ID E3JRP5_PUCGT Unreviewed; 352 AA.
AC E3JRP5;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 2.
DT 03-MAY-2023, entry version 68.
DE RecName: Full=CMP/dCMP-type deaminase domain-containing protein {ECO:0000259|PROSITE:PS51747};
GN ORFNames=PGTG_00494 {ECO:0000313|EMBL:EFP74538.2};
OS Puccinia graminis f. sp. tritici (strain CRL 75-36-700-3 / race SCCL)
OS (Black stem rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=418459 {ECO:0000313|EMBL:EFP74538.2, ECO:0000313|Proteomes:UP000008783};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CRL 75-36-700-3;
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Cuomo C., Jaffe D.,
RA Butler J., Alvarez P., Gnerre S., Grabherr M., Mauceli E., Brockman W.,
RA Young S., LaButti K., Sykes S., DeCaprio D., Crawford M., Koehrsen M.,
RA Engels R., Montgomery P., Pearson M., Howarth C., Larson L., White J.,
RA Zeng Q., Kodira C., Yandava C., Alvarado L., O'Leary S., Szabo L., Dean R.,
RA Schein J.;
RT "The Genome Sequence of Puccinia graminis f. sp. tritici Strain CRL 75-36-
RT 700-3.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000008783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRL 75-36-700-3 / race SCCL
RC {ECO:0000313|Proteomes:UP000008783};
RX PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA Grigoriev I.V., Szabo L.J., Martin F.;
RT "Obligate biotrophy features unraveled by the genomic analysis of rust
RT fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS178262; EFP74538.2; -; Genomic_DNA.
DR RefSeq; XP_003307544.2; XM_003307496.2.
DR AlphaFoldDB; E3JRP5; -.
DR STRING; 418459.E3JRP5; -.
DR EnsemblFungi; EFP74538; EFP74538; PGTG_00494.
DR GeneID; 10546499; -.
DR KEGG; pgr:PGTG_00494; -.
DR VEuPathDB; FungiDB:PGTG_00494; -.
DR HOGENOM; CLU_787870_0_0_1; -.
DR InParanoid; E3JRP5; -.
DR OrthoDB; 3626893at2759; -.
DR Proteomes; UP000008783; Unassembled WGS sequence.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0052717; F:tRNA-specific adenosine-34 deaminase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:InterPro.
DR GO; GO:0002100; P:tRNA wobble adenosine to inosine editing; IBA:GO_Central.
DR CDD; cd01285; nucleoside_deaminase; 1.
DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR Gene3D; 1.10.400.10; GI Alpha 1, domain 2-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR InterPro; IPR001019; Gprotein_alpha_su.
DR InterPro; IPR011025; GproteinA_insert.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11079; CYTOSINE DEAMINASE FAMILY MEMBER; 1.
DR PANTHER; PTHR11079:SF149; TRNA-SPECIFIC ADENOSINE DEAMINASE 2; 1.
DR Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR Pfam; PF00503; G-alpha; 1.
DR SMART; SM00275; G_alpha; 1.
DR SUPFAM; SSF53927; Cytidine deaminase-like; 1.
DR SUPFAM; SSF47895; Transducin (alpha subunit), insertion domain; 1.
DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE 4: Predicted;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008783};
KW Transducer {ECO:0000256|ARBA:ARBA00023224};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 178..292
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 352 AA; 39432 MW; 4450C39724619CEF CRC64;
MAQNVSSNRS SGKTTPLKQM EITHNRGGLT PSQREHYRQQ VFGKICEGMR LCLELMNKED
IELENADLMK FVPMFNHCVN LEPRQPFPHE YLEPLSLLCG DGGIKKALDS GNNSVLLENM
KYFFPELDRL FQPSYVPTDL DILHCEGKTC QGKATGKTET TMIDQSKLRM IDRSQQNLSD
LLLMDQAIEM ANEALVANEI PVGCVLVSKT TDKVLSKGRN RTNETKNACL HAEFDAIGGL
HSVTPADKID WNDVKLYVTV EPCLMCSSAL RQIGINLVYF GCSNDRFGGC GGVVSIHNDP
RLIHSQPLTA LGGYRREDAI ILLRKFYITE NTNAPVPKKK TNRVLKMEIP DL
//
