ID A0A2J7R4U0_9NEOP Unreviewed; 1113 AA.
AC A0A2J7R4U0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Peptidase M12B domain-containing protein {ECO:0000259|PROSITE:PS50215};
GN ORFNames=B7P43_G09399 {ECO:0000313|EMBL:PNF35841.1};
OS Cryptotermes secundus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Termitoidae;
OC Kalotermitidae; Cryptotermitinae; Cryptotermes.
OX NCBI_TaxID=105785 {ECO:0000313|EMBL:PNF35841.1, ECO:0000313|Proteomes:UP000235965};
RN [1] {ECO:0000313|EMBL:PNF35841.1, ECO:0000313|Proteomes:UP000235965}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole body {ECO:0000313|EMBL:PNF35841.1};
RA Harrison M.C., Jongepier E., Robertson H.M., Arning N., Bitard-Feildel T.,
RA Chao H., Childers C.P., Dinh H., Doddapaneni H., Dugan S., Gowin J.,
RA Greiner C., Han Y., Hu H., Hughes D.S.T., Huylmans A.-K., Kemena C.,
RA Kremer L.P.M., Lee S.L., Lopez-Ezquerra A., Mallet L., Monroy-Kuhn J.M.,
RA Moser A., Murali S.C., Muzny D.M., Otani S., Piulachs M.-D., Poelchau M.,
RA Qu J., Schaub F., Wada-Katsumata A., Worley K.C., Xie Q., Ylla G.,
RA Poulsen M., Gibbs R.A., Schal C., Richards S., Belles X., Korb J.,
RA Bornberg-Bauer E.;
RT "Hemimetabolous genomes reveal molecular basis of termite eusociality.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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:PNF35841.1}.
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DR EMBL; NEVH01007402; PNF35841.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J7R4U0; -.
DR STRING; 105785.A0A2J7R4U0; -.
DR InParanoid; A0A2J7R4U0; -.
DR OrthoDB; 3042901at2759; -.
DR Proteomes; UP000235965; 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; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR PANTHER; PTHR13723:SF275; STALL, ISOFORM C; 1.
DR Pfam; PF17771; ADAMTS_CR_2; 1.
DR Pfam; PF01421; Reprolysin; 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:UP000235965};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..1113
FT /note="Peptidase M12B domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014370161"
FT DOMAIN 348..565
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT REGION 183..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 505
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 504
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 508
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 514
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 1113 AA; 124417 MW; 87B2CC7FC568F41C CRC64;
MVFRLLWVCF FLGASRAATT AAHRQEVNEA NLRDLLTAAE WTSLLGTSAT APEFAVVRPR
LPSKRGKRWA LPDETSVMPV VFEAQSLGRR FELQFRPSPA LLDPQFVLLR RWSNHTEMLS
PHLAEQSCFY RSDVGHRAAV ALCGGMRGII SSPNNEYYII NPLPRRFRRS SASIPHVVVR
WTPPSLTTDS KTPSCASHHP QDTNKQIPDE NSRTNSPDRD HRLQSNAPIS AVDNSRTLNW
SNNNNSKNSS TEHVYDLHIS DKVELKKTEA LTSKQDMSEE STKRSHKPSS GVLKTILLSS
AESKTKLGYG ALNAIEDVKK SSNCSEEEHS EVLRRKKRSA VLVPGTPIHV ETAVFIDKDL
YQHMALNFPT DTERELVRVV LAMINAVQLL YHDPSLGRQV NFVLKRLEIL HVDPVSLQRP
HDIDRFLSSF CTWQRGENPP ADSDPLHWDH ALILTGLDLY VVSKNGKVSS QVVGLAPVAG
MCTATSSCTV NEGRHFESVY VVAHEIGHNL GMRHDGPSAE NECDPGSYIM SPTLGSGKIT
WSSCSRRYLQ MFLETPQSQC LLDHSSSGGQ LDHSAEGALP GERFNADQQC MLKYGHGSIH
AIQQPLDDVC RDLHCQRDRY TWTSHPALEG TFCGNNKWCR SGRCVGRGLS ALQAGFSPNQ
RVDGAWSEWS PFSECASGCL YSEEGRLHAG STGIMVSTRR CNNPRPENDG LPCKGSDHRY
RTCLAEQCGN VQRTTIKDFA DQICIRAREV DKELLGTGLQ KPSSDPGEAC TVWCYKRSGG
SKSRGWTFPD GTTCQSHRSQ YRKSMYCISG RCEEFVCDRY DAATFSTLPE LCHGSSNGGG
GRLQVHDSSL FFRNKGQRRE VPETRIQWSP ASGCHFNCLA PGRGLRLVVA KDMKCQLEDN
CEGGRITSIQ LCEPDKQGCG RLKTPFEHAT TVCSKYRERV RRLSGFGMQI SPVAQDPDRP
CHVACQDDEV NHRFYLVNGE DGWFPFGTDC SRGVPEKRAY CISGKCLEFG SDDTPLHESE
YTLPLLSRMK RSLINNSTKV QTRLDQTMLN NIISRLNFRE NFYQELSSHS NQYSIDLSNP
IHIEVQTGVQ DLVNVVLNNK GNDEIWRSTR TLG
//
