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Database: UniProt
Entry: A0A1I7S5N8_BURXY
LinkDB: A0A1I7S5N8_BURXY
Original site: A0A1I7S5N8_BURXY 
ID   A0A1I7S5N8_BURXY        Unreviewed;       646 AA.
AC   A0A1I7S5N8;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Col_cuticle_N domain-containing protein {ECO:0000313|WBParaSite:BXY_0832300.1};
OS   Bursaphelenchus xylophilus (Pinewood nematode worm) (Aphelenchoides
OS   xylophilus).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Tylenchomorpha; Aphelenchoidea; Aphelenchoididae;
OC   Bursaphelenchus.
OX   NCBI_TaxID=6326 {ECO:0000313|Proteomes:UP000095284, ECO:0000313|WBParaSite:BXY_0832300.1};
RN   [1] {ECO:0000313|WBParaSite:BXY_0832300.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
CC   -!- SUBUNIT: Collagen polypeptide chains are complexed within the cuticle
CC       by disulfide bonds and other types of covalent cross-links.
CC       {ECO:0000256|ARBA:ARBA00011518}.
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DR   AlphaFoldDB; A0A1I7S5N8; -.
DR   WBParaSite; BXY_0832300.1; BXY_0832300.1; BXY_0832300.
DR   eggNOG; KOG3544; Eukaryota.
DR   Proteomes; UP000095284; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042302; F:structural constituent of cuticle; IEA:InterPro.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 2.
DR   InterPro; IPR002486; Col_cuticle_N.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR24637:SF328; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR24637; COLLAGEN; 1.
DR   Pfam; PF01484; Col_cuticle_N; 1.
DR   Pfam; PF01391; Collagen; 1.
DR   SMART; SM01088; Col_cuticle_N; 1.
DR   SMART; SM00355; ZnF_C2H2; 2.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT   TRANSMEM        16..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          588..616
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          617..645
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   REGION          176..380
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          495..517
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          559..580
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   646 AA;  68520 MW;  ECEB635627DED080 CRC64;
     MESTPVEEKN STIRSVGFLA IGLSLAATFS CVLGVAFVVT QADEIRYELH RELFGFKQDT
     DFLWTSLMTQ SQPRRLKRQY DSYAPPPASA AYGSNPYDSI PTSSGANAYA QPPANPYASS
     AGYTASSSYA AAPPAAGYES GPVKVGDRSY GAFQPAAQPP AIQFCTCDDF KCPPGPPGPK
     GVKGKDGEQG EPGIDGEDGE EAQDAPAQVQ QYEKCFHCPS GQPGPQGPPG RPGPRGMRGA
     RGQPGVPGRD GQPGFPGGLG PEGPLGHRGE DGPQGLPGED TEHKVGSPGA RGQPGPIGDA
     GEPGKPGPDG PIGPQGPSGD PGLPGKAGKD GELGPVGEPG DEGEPGADAT YCPCPGRGAP
     LAEPKKQESP KVEVTTTTTT TTSKPDIGVV KSGYAPILGI HKIQNFMRQC IELNKLQPQY
     ITDLSHSEKF FIRFSRLSFS PNWVFSTELV PRFGRQSTMS QSVDVNLNLE QLQQCMQIYY
     SMLCQQAQQS QGLGHSGLQV KPEVQPTPSS TNSPSSDFPL SSNFSIASLM SSTPNSSISN
     DSGISSPSPA SVGFATPSQA KILSSTPARR PIRTQDGEEI RRDADGKYVC PICQKAFSRK
     FYLQTAHMNI HNNISPYQCR KCHRAFKDSS NRRNHEKICQ IAPLPE
//
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