ID A0A9D3NAT7_9TELE Unreviewed; 477 AA.
AC A0A9D3NAT7;
DT 03-MAY-2023, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2023, sequence version 1.
DT 28-JAN-2026, entry version 12.
DE RecName: Full=Peptidase metallopeptidase domain-containing protein {ECO:0000259|SMART:SM00235};
GN ORFNames=KOW79_017518 {ECO:0000313|EMBL:KAG7319044.1};
OS Hemibagrus wyckioides.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Bagridae; Hemibagrus.
OX NCBI_TaxID=337641 {ECO:0000313|EMBL:KAG7319044.1, ECO:0000313|Proteomes:UP000824219};
RN [1] {ECO:0000313|EMBL:KAG7319044.1, ECO:0000313|Proteomes:UP000824219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC202008001 {ECO:0000313|EMBL:KAG7319044.1};
RC TISSUE=Blood {ECO:0000313|EMBL:KAG7319044.1};
RA Shao F.;
RT "Chromosome-level genome assembly of the red-tail catfish (Hemibagrus
RT wyckioides).";
RL Submitted (JUN-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PIRSR:PIRSR621190-2};
CC Note=Can bind about 5 Ca(2+) ions per subunit.
CC {ECO:0000256|PIRSR:PIRSR621190-2};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR621190-2};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR621190-
CC 2};
CC -!- SIMILARITY: Belongs to the peptidase M10A family.
CC {ECO:0000256|ARBA:ARBA00010370}.
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:KAG7319044.1}.
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DR EMBL; JAHKSW010000021; KAG7319044.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9D3NAT7; -.
DR OrthoDB; 406838at2759; -.
DR Proteomes; UP000824219; Linkage Group LG21.
DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030574; P:collagen catabolic process; IEA:TreeGrafter.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00094; HX; 1.
DR CDD; cd04278; ZnMc_MMP; 1.
DR FunFam; 2.110.10.10:FF:000008; Matrix metallopeptidase 19; 1.
DR FunFam; 2.110.10.10:FF:000021; Matrix metallopeptidase 19; 1.
DR FunFam; 3.40.390.10:FF:000091; Matrix metalloproteinase-16-like Protein; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.110.10.10; Hemopexin-like domain; 2.
DR InterPro; IPR000585; Hemopexin-like_dom.
DR InterPro; IPR036375; Hemopexin-like_dom_sf.
DR InterPro; IPR018487; Hemopexin-like_repeat.
DR InterPro; IPR018486; Hemopexin_CS.
DR InterPro; IPR033739; M10A_MMP.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001818; Pept_M10_metallopeptidase.
DR InterPro; IPR021190; Pept_M10A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR PANTHER; PTHR10201; MATRIX METALLOPROTEINASE; 1.
DR PANTHER; PTHR10201:SF166; MATRIX METALLOPROTEINASE-19; 1.
DR Pfam; PF00045; Hemopexin; 3.
DR Pfam; PF00413; Peptidase_M10; 1.
DR Pfam; PF01471; PG_binding_1; 1.
DR PIRSF; PIRSF001191; Peptidase_M10A_matrix; 1.
DR PRINTS; PR00138; MATRIXIN.
DR SMART; SM00120; HX; 4.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF50923; Hemopexin-like domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF47090; PGBD-like; 1.
DR PROSITE; PS00024; HEMOPEXIN; 1.
DR PROSITE; PS51642; HEMOPEXIN_2; 3.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR621190-2};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001191-2};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000824219};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR001191-2};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..477
FT /note="Peptidase metallopeptidase domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038953744"
FT DOMAIN 106..261
FT /note="Peptidase metallopeptidase"
FT /evidence="ECO:0000259|SMART:SM00235"
FT REPEAT 337..375
FT /note="Hemopexin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01011"
FT REPEAT 380..428
FT /note="Hemopexin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01011"
FT REPEAT 429..475
FT /note="Hemopexin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01011"
FT ACT_SITE 217
FT /evidence="ECO:0000256|PIRSR:PIRSR001191-1"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 125
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 175
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 176
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 195
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 198
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 198
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001191-2"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001191-2"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001191-2"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 297
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 299
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 343
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 386
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 433
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT MOD_RES 372
FT /note="Phosphotyrosine; by PKDCC"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-4"
SQ SEQUENCE 477 AA; 55221 MW; 96FFB460780D7F30 CRC64;
MKNLHLSVLL FTAFYVVSSS VLQNRMEFAE AMTYLRQFGY LDTPLDKETQ VDISEEAIRE
ALRLFQRVSG LPVTGKVDEP TVTKMRQPRC GVEDPFNQKT NKYRRFGGIW KKRNLTYRIY
NFTPDLGKVA TQRAIRLAFK YWSDVTPLSF KEIEYGRADI RISFHARTGC LSPFDGPGHV
LAHAEGPPSG IIHFDEDEFW TEGKYYGSNL RIVAAHEIGH ALGLGHSQYR DALMASYYSG
YKVNFRLHPD DIRGIQALYG KRIISTTTDE DIRAMGPTTI SPVPRVDIPD PCDAKLDAIM
LGPWRKTFAF SGDYMWTITD MGHNAPIKIK QLWNDLPGNL NAAVHSPRTN KTYFFKGDKV
WRYTNFRLDF GYPKQLTRIP ANIDAALYYE KNKKIFFFKG SGFWQWDEMM YNDLSIYPKP
ISRLFTGIPS NLDAAFTWTN GKVYFFKGDK YWRMNEQLIV ESGYPLSKRE RWMRCTH
//
