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Database: UniProt
Entry: A0A4E9FM88_BRUMA
LinkDB: A0A4E9FM88_BRUMA
Original site: A0A4E9FM88_BRUMA 
ID   A0A4E9FM88_BRUMA        Unreviewed;      1195 AA.
AC   A0A4E9FM88; A0A8L7TH74;
DT   11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 1.
DT   28-JAN-2026, entry version 26.
DE   SubName: Full=Collagenase NC10 and Endostatin family protein {ECO:0000313|EMBL:VIO97439.1, ECO:0000313|WBParaSite:Bm8092a.1};
GN   Name=Bm8092 {ECO:0000313|EMBL:VIO97439.1};
GN   ORFNames=BM_BM8092 {ECO:0000313|EMBL:VIO97439.1};
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|EMBL:VIO97439.1};
RN   [1] {ECO:0000313|Proteomes:UP000006672}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FR3 {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:VIO97439.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FR3 {ECO:0000313|EMBL:VIO97439.1};
RA   Howe K., Paulini M., Williams G.;
RL   Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|WBParaSite:Bm8092a.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2022) to UniProtKB.
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DR   EMBL; CAAKNF010000194; VIO97439.1; -; Genomic_DNA.
DR   RefSeq; XP_042937046.1; XM_043081112.1.
DR   AlphaFoldDB; A0A4E9FM88; -.
DR   GeneID; 6095261; -.
DR   KEGG; bmy:BM_BM8092; -.
DR   WBParaSite; Bm8092a.1; Bm8092a.1; WBGene00228353.
DR   CTD; 6095261; -.
DR   OrthoDB; 5983381at2759; -.
DR   Proteomes; UP000006672; Unassembled WGS sequence.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0031012; C:extracellular matrix; IEA:TreeGrafter.
DR   GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR   GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR   GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR   Gene3D; 3.40.1620.70; -; 1.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR050149; Collagen_superfamily.
DR   InterPro; IPR010515; Collagenase_NC10/endostatin.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR   PANTHER; PTHR24023:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR   Pfam; PF01391; Collagen; 2.
DR   Pfam; PF20010; Collagen_trimer; 1.
DR   Pfam; PF06482; Endostatin; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
PE   4: Predicted;
KW   Collagen {ECO:0000256|ARBA:ARBA00023119};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006672};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          694..739
FT                   /note="Collagen type XV/XVIII trimerization"
FT                   /evidence="ECO:0000259|Pfam:PF20010"
FT   DOMAIN          1012..1177
FT                   /note="Collagenase NC10/endostatin"
FT                   /evidence="ECO:0000259|Pfam:PF06482"
FT   REGION          100..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          279..301
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          440..580
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          596..621
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          637..687
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          857..938
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          964..994
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..116
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        449..458
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        460..477
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        501..511
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        513..522
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        546..561
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        651..678
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        874..892
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        910..927
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        972..994
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1195 AA;  132766 MW;  9AC68EEF925CC40A CRC64;
     MKSYQLLLLS NHILRIFFLF SALIITINTK QAEDIHHSSV VDFKIHIDKF KNQNSKNHDT
     GNYHQLVSTI AKSGLSKKFE DLVTDEGFIL TALKQQQRQQ RQRQRQQQQQ QGQQQNENEK
     GVNNEGNSAV ATTTATTIII ESANSTITDK QNLSIVGTNF IDFSYPTNNP VNKEISLAIH
     SISNNSNLFQ SLINQSIRND NNGDSSSSSN SKDSSSNIKW KFLNQRMINL NDGDSNHRRK
     RWATDDTSDK DEMNKIFDTL SSTNYDSPTS ASDEMLTSSD YHIHDNGDDD DVDKSDNTDD
     SRFRIPVENI VIMGSDADAD VDDSSSDNNG MFKGTTFDEI ETTDSYEQMN SVEETEKDDE
     NMEMGIVRIA PEILPKDSIE NLMEPTMHQF GLEAKTDEIM DEKLLKSDII GRKNHMGKED
     EIDWEGSGVQ DEELQEYEKT GKTTIAVPEQ SSIHTSSDYP RVKPEKGEKG DKGDRGEPGP
     PGEPGTCPIE CQPGRDGRDG IPGMPGEMGP MGPIGPPGPA GPPGLSTQIV QEGPQGVRTV
     AGPTGPQGPP GPMGPRGPPG PRGVGEPGFP GAPGVPGRCE RLHPEDIERI VSDPRIKGEK
     GDCLPGIPIR HPGESKELPP YDSYQRHYAM KGERGERGEI GRMGPMGPIG HPGPPGPPGP
     PGPPGPPGPP GHPGPAGPPL AAYPQPTHIA PGGVQVYPTT IELFTASHGM PIGSLTFCIS
     SQQLYIRVNG GFKDIKLEGF HPIMERRPTV DESSKSEVQY QIPLMSNDDS LIPSQVSLSH
     HRISPKLNIP QKNQHLISDT YDKQSRTADI IHRPQIFDAS QSIKSYQQHH KSLLSSEITP
     STFSNQQSWQ TFESKHHLSY PRTEYRPPAG QLYPRYRLPS GSSGSSGLSR LSPNERLHKS
     HHLSQRLDHT PSTLQSFPSS QHISVQHQRI EHQNPSVKPD YHSEHIALAT VATTFSPEWS
     KQQATISLPD EQEAHRSRYP DHERLRYRER PGPDRTHSAL LPHSLQAKDL VLHLIALNTP
     MSGNMRGVRG ADLACYQQAR QANFRTTFRA FLSSHVQDLN KVVHSGDRDT PVVNLRGERL
     FDSWSDIFQQ RQMADLPIYS FNRRNVFADS IWPEKRIWHG SDLSGMRSES GYCSAWRSAS
     TTQVGRASFI GRGLPLLRDS RDSECSRELV VLCIENMSKY NADKRLGKKR AYFSE
//
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