ID A0A1P6BZ30_BRUMA Unreviewed; 2186 AA.
AC A0A1P6BZ30;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=BMA-GON-1, isoform e {ECO:0000313|EMBL:CDP93015.1};
DE SubName: Full=Peptidase M12B domain-containing protein {ECO:0000313|WBParaSite:Bm3594b.1};
GN Name=Bma-gon-1 {ECO:0000313|EMBL:CDP93015.1,
GN ECO:0000313|WBParaSite:Bm3594b.1};
GN ORFNames=BM_Bm3594 {ECO:0000313|EMBL:CDP93015.1};
OS Brugia malayi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=6279 {ECO:0000313|Proteomes:UP000006672, ECO:0000313|WBParaSite:Bm3594b.1};
RN [1] {ECO:0000313|EMBL:CDP93015.1, ECO:0000313|Proteomes:UP000006672}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FR3 {ECO:0000313|EMBL:CDP93015.1,
RC ECO:0000313|Proteomes:UP000006672};
RX PubMed=17885136; DOI=10.1126/science.1145406;
RA Ghedin E., Wang S., Spiro D., Caler E., Zhao Q., Crabtree J., Allen J.E.,
RA Delcher A.L., Guiliano D.B., Miranda-Saavedra D., Angiuoli S.V., Creasy T.,
RA Amedeo P., Haas B., El-Sayed N.M., Wortman J.R., Feldblyum T., Tallon L.,
RA Schatz M., Shumway M., Koo H., Salzberg S.L., Schobel S., Pertea M.,
RA Pop M., White O., Barton G.J., Carlow C.K., Crawford M.J., Daub J.,
RA Dimmic M.W., Estes C.F., Foster J.M., Ganatra M., Gregory W.F.,
RA Johnson N.M., Jin J., Komuniecki R., Korf I., Kumar S., Laney S., Li B.W.,
RA Li W., Lindblom T.H., Lustigman S., Ma D., Maina C.V., Martin D.M.,
RA McCarter J.P., McReynolds L., Mitreva M., Nutman T.B., Parkinson J.,
RA Peregrin-Alvarez J.M., Poole C., Ren Q., Saunders L., Sluder A.E.,
RA Smith K., Stanke M., Unnasch T.R., Ware J., Wei A.D., Weil G.,
RA Williams D.J., Zhang Y., Williams S.A., Fraser-Liggett C., Slatko B.,
RA Blaxter M.L., Scott A.L.;
RT "Draft genome of the filarial nematode parasite Brugia malayi.";
RL Science 317:1756-1760(2007).
RN [2] {ECO:0000313|EMBL:CDP93015.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FR3 {ECO:0000313|EMBL:CDP93015.1};
RG WormBase Consortium;
RA Ghedin E., Paulini M.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|WBParaSite:Bm3594b.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (DEC-2019) to UniProtKB.
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR EMBL; LN856865; CDP93015.1; -; Genomic_DNA.
DR STRING; 6279.A0A1P6BZ30; -.
DR EnsemblMetazoa; Bm3594b.1; Bm3594b.1; WBGene00223855.
DR WBParaSite; Bm3594b.1; Bm3594b.1; WBGene00223855.
DR OMA; WPSDLCL; -.
DR OrthoDB; 2910701at2759; -.
DR Proteomes; UP000006672; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; 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; 16.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR041645; ADAMTS_CR_2.
DR InterPro; IPR010294; ADAMTS_spacer1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR012314; Pept_M12B_GON-ADAMTSs.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723:SF278; ADAM METALLOPEPTIDASE WITH THROMBOSPONDIN TYPE 1 MOTIF A, 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; PF05986; ADAMTS_spacer1; 1.
DR Pfam; PF08685; GON; 1.
DR Pfam; PF13582; Reprolysin_3; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 16.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 18.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 17.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS51046; GON; 1.
DR PROSITE; PS50092; TSP1; 17.
PE 4: Predicted;
KW Calcium {ECO:0000256|PIRSR:PIRSR613273-2};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR613273-3};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023049};
KW Membrane {ECO:0000256|SAM:Phobius};
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:UP000006672};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW ProRule:PRU00276}.
FT TRANSMEM 58..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 369..582
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1975..2176
FT /note="GON"
FT /evidence="ECO:0000259|PROSITE:PS51046"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 514
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 372
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 372
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 455
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 455
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 462
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 513
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 517
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 523
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 577
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 580
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 580
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 444..497
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 473..479
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 491..577
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 529..559
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 607..629
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 618..639
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 624..658
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 652..663
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 687..724
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 691..729
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 702..714
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 2186 AA; 247547 MW; 2F01356D2E144FD7 CRC64;
MLEVETSASE PLILHPDINN NNNSNNNNSN DNNNNNNDNN SNFDSDSNSS IDSQKPEYFV
AIVFALAVLF SSLYLRGLSF TRIPQSRNRL IAAAVTDAKL QDGEVWHINR HQTRRRRSTW
NDAKWHGVRG LARDCGFTCY FRLRQDTGDR MSKSELHIHL TRWKQLPQPN NKSLPMLENN
RIRPIVQFMD SLDATHARMS RFVPDCLYSA HVKGATESSI VNLCDISGGL FGTLALPDGT
YLIEPVKDDQ MPSKSSSSRA HIVYKSRSHS FHKYGFHSSS AAIITTTPSL NTASATTSTN
SHSTSNHRSN NNNSTNDVQT HNYTAYRISN DNANYDNNTA QYTTIFDPNI NITDSSFARS
RRSANSWDHY VEVLVVADNK MLLYHQNNLE NYVLTLFSTV ASIYRHPSLH AAINIIVTRL
IVLKHETAGP HISDNAQDTL QQFCRWQETY NDKNDDAPNH HDVAILLTRH DICRAPGKCD
TLGLAELGTM CDSLRSCAII EDNGLSAAFT ITHELGHIFN IPHDDERKCG RYMALNKHNY
HIMAPTLEYN THPWSWSPCS AAMLAKFLDA NRAQTQCILD QPIERRYYDR MFEDPAPGAM
FSANQQCQFV FGPSAELCPY MPACRRLWCA TYYGYQMGCR TQHMPWADGT PCGDNQWCHR
GECVGMAPQQ RAKLDGSWGE WKNWGDCSRT CGGGIQKALR DCDNPRPING GKYCVGQRER
YRPCNIQDCP WDTPGFREVQ CSEFDNKDVG IHGVPPKSRW LPKYTGVSDN ERCKLYCRIS
GSAAFYLLKD KVLDGTPCYR HGDDMCIDGT CHKAGCDHRL GSEMRRDKCG ICGGDGSTCR
VVSGSYNERG SFGYNEVLKI PAGSANIQIT QHGYGNQKED DNYLALRNAN GEFLLNGHYQ
VSVFRQQISI QDTVLEYSGS DHVIERINGT GPIRTDIYLH VLSVGNLYPP DIHYEFMVPA
QNVRFGYETS VTNYYWRISE RWSECSSLCQ GQQKQELICV DAISSRSVTD NLCISHRPPT
ETRMCNIDCT IKWRVVPVGQ CNATCGRGEK HQKSECIRSY VDGRETIISD SQCHQLKKPS
DRAPCYVDCA GRKWTYTEWT PCSESCGISG ITRRQAFCSD QTNRRLDDRA CEQAMKDKTE
KECNRIPCPK WVYGEWSECS RSCDGGVKVR HASCQDAAGR EVHLTMCNSK EKHDWEKCNQ
QICTQWRFGT WGSCSVSCGD GIETRDAVCT DLNSRHLDEN LCDRRERIVQ KPCHRMACPS
WRLGTWSACS VSCLDGWKTR HVSCVDANDN EVSDEQCLRQ GEARPQSHQP CNQGPCPFWR
ASDWTKCSVS CGVGVRARNV ECIYRDQVVD GSLCSDTQVS KVEQCSLLPC AKWKVLPWSH
CSVTCGTGQQ TRTIHCLRGK SIVHESECDM AIRPKTEKVC ERDNCEAFTQ NVVESTVSDQ
PKIRWAIGPW SDCSRTCGNG TQRRLIVCRD HIRDLTDTYC QHLEPIETYR YCQIKPCAQW
TVGPWKSCSV TCGMHATTDR RVSCESMEGN EQVRETDCDL TNRPQSIRSC NLNPCPMGEP
PLGFWITKEW EKCSVSCGGG WRRRLITCST RFCNEGEKPE QFERCNQQGC VKVSKVWQMS
PWSHCPVTCG GSVQKRTVWC EDEKIRERVQ DTECLLPEKP STVRECNKIE CQMIPMKNEY
YHWYAGKWNP CSTTCGRGVR KRIVSCVNSH SHSVASKYCD PAKRPIDSHR CRMTHCPRWK
TGKWSMCSVT CGRGIRTREV TCQKGRRTHL SDMECGKLPK PLENSMCMTI SCPAYHWTAT
PWSKCNDPCK KSDQHRRVYC VSNLGKRAAP KMCSNETAPE MTRSCPVTDC LYHWVPGPWS
TCSKTCGTGF QFRRIECRVR SQNHSLSAEP NVQSRMCNGL TRLSVSKECA MNPCDAKYRW
SVGPWSQCST SCGPGYRRRR VRCLDRDGRR VSRDLCDQSP DRPKRRESCF LRNCLPGDCA
ELKAYYMQEN SVDGNYTVLV AGFRITVYCH LMNETLPKTY INLNSETNFA EIYGKRLLYP
FTCPHNGQRN DTCMCTDDGS ASAGFSSFSK VRVDLHNMKI NIHDHTFATT SHGEEVAFAT
AGDCYSAVDC PQGQFGIDLR GTGLRVMDDL RWVDQGHRTS SRIERSDNNA RIFGRCGGYC
GQCSPDKFKG LVIEIDHKQN PSIGVG
//
