ID   C4JPX6_UNCRE            Unreviewed;       671 AA.
AC   C4JPX6;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   ORFNames=UREG_04619 {ECO:0000313|EMBL:EEP79773.1};
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:EEP79773.1, 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CH476616; EEP79773.1; -; Genomic_DNA.
DR   RefSeq; XP_002545102.1; XM_002545056.1.
DR   AlphaFoldDB; C4JPX6; -.
DR   GeneID; 8440817; -.
DR   KEGG; ure:UREG_04619; -.
DR   VEuPathDB; FungiDB:UREG_04619; -.
DR   eggNOG; ENOG502RV5I; Eukaryota.
DR   HOGENOM; CLU_009988_1_1_1; -.
DR   InParanoid; C4JPX6; -.
DR   OMA; WIPSYSY; -.
DR   OrthoDB; 1831139at2759; -.
DR   Proteomes; UP000002058; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd05471; pepsin_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR034164; Pepsin-like_dom.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47965:SF109; ASPARTIC PROTEINASE 3-RELATED; 1.
DR   PANTHER; PTHR47965; ASPARTYL PROTEASE-RELATED; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002058};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..36
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           37..671
FT                   /note="Peptidase A1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002937998"
FT   TRANSMEM        415..439
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          51..376
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          532..566
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          590..671
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        590..646
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   671 AA;  73233 MW;  61086D5B4C711494 CRC64;
     MRLRFRSGRG IDALSRSQIA LEVLLFVALS WHVVHAAQDS PAPLAVPSGS DWVAIRVGSP
     PQWINVFPNT GSSETWVIGR DGCDSTMECR TARGGFFLSN ESSTWNGIGF YELGNDLQLD
     HSGVGNYGFD NISLDDRTVL ADQIVSMVNT TDWWVGSLGL GIKKTTFTSE DKLSFLKLQG
     VRSSLTLGGV DRNRFVENTV SFVLSPDDLP MVAVKSIKVS SNVESSGSDI VDLHTLNRLE
     RYTIDSSSPF FWFPEYICDA FAKELDLEYD DALQLYTYGT NSTTYDNVMN ANMSFTFTLS
     DIPDSGNSID ITLPFCAFDH QLSYPFPNLD ANASSQGLHY FPMRRTSDPK QFTIGRTFLQ
     EAYLAVDYER HNFSISQARF PSDGGISRDL VEISRPTESS YKGPSKPQNS LSTSALIGIG
     VGVGVFVVIA TCIGITVCLR KKGRKPKLLP EPLQEKAKMK WQRRRYWPFS CSRISSTPSE
     LSSEAHFVVE APANPAATRY ELEGSNQPVE LEASEVINTF YSVSGKRRDV AIPPPVYRNE
     VDDKDTSEPA TPQGPPQSGA GPPVYILTSI PLDASHSEPI LVSPLAPSMT VNGSLSTSGP
     SPLTPNRSFN GSFLGNGSLS IRQPGDSYSS QVTASGVGTG GSTLETGPDG PSHPVDGQPP
     RVIRRKFSWE E
//