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Database: UniProt
Entry: A0CRF7_PARTE
LinkDB: A0CRF7_PARTE
Original site: A0CRF7_PARTE 
ID   A0CRF7_PARTE            Unreviewed;       501 AA.
AC   A0CRF7;
DT   28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   SubName: Full=Chromosome undetermined scaffold_25, whole genome shotgun sequence {ECO:0000313|EMBL:CAK73374.1};
GN   ORFNames=GSPATT00009689001 {ECO:0000313|EMBL:CAK73374.1};
OS   Paramecium tetraurelia.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX   NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK73374.1, ECO:0000313|Proteomes:UP000000600};
RN   [1] {ECO:0000313|EMBL:CAK73374.1, ECO:0000313|Proteomes:UP000000600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK73374.1,
RC   ECO:0000313|Proteomes:UP000000600};
RX   PubMed=17086204; DOI=10.1038/nature05230;
RG   Genoscope;
RA   Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA   Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA   Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA   Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA   Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA   Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA   Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA   Cohen J., Wincker P.;
RT   "Global trends of whole-genome duplications revealed by the ciliate
RT   Paramecium tetraurelia.";
RL   Nature 444:171-178(2006).
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DR   EMBL; CT868152; CAK73374.1; -; Genomic_DNA.
DR   RefSeq; XP_001440771.1; XM_001440734.1.
DR   AlphaFoldDB; A0CRF7; -.
DR   STRING; 5888.A0CRF7; -.
DR   EnsemblProtists; CAK73374; CAK73374; GSPATT00009689001.
DR   GeneID; 5026556; -.
DR   KEGG; ptm:GSPATT00009689001; -.
DR   eggNOG; KOG2550; Eukaryota.
DR   HOGENOM; CLU_022552_2_1_1; -.
DR   InParanoid; A0CRF7; -.
DR   OMA; GSHCTTR; -.
DR   Proteomes; UP000000600; Partially assembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0003938; F:IMP dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0006183; P:GTP biosynthetic process; IBA:GO_Central.
DR   CDD; cd04601; CBS_pair_IMPDH; 1.
DR   CDD; cd00381; IMPDH; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000644; CBS_dom.
DR   InterPro; IPR046342; CBS_dom_sf.
DR   InterPro; IPR005990; IMP_DH.
DR   InterPro; IPR001093; IMP_DH_GMPRt.
DR   PANTHER; PTHR11911:SF122; GMP REDUCTASE; 1.
DR   PANTHER; PTHR11911; INOSINE-5-MONOPHOSPHATE DEHYDROGENASE RELATED; 1.
DR   Pfam; PF00571; CBS; 1.
DR   Pfam; PF00478; IMPDH; 1.
DR   PIRSF; PIRSF000130; IMPDH; 1.
DR   SMART; SM01240; IMPDH; 1.
DR   SUPFAM; SSF54631; CBS-domain pair; 1.
DR   SUPFAM; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 1.
DR   PROSITE; PS51371; CBS; 1.
PE   4: Predicted;
KW   CBS domain {ECO:0000256|ARBA:ARBA00023122, ECO:0000256|PROSITE-
KW   ProRule:PRU00703}; NAD {ECO:0000256|PIRSR:PIRSR000130-3};
KW   Potassium {ECO:0000256|PIRSR:PIRSR000130-4};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000600}.
FT   DOMAIN          179..239
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   ACT_SITE        329
FT                   /note="Thioimidate intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000130-1"
FT   ACT_SITE        424
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000130-1"
FT   BINDING         273..275
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000130-3"
FT   BINDING         322..324
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000130-3"
FT   BINDING         324
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_note="ligand shared between two tetrameric
FT                   partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000130-4"
FT   BINDING         326
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_note="ligand shared between two tetrameric
FT                   partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000130-4"
FT   BINDING         329
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_note="ligand shared between two tetrameric
FT                   partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000130-4"
SQ   SEQUENCE   501 AA;  54834 MW;  0A3617F981535A3A CRC64;
     MLSSNWRNGI QTALTFDDVL MVPQYSTIES RTNCIVETHC SQNIKLKIPF ISSPMDTVTE
     TEMAIHMAAN GGLGVIHRFM TANEQVEQIK KVKRSEAYIK NRPFVVGLNY TLKKVLILAE
     EWKCKTFLVT DDNLIENNED YEETDETGSP RYKSLPLLGI ITNRDCYEQP LTKLVKELMT
     PREKLVTLHY LDVSKENARQ MMLSHKLEKL PVVDDKNNIK GLINLKDLKL DSELKVLDQM
     GRLIVGGAVG ANDDEITRAK RLVNSGCDVI VLDVANGHSQ LAIRTVEQLK KEVSVDVIAG
     SIATGDGARR LIQAGADGIR CGIGNGSICI TRVVSGCGVP QFSALMDVAP VCKEYKIPLM
     SDGGNKNSGN MCKALAVGAD CIMLGRLLAG CQESPSKEIY REGKILKVYR GMAGFGANVS
     KAQRTGKDEP SSTTFAPEGV EGYIPFAGKV SIVLEQFKKG IQSGMSYCGA SNIEELQKNV
     QFIQMTNAGF VESGVHGITK I
//
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