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Database: UniProt
Entry: A0A1X0NZK1_9TRYP
LinkDB: A0A1X0NZK1_9TRYP
Original site: A0A1X0NZK1_9TRYP 
ID   A0A1X0NZK1_9TRYP        Unreviewed;       863 AA.
AC   A0A1X0NZK1;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ORC89639.1};
GN   ORFNames=TM35_000111730 {ECO:0000313|EMBL:ORC89639.1};
OS   Trypanosoma theileri.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=67003 {ECO:0000313|EMBL:ORC89639.1, ECO:0000313|Proteomes:UP000192257};
RN   [1] {ECO:0000313|EMBL:ORC89639.1, ECO:0000313|Proteomes:UP000192257}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Edinburgh {ECO:0000313|EMBL:ORC89639.1};
RA   Kelly S., Ivens A., Mott A., O'Neill E., Emms D., Macleod O., Voorheis P.,
RA   Matthews J., Matthews K., Carrington M.;
RT   "An alternative strategy for trypanosome survival in the mammalian
RT   bloodstream revealed through genome and transcriptome analysis of the
RT   ubiquitous bovine parasite Trypanosoma (Megatrypanum) theileri.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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:ORC89639.1}.
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DR   EMBL; NBCO01000011; ORC89639.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X0NZK1; -.
DR   STRING; 67003.A0A1X0NZK1; -.
DR   VEuPathDB; TriTrypDB:TM35_000111730; -.
DR   OrthoDB; 167616at2759; -.
DR   Proteomes; UP000192257; 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; SSF64518; Phase 1 flagellin; 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:UP000192257};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          370..586
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          607..699
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          707..723
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50868"
FT   REGION          63..255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          743..863
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        63..165
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..198
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        199..244
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        743..765
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        767..855
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   863 AA;  93082 MW;  52E47802CDB8B773 CRC64;
     MFTFSMRRQG VVAVGSWTSP ASAVSLLRGP FHHYHLNNSG VFSLMILAPQ CWARRYRASQ
     ATLTSSSRNS TGTRHHGNAG NASSSHTSVT SVSAGNGNSN SNGVSGGNHS SVAHTSGGNV
     GTGSTTTHSH SSGGNGNNNN NNNNNSGGNG NGGSSHNSSS GGGGGVSMAQ AAKKKKNTRK
     VLKRTTVLKK KKRIKKVLSS TKVSSPSGAT TLSRTTTAAS TGTGSTNVSS ATTSSTNSTT
     TKTTSSHRLR RKTITKKPTP KFRICVLNSS YEGADSVTAD VDNYHCSPAH WVKDKKQFAF
     TEVSVKKNDS YRQIRELVTS NKFDVFFNLC DGGRDEKRAG VDVVEALEEH NAAFTGTDSH
     SFEPSKIDMK LLVGAAGVNT PNFVLLESAE GLAKKCRHLR FPVIVKHLSG YASVGIHKDN
     RCDTLEELKT KVPKFLKEFN HALIEEFIRG REGTVLTCAD SGSQFGVKVF KPLMFKFLQG
     DDDFAYFEKK WSMECNDEAY DFLPHNDPAY PQVVDMARNA FKHIMNGVGY GRVDFRIDPK
     GDVYFLEINP NCGMWYSEKD GGDFADVMVQ GDKSWNHDRF IRNAVLRAVR EQVARRPWYF
     ISHDSKGNFS TRASKTVRAG KGLFCDAAHP VPVIAQALYK LGEEDPTVGC VIMRGDRLHQ
     AVAIRHSCEP NMQFMQGRTL TLVAKRKINV GEELTVDYAT LCDENMPAFA CSCGTSNCRS
     VIFPAPPTPR TLEGKNVRQM MREKKKAWYK EKEDREAERM LKKRASKGKN NSNNSGNNSN
     GGSGAGTGSG NNSSSSGNST NSNNNNNNVS SYSSSSSSAS SSGANGSMTS GVSARGNNAQ
     TNNNVNNNTG SGEGATKGVS GRR
//
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