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IPI1_EMENI
ID   IPI1_EMENI              Reviewed;         375 AA.
AC   Q5ASR2; C8VA53;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Pre-rRNA-processing protein ipi1;
GN   Name=ipi1; ORFNames=AN8668;
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).
CC   -!- FUNCTION: Component of the RIX1 complex required for processing of ITS2
CC       sequences from 35S pre-rRNA. {ECO:0000250|UniProtKB:P38803}.
CC   -!- SUBUNIT: Component of the RIX1 complex, composed of ipi1, rix1/ipi2 and
CC       ipi3 in a 1:2:2 stoichiometry. The complex interacts (via rix1) with
CC       mdn1 (via its hexameric AAA ATPase ring) and the pre-60S ribosome
CC       particles. {ECO:0000250|UniProtKB:P38803}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P38803}.
CC   -!- SIMILARITY: Belongs to the IPI1/TEX10 family. {ECO:0000305}.
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DR   EMBL; AACD01000158; EAA60702.1; -; Genomic_DNA.
DR   EMBL; BN001303; CBF78219.1; -; Genomic_DNA.
DR   RefSeq; XP_681937.1; XM_676845.1.
DR   AlphaFoldDB; Q5ASR2; -.
DR   SMR; Q5ASR2; -.
DR   STRING; 162425.CADANIAP00006377; -.
DR   EnsemblFungi; CBF78219; CBF78219; ANIA_08668.
DR   EnsemblFungi; EAA60702; EAA60702; AN8668.2.
DR   GeneID; 2868483; -.
DR   KEGG; ani:AN8668.2; -.
DR   VEuPathDB; FungiDB:AN8668; -.
DR   eggNOG; KOG2149; Eukaryota.
DR   HOGENOM; CLU_050252_2_0_1; -.
DR   InParanoid; Q5ASR2; -.
DR   OMA; CAGGWVK; -.
DR   OrthoDB; 1145058at2759; -.
DR   Proteomes; UP000000560; Chromosome III.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0097344; C:Rix1 complex; IBA:GO_Central.
DR   GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR024679; Ipi1_N.
DR   InterPro; IPR037947; TEX10/Ipi1.
DR   PANTHER; PTHR16056:SF2; PTHR16056:SF2; 1.
DR   Pfam; PF12333; Ipi1_N; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   3: Inferred from homology;
KW   Nucleus; Reference proteome; Ribosome biogenesis; rRNA processing.
FT   CHAIN           1..375
FT                   /note="Pre-rRNA-processing protein ipi1"
FT                   /id="PRO_0000308720"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          208..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..33
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..229
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   375 AA;  40062 MW;  F7D56A8DAE7D0E6D CRC64;
     MGASTKRKKE KQKDFQKPKL KVGKAKAKPD NFTDTSFKSK AITLNQQSLT LTAPSANTQF
     SHHLSLLSSK SDSQRRDSLA HLTTTLTSQP THLPPPQPVS VILPSLLPLI LDSNASVRAN
     LLKLLRALPQ HDVKDHVGTL MPYIRAGMTH LAAEVRVSSV EVLGWLVSIA GDEVVGVAGG
     WVKTLNCFLS VLGWHVAAKS KWTSLATSTS TSASGSGNGT GSSTSGKASY GKAGAKGRPQ
     VRFLTILADF LDAGIGSSGS QSMDTTADSA SESENQYCTF PITTFASHLI PSNFASPYLT
     LNLFGTPRDE EGEMYETRED RWRVFVARGF LGAVERGLET ARGEGGEVGR VSALAAKVLR
     NARDDLEGDG FGDEL
 
 
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