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Database: UniProt
Entry: A0A3B4BG55_9GOBI
LinkDB: A0A3B4BG55_9GOBI
Original site: A0A3B4BG55_9GOBI 
ID   A0A3B4BG55_9GOBI        Unreviewed;       635 AA.
AC   A0A3B4BG55;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=FZ domain-containing protein {ECO:0000259|PROSITE:PS50038};
OS   Periophthalmus magnuspinnatus.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX   NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000027816.1, ECO:0000313|Proteomes:UP000261520};
RN   [1] {ECO:0000313|Ensembl:ENSPMGP00000027816.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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; A0A3B4BG55; -.
DR   STRING; 409849.ENSPMGP00000027816; -.
DR   Ensembl; ENSPMGT00000029626.1; ENSPMGP00000027816.1; ENSPMGG00000022437.1.
DR   Proteomes; UP000261520; 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; PS00133; CARBOXYPEPT_ZN_2; 1.
DR   PROSITE; PS50038; FZ; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00090}.
FT   DOMAIN          20..142
FT                   /note="FZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50038"
FT   REGION          563..585
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        104..128
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ   SEQUENCE   635 AA;  72086 MW;  544A1008C80C7214 CRC64;
     RILVKIVHFW TSKSPATLNF HHSKCTDVLL SYCDDMSYTK TMFPNLLGHK TRHDAESGAE
     YLLMSVVESL LGGECNPEIR MLGCSVVAPR CDGGNVLKPC RSTCEAVRSR CTPAFDDIRM
     AWPYFLDCDR YFTSEEEGCY NPLEGLREPH YDPGRNLSTK MQFSYQSYTQ MNNILKRTEE
     RCPDIAKTYS IGQSTEGREL LVIEFSNNPG RHELLEPEVK YVGNIHGDEA TGRQLLIYLA
     QSLCSEYLQG NQRVQALVNS TRIHILPSLN PDGYEAAAGR QDSRYDDDEV ASENWNVGRT
     NAQNVDLNRN FPDLTSIAYR RRRNKRYRTD HIPIPDFYWF GKVAPETYAV MKWVRSIPFV
     LSASFHSGDL VVSYPYDLSK HPLEVNMLSP TPDDKVFKFI SKIYATSHES MSNENAQCGS
     SRSGSKAGTI NGAQWSRMQD FNYLHTNCFE VKVSLGCDKF PPEEELFNVW HENAEALLAF
     VEAAHRGIKG TVTDEEGNAV KGARISVRGI RHDVTTAEDG DYWRLLTPGI HIVSAHAPGF
     ARSLKKVHLP PNMHTAGRVD FTLQRSGPET SAPEDDDSLP SMGTYERFDP YNQYQRYTSR
     PAEAAQAREE RVDKPWWWSY FTMPGGPPPT WLLKL
//
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