ID A0A232FIY1_9HYME Unreviewed; 964 AA.
AC A0A232FIY1;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 28-JAN-2026, entry version 33.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OXU30632.1};
GN ORFNames=TSAR_001838 {ECO:0000313|EMBL:OXU30632.1};
OS Trichomalopsis sarcophagae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Proctotrupomorpha;
OC Chalcidoidea; Pteromalidae; Pteromalinae; Trichomalopsis.
OX NCBI_TaxID=543379 {ECO:0000313|EMBL:OXU30632.1, ECO:0000313|Proteomes:UP000215335};
RN [1] {ECO:0000313|EMBL:OXU30632.1, ECO:0000313|Proteomes:UP000215335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Alberta {ECO:0000313|EMBL:OXU30632.1,
RC ECO:0000313|Proteomes:UP000215335};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXU30632.1};
RX PubMed=28648823; DOI=10.1016/j.cub.2017.05.032;
RA Martinson E.O., Mrinalini, Kelkar Y.D., Chang C.H., Werren J.H.;
RT "The Evolution of Venom by Co-option of Single-Copy Genes.";
RL Curr. Biol. 27:2007-2013(2017).
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:OXU30632.1}.
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DR EMBL; NNAY01000139; OXU30632.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A232FIY1; -.
DR STRING; 543379.A0A232FIY1; -.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000215335; 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 CDD; cd00247; Endostatin-like; 1.
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; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 1.
DR Pfam; PF01391; Collagen; 3.
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:UP000215335}.
FT DOMAIN 664..712
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 748..913
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 49..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 920..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..95
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..199
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..456
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..500
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..576
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..600
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 928..947
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 964 AA; 99674 MW; EE79BD54E01F706A CRC64;
MTHFVYRLVA YYVLIVCFKG LLQSLKLHLG FPQDLVKCNE DFDFHSGDDG SGDHELISGS
GEIDPDDVPI ARGDDEVESE EVKPPPLITP PPPNPNSKEV TKGEKGEKGE SVRGPPGPPG
TSYDLNDEEW IAKLPEGPPG PKGDPGDCSC NASALLTSFS MPKLVHGEKG EPGTPGKEGK
QGPLGLTGAA GPPGERGQPG PQGPKGDKGD LGNTGPEGSQ GEKGEPGRDG APGEKGAQGP
PGPPGKGEFA GYDTEGYAMR PGLPGQKGDD GKPGHPGPKG EPGVHGAKGD KGDAGHKGTK
GLHGKEGPRG VQGVKGEPGA PGVPGLPGAV GEVGRTGDKG AKGDMGPEGK TGPAGPPGPP
GHGGVSVSDV VGPGRGQKGE PGERGYKGDL GHKGEKGDKG DFGPAGVPGI NGIQGPQGDK
GEPGKDGSPG FPGTPGMKGE RGERGPPGAT TIAGTGDYVT IKGEQGAMGP MGKRGRRGRP
GPPGNEGPPG PPGPEGPPGK PGINGEIGLP GWMGRPGTPG IPGLPGSKGE KGEPGAPSPY
GSAHGIKGDK GADGFPGIPG APGMRGPPGP AGPPGVPSQG SYIPVPGPPG PPGPPGPPGP
GIGKSHIYGE RDYYGSRQGL RSSMDELKAL RELKELKELK EHLGANAAAT RGPLETTTKI
VPGAVTFQNT EAMTKMSGVS PVGTLAYIID EQALLVRVNN GWQYIPLGTL LPITTPAPPT
TASPPVNPPF EASNLINQVP VKADGTSLRM AALNEPFTGD MHGVRGADYA CYRQAKRAGL
KGTFRAFLSS RVQNVDSIVR LGDRDLPIVN VKGDVLFNSW KEMFNGNGAY FSQNPRIYSF
NGKNILSDFT WPQKVVWHGS HTLGDRAMDT YCDAWHSGSS DRYGLGSPLT GGRLLEQVRY
SCDNKFALLC IEVTSEQTKR RRRRRSLDED EDEDEEEEDV DEEDESLLTE AEYAEQLRQL
FRAD
//
