ID A0A1I8PMI4_STOCA Unreviewed; 1410 AA.
AC A0A1I8PMI4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Peptidase M12B domain-containing protein {ECO:0000259|PROSITE:PS50215};
GN Name=106087759 {ECO:0000313|EnsemblMetazoa:SCAU009446-PB};
OS Stomoxys calcitrans (Stable fly) (Conops calcitrans).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC Muscidae; Stomoxys.
OX NCBI_TaxID=35570 {ECO:0000313|EnsemblMetazoa:SCAU009446-PB, ECO:0000313|Proteomes:UP000095300};
RN [1] {ECO:0000313|EnsemblMetazoa:SCAU009446-PB}
RP IDENTIFICATION.
RC STRAIN=USDA {ECO:0000313|EnsemblMetazoa:SCAU009446-PB};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR RefSeq; XP_013108364.1; XM_013252910.1.
DR RefSeq; XP_013108365.1; XM_013252911.1.
DR STRING; 35570.A0A1I8PMI4; -.
DR EnsemblMetazoa; SCAU009446-RA; SCAU009446-PA; SCAU009446.
DR EnsemblMetazoa; SCAU009446-RB; SCAU009446-PB; SCAU009446.
DR KEGG; scac:106087759; -.
DR VEuPathDB; VectorBase:SCAU009446; -.
DR OrthoDB; 3042901at2759; -.
DR Proteomes; UP000095300; Unassembled WGS sequence.
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 InterPro; IPR041645; ADAMTS_CR_2.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR000884; TSP1_rpt.
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 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}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1410
FT /note="Peptidase M12B domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014271791"
FT DOMAIN 526..740
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT REGION 69..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1044..1089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..493
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1044..1072
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 682
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 681
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 685
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 691
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 1410 AA; 159839 MW; F8484474A3CA214C CRC64;
MCSTGGFVLF LLIALFYNCF TNAESLTPHT TIHTNVANAG NPVGSKHLNN PSLGGHGNAI
AQEVVADGNV HDDDGEGDDH NNNDDDDVGD FQHRLWHASP TPTPADANDG KTTAGADHHH
IIDITRKHQI HYNGHVIDED NIIEHLEEHE RQLIFGKSRK KRSIKLVHLT YRPVVEQSNN
AATTYPTDVN SYENEAYQKP QKEEEEEEME LQIPNNNLEA VTAAIVHRTK RSDNDAAAAA
ASTTTATHQQ PSKNGQGGGA PAIPPTVSVQ IKDNDHLVNL KLQQTPKLID DAFVFIRRSA
NTSQLVENSH KLAERLEKCF YHNENSALDL CDDENVRGVY HHNQTDYIIH PLPERFGNNT
HIILESEGEI YDSRWSNSSV LGENIQFEPE MEDFNDLNIE SMGDYENTTR STRNIEMDAH
HQRHTAEHRR KSHHNHAMPL NLRYRPRHHH MSEARQDKAN HPHQYARNNH HSQKRHSQTT
LHKKHHSHPQ PNYRHHSHSS ESQRASKRTR RFISPLKDWR SANDVLYIET AIFVDTDLYT
HMAQNFPKDT SSHLIRFVLA MINGVQLLYH HPSLGRRVNF VLKRLEILEK DPSDLARSSD
IDVYLSNFCK WQTRWNTAKD LKLHYDHAVI LTGLDLYVVD KNGKMISQVV GLAPVAGMCI
ETSSCTINEG KHFESVFVVA HEIGHNLGMR HDSIENGCEP TSHIMSPTLG SGKITWSKCS
RDSLNVFLDK SQAKCLFNRA EFNQNLDHSA EGMLPGERFD ANQQCMLKYG KESARARSQS
LADICRDLHC QRDRYTWTSH PALEGTACGD NMWCRSGFCV VKRIELYTAT KQSASLSKPN
YDKSNYMENA KSSNLVHEYQ KTSSSWSEWS EPSPCDSSCL YGPSKRLREG STGLKTFSRK
CIDYKRRCMG RDHKFETCVA KQCYSVPIVT IADFAKQVCE RAQKFDGDLT GEGEQVSGNI
EESCKVYCKT KSNGTKSRSW TFPDGTTCRT HLYGDNDPSY CIQGRCEKFS CDNSTANYYK
IDNIFCKQQE KKFDNNAMDN ETIRRSSTGA SSSSSASSAY THQSYSNQIP MGPPTTQAPP
PPPLAYNNYN EYKYRTSNSN QNYYDNGSSD RIYGPTTVRS KYENEVAAKS FRGQQYPHDA
VPYKRKSDNY SPWNKYSYRL NDHTPSENAV AKTSTTLSGA IPPAAGDNEW IVKSGCYSNC
MARSKGIQVV MNRKSGEKNL QLCTHSIKPC DRLQTTGEYA DHLCSRYKLK VQGLSGHGTQ
IAASVEDPDR SCRVGCQDEF IQHRFFLVNG NYGHFPLGTR CSAGDDRFCV QGKCLEFGPD
QIPLQESHIS LALFRSRRSA RKHRHRRTKR SFLYYDPVNI TETLTQDFID NIVDSIITLD
GQTTTEDPLV GHHIEFTNPI HYSMDEMHEH
//