CIPB_EMENI
ID CIPB_EMENI Reviewed; 314 AA.
AC Q5AUY5; C8V4J3; Q8NKD0;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Zinc-binding alcohol dehydrogenase domain-containing protein cipB;
DE EC=1.-.-.-;
DE AltName: Full=Concanamycin-induced protein B;
GN Name=cipB; ORFNames=AN7895;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-148, INDUCTION, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=12207217; DOI=10.1007/s00438-002-0695-0;
RA Melin P., Schnuerer J., Wagner E.G.H.;
RT "Proteome analysis of Aspergillus nidulans reveals proteins associated with
RT the response to the antibiotic concanamycin A, produced by Streptomyces
RT species.";
RL Mol. Genet. Genomics 267:695-702(2002).
RN [4]
RP INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17258477; DOI=10.1016/j.fgb.2006.12.001;
RA Kim Y., Nandakumar M.P., Marten M.R.;
RT "Proteome map of Aspergillus nidulans during osmoadaptation.";
RL Fungal Genet. Biol. 44:886-895(2007).
CC -!- FUNCTION: Involved in osmoadaptation.
CC -!- INDUCTION: Induced by the antibiotic concanamycin A. Down-regulated
CC when grown with elevated levels of potassium chloride.
CC {ECO:0000269|PubMed:12207217, ECO:0000269|PubMed:17258477}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CBF73475.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AACD01000135; EAA59549.1; -; Genomic_DNA.
DR EMBL; AJ344257; CAC87271.1; -; Genomic_DNA.
DR EMBL; BN001302; CBF73475.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_681164.1; XM_676072.1.
DR AlphaFoldDB; Q5AUY5; -.
DR SMR; Q5AUY5; -.
DR STRING; 162425.CADANIAP00003912; -.
DR EnsemblFungi; EAA59549; EAA59549; AN7895.2.
DR GeneID; 2869221; -.
DR KEGG; ani:AN7895.2; -.
DR eggNOG; KOG1198; Eukaryota.
DR HOGENOM; CLU_026673_16_5_1; -.
DR InParanoid; Q5AUY5; -.
DR OrthoDB; 727365at2759; -.
DR Proteomes; UP000000560; Chromosome II.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0070402; F:NADPH binding; IBA:GO_Central.
DR GO; GO:0003960; F:NADPH:quinone reductase activity; IBA:GO_Central.
DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IBA:GO_Central.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Oxidoreductase; Reference proteome; Stress response.
FT CHAIN 1..314
FT /note="Zinc-binding alcohol dehydrogenase domain-containing
FT protein cipB"
FT /id="PRO_0000363402"
FT CONFLICT 141
FT /note="S -> L (in Ref. 3; CAC87271)"
FT /evidence="ECO:0000305"
FT CONFLICT 145..148
FT /note="QDDV -> RTSF (in Ref. 3; CAC87271)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 314 AA; 32857 MW; C3A1DD1861FE0ACF CRC64;
MAANINNAAA WLTEAKAHPF QVKEAPSYTP EENEILVKNH AVAINPVDGS LQSKAWWPMN
YPTILGQDVA GEVVQVGPNV ARFQPGDRVV GHAVGMATKR LQDNAFQAYT ILQTNMASQL
PSEISYEDAA VLPLGLSTAA SGLFQDDVGS NAIQLGVAAG YEVFTTASPK NFDYVKELGA
SQVFDYHSAT VAQDLVAALQ GKTVAGAMDC IGFAATPLTV EVVSKSQGVK FVSTVKGGFQ
APEGVTVKSV FGTTIKDNQV GKAIYEDYLP KALKAGSFIP APVALVAGKG LESVQAAVDL
QAQGTSAQKV VVSL
