ID A0A401S884_CHIPU Unreviewed; 338 AA.
AC A0A401S884;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 03-MAY-2023, entry version 12.
DE RecName: Full=Peptidase M12B domain-containing protein {ECO:0000259|PROSITE:PS50215};
GN ORFNames=chiPu_0005027 {ECO:0000313|EMBL:GCC26609.1};
OS Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC Chiloscyllium.
OX NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC26609.1, ECO:0000313|Proteomes:UP000287033};
RN [1] {ECO:0000313|EMBL:GCC26609.1, ECO:0000313|Proteomes:UP000287033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(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:GCC26609.1}.
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DR EMBL; BEZZ01000131; GCC26609.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401S884; -.
DR STRING; 137246.A0A401S884; -.
DR OMA; REPYKIE; -.
DR Proteomes; UP000287033; Unassembled WGS sequence.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF19; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 19; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Reference proteome {ECO:0000313|Proteomes:UP000287033}.
FT DOMAIN 178..299
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
SQ SEQUENCE 338 AA; 39618 MW; C9F4C57E45FD04C1 CRC64;
MHNHIVKYET IVPQWLTSGP LEHPPSQNQH PAWAEIQVTA EGRHYILEIQ KNEQLMALGY
AETHYSPTGE QRTSYPDHKS HCLYHGNVKG FKHSSVVLST CRGLRGLIIL NMNLSYLVQP
LEDSLDHHLI YRTEHLKLKG GTCGHQESKR EENWVKDFTR QFHPEHHREK RDVVKDMKYV
ELYVVADYAE FQKHNWDLEK TKLKLKETVN YVDKYYRSLN IRIALVHLEV WTHENKCDVR
EDPYITLWSF LKWRRQTLTR KKHDNAQLIT GTSFNGTTIG FAPLMGMCSD YQSGGINMDF
PLKAVQKTLY SERMLTKNIL AIVSAVSEVT KQQRRLDY
//
