ID A0A401NHN1_SCYTO Unreviewed; 513 AA.
AC A0A401NHN1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 03-MAY-2023, entry version 18.
DE RecName: Full=Peptidase M14 carboxypeptidase A domain-containing protein {ECO:0000259|PROSITE:PS00132, ECO:0000259|PROSITE:PS00133};
GN ORFNames=scyTo_0006862 {ECO:0000313|EMBL:GCB60386.1};
OS Scyliorhinus torazame (Cloudy catshark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Scyliorhinidae;
OC Scyliorhinus.
OX NCBI_TaxID=75743 {ECO:0000313|EMBL:GCB60386.1};
RN [1] {ECO:0000313|EMBL:GCB60386.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
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:GCB60386.1}.
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DR EMBL; BFAA01002392; GCB60386.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401NHN1; -.
DR STRING; 75743.A0A401NHN1; -.
DR OMA; HIERIVF; -.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd11308; Peptidase_M14NE-CP-C_like; 1.
DR Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11532:SF84; CARBOXYPEPTIDASE M; 1.
DR PANTHER; PTHR11532; PROTEASE M14 CARBOXYPEPTIDASE; 1.
DR Pfam; PF13620; CarboxypepD_reg; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
PE 3: Inferred from homology;
FT DOMAIN 150..172
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00132"
FT DOMAIN 268..278
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00133"
SQ SEQUENCE 513 AA; 58683 MW; 01D92B48E49F7E5A CRC64;
MENRKLDDLH YGFGRKTHDY VSFENEKYQN VQADKYCEMI ADFMVSKEST QVKESESIAA
INGPWENSQT SRWKMFRSIK LLWIWAILPD LIALKLQYHS TQELEGFLHA INRKYPSITH
LYYIGGSVAG IKLWVLAIGK YPKVHTVGIP DVKYIANIHG DEVVGREMLL QLIEHLVKMY
KHDATITRLI NNARIHIMPS MNPDGFEITQ HEERSCTYSI GRYNKERVDL NRNFPDAFEN
STSATQPETK AVMNWILSET FVLSISLHGG AVVASYPYDN KQTDKQPAGY SKCPDDDVFV
YLAKNYSYNH LSMFSGDECE RTPYFQDGIT NGAEWYHFSG GMQDFNYISG QCFELTVELS
CCKNPPEIYL MEYWNENQES LINFLKLVHL GIKGQVLTMD GAPIENAIVE VQGRENINPF
RTNKWGEYYR LLLPGTYILN VTVPGFGSNT TEFQVLNDVE NFSALVFNFH FNVNATDATS
SKHSIQQQHG TASSKQQNAV LLISIVIYSA LIY
//