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Database: UniProt
Entry: A0A401NHN1_SCYTO
LinkDB: A0A401NHN1_SCYTO
Original site: A0A401NHN1_SCYTO 
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
//
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