ID   F1KPY0_ASCSU            Unreviewed;      2012 AA.
AC   F1KPY0;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Carboxypeptidase {ECO:0000256|RuleBase:RU361156};
DE            EC=3.4.16.- {ECO:0000256|RuleBase:RU361156};
OS   Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX   NCBI_TaxID=6253 {ECO:0000313|EMBL:ADY39934.1};
RN   [1] {ECO:0000313|EMBL:ADY39934.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21685128; DOI=10.1101/gr.121426.111;
RA   Wang J., Czech B., Crunk A., Wallace A., Mitreva M., Hannon G.J.,
RA   Davis R.E.;
RT   "Deep small RNA sequencing from the nematode Ascaris reveals conservation,
RT   functional diversification, and novel developmental profiles.";
RL   Genome Res. 21:1462-1477(2011).
CC   -!- SIMILARITY: Belongs to the peptidase S10 family.
CC       {ECO:0000256|ARBA:ARBA00009431, ECO:0000256|RuleBase:RU361156}.
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DR   EMBL; JI163983; ADY39934.1; -; mRNA.
DR   ESTHER; ascsu-f1kpy0.2; Carboxypeptidase_S10.
DR   ESTHER; ascsu-f1kpy0.3; Carboxypeptidase_S10.
DR   ESTHER; ascsu-f1kpy0.4; Carboxypeptidase_S10.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 4.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001563; Peptidase_S10.
DR   InterPro; IPR033124; Ser_caboxypep_his_AS.
DR   InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR   PANTHER; PTHR11802:SF480; CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 1.
DR   Pfam; PF00450; Peptidase_S10; 4.
DR   PRINTS; PR00724; CRBOXYPTASEC.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 4.
DR   PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 3.
DR   PROSITE; PS00131; CARBOXYPEPT_SER_SER; 3.
PE   2: Evidence at transcript level;
KW   Carboxypeptidase {ECO:0000256|RuleBase:RU361156};
KW   Hydrolase {ECO:0000256|RuleBase:RU361156};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|RuleBase:RU361156};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        1984..2003
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1900..1981
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1908..1981
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2012 AA;  225100 MW;  45C010B8A5BD87E1 CRC64;
     MTRRNSIHCR NAATYLVLHS NHSATVIFRS MLKSKREVAE WSKKTFSDPT KRNCAQLVQQ
     MSYDRVWNTI NDVYNTYQDC YMDTVTAASM RAMRQTDFRK RRSQKAIISD GKNPFIDQGS
     KMNMASTDAQ QAFPCWMDAA TQNYLNLPEV RTALHIPSSV PYWTVCSMMV NMFYTWQTFD
     TAPIFEEMFR SGHPLRILIY SGDLDTVCNF LGNEWFVDEL TARNNFTKTA WTQWDFAESE
     EFAPALAGYE QRYQSADRKI ALDFVTIKGA GHFAPLDRGG PSLQMIENFL QSKPYSNLTG
     LDLAKKPLLL QYQPPQPPLW SRKDADRVWS LPGITYNLNF KHYSGYLNPS KGNYLHYWLT
     ESQSNPSRDP LVLWLNGGPG CSSLLGLLTE LGPFWPNPDG QTLTENIYSW NRMANVLFLE
     SPRQVGYSYQ NMSENSDVTF SDEETARDNF LAIMDFLSAF PEYYNRSFYV AGESYAGVYI
     PTLVSLMIDM IQAGKAPGLN LAGVAIGNGK MADKYQLNSA ISLLYNRGLY GTDIMDSLSG
     CCPKNQPLHD CDFSQWVGFD DHGDAHPINS SQCGTLVAEY GRNALWAKSD IQDPYNMFQD
     CYLEKAAVVA STARELKQRI DRRAAPGFLD QLTKMNFAST DSQGAFQCYS SLGAEKWLQW
     DDVRAALHIA PEAPPYSECN SGVSSNYTKQ NGDTSPVFDH IVRSGYPLRM LVYSGDLDTV
     CNFIGVEWFI EALVSRFAMN QTIAWENWMY MQQIAGYYKR FQYQSTFTVD VLTVKGAGHM
     VPTDRPGPAL QMFHNFLLGI PYSTKVPFNL AHTPLKPEYQ NLLQIAASSP SITRSRMSRL
     LSEPNQIVPK QKKQRSAYRV GDPPTGSKVA DKITALPGAT FNITFNHYSG YLQASRGNYL
     HYWLVESQGN PSSDPLILWL NGGPGCSSLG GLLTELGPFR PNPDGTTLYE NQFAWNKVGN
     VLFIESPRDV GFSYRSDSVP ADTVYNDDKT AEDNVLALQS FFDRFPEYKG REFFVTGESY
     AGVYTPTLTD LLIKRIQDNT MNYVNLKGLA IGNGIISAVE QINSAPQLLY YRGILGKREL
     DRLKPCCLND DVYDNYCDLS QFITFDSAGN AHAKPSNDSV LNECGKLVED MAFMKIWESG
     NDVYNTYQDC YIANSKSSTK KRRQKRNAAS LGGIPLTNDY PFVDQASRVN HMSTDAFGTF
     RCYMDEATAN YLNIAEVQKA LHIQAGLPEW SDCNLEMNNN YQQQHNDTTS VFQSIITSKY
     PLRILIYNGD TDAACNFLGD EWFIEKLAKT NRMTSTSRTE WNYTHPGGYL SRVGGWVKTF
     NMQNITIDLL TVKGGGHFVP TDRPAPALQM IANFVKKTPY STTVAYDVNS KPLLPEYAPT
     SAPPVSRQEA NKIYDLPGVT FEVSFNQYSG YLHSSTPGNY LHYWFVESQG NPASDPVVLW
     LNGGPGCSSL GGLLTELGPF RPNPDGRTLY ENVYSWNKAA NMLFLETPRG VGFSYQDTAV
     NNDTTWDDAK TALESAAAVE DFFTVFEQFR GNDFYITGES YAGIYIPTLT DELIKRIQAG
     KLRINLVGIA IGNGAFSNIQ EVRSNPDFLY FHGIYGKDEW DQLLKCCTST NGSSSSVCEY
     ERYVQIDGFG NVVGINSTNA LHTECGRLVA QLAYDRVWNT ANDAYNLYQD CYRMSLTGAF
     IPDDRRLKSP EAIFDELRRT PRNIRAAYAS VMASVNMVST DATGGFQCFM KKAIVEYLSQ
     AHVRDAIHIP NYVPAYQKCS DTVGDHYTQL YNDSTPVFQS ILNSNYPLKM LIYNGDVDSV
     CSILEAQWFF EAFATSNQMN STTRVPWYYQ LSSEYFEEIG GYIKSFSKGS LKIDLLTVKG
     AGHYVPTDRP GPALQMFTNF IRNSSSYSIM APFDLTRKPL LPEYQPPQQG AETVTPGTSP
     VKPGTSPVTP GTSPVKPGTS PVTPWTSPVT PGTSPVTPGT SPVTTTGGLS TTSTTPTTGT
     TSKASLASIS MSLFIPFLLL LLFDEGRRSA QC
//