ID A0A1I7RYT7_BURXY Unreviewed; 522 AA.
AC A0A1I7RYT7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 22-FEB-2023, entry version 21.
DE SubName: Full=ZnMc domain-containing protein {ECO:0000313|WBParaSite:BXY_0590500.1};
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_0590500.1};
RN [1] {ECO:0000313|WBParaSite:BXY_0590500.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01211}.
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DR AlphaFoldDB; A0A1I7RYT7; -.
DR WBParaSite; BXY_0590500.1; BXY_0590500.1; BXY_0590500.
DR Proteomes; UP000095284; Unplaced.
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:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR PANTHER; PTHR10127:SF877; ZINC METALLOPROTEINASE NAS-34; 1.
DR Pfam; PF01400; Astacin; 1.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS51864; ASTACIN; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 200..218
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 230..251
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 271..293
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 367..389
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 410..435
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 455..475
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 96..191
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT ACT_SITE 190
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ SEQUENCE 522 AA; 60497 MW; 7AA5C2EE7E3590B9 CRC64;
MNRLNFIEGK LLDVEEVKSP SSIPYLDDLF AAHDEHGNPQ RVLASQDKPE EKPFLFEGDM
LLTSKQMDEI VMNVEHQLFL KDIGKPELMM RNRFKRTLTS NIISRWTELR IPYRIHPERG
PNKTLIEAGI KAWTDATCLE FEEKTGGLLQ PHIVFIKGSG CYSNVGKSSM NGQYVSIGRG
CENPYIVAHE IEEVFNFVRI VEPVVSLVTL ALSVYGACKI YNVSTINGNL KVIFITTAAL
CLYLSIAHSI YNFIPREYYQ TSSGDYGRAY LLHGFAGTIH FLIIVVEFKY LLIAIERLYA
YRVRGRYEEF GHGFSFRLLV MAFLASLCIL SFRMRAAWIE YDYLPIDERL IKTIHPHSTL
WGHFSCFFLL SSVITAIAAM IFYCLHVTIK RDEIIYYPLH VRYEIEQTKY VLKYILSLLS
LATILLVCCV LYYAVIFYLV RWKKVDEDGF EVKSLVALIM VSLCIYNFTC MLYMVREFPQ
LQKAVRKDLP FLHRHILEDR PHRVVPADEA DAYFKQLSHH WA
//
