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Database: UniProt
Entry: A0A3L8SEG3_CHLGU
LinkDB: A0A3L8SEG3_CHLGU
Original site: A0A3L8SEG3_CHLGU 
ID   A0A3L8SEG3_CHLGU        Unreviewed;       599 AA.
AC   A0A3L8SEG3;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Peptidase M12B domain-containing protein {ECO:0000259|PROSITE:PS50215};
GN   ORFNames=DV515_00008769 {ECO:0000313|EMBL:RLW00362.1};
OS   Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC   Chloebia.
OX   NCBI_TaxID=44316 {ECO:0000313|EMBL:RLW00362.1, ECO:0000313|Proteomes:UP000276834};
RN   [1] {ECO:0000313|EMBL:RLW00362.1, ECO:0000313|Proteomes:UP000276834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Red01 {ECO:0000313|EMBL:RLW00362.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:RLW00362.1};
RX   PubMed=30282656;
RA   Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA   Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT   "A non-coding region near Follistatin controls head colour polymorphism in
RT   the Gouldian finch.";
RL   Proc. R. Soc. B 285:0-0(2018).
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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:RLW00362.1}.
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DR   EMBL; QUSF01000027; RLW00362.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3L8SEG3; -.
DR   STRING; 44316.ENSEGOP00005007797; -.
DR   Proteomes; UP000276834; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04273; ZnMc_ADAMTS_like; 1.
DR   Gene3D; 3.40.1620.60; -; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 1.
DR   InterPro; IPR041645; ADAMTS_CR_2.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR000884; TSP1_rpt.
DR   InterPro; IPR036383; TSP1_rpt_sf.
DR   PANTHER; PTHR13723:SF20; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 13; 1.
DR   PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR   Pfam; PF17771; ADAMTS_CR_2; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   Pfam; PF00090; TSP_1; 1.
DR   SMART; SM00209; TSP1; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   SUPFAM; SSF82895; TSP-1 type 1 repeat; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS50092; TSP1; 1.
PE   4: Predicted;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00023049};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000276834};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..599
FT                   /note="Peptidase M12B domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018163304"
FT   DOMAIN          202..407
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
FT   ACT_SITE        347
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         346
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         350
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         356
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ   SEQUENCE   599 AA;  65077 MW;  8216ABE94E08A14F CRC64;
     MSLSWALRAL AVLPLGLCWL PEKFLGALDG EDVMAYFGTS SAPDVPEFVV AEPACPCKEE
     HFGLRPCQVQ HCSIQAWGQL YAFEFLEDHA LLSSSFVSSQ VVNSSFILLK RFPGSCFAGG
     KALQPPGARS RVTFCEGQLQ GVVTVGEEKV HIRPVRSKDV ALLKDLGFSS PHILFKSAAR
     EAKPARGWAP PRLHKRAEAA VKHLELMVVA GPDVYLYHRE DTERYILANL NIGAELLRDA
     SLGAHFRVHL MQMLVLREPE AEVNITTNIT SSLISVCEWS KKVNPQNDSD PQHADIVLYI
     TRFDLELPDG NKELRGVTQL GGVCSSFWSC VITQDTGFDL GVTIAHEIGH SLGIAHDGEG
     NVCSSSGYIM GSAGNHNSID LTWSLCSREQ FQALVSTGQT SCLNDLPAMD GSIPGWKPGL
     YYGADEQCKI AFGSVATACT FADTNVDICK VLSCHVQPAD KSSCTRLLVP LLDGTECGLN
     KWCSKGQCSS LEELNPLAVV HGHWSAWSPL SPCSRSCGGG VVLRQRFCNN PRPAFGGQEC
     HGVSLQAEMC NTQACLMTQQ DFMAEQCAAT NLKPLYLDAE TPSFYTWTSA VGFAKGIRV
//
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