ID A0A2A4IYQ3_HELVI Unreviewed; 2001 AA.
AC A0A2A4IYQ3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Peptidase M12B domain-containing protein {ECO:0000259|PROSITE:PS50215};
GN ORFNames=B5V51_10899 {ECO:0000313|EMBL:PCG64292.1};
OS Heliothis virescens (Tobacco budworm moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC Noctuidae; Heliothinae; Heliothis.
OX NCBI_TaxID=7102 {ECO:0000313|EMBL:PCG64292.1, ECO:0000313|Proteomes:UP000218220};
RN [1] {ECO:0000313|EMBL:PCG64292.1, ECO:0000313|Proteomes:UP000218220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HvINT- {ECO:0000313|EMBL:PCG64292.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:PCG64292.1};
RA Fritz M.L., Deyonke A.M., Papanicolaou A., Micinski S., Westbrook J.,
RA Gould F.;
RT "Contemporary evolution of a Lepidopteran species, Heliothis virescens, in
RT response to modern agricultural practices.";
RL Submitted (SEP-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:PCG64292.1}.
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DR EMBL; NWSH01005320; PCG64292.1; -; Genomic_DNA.
DR STRING; 7102.A0A2A4IYQ3; -.
DR Proteomes; UP000218220; 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:UP000218220};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT DOMAIN 233..450
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT ACT_SITE 390
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 389
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 393
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 399
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 2001 AA; 219382 MW; 25381E02496057BF CRC64;
MDVMTDHSKQ LLEHLTESEK IFLFGANPNE AQFEVAHLKQ PKRRKRSLLY DDQDLVGLKK
HLDIKLRPRN SFLDPQFLLM RRWSNSTEAV LDQHNDEEVD ACYYRSDNAA LYVCDDVRGL
VKSNDTYYFI HPLPERFHDD HAKAHVIVKK QIDKTDNEDQ TCLERENLIT NEPEPVNTWK
KHRRKREIPS SHVNNNLEGF KVNLAHRNKT ISDFIQKLSV GSNRQRRAIL PAVFVETAVF
VDRDLYKHMT INFPKDTERE LVRFVLAMIN AVQLIYHDPS LGRPVNFILK RLEILHEDPA
NLKRPHDIDR FLSNFCTWQR LENPPGDNDP LHWDHALILT GLDLYVVNKN GKVSSQVVGL
APVAGMCTVT SSCTVNEGRH FESVYVVAHE IGHNLGMRHD GPLADNGCDP SAYIMSPTLG
SGKITWSQCS KNYLQKFLDT VQSRCLLDHG NSAGQLDHSA EGILPGERFD ADQQCMLKYG
RGSRHSGAQS LEDICRDLHC QRERYTWTSH PALEGTRCGE DMYCRGGECV EREGSTVIRG
SWGRWSGWSE CASACLVDDT HAPAAAGVAV ATRRCNRPRH DNGKNYCVGH DKKFQSCHAQ
QCSNVPRMTV REFADQICLR ARDVDPDLIG TGLQRIDSDD VSSACAVWCD TRGGGYKSRG
WSLPDGTACS TAAPMFCISG VCQVTHNVYT KVWCDTRGGG YKSRGWSLPD GTACSTAAPM
FCISGVCQVT HNVYTKVWCD TRGGGYKSRG WSLPDGTACS TAAPMFCISG VCQVTHNVYT
KVWCDTRGGG YKSRGWSLPD GTACSTAAPM FCISGVCQVT HNVYTKVWCD TRGGGYKSRG
WSLPDGTACS TAAPMFCISG VCQVTHNVYT KVWCDTRGGG YKSRGWSLPD GTACSTAAPM
FCISGVCQVT HNVYTKVWCD TRGGGYKSRG WSLPDGTACS TAAPMFCISG VCQVTHNVYT
KVWCDTRGGG YKSRGWSLPD GTACSTAAPM FCISGVCQVT HNVYTKVWCD TRGGGYKSRG
WSLPDGTACS TAAPMFCISG VCQVTHNVYT KVWCDTRGGG YKSRGWSLPD GTACSTAAPM
FCISGVCQVT HNVYTKVWCD TRGGGYKSRG WSLPDGTACS TAAPMFCISG VCQVTHNVYT
KVWCDTRGGG YKSRGWSLPD GTACSTAAPM FCISGVCQVT HNVYTKVWCD TRGGGYKSRG
WSLPDGTACS TAAPMFCISG VCQVTHNVYT KVWCDTRGGG YKSRGWSLPD GTACSTAAPM
FCISGVCQVT HNVYTKVWCD TRGGGYKSRG WSLPDGTACS TAAPMFCISG VCQVTHNVYT
KVWCDTRGGG YKSRGWSLPD GTACSTAAPM FCISGVCQVT HNVYTKVWCD TRGGGYKSRG
WSLPDGTACS TAAPMFCISG VCQVTHNVYT KVWCDTRGGG YKSRGWSLPD GTACSTAAPM
FCISGVCQVT HNVYTKVWCD TRGGGYKSRG WSLPDGTACS TAAPMFCISG VCQVTHNVYT
KVWCDTRGGG YKSRGWSLPD GTACSTAAPM FCISGVCQVT HNVYTKVWCD TRGGGYKSRG
WSLPDGTACS TAAPMFCISG VCQVTHNVYT KVWCDTRGGG YKSRGWSLPD GTACSTAAPM
FCISGVCQVT HNVYTKVWCD TRGGGYKSRG WSLPDGTACS TAAPMFCISG VCQVTHNVYT
KVWCDTRGGG YKSRGWSLPD GTACSTAAPM FCISGVCQKF TCSSNPDTEF SLKPSECEWE
ALRTATHSPP TKSSGTWRRA VGSQWTAASG CHYHCVSGGA GLRLVRARRA TTIQLCEPLA
SDTGCTQKKS PYQYATMVCT KYKDRVRRLS GLGMQISPAL EDPDRPCRIA CQDERVSHRF
YLVNGQEGWF PLGTSCGKRN SSYCVSGKCL EFGPDHTPLS EMVFTLPLLS RASNSTSRVT
WHTRSSRHRR SLRTDRITVK ATLDQAHLDD IIARLNLTHN LNDHITYFDS IPEHIEVDFN
NPIHIAPEDT LLRKPPRPTW D
//
