ID A0A3Q1JNY7_ANATE Unreviewed; 636 AA.
AC A0A3Q1JNY7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Carboxypeptidase Z {ECO:0000313|Ensembl:ENSATEP00000032433.2};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000032433.2, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000032433.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 AlphaFoldDB; A0A3Q1JNY7; -.
DR STRING; 64144.ENSATEP00000032433; -.
DR Ensembl; ENSATET00000032908.2; ENSATEP00000032433.2; ENSATEG00000022334.2.
DR GeneTree; ENSGT00940000156391; -.
DR InParanoid; A0A3Q1JNY7; -.
DR Proteomes; UP000265040; Unplaced.
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; 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; 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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Reference proteome {ECO:0000313|Proteomes:UP000265040}.
FT DOMAIN 6..119
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
SQ SEQUENCE 636 AA; 72459 MW; 70E2C4EC78FB317E CRC64;
MQHVSSSAAA CQQDLWTFKH PIMYYYLLSK CKYHVLNHCS SRTIFPNILG HQNRLEAESG
AEYLLLSVIH GLLNGECSPE IRLVGCSVLA SPCKDNKMIK PCRSTCEAIE MAWPYFLDCD
RFFASDQEGC FDPLGGLKGN EIAMAGISPE EPSTIIQFTH TSNSQMYSIL RRTAAKCSHI
SHVYSIGRST EGRDLLVIEF TNNPGQHELL EPEIKLVGNM HGNEVLGRQL LIYLAQYLCS
EYILGNHRIQ SIINTTRIHI LASMNPDGYE VAASEVEDSD DPELSNPEGH LLNGWTNGRT
NAQNIDLNRN FPDLTTIYYR NRRSRHYRID HIPIPDSYWS EKVAPETYAV MKWTRSLPFV
QSASLHGGEL VVTYPFDFSR HPLEERMFSP TPDERIFKQL ARTYADAHAT MSNNDTERCG
AGFYRTRGIL NGAQWYSFAG GMPDFNYLHT NCLEITVELG CDKFPSEVEL YPEWKRNKEA
LLSFLESVHR GLKGKVTDPD GNGIKGATIS VKGMRKDITT AEDGDYWRLL NSGTHILTAT
AKGYSKVSKR VRLPANMNKA GRVDFVLKKV PVKPDIDDHL FPTIDTWDRF DPYNQFERNR
EPENEEMIEQ QEKPWWWAYF SQSGSVSPPQ WLLRNV
//
