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
//