ID A0A094KTD0_ANTCR Unreviewed; 611 AA.
AC A0A094KTD0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 22-FEB-2023, entry version 27.
DE SubName: Full=Carboxypeptidase Z {ECO:0000313|EMBL:KFZ54222.1};
DE Flags: Fragment;
GN ORFNames=N321_10873 {ECO:0000313|EMBL:KFZ54222.1};
OS Antrostomus carolinensis (Chuck-will's-widow) (Caprimulgus carolinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Caprimulgiformes;
OC Caprimulgidae; Antrostomus.
OX NCBI_TaxID=279965 {ECO:0000313|EMBL:KFZ54222.1, ECO:0000313|Proteomes:UP000053620};
RN [1] {ECO:0000313|EMBL:KFZ54222.1, ECO:0000313|Proteomes:UP000053620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N321 {ECO:0000313|EMBL:KFZ54222.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00090}.
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DR EMBL; KL343227; KFZ54222.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094KTD0; -.
DR Proteomes; UP000053620; Unassembled WGS sequence.
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; cd07447; CRD_Carboxypeptidase_Z; 1.
DR CDD; cd03867; M14_CPZ; 1.
DR CDD; cd11308; Peptidase_M14NE-CP-C_like; 1.
DR Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR034239; M14_CPZ_CPD.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11532:SF63; CARBOXYPEPTIDASE Z; 1.
DR PANTHER; PTHR11532; PROTEASE M14 CARBOXYPEPTIDASE; 1.
DR Pfam; PF13620; CarboxypepD_reg; 1.
DR Pfam; PF01392; Fz; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00063; FRI; 1.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
DR SUPFAM; SSF63501; Frizzled cysteine-rich domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
DR PROSITE; PS50038; FZ; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:KFZ54222.1};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00090}; Hydrolase {ECO:0000313|EMBL:KFZ54222.1};
KW Protease {ECO:0000313|EMBL:KFZ54222.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053620}.
FT DOMAIN 1..120
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DISULFID 82..106
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFZ54222.1"
FT NON_TER 611
FT /evidence="ECO:0000313|EMBL:KFZ54222.1"
SQ SEQUENCE 611 AA; 69603 MW; 7069784A7E9D70C3 CRC64;
AKCVDIALSS CTDVAYTQTM YPNFLDQKSR EVIEYSSEYI LISVLHNLLQ GECNPDLRLL
GCSVLAPQCE KDKVIKPCRH VCENLKKNCL PAFDAIDMAW PYFLDCDRFF AGEEEGCFDP
LAKLRGEVDI EEDLPSDLPA TFIQFKHHSY SQMVSTLKKT ASKCSHIAKT YSIGRSFEGK
DLFVIEFSTK PGHHELLKPE FKYIGNMHGN EVVGKELLIY LAQYLCSEYL LGNPRIQTLI
NNTRIHLLPS LNPDGYELAA EEGAGYNGWV IGRQTAQNLD LNRNFPDLTS EAYRRAGIHG
ARLDHIPIPQ SYWWGKVAPE TKAVMKWLRS IPFVLSASLH GGELVVTYPY DYSRHPMEEK
MFSPTPDEKM FKMLAKAYAD AHPVISDRSE LRCGGNFVKR GGIINGAEWY SFTGGMADFN
YLHTNCFEVT VEVGCEKFPL EEELFTIWHE NRDALLNYME MVHRGIKGIV SDKFGNPIKN
ARISVRGIQH DITTAADGDY WRLLPPGTYV ISAQAAGYSR VMKRVTLPAK MKRAGRVDFV
LRPVETWPNK LLRRSMEDMY DPYDPLELFD PHAQHGQPEA RGGSPSGREK PWWWSYFSSL
DLHKPLWLLK Q
//
