ID A0AAD4MWH4_9BILA Unreviewed; 897 AA.
AC A0AAD4MWH4;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 6.
DE SubName: Full=Collagenase NC10 and endostatin domain-containing protein {ECO:0000313|EMBL:KAI1708279.1};
GN ORFNames=DdX_11959 {ECO:0000313|EMBL:KAI1708279.1};
OS Ditylenchus destructor.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Tylenchomorpha; Sphaerularioidea; Anguinidae; Anguininae;
OC Ditylenchus.
OX NCBI_TaxID=166010 {ECO:0000313|EMBL:KAI1708279.1, ECO:0000313|Proteomes:UP001201812};
RN [1] {ECO:0000313|EMBL:KAI1708279.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BazhouSP {ECO:0000313|EMBL:KAI1708279.1};
RA Zhang H., Lin R., Xie B.;
RT "Genome Sequence Resource for Two Populations of Ditylenchus destructor,
RT the Migratory Endoparasitic Phytonematode.";
RL Submitted (JAN-2022) to the EMBL/GenBank/DDBJ databases.
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:KAI1708279.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JAKKPZ010000036; KAI1708279.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AAD4MWH4; -.
DR Proteomes; UP001201812; Unassembled WGS sequence.
DR GO; GO:0031012; C:extracellular matrix; IEA:TreeGrafter.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR FunFam; 3.40.1620.70:FF:000003; Collagen type XVIII alpha 1; 1.
DR Gene3D; 3.40.1620.70; -; 1.
DR Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 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; IPR050149; Collagen_superfamily.
DR InterPro; IPR010515; Collagenase_NC10/endostatin.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 1.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP001201812};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..897
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5042194389"
FT DOMAIN 579..625
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 715..881
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 34..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..269
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..426
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..510
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..550
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..560
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 897 AA; 99812 MW; 696543D6F23A6B06 CRC64;
MRFRSNFAGH WPKFSVYFVI FLLPHINALS NQVNSQRSNE DSRIQNHNRY SNYDRYDRRE
DLEKEKLIYG PEPDSGQNSR PGKRKIVTLP ENEDNRHNSK FHGTEIRRNR KSRQVKDYTV
KTKDRPVIVF HDIDSATTPF WNYVKSPDVT PNISQSDQDE MIVEAIAETP RTTENPEKSI
NDQAKYVEDP MDRIQIGDGE GDKPPEILAT QDSATVILEE EEDPSKKLLR MLTEYGSDPE
TDHQRAEIDV PAEYNDENVE IEEDEDFEVP EVRAIASPVD SPEETDSEKK RGKESEKRPE
KRPKMTPKDP ETNLPLIANG ESMTDLDGPN GEGPKAKIGE NGESLIAEEG DEGSGLREFS
PDSAALPQQW PSGAGETDPR TAGRKEETED LQQSPPPEKP AFFTSDSTVG EKDKYSGVVK
GEKGDPGDPG PPGVCSAECV GMTGPIGPPG PPGPKGEQGD PGVPGIGRPG LPGTFDGLAD
QDLARIAAWP GVKGEKGECV NAPDPRRQDA PEIDNTLSDG LPPYDSRVHQ YQTAARGEKG
DRGDRGERGE PGPPGPPGMP APRIDGTHTA HPQPVASAVT IYQTAVELLA AAHLHSVGAL
AFAISSQQLF IRVNNGWRLI QLDRFYPAVE QQPSARTQED QVLPPSAAEY DVWVPGLTRR
PPPVAHTQHH HHHRPQHPEG DRRATAYNAY DTYYSATDQQ HRLDDTNVRH RDRVIHLIAL
NEPYNGDFRG VRGADLACYK AARQAGFDTT FRAFISSHVQ DVNKIVHFDD RQSTPVVNLR
GERLFDSWNA LFDGTAHSHV PLYSFNRRDI YTDEFWRDRW LWHGSHSNGL RALGSFCDGW
RSSASSQFGM ASPLHSSRSL THASVAAPCH RRLAMLCVEN MSKFNVNRRV GKRIPPG
//
