ID A0A162K6A8_CORDF Unreviewed; 573 AA.
AC A0A162K6A8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Carboxypeptidase {ECO:0000256|RuleBase:RU361156};
DE EC=3.4.16.- {ECO:0000256|RuleBase:RU361156};
GN ORFNames=LEL_04346 {ECO:0000313|EMBL:OAA77523.1};
OS Akanthomyces lecanii RCEF 1005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC Cordyceps confragosa.
OX NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA77523.1, ECO:0000313|Proteomes:UP000076881};
RN [1] {ECO:0000313|EMBL:OAA77523.1, ECO:0000313|Proteomes:UP000076881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA77523.1,
RC ECO:0000313|Proteomes:UP000076881};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
CC -!- SIMILARITY: Belongs to the peptidase S10 family.
CC {ECO:0000256|ARBA:ARBA00009431, ECO:0000256|RuleBase:RU361156}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAA77523.1}.
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DR EMBL; AZHF01000003; OAA77523.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A162K6A8; -.
DR STRING; 1081108.A0A162K6A8; -.
DR OrthoDB; 1647009at2759; -.
DR Proteomes; UP000076881; Unassembled WGS sequence.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR PANTHER; PTHR11802:SF479; CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000256|RuleBase:RU361156};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361156};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361156};
KW Reference proteome {ECO:0000313|Proteomes:UP000076881};
KW Signal {ECO:0000256|RuleBase:RU361156}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|RuleBase:RU361156"
FT CHAIN 20..573
FT /note="Carboxypeptidase"
FT /evidence="ECO:0000256|RuleBase:RU361156"
FT /id="PRO_5007747874"
FT REGION 41..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 573 AA; 64179 MW; 3AA59EB04B82048A CRC64;
MKSQFLLSGL VGLAGLVSAG RNSNSGDAFL RRHMPEFSAQ HLSRRATTAA EPKNQTGEVL
PPRFRNNGTE KFYVDGKKLP LINWDVGESY AGNLPITDKK NETSELFFWF FPTATKEFVE
KKEIVIWLNG GPGCSSLLGF LEENGPISWG EGMEKPKRNP FSFHLLSNIV WLEQPVGVGF
TKGNETIYNE DDIAKQFIGF WKNFVKTFGM EGWKVYIAGE SYAGMYGPYL AKHMLDQDDK
TYYDMSGLLV WDGISWGETL QSSPVAFPYL DQHYNLMPVD QPSFAKLRDL DKSCGFADFR
DEYFVYPPKG LIPNPLPHAK VHPNGSYVDQ NCARIFDLIY IEALKKNPCF NIYNIVDRCP
ERNDPLSGKD SWFNRRDVQS AIHVKPHVKW AQCKQVFPEG VDDQSVPAGV YALPQVIEQT
KNVIIAEGTS DYLLSLNGIL LGIQNMTWAG QLGFQQAPSD PFYVPAYGFD PEQLFTDEGD
PNFYANELPA GYGVMGTTHH ERGLSFVVSQ LAGHEGPEYT PSASFRTLEK LLGRIDSLSQ
VSAFTLPQIS NITQPKGDLG NGTVKIPCWT RDC
//
