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Database: UniProt
Entry: B4KH43_DROMO
LinkDB: B4KH43_DROMO
Original site: B4KH43_DROMO 
ID   B4KH43_DROMO            Unreviewed;       612 AA.
AC   B4KH43;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 88.
DE   RecName: Full=Cytokine-like nuclear factor N-PAC {ECO:0000256|ARBA:ARBA00034140};
DE   AltName: Full=Glyoxylate reductase 1 homolog {ECO:0000256|ARBA:ARBA00030287};
GN   Name=Dmoj\GI17584 {ECO:0000313|EMBL:EDW12254.1};
GN   ORFNames=Dmoj_GI17584 {ECO:0000313|EMBL:EDW12254.1};
OS   Drosophila mojavensis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7230 {ECO:0000313|EMBL:EDW12254.1, ECO:0000313|Proteomes:UP000009192};
RN   [1] {ECO:0000313|EMBL:EDW12254.1, ECO:0000313|Proteomes:UP000009192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15081-1352.22 {ECO:0000313|Proteomes:UP000009192};
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RA   Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA   Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA   Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA   Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA   Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA   Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA   Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA   Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA   Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA   Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA   David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA   Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA   Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA   Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA   Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA   Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA   Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA   Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA   Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA   Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA   Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA   Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA   Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA   Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA   McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA   Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA   Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA   Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA   Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA   Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA   Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA   Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA   Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA   Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA   Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA   Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA   Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA   Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA   Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA   Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA   Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA   Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA   Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC   -!- SIMILARITY: Belongs to the HIBADH-related family. NP60 subfamily.
CC       {ECO:0000256|ARBA:ARBA00007598}.
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DR   EMBL; CH933807; EDW12254.1; -; Genomic_DNA.
DR   RefSeq; XP_002002812.1; XM_002002776.2.
DR   AlphaFoldDB; B4KH43; -.
DR   SMR; B4KH43; -.
DR   EnsemblMetazoa; FBtr0168309; FBpp0166801; FBgn0140328.
DR   GeneID; 6576827; -.
DR   eggNOG; KOG0409; Eukaryota.
DR   HOGENOM; CLU_018075_0_0_1; -.
DR   OMA; DIGNACK; -.
DR   OrthoDB; 103196at2759; -.
DR   PhylomeDB; B4KH43; -.
DR   Proteomes; UP000009192; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd05836; PWWP_GLYR1; 1.
DR   Gene3D; 2.30.30.140; -; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR006115; 6PGDH_NADP-bd.
DR   InterPro; IPR035501; GLYR1_PWWP.
DR   InterPro; IPR029154; HIBADH-like_NADP-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR000313; PWWP_dom.
DR   PANTHER; PTHR43580; OXIDOREDUCTASE GLYR1-RELATED; 1.
DR   PANTHER; PTHR43580:SF2; OXIDOREDUCTASE GLYR1-RELATED; 1.
DR   Pfam; PF14833; NAD_binding_11; 1.
DR   Pfam; PF03446; NAD_binding_2; 1.
DR   Pfam; PF00855; PWWP; 1.
DR   SMART; SM00293; PWWP; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR   PROSITE; PS50812; PWWP; 1.
PE   3: Inferred from homology;
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW   Oxidoreductase {ECO:0000313|EMBL:EDW12254.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009192}.
FT   DOMAIN          21..80
FT                   /note="PWWP"
FT                   /evidence="ECO:0000259|PROSITE:PS50812"
FT   REGION          115..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..141
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        163..237
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   612 AA;  66520 MW;  60E1B63FA7DC6AA5 CRC64;
     MSKNKKLSLS GDSTEKFIYK PKDLIWAKMK GFTPWPGMIV EPPLDLLAQQ RRANTKCVFF
     FGSRNFAWIE EHNIKPFEGP WKDELAKVSK PAAFRHAMAD IDKYVENPAE IDSQIDESCG
     MGNHTTEADF DKIRDGLDSD ESPETGTDGN NGVVPHVVGS PDESDGLTSN AAVENNATSP
     VVTTTPTVKS QAKRTPKAKS SAAVAVSSKQ ASKAASAKSA AAQKRRISAQ HTPTGASTAK
     RGRRAASGEA DHYESPNADY DGASSSSLAA RARIDTDAFL GSLTKRTPNA IALLDRPVVT
     RPETQAIDMN SRSNTLADRD IVPSDQTFGF LGLGMMGSTI VKDLIYTKHK VVVWNRTIDK
     CQPFVDAGAE VKDTPMDVVE AADIIFCCVS DPKGAKDLVF GNCGVLQLKD LRNKAYVEMS
     TIDPETSMDI GEGIKQCNGR YLEAQIHGSR QEAAEGMLII LAGGDRTVFE ECHSCFKTIA
     KNTFFLGNVG NACKVNLILQ TILGVSLVGL AEALALADRF SISLNDIIDI FDLTSMKSPL
     LLAKGKEMAK GDFNPQQPLS HMQRDLRLVL NMAENLDQSM PVTSITNEVF KHTKRLGYSE
     HDSSAVFVRS RF
//
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