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Database: UniProt
Entry: A0A1I8BQT6_MELHA
LinkDB: A0A1I8BQT6_MELHA
Original site: A0A1I8BQT6_MELHA 
ID   A0A1I8BQT6_MELHA        Unreviewed;       894 AA.
AC   A0A1I8BQT6;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   05-JUN-2019, entry version 19.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|WBParaSite:MhA1_Contig389.frz3.gene2};
OS   Meloidogyne hapla (Root-knot nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Tylenchomorpha; Tylenchoidea; Meloidogynidae;
OC   Meloidogyninae; Meloidogyne.
OX   NCBI_TaxID=6305 {ECO:0000313|Proteomes:UP000095281, ECO:0000313|WBParaSite:MhA1_Contig389.frz3.gene2};
RN   [1] {ECO:0000313|Proteomes:UP000095281, ECO:0000313|WBParaSite:MhA1_Contig389.frz3.gene2}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=18809916; DOI=10.1073/pnas.0805946105;
RA   Opperman C.H., Bird D.M., Williamson V.M., Rokhsar D.S., Burke M.,
RA   Cohn J., Cromer J., Diener S., Gajan J., Graham S., Houfek T.D.,
RA   Liu Q., Mitros T., Schaff J., Schaffer R., Scholl E., Sosinski B.R.,
RA   Thomas V.P., Windham E.;
RT   "Sequence and genetic map of Meloidogyne hapla: A compact nematode
RT   genome for plant parasitism.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:14802-14807(2008).
RN   [2] {ECO:0000313|WBParaSite:MhA1_Contig389.frz3.gene2}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   WBParaSite; MhA1_Contig389.frz3.gene2; MhA1_Contig389.frz3.gene2; MhA1_Contig389.frz3.gene2.
DR   OMA; CAPENER; -.
DR   Proteomes; UP000095281; Whole Genome Shotgun Assembly.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   Gene3D; 3.40.390.10; -; 1.
DR   Gene3D; 4.10.70.10; -; 1.
DR   InterPro; IPR006586; ADAM_Cys-rich.
DR   InterPro; IPR001762; Disintegrin_dom.
DR   InterPro; IPR036436; Disintegrin_dom_sf.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR013111; EGF_extracell.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR002870; Peptidase_M12B_N.
DR   Pfam; PF08516; ADAM_CR; 1.
DR   Pfam; PF00200; Disintegrin; 1.
DR   Pfam; PF07974; EGF_2; 1.
DR   Pfam; PF01562; Pep_M12B_propep; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   SMART; SM00608; ACR; 1.
DR   SMART; SM00050; DISIN; 1.
DR   SUPFAM; SSF57552; SSF57552; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS50214; DISINTEGRIN_2; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
PE   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000095281};
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068,
KW   ECO:0000256|SAAS:SAAS00117091};
KW   EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   Membrane {ECO:0000256|SAAS:SAAS01078504, ECO:0000256|SAM:Phobius};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAAS:SAAS01078486,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS01078482,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20    894       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5009316078.
FT   TRANSMEM    757    779       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    866    884       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      247    443       Peptidase M12B. {ECO:0000259|PROSITE:
FT                                PS50215}.
FT   DOMAIN      450    537       Disintegrin. {ECO:0000259|PROSITE:
FT                                PS50214}.
FT   DOMAIN      676    714       EGF-like. {ECO:0000259|PROSITE:PS50026}.
FT   REGION      206    237       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1I8BQT6}.
FT   REGION      799    823       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1I8BQT6}.
FT   COMPBIAS    213    227       Basic. {ECO:0000256|MobiDB-lite:
FT                                A0A1I8BQT6}.
FT   DISULFID    509    529       {ECO:0000256|PROSITE-ProRule:PRU00068}.
FT   DISULFID    704    713       {ECO:0000256|PROSITE-ProRule:PRU00076}.
SQ   SEQUENCE   894 AA;  100272 MW;  D419FA0081730B65 CRC64;
     MFSLFSFILI GQLSLIANAN QLRHSLVNKQ FIDQLTEGSY EIIHPFQLRE KSRERMGIDT
     REYFLNTTPI QHFRQVSFVL RSSVLLNQRL RIALSLNEHL LSGGSKQQNE AHLFDKTTQS
     TLMDSEQDME VIRPSAVENC FYQGTVIGEP GSMVTLSTCD GLWGLLAFAN GSALGIWPLE
     GGDKGKRHPH VLFRVFGNGT ECNDIEGQHQ EKSIKRRRKR TRKFRGKRKS EGGGSEENWR
     HLRQQRLFLD IALLVNKEMQ NLFNIGQSKL LEYSLNSLNI ADLIFKRGLN IRIFLNYFAL
     IENLNKNNSN QLIDDLLDFT SIKLFKEEKD ATIYLTNGYL NKQNNNIALN VDNSVCSGRA
     VGLTQISNLY APQTAALSFV HSLSHILGLE HDLTECGCDM EECIMSARKG QFNHFPWHFS
     ACSSARLERK RSDPKMECLV KSNLFSQFSS FLCGNGQLDK GEECDCGRRD QCTDPCCDPF
     TCRLRPHANC AAHEECCHRC HIRPSGHLCR PTRSICDVAE RCDGKSGECP PDSHLLDGTH
     CGLGNNGQCW QGDCIDSDAQ CRELWGKGAR VAEALCFSKN GHALEYGNCG RDGDGRFMEC
     APENERCGLL QCHEGSASPT VPNATAFAFQ FVQEERPVQC KVVTNSPLGF VRDGTSCGEG
     RVCIKNVCLP LAQVSPPVKC PTSGSNVSQC SGHGDCTSSG QCLCFDGWTG KSCDLRTPTR
     RADNHHSPSL EFSSLRDIST RFVGVSDGKV ILETTTLLII LLFVGLLLLL LLLFLLLFYR
     RSSADSFQHA NIQFKQTTTT TADEEDIKNE NEQNEGNNAR TIKFGQMPSW REEKRKRKTN
     KRVYDALQRI TEANEVRNER GILGNVYKTG CLLFLGIFIV YLGLREGGYD SQKD
//
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