ID A0A232FIZ3_9HYME Unreviewed; 1100 AA.
AC A0A232FIZ3;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Peptidase M12B domain-containing protein {ECO:0000259|PROSITE:PS50215};
GN ORFNames=TSAR_006334 {ECO:0000313|EMBL:OXU30714.1};
OS Trichomalopsis sarcophagae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Proctotrupomorpha;
OC Chalcidoidea; Pteromalidae; Pteromalinae; Trichomalopsis.
OX NCBI_TaxID=543379 {ECO:0000313|EMBL:OXU30714.1, ECO:0000313|Proteomes:UP000215335};
RN [1] {ECO:0000313|EMBL:OXU30714.1, ECO:0000313|Proteomes:UP000215335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Alberta {ECO:0000313|EMBL:OXU30714.1,
RC ECO:0000313|Proteomes:UP000215335};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXU30714.1};
RX PubMed=28648823; DOI=10.1016/j.cub.2017.05.032;
RA Martinson E.O., Mrinalini, Kelkar Y.D., Chang C.H., Werren J.H.;
RT "The Evolution of Venom by Co-option of Single-Copy Genes.";
RL Curr. Biol. 27:2007-2013(2017).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR613273-2};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR613273-2};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
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:OXU30714.1}.
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DR EMBL; NNAY01000128; OXU30714.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A232FIZ3; -.
DR STRING; 543379.A0A232FIZ3; -.
DR Proteomes; UP000215335; 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:0030198; P:extracellular matrix organization; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04273; ZnMc_ADAMTS_like; 1.
DR Gene3D; 2.60.120.830; -; 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; 2.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR041645; ADAMTS_CR_2.
DR InterPro; IPR045371; ADAMTS_CR_3.
DR InterPro; IPR010294; ADAMTS_spacer1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723:SF200; ADAM METALLOPEPTIDASE WITH THROMBOSPONDIN TYPE 1 MOTIF B, ISOFORM B; 1.
DR PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR Pfam; PF17771; ADAMTS_CR_2; 1.
DR Pfam; PF19236; ADAMTS_CR_3; 1.
DR Pfam; PF05986; ADAMTS_spacer1; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 1.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 3.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 2.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50092; TSP1; 3.
PE 4: Predicted;
KW Calcium {ECO:0000256|PIRSR:PIRSR613273-2};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR613273-3};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR613273-2};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000215335};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR613273-2}.
FT DOMAIN 282..494
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT REGION 253..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 998..1038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 430
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 285
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 285
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 378
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 429
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 433
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 439
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 489
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 389..395
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 407..489
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 447..473
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 518..542
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 528..549
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 537..568
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 562..573
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 596..633
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 600..638
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 611..623
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1100 AA; 123682 MW; 7BBE941B7A3EB9E1 CRC64;
MAPKKNRKIL FTLYTKNYIM YNEKYTIEKV YVIFYLFAAE TLLVIGDKLD DYQRNPNDIY
NGRYTRDIKD AELLIPRHVQ ENGALHTYQL AKFYQREKLE KERRRRENTL LHLVLPFNGA
DNHVELKPYH DFISPDMVVE TRSLDSEASR FNESNLHFKW PSDNQCHYRG ALRGHANSRA
TLSLCEGVVG YVNTDHGRYY IEPLDGDLPD DDGQHIHLIY KKEISHENMP HTNKAPFCGV
NDDWESAWSE QLARRQRNEA ESSNSVPINE KRASSSTHSI HRYIEVALVA DRRFLDFHKG
TNYEQYLLTV MNMVSDYYHD ASVGNQIDVV VVRIIYLEKE KNEIDLQISP DAEKTLESFA
KWIEKLNPTD TEHPNHFDIG ALVTRHDICA EGNNCNLLGL AFVAAACERK KAACINEDSG
LLLGIVIAHE IGHTLGCSHD TEEISGCPST DKDESYFVMS PIVFIYTIRW SPCSKKFITS
FLESGLGECL INNPKNPPDK YKFPNMLPGA MYDADFQCKL NYPGSTPCES DPDEDLCEEL
WCNVGGDNCK SKGAPPADGT KCAENKWCIH KKCVEMGSRG DVVNGEWGNW GKLGECSRTC
GGGIKFAERE CNNPAPKNGG RYCIGERKKF DTCNTKPCDS SKPSFRAVQC TEYDKKTDVT
GGPHKWQPFS RADLDACALY CINEKRSFTK LSPTSKDGTP CKTGTYNMCI SGVCRKVGCD
WLIDSDAVED VCGVCKGGGD KCTKIEGDYT EKAKNSGYSR IVVVPKGSRN IRAYEMREHD
NTLAVKLAKK NSYCLNGNLV EEKSGDYPCA GSSINYKHVK PNLEEMEIRG PITEDIEIQY
VFYAANNPGV HYEYYVDSPN KSHKPKYSWE YLEWSDCDAK CGGGTKISEA SCVEEKAGKV
TAEFCNGIKQ PPPKSQTCNE APCYPKWRVS QWSRCSSCGG KVGEMRRKIQ CVRPGPHVGD
DYVQTNFEAC PAKPPTQTKV CYGTEPCRKP CPPKNVRNTY ALSPSQQASN KDNEMENSDC
LENDGTGSDF TTPMPGSIVV DSATENIDSR VPAANFYHRS RNVDCNLRCM QKKKDSRRRA
FLSPVKANAA RLAGSAESAE
//
