ID Q4CUZ7_TRYCC Unreviewed; 789 AA.
AC Q4CUZ7;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=ATP-grasp domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=Tc00.1047053508267.10 {ECO:0000313|EMBL:EAN84094.1};
OS Trypanosoma cruzi (strain CL Brener).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=353153 {ECO:0000313|EMBL:EAN84094.1, ECO:0000313|Proteomes:UP000002296};
RN [1] {ECO:0000313|EMBL:EAN84094.1, ECO:0000313|Proteomes:UP000002296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL Brener {ECO:0000313|EMBL:EAN84094.1,
RC ECO:0000313|Proteomes:UP000002296};
RX PubMed=16020725; DOI=10.1126/science.1112631;
RA El-Sayed N.M., Myler P.J., Bartholomeu D.C., Nilsson D., Aggarwal G.,
RA Tran A.N., Ghedin E., Worthey E.A., Delcher A.L., Blandin G.,
RA Westenberger S.J., Caler E., Cerqueira G.C., Branche C., Haas B.,
RA Anupama A., Arner E., Aslund L., Attipoe P., Bontempi E., Bringaud F.,
RA Burton P., Cadag E., Campbell D.A., Carrington M., Crabtree J., Darban H.,
RA da Silveira J.F., de Jong P., Edwards K., Englund P.T., Fazelina G.,
RA Feldblyum T., Ferella M., Frasch A.C., Gull K., Horn D., Hou L., Huang Y.,
RA Kindlund E., Klingbeil M., Kluge S., Koo H., Lacerda D., Levin M.J.,
RA Lorenzi H., Louie T., Machado C.R., McCulloch R., McKenna A., Mizuno Y.,
RA Mottram J.C., Nelson S., Ochaya S., Osoegawa K., Pai G., Parsons M.,
RA Pentony M., Pettersson U., Pop M., Ramirez J.L., Rinta J., Robertson L.,
RA Salzberg S.L., Sanchez D.O., Seyler A., Sharma R., Shetty J., Simpson A.J.,
RA Sisk E., Tammi M.T., Tarleton R., Teixeira S., Van Aken S., Vogt C.,
RA Ward P.N., Wickstead B., Wortman J., White O., Fraser C.M., Stuart K.D.,
RA Andersson B.;
RT "The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas
RT disease.";
RL Science 309:409-415(2005).
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC {ECO:0000256|ARBA:ARBA00010871}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAN84094.1}.
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; AAHK01001795; EAN84094.1; -; Genomic_DNA.
DR RefSeq; XP_805945.1; XM_800852.1.
DR AlphaFoldDB; Q4CUZ7; -.
DR SMR; Q4CUZ7; -.
DR STRING; 353153.Q4CUZ7; -.
DR PaxDb; 353153-Q4CUZ7; -.
DR EnsemblProtists; EAN84094; EAN84094; Tc00.1047053508267.10.
DR GeneID; 3535843; -.
DR KEGG; tcr:508267.10; -.
DR eggNOG; ENOG502RFSY; Eukaryota.
DR InParanoid; Q4CUZ7; -.
DR OMA; RANCGHA; -.
DR OrthoDB; 167616at2759; -.
DR Proteomes; UP000002296; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR011095; Dala_Dala_lig_C.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR PANTHER; PTHR23132; D-ALANINE--D-ALANINE LIGASE; 1.
DR PANTHER; PTHR23132:SF28; PROTEIN WITH D-ALANINE--D-ALANINE LIGASE C-TERMINAL DOMAIN; 1.
DR Pfam; PF07478; Dala_Dala_lig_C; 1.
DR Pfam; PF00856; SET; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50280; SET; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000002296};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 341..557
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 567..670
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 678..694
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 46..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..168
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..736
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..789
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 789 AA; 85333 MW; 694F6EF6499A864B CRC64;
MLRLALQRSG VAIAACYAVP SAAMCGTAWS AMMVTAARAA RFESRRYKAS SAPATTPQKS
AGSSRGHGSG TSHAGSGQVT GSPSTAGHLS GNSSHNGATA SMTVSHASGT NNNNSNNSNV
CNSGGSDGGG SSGGGNGNMN NSGGVSWLRR KKQTKKVLKR KAGLKKKQVK KSVSVANTAS
AHIGGGASRN AASGGANTTS STTPTVTASR AVNSRRIKRK LEPKKKKMAT PKLRVCVLNS
SYEGSDSVTA DIDNYHCSPA HWVKDKKRYT FTEVSLRKSE SYLRVRELVT SNNFDVFFNL
CDGGKDEKRA GVEVVEALEE HNAAFTGTDS HSFEPSKIDM KLLVGAAGVN TPNFVLLEST
EGLAKKCRHL RFPVIVKHLS GYASVGIHKD NRCDTLDELK VKVRAFLAEF NHALVEEFIR
GREGTVLACA DRGSLFGVKV FKPLMFKFLQ NDDDFAYFEK KWTMECNENA YSFLPHNDPA
YPQIIDTARN AFRHIMNGVG YGRVDFRIDP KGDVYFLEIN PNCGMWYNQK DGGDFADVMV
QGDKSWDHDR FIRNAIIRAV REQAARRPWY FISHDSKGNF STRASKTVRA GKSLFSDAIH
PIPVVAQALY KLGEEDPTVG CVILRGDRPH QAVAIRHSCE PNMQFMQGRT LTLVSKRRIN
VGEELTVDYA TLCDENMPPF ACSCGTSNCR SVIFPSAPTP RTLEGKNIRQ MLREKKKAWY
KEKEDREAER ILKKRASKGK GNSGSSASSP SSSPSVSSTS AAGVSSNAAT GVNGSSNSGS
VAHGINSKK
//