GenomeNet

Database: UniProt
Entry: A0A182N1V8_9DIPT
LinkDB: A0A182N1V8_9DIPT
Original site: A0A182N1V8_9DIPT 
ID   A0A182N1V8_9DIPT        Unreviewed;      3702 AA.
AC   A0A182N1V8;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   03-JUL-2019, entry version 21.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|VectorBase:ADIR001616-PA};
OS   Anopheles dirus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Nematocera; Culicoidea;
OC   Culicidae; Anophelinae; Anopheles.
OX   NCBI_TaxID=7168 {ECO:0000313|Proteomes:UP000075884, ECO:0000313|VectorBase:ADIR001616-PA};
RN   [1] {ECO:0000313|VectorBase:ADIR001616-PA}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WRAIR2 {ECO:0000313|VectorBase:ADIR001616-PA};
RA   Neafsey D.E., Walton C., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J.,
RA   Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA   Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Anopheles dirus WRAIR2.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000075884}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WRAIR2 {ECO:0000313|Proteomes:UP000075884};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Walton C., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J.,
RA   Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA   Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Anopheles dirus WRAIR2.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|VectorBase:ADIR001616-PA}
RP   IDENTIFICATION.
RC   STRAIN=WRAIR2 {ECO:0000313|VectorBase:ADIR001616-PA};
RG   VectorBase;
RL   Submitted (JUN-2016) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00122}.
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DR   VectorBase; ADIR001616-RA; ADIR001616-PA; ADIR001616.
DR   Proteomes; UP000075884; Unassembled WGS sequence.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0030155; P:regulation of cell adhesion; IEA:InterPro.
DR   GO; GO:0030334; P:regulation of cell migration; IEA:InterPro.
DR   GO; GO:0045995; P:regulation of embryonic development; IEA:InterPro.
DR   Gene3D; 2.60.120.1490; -; 1.
DR   Gene3D; 2.60.120.260; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR009254; Laminin_aI.
DR   InterPro; IPR010307; Laminin_dom_II.
DR   InterPro; IPR002049; Laminin_EGF.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR000034; Laminin_IV.
DR   InterPro; IPR008211; Laminin_N.
DR   InterPro; IPR038684; Laminin_N_sf.
DR   Pfam; PF00052; Laminin_B; 1.
DR   Pfam; PF00053; Laminin_EGF; 20.
DR   Pfam; PF02210; Laminin_G_2; 5.
DR   Pfam; PF06008; Laminin_I; 1.
DR   Pfam; PF06009; Laminin_II; 1.
DR   Pfam; PF00055; Laminin_N; 1.
DR   SMART; SM00181; EGF; 9.
DR   SMART; SM00180; EGF_Lam; 22.
DR   SMART; SM00281; LamB; 1.
DR   SMART; SM00282; LamG; 5.
DR   SMART; SM00136; LamNT; 1.
DR   SUPFAM; SSF49899; SSF49899; 5.
DR   PROSITE; PS01248; EGF_LAM_1; 7.
DR   PROSITE; PS50027; EGF_LAM_2; 22.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 5.
DR   PROSITE; PS51115; LAMININ_IVA; 1.
DR   PROSITE; PS51117; LAMININ_NTER; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000075884};
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00122,
KW   ECO:0000256|SAAS:SAAS00814887};
KW   Laminin EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00460,
KW   ECO:0000256|SAAS:SAAS00580772};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075884};
KW   Repeat {ECO:0000256|SAAS:SAAS00814929};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     23       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        24   3702       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5008129267.
FT   DOMAIN       21    274       Laminin N-terminal. {ECO:0000259|PROSITE:
FT                                PS51117}.
FT   DOMAIN      275    334       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      335    404       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      405    449       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      450    495       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      496    541       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      542    587       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      588    632       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      633    677       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      678    732       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      733    785       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      786    826       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1371   1416       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1417   1461       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1462   1509       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1510   1560       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1586   1772       Laminin IV type A. {ECO:0000259|PROSITE:
FT                                PS51115}.
FT   DOMAIN     1769   1805       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1806   1855       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1856   1913       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1914   1966       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1967   2013       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     2014   2060       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     2061   2108       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     2670   2864       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   DOMAIN     2872   3045       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   DOMAIN     3052   3221       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   DOMAIN     3341   3519       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   DOMAIN     3525   3699       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   REGION     2473   2497       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A182N1V8}.
FT   REGION     3247   3329       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A182N1V8}.
FT   COILED     2178   2198       {ECO:0000256|SAM:Coils}.
FT   COILED     2378   2398       {ECO:0000256|SAM:Coils}.
FT   COILED     2417   2444       {ECO:0000256|SAM:Coils}.
FT   COILED     2594   2628       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS   3276   3290       Pro-rich. {ECO:0000256|MobiDB-lite:
FT                                A0A182N1V8}.
FT   COMPBIAS   3291   3315       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A182N1V8}.
FT   DISULFID    300    309       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    372    381       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    425    434       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    450    462       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    452    469       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    471    480       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    496    508       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    498    515       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    517    526       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    542    554       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    544    561       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    563    572       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    588    600       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    608    617       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    633    645       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    653    662       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    703    712       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    756    765       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    786    798       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    788    805       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    807    816       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1371   1383       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1373   1390       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1392   1401       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1434   1443       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1485   1494       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1510   1522       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1512   1529       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1531   1540       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1775   1784       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1825   1834       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1884   1893       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1938   1947       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1950   1964       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1986   1995       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   2034   2043       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   2061   2073       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   2063   2080       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   2082   2091       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   3194   3221       {ECO:0000256|PROSITE-ProRule:PRU00122}.
FT   DISULFID   3672   3699       {ECO:0000256|PROSITE-ProRule:PRU00122}.
SQ   SEQUENCE   3702 AA;  411905 MW;  E5667DE6CB6B2210 CRC64;
     MGGITALAPI ALLVALGIGT VRSELTPPYF NLAEGRKITA TATCGVDTDG PELYCKLVGA
     NTENDNQNQY SVIQGQVCDV CDPSDPDKSH PPEYAIDGTQ NWWQSPPLSR GMKYNEVNLT
     IDFGQEFHVA YLFIRMGNSP RPGLWSLEKS SDYGKTWTPW QHFSDSPTDC VTYFGANSLK
     PLQNDNDVIC TMDHSKIVPL EGGEIPIRLL NNRPSANNYF NSSTLQEWSR ATNVRIRLLR
     TKNLLGHLMS VARQDPTVTR RYFYSIKDIS IGGRCVCNGH ANTCNVLDPR SPTRILACQC
     QHNTCGIQCA ECCPGFEQKK WRQNTNARPF QCEPCNCHGH SDECVYSEDI DAKGLSLDIH
     GNYEGGGVCQ NCQDNTKGIN CNQCEDKFYR PYGRHWNETD VCQPCDCDHF YSTGNCEEET
     GRCECRVEFE PPHCDACSYG HFGYPNCRQC ECNLNGTIGY YCEAVDGTCP CKHNFDGPHC
     KQCAKEYYGF PECDPCDCNM HGSVDRVCDE GSGQCQCKPN FAGQLCDTCK DGFYRYPECT
     YCNCDVRGTL DEVCDKNSGT CLCREGYGGP RCDQCIPGYY NYPDCVPCNC SSAGSTSTVC
     DITGRCSCLE NFGGRQCTAC LAGYYQYPEC LPCHCDSYGS LAKSCTNDGQ CQCKDNFDGK
     TCQQCREGFY NFPACEECNC DPAGVIARFA GCGSVPAGEL CQCKERVHGR ICDKCRPLYW
     NLSASNTHGC QECECFIDGT IGALDTCDTK SGQCACKPSV KGRQCTECKD GTFDLFGSNL
     FGCKDCGCDI GGAADNVCNK ETGQCRCHPR VSGRTCSYPL TTHYFPTLYQ FQFEYEDGYT
     QSGAQVRYQF HEDIFPGFSS RGYAVMSSLQ NEVINEVSVL KSSVYRLVIR YKNPNPDNVV
     ATILITPDNP TEVEQRTKVL FKPTEHPEFV TVSDARGEVP SPVVLDPGSY TISIKTDKTV
     FLDYFVLLPA AYYEASILTK KIENPCEFND LGLCRHYQYP SVAPYNPQAE AVIIEDEQSF
     KPVEYFKDYE HLDVIKEQEL PTLTDAQREL LYPMEVPHAG RYIVVVDYIT YRNNPEVAIL
     QVNLVGDIDQ DGSVTAYPCT YTTVCRQPVI DRESREKIFF LDPNNRKSIQ VKSADFSSAI
     AIKSVTAIPY EDWSADYIRP NSVCVMQNGK CVQTSYRTAP DSKKIEFETE NEYRVAEEVP
     RELYDNSTKL ILLDQNQPDV SIKAKVHHPN RYVLIVKFFQ PDHPSFNVQY RIETERQNYD
     GRLEVRHCPA NSGCREVLKQ DNGYIEFDLE DNIEFTIHNN GSKRVWVDYV QLVPAEQFHN
     GLLQEETFDQ TNEFIQHCGQ DHFHIQTNAT DFCKKAVFSL TADYNSGALP CNCDYSGSTS
     FECEPFGGQC QCKAHIIGRK CEACKTGYYG FPDCKPCNCP STAQCHKDTG ECVCPDRVTG
     EKCDQCMPYT FGFDQIIGCE ECNCNPLGVS NNNLQCDMDS GLCECKSNVV GRKCDRCQYG
     FFNFPYCEPC HCDIRGTTFE ICDQTDETCF CKKNVQGREC NTCVDGTYNL QAGNPDGCTK
     CFCFGHSSRC QTAFLRPFNV SMMKDMTVNT IRLSGGKVTI TPWVLGENIM LNETSAEVSL
     SAFDNRDPSV GMVYFGMLDH LFDLNNHLSA YGGHLTYKIH FTNGLFGSSL IGADVILEGK
     QLEVMHQSYR QPSSNQLFSG SVEIVESNFQ TAAGGPVSRE QFMMLLRDLK NIYIRASYWE
     NGLVTVISDV SLTMAHDDLE HPQLYRELSV ENCECPPGYT GRSCEDCAPG YYRDPNGPHL
     GYCIPCECNG HAATCDCNTG VCHDCQHYTT GEHCDQCIEG YYGNATRGTP NDCMICACPL
     PVESNNFATS CEVSEDGYEI HCACKPGYHG EKCQSCAPGY YGQPQVEGEF CKQCDCSGNI
     NAEEPGACDS VSGECLLCLN NTSGRACNLC APGFYGDAVH LKDCQSCICD KTGMDYCDNF
     VGTCNCLPNV IGEKCDRCED DHYGFESGRG CTACDCGIAS NSSQCDDHTG KCACKPGVTG
     RQCDRCEPGY WNYSEEGCVP CSCNTDYSRG LGCNALTGQC ECLSGVVGEK CDSCPYRWVL
     IPDTGCQECD VCHHALLDVT DGLKADVDPV LQDIKTIADD YYTSQKLKYF DDMVDQLEPK
     VRSLDPHGVN LNPSRQKVES LELDVKSLDR RIQYADENAK DISTNSENLL AAGSNVLDDC
     RLVHINTKNT IEEVLVLAEN LGSSEITKLD QAFAEAKNYL DNIKQYSTTP ESLNSQLENA
     TRLLERVELF GEPVQSQHEK LEKLMHDIGD FDVKLEDLYT WSLKVEKESS ITSKLNNKNK
     GAANTKFDTV SAHAKEATEN IENSKTLLAN SSNIMMDIEI THREVDQVNN ELSELNNGVD
     TELPLTFDEY QKLNPLIEKA SRHAADLKIE AEGLSEKYSD VSANSETALQ AATAHSKIVD
     AVNEAADNIR NATSTAQKAT DQTEGIDNRA AESDSASREL LDEARRMFTT LQTELEPQSK
     QSIDTVDGIK EKNAQSDDML YSINAAMDGI PEESHTDSWE NARDQAVEAH AKSHNSMKIL
     DPMISDLSKS VYLAEQLPKE VDNTQKDIKQ ATAQIERLKT MIPNIRQLVE KLDTKQNQVD
     SIVSDIGDRL EALRRQIGEA RSVANTIKVG VQFHPNTTVE LKPPPSLSQM ATNSNVSVFF
     RTDKPEGFLL YLGNEVKPDA KKSSRDDYMA LEIENGYPVL SIDLGNDPEK VISPKYVADD
     KWYQAIVERT GNNVKLIIRE ELDNGTDVFH TKEQVLPGAY NVFNVDQNSK LFIGGYPPDY
     NMPQDVKSSE FDGRVEQLQI GGEHVGLWNF VDAQNVYGTP ERESLRNEEN PSTGFRFSGN
     GYVAIDSKPY TFKQQSQLQF QFKAPPETRD GLLFFAGKNK HFISVEMRNG AVVFQFKLGQ
     HAQAVTMGSS SAFNDDKWHK ISVERDGNIG KLTVDDQEVF QQTGSADHQQ LHISEALYFG
     GYHSRVNHSE VTSKGFDGCI DDVYILGNKV DLSINLKALD VRPGCPMKFS PLVSFPPRQF
     GYVSQPEVVS MDNLQVNLKF RTTQRDGVLF YTRNFDQSGT FGLALRNGVL VLSSTDVEVT
     TGHQTYNDGE WHAVTASHDP DRLTLLVDDH DPHYSSEKLK VLYIENGDID FGGLPKNYVT
     PRNALASTAY FMGCISDVTV NGQIVNFATL TDKKSAVLDQ CSKELFAVGD VPLFYPDDGR
     DPQVFVHSRI DVDREQPDED EEEDSRRYDY GRKPTPAAAP PTPAPTVPAS EAPTTVPTTT
     TTTTTTTTTT TRRPRPSQPD EPPPVCRLPV TPEQDVDFDS GYRFGTGQFS HIEFSEVPLK
     NKRQYDFSLS FKTEFSEGVL FYVADLRHTD FIALHLRDGK VIHSFNCGSG SANMTSDRRY
     DDNEWHTVHF TRHNNKGKLV VDSEDESHGE SSGTTRTMAL QAPMFVGGVS GENYEEVALN
     LKIDKNVLER NQFVGCINEI EANRQPLATP SNITRTIPCS TQIESGTFFG NGGGFVKLYD
     KFKVGSELTV SMDIRPRAPS GLLMSVHGRK AYFVLEMING TISLSVNNGD DPFTATYTPL
     PDENLCDGQW RTVSAIKSQY VITIKVNDVS SNPAIGDARA PSTDTTRPLF LGGHPHLQRI
     RGFVARTPFQ GCIRNVKVRD TVEQITPKMT VGNVQTGVCP TI
//
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