ID C3YY10_BRAFL Unreviewed; 1620 AA.
AC C3YY10;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 72.
DE RecName: Full=Peptidase M14 carboxypeptidase A domain-containing protein {ECO:0000259|PROSITE:PS00132, ECO:0000259|PROSITE:PS00133};
GN ORFNames=BRAFLDRAFT_79888 {ECO:0000313|EMBL:EEN54969.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN54969.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN54969.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN54969.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
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DR EMBL; GG666563; EEN54969.1; -; Genomic_DNA.
DR RefSeq; XP_002598957.1; XM_002598911.1.
DR STRING; 7739.C3YY10; -.
DR MEROPS; M14.016; -.
DR eggNOG; KOG2649; Eukaryota.
DR InParanoid; C3YY10; -.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR CDD; cd03868; M14_CPD_I; 1.
DR CDD; cd11308; Peptidase_M14NE-CP-C_like; 3.
DR Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 4.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 4.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR000834; Peptidase_M14.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR PANTHER; PTHR11532:SF57; PEPTIDASE_M14 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR11532; PROTEASE M14 CARBOXYPEPTIDASE; 1.
DR Pfam; PF13620; CarboxypepD_reg; 4.
DR Pfam; PF00246; Peptidase_M14; 5.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 3.
DR SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 4.
DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 4.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 2.
DR PROSITE; PS00133; CARBOXYPEPT_ZN_2; 2.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1620
FT /note="Peptidase M14 carboxypeptidase A domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002935760"
FT TRANSMEM 1541..1562
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 86..108
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00132"
FT DOMAIN 205..215
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00133"
FT DOMAIN 537..547
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00133"
FT DOMAIN 1252..1274
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00132"
SQ SEQUENCE 1620 AA; 180552 MW; E19A7399AACE1A80 CRC64;
MLKLWAVLCV VVCFPATVNL AGFVGARQID TTHYHGYVEM SALLQDYANR YPHITQLSSI
GQTVEGREMW VLRVTDNPDQ TEAGEPAVKL VGNMHGNEAI SREVLIFLTQ YLCENYRHDD
QVTQLVDTTD IYVMPSMNPD GFENAREGQC GGTLGRENAN GVDLNRDFPD QFSSQDYQDS
QFEPETVHMM KWVMENKFVL SGNFHGGDLV ASYPFDDSAR HGNGIYSRAP DDDVFKHLAH
VYANNHLTMH NNKGCDRWEH FKDGITNGAK WYDVPGGMQD FNYLYSNCFE ITLELSCCKY
PTADHLSEEW DNNRPALLAY LTQVHQGVQG FVVRSDSGQG MEDATITVQG IDHNVTTAGH
GDFWRLLVPG TYTITASKQG YVSETFTDVT VDADQATELN FTLHAVGGQK TPPLSTPHPT
QDTPHPDHIK HHDYVEMKNF LTKLIELLCE NYGKVDDLTR LVNTTRIHIL PSMNPDGYER
AQEGDVRGIT GRTNAHGLDL NRNFPDQYFG EEELEPETMA VMEWAKRVPF VLSASLHGGN
LVADYPFDDS RKKGHAVYSK SPDDAVFQQL ARTYSLAHPT MHSGHPCDDI KPDEYFQDGI
TNGGAWYNVP GVMQDWDYVN TNDFEVAIEL GCVKFPYGED LPEYWQANKE ALVEYIKQVH
KGVKGFVVTN DGSGIPDASI TVHGINHTVT SAAGGDYWRL LVPGTYQVTA AAQGFQSVTQ
ELTVGDGDAT WLNFTLQSWN EENDYGLPNE PSYITNEDLV KTVKKYTEEH EGIIRIEETS
DNNVVDVEIF GKLARRKRDD DDVTRVQPHV ALIGGLNGDE PIGREILTRL IRHLVEGYDR
DDRIKSLVDN THIHVLAAVD LSAFNQAVEG DCAGENYIGT RIGDRFTLDS HAQVRREHYT
GTRIGDGFTL DSHAQVRGEH YTGTRIADGF TLDSHAQVRG EHYTGTRIGD GFTLDSHAQV
RGEHYTGTRI GDGFTLDSHA QVRGEHYTGT RIGDGFTLDS HAQVRGEHYT GTRIGDGFTL
DSHAQVRREH YTGTRIGDGF TLDSHAQFPQ IATVKQWFEK HQFDLALSLE AGGLVVRYPL
DYPREGLLVA DGATTQDDLL FKEIAREYAD SNPALGAGVH AVVRDQEGNP VSGAWMFTEG
DPRNVSVDPE KGTFKMLPSG QHRLRVEALG FSSETKQVDV KDGQTEELDF VMVREETLSY
HGYEDMQQML TDLAKEYPKI TKFYSIGETV NFRRLWVLEI SKTPGTHRPG QPEVKFVGNL
HGNEVVGREL LLAFIDHLCS SYGYDDDVTK LIDTTRIHIL PSLNPDGATC STEGTCEGDT
CRGNSNNVDL NTNFPSGGKN VSSAPLQPET QAIMGWMADH PFVLSVSLFA GHLVATYPYD
RPSKLGEAFP DGITNGAKMD SHQGSMQDYN YNAQSCMEIA VWVSCCKYPF SSELDQLWRD
NRESLMDMLR QVHTGVKGFV RTKDGTAVPG ASITVGGRGS VVVTATDGDY WRLLAPGEYV
IRADMEGYEQ GERKVIVTEG DAKEVDFVLS KKYQIFGMSP IIIIIATAVS MAAIVCTAVV
ICRMCRTPAY SYSKLGTSEY GDSILMNRLK KDASQKSLLK DNEYHDDLSG SEDDTIYWKR
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