AA.
AC C4JDF6;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 03-MAY-2023, entry version 64.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=UREG_00382 {ECO:0000313|EMBL:EEP75536.1};
OS Uncinocarpus reesii (strain UAMH 1704).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Uncinocarpus.
OX NCBI_TaxID=336963 {ECO:0000313|EMBL:EEP75536.1, ECO:0000313|Proteomes:UP000002058};
RN [1] {ECO:0000313|Proteomes:UP000002058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 1704 {ECO:0000313|Proteomes:UP000002058};
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 -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; CH476615; EEP75536.1; -; Genomic_DNA.
DR RefSeq; XP_002540869.1; XM_002540823.1.
DR AlphaFoldDB; C4JDF6; -.
DR STRING; 336963.C4JDF6; -.
DR MEROPS; A01.079; -.
DR GeneID; 8444465; -.
DR KEGG; ure:UREG_00382; -.
DR VEuPathDB; FungiDB:UREG_00382; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_0_0_1; -.
DR InParanoid; C4JDF6; -.
DR OMA; SDTWVFN; -.
DR OrthoDB; 2900143at2759; -.
DR Proteomes; UP000002058; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06097; Aspergillopepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR034163; Aspergillopepsin-like_cat_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966:SF23; ASPARTIC ENDOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G15950)-RELATED; 1.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000002058};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..426
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002939141"
FT DOMAIN 106..423
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 122
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 310
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 426 AA; 45986 MW; 4A2E5F4A217B9153 CRC64;
MHWIQFLLGL SLLCLQASSS PTPPKKTTRS FKIDLVRRSD YLPDGPRALK KAYAKFGIIP
TNINYGHFND FIPLASGLDR DAISKAKQPD ETGAVTNTPT AHDVQYLSPV TIGGQQFVMN
LDTGSSDTWV FNTQLPESAR KGHSSFNPTK SRTFSKMDGS SFNITYGDAS FAFGSVGTDT
VDIGGATVAK QAIGLPSQVS ASFIKDEISD GLVGLGFDKL STMRPKRQKS FLTNLAADLD
EPVFAAQLKK GAPGSYEFGT IDRTKFKGNL TKVPVNSARG FWEFKSSLFK VGNDTQLRQI
KLKTPNAIAD TGTTLILVDG EMVKAYYEQV KDAKLSTQAG GYIFPCDTTL PALYVSLADT
HLAKIPGNLL NFSPVGSDAK TGEELCFGGV QSNMGTGLQI FGDIFFKALF VVFDLRGPCL
HVAAHA
//