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Conserved domains on  [gi|496169756|ref|WP_008894263|]
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TIGR00269 family protein [Haloterrigena salina]

Protein Classification

tRNA 2-thiolation protein( domain architecture ID 18932641)

tRNA 2-thiolation protein is a nucleotide alpha hydrolase (AANH) superfamily protein that directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation; such as cytoplasmic tRNA 2-thiolation protein 1

CATH:  3.40.50.620
EC:  2.7.7.-
Gene Ontology:  GO:0000049|GO:0034227|GO:0016779
PubMed:  12012333|18391219
SCOP:  3001593

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CTU1-like cd01713
cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human ...
 46-248 1.28e-88

cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human cytoplasmic tRNA 2-thiolation protein 1, also called cytosolic thiouridylase subunit 1 (CTU1), ATP-binding domain-containing protein 3 (ATPBD3), cancer-associated gene protein, or cytoplasmic tRNA adenylyltransferase 1. CTU1 plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). It directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. The CTU1-like subfamily belongs to the nucleotide alpha hydrolase (AANH) superfamily that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.


:

Pssm-ID: 467486  Cd Length: 208  Bit Score: 263.68  E-value: 1.28e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496169756  46 RDATPENPQTWVIGLSGGKDSVVLTQILHDTFAE-DPRIELVGLTIHEGIEGYRDKSIDACVELADDLGIRHELVSYEEE 124
Cdd:cd01713   11 KYRLIKPGDRVAVGLSGGKDSTVLLYVLKELNKRhDYGVELIAVTIDEGIKGYRDDSLEAARKLAEEYGIPLEIVSFEDE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496169756 125 FGVRMDDVVEDDPENMAACAYCGVFRRDLLEKYAEKLEADLLLTGHNLDDEAQTALMNFLEGDVEQIakhfdaSLGALSE 204
Cdd:cd01713   91 FGFTLDELIVGKGGKKNACTYCGVFRRRALNRGARELGADKLATGHNLDDEAETILMNLLRGDVARL------LRTGPEP 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 496169756 205 REEQGEFVPRAKPLRDVPEKEVALYAHVNDLPAHITECPHASEA 248
Cdd:cd01713  165 RSEGEGLVPRIKPLRYIPEKEIVLYAHLNGLPYFSTECPYAPEA 208
TIGR00269 super family cl42867
TIGR00269 family protein; [Hypothetical proteins, Conserved]
 212-318 2.08e-28

TIGR00269 family protein; [Hypothetical proteins, Conserved]


The actual alignment was detected with superfamily member TIGR00269:

Pssm-ID: 129370 [Multi-domain]  Cd Length: 104  Bit Score: 105.66  E-value: 2.08e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496169756  212 VPRAKPLRDVPEKEVALYAHVNDLPAHITECPHASEAYRGEIQQLLYDLEENHPGTRHSILAGYEDLAAIAADEFsgdDG 291
Cdd:TIGR00269   1 VPRIKPLRYIPEKEVVLYAFLNELKVHLDECPYSSLSVRARIRDFLYDLENKKPGVKFSVLRGFEKLIPLLKELS---EQ 77

                          90       100
                  ....*....|....*....|....*..
gi 496169756  292 ADLRECAECGSTTTREICRKCSLLESL 318
Cdd:TIGR00269  78 EDLRRCERCGEPTSGRICKACKFLEEL 104
 
Name Accession Description Interval E-value
CTU1-like cd01713
cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human ...
 46-248 1.28e-88

cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human cytoplasmic tRNA 2-thiolation protein 1, also called cytosolic thiouridylase subunit 1 (CTU1), ATP-binding domain-containing protein 3 (ATPBD3), cancer-associated gene protein, or cytoplasmic tRNA adenylyltransferase 1. CTU1 plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). It directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. The CTU1-like subfamily belongs to the nucleotide alpha hydrolase (AANH) superfamily that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.


Pssm-ID: 467486  Cd Length: 208  Bit Score: 263.68  E-value: 1.28e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496169756  46 RDATPENPQTWVIGLSGGKDSVVLTQILHDTFAE-DPRIELVGLTIHEGIEGYRDKSIDACVELADDLGIRHELVSYEEE 124
Cdd:cd01713   11 KYRLIKPGDRVAVGLSGGKDSTVLLYVLKELNKRhDYGVELIAVTIDEGIKGYRDDSLEAARKLAEEYGIPLEIVSFEDE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496169756 125 FGVRMDDVVEDDPENMAACAYCGVFRRDLLEKYAEKLEADLLLTGHNLDDEAQTALMNFLEGDVEQIakhfdaSLGALSE 204
Cdd:cd01713   91 FGFTLDELIVGKGGKKNACTYCGVFRRRALNRGARELGADKLATGHNLDDEAETILMNLLRGDVARL------LRTGPEP 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 496169756 205 REEQGEFVPRAKPLRDVPEKEVALYAHVNDLPAHITECPHASEA 248
Cdd:cd01713  165 RSEGEGLVPRIKPLRYIPEKEIVLYAHLNGLPYFSTECPYAPEA 208
TilS COG0037
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ...
 51-283 4.84e-55

tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA(Ile)-lysidine synthase TilS/MesJ is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439807 [Multi-domain]  Cd Length: 235  Bit Score: 178.87  E-value: 4.84e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496169756  51 ENPQTWVIGLSGGKDSVVLTQILHDtFAEDPRIELVGLTIHEGIEGYRDKSIDACVELADDLGIRHELVSYEEEFgvrmd 130
Cdd:COG0037   13 EPGDRILVAVSGGKDSLALLHLLAK-LRRRLGFELVAVHVDHGLREESDEDAEFVAELCEELGIPLHVVRVDVPA----- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496169756 131 dVVEDDPENMaaCAYCGVFRRDLLEKYAEKLEADLLLTGHNLDDEAQTALMNFLEGDveQIakhfdASLGALSEREEQGe 210
Cdd:COG0037   87 -IAKKEGKSP--EAAARRARYGALYELARELGADKIATGHHLDDQAETFLLNLLRGS--GL-----AGLAGMPPSRGGG- 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496169756 211 fVPRAKPLRDVPEKEVALYAHVNDLPAHITECPHASEAYRGEI-QQLLYDLEENHPGTRHSILAGYEDLAAIAA 283
Cdd:COG0037  156 -VRLIRPLLYVSRKEIEAYAKENGLPWIEDPCNYDPRYTRNRIrHLVLPELEERNPGFKENLARSAENLAEEED 228
TIGR00269 TIGR00269
TIGR00269 family protein; [Hypothetical proteins, Conserved]
 212-318 2.08e-28

TIGR00269 family protein; [Hypothetical proteins, Conserved]


Pssm-ID: 129370 [Multi-domain]  Cd Length: 104  Bit Score: 105.66  E-value: 2.08e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496169756  212 VPRAKPLRDVPEKEVALYAHVNDLPAHITECPHASEAYRGEIQQLLYDLEENHPGTRHSILAGYEDLAAIAADEFsgdDG 291
Cdd:TIGR00269   1 VPRIKPLRYIPEKEVVLYAFLNELKVHLDECPYSSLSVRARIRDFLYDLENKKPGVKFSVLRGFEKLIPLLKELS---EQ 77

                          90       100
                  ....*....|....*....|....*..
gi 496169756  292 ADLRECAECGSTTTREICRKCSLLESL 318
Cdd:TIGR00269  78 EDLRRCERCGEPTSGRICKACKFLEEL 104
lysidine_TilS_N TIGR02432
tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble ...
 57-236 1.82e-18

tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble position of a tRNA must discriminate between G and A of mRNA are AUA (Ile) vs. AUG (Met) and UGA (stop) vs. UGG (Trp). In all bacteria, the wobble position of the tRNA(Ile) recognizing AUA is lysidine, a lysine derivative of cytidine. This family describes a protein domain found, apparently, in all bacteria in a single copy. Eukaryotic sequences appear to be organellar. The domain archictecture of this protein family is variable; some, including characterized proteins of E. coli and B. subtilis known to be tRNA(Ile)-lysidine synthetase, include a conserved 50-residue domain that many other members lack. This protein belongs to the ATP-binding PP-loop family ( pfam01171). It appears in the literature and protein databases as TilS, YacA, and putative cell cycle protein MesJ (a misnomer). [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274129 [Multi-domain]  Cd Length: 189  Bit Score: 81.52  E-value: 1.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496169756   57 VIGLSGGKDSVVLTQILHDtFAEDPRIELVGLTIHEGIEGYRDKSIDACVELADDLGIRHELVSYeeefgvrmdDVVEDD 136
Cdd:TIGR02432   3 LVAVSGGVDSMALLHLLLK-LQPKIKIKLIAAHVDHGLRPESDEEAEFVQQFCRKLNIPLEIKKV---------DVKALA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496169756  137 PEN-----MAACAycgvFRRDLLEKYAEKLEADLLLTGHNLDDEAQTALMNFLEGdveqiaKHFD--ASLGALSEREEQG 209
Cdd:TIGR02432  73 KGKkknleEAARE----ARYDFFEEIAKKHGADYILTAHHADDQAETILMRLLRG------SGLRglSGMKPIRILGSGI 142

                         170       180
                  ....*....|....*....|....*..
gi 496169756  210 EFVpraKPLRDVPEKEVALYAHVNDLP 236
Cdd:TIGR02432 143 QII---RPLLGISKSEIEEYLKENGLP 166
PRK10696 PRK10696
tRNA 2-thiocytidine biosynthesis protein TtcA; Provisional
 55-272 9.56e-17

tRNA 2-thiocytidine biosynthesis protein TtcA; Provisional


Pssm-ID: 236737 [Multi-domain]  Cd Length: 258  Bit Score: 78.36  E-value: 9.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496169756  55 TWVIGLSGGKDSVVLTQILHDTFAEDP-RIELVGLTIHEGIEGYRDKSIDACVEladDLGIRHELVsYEEEFGVrmddVV 133
Cdd:PRK10696  31 RVMVCLSGGKDSYTLLDILLNLQKRAPiNFELVAVNLDQKQPGFPEHVLPEYLE---SLGVPYHIE-EQDTYSI----VK 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496169756 134 EDDPENMAACAYCGVFRRDLLEKYAEKLEADLLLTGHNLDDEAQTALMNFLegdveqiakhFDASLGALSE--REEQGE- 210
Cdd:PRK10696 103 EKIPEGKTTCSLCSRLRRGILYRTARELGATKIALGHHRDDILETLFLNMF----------YGGKLKAMPPklLSDDGKh 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496169756 211 FVPRakPLRDVPEKEVALYAHVNDLPAHITECPHASE-AYRGEIQQLLYDLEENHPGTRHSIL 272
Cdd:PRK10696 173 IVIR--PLAYVAEKDIIKFAEAKEFPIIPCNLCGSQEnLQRQVVKEMLRDWEKEYPGRIETMF 233
ATP_bind_3 pfam01171
PP-loop family; This family of proteins belongs to the PP-loop superfamily.
 58-236 4.11e-13

PP-loop family; This family of proteins belongs to the PP-loop superfamily.


Pssm-ID: 426097 [Multi-domain]  Cd Length: 178  Bit Score: 66.50  E-value: 4.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496169756   58 IGLSGGKDSVVLTQILHDtFAEDPRIELVGLTIHEGIEGYRDKSIDACVELADDLGIRHELVSYeeefgvrmdDVVEDDP 137
Cdd:pfam01171   1 VAVSGGPDSMALLYLLAK-LKIKLGIELTAAHVNHGLREESDREAEHVQALCRQLGIPLEILRV---------DVAKKSG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496169756  138 ENMAACAYcgVFRRDLLEKYAEKLEADLLLTGHNLDDEAQTALMNFLEGDveqiakhFDASLGALSEREEQGEfVPRAKP 217
Cdd:pfam01171  71 ENLEAAAR--EARYDFFEEALKKHGADVLLTAHHLDDQLETFLMRLKRGS-------GLAGLAGIPPVREFAG-GRIIRP 140

                         170
                  ....*....|....*....
gi 496169756  218 LRDVPEKEVALYAHVNDLP 236
Cdd:pfam01171 141 LLKVSKAEIEAYAKEHKIP 159
 
Name Accession Description Interval E-value
CTU1-like cd01713
cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human ...
 46-248 1.28e-88

cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human cytoplasmic tRNA 2-thiolation protein 1, also called cytosolic thiouridylase subunit 1 (CTU1), ATP-binding domain-containing protein 3 (ATPBD3), cancer-associated gene protein, or cytoplasmic tRNA adenylyltransferase 1. CTU1 plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). It directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. The CTU1-like subfamily belongs to the nucleotide alpha hydrolase (AANH) superfamily that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.


Pssm-ID: 467486  Cd Length: 208  Bit Score: 263.68  E-value: 1.28e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496169756  46 RDATPENPQTWVIGLSGGKDSVVLTQILHDTFAE-DPRIELVGLTIHEGIEGYRDKSIDACVELADDLGIRHELVSYEEE 124
Cdd:cd01713   11 KYRLIKPGDRVAVGLSGGKDSTVLLYVLKELNKRhDYGVELIAVTIDEGIKGYRDDSLEAARKLAEEYGIPLEIVSFEDE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496169756 125 FGVRMDDVVEDDPENMAACAYCGVFRRDLLEKYAEKLEADLLLTGHNLDDEAQTALMNFLEGDVEQIakhfdaSLGALSE 204
Cdd:cd01713   91 FGFTLDELIVGKGGKKNACTYCGVFRRRALNRGARELGADKLATGHNLDDEAETILMNLLRGDVARL------LRTGPEP 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 496169756 205 REEQGEFVPRAKPLRDVPEKEVALYAHVNDLPAHITECPHASEA 248
Cdd:cd01713  165 RSEGEGLVPRIKPLRYIPEKEIVLYAHLNGLPYFSTECPYAPEA 208
TilS COG0037
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ...
 51-283 4.84e-55

tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA(Ile)-lysidine synthase TilS/MesJ is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439807 [Multi-domain]  Cd Length: 235  Bit Score: 178.87  E-value: 4.84e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496169756  51 ENPQTWVIGLSGGKDSVVLTQILHDtFAEDPRIELVGLTIHEGIEGYRDKSIDACVELADDLGIRHELVSYEEEFgvrmd 130
Cdd:COG0037   13 EPGDRILVAVSGGKDSLALLHLLAK-LRRRLGFELVAVHVDHGLREESDEDAEFVAELCEELGIPLHVVRVDVPA----- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496169756 131 dVVEDDPENMaaCAYCGVFRRDLLEKYAEKLEADLLLTGHNLDDEAQTALMNFLEGDveQIakhfdASLGALSEREEQGe 210
Cdd:COG0037   87 -IAKKEGKSP--EAAARRARYGALYELARELGADKIATGHHLDDQAETFLLNLLRGS--GL-----AGLAGMPPSRGGG- 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496169756 211 fVPRAKPLRDVPEKEVALYAHVNDLPAHITECPHASEAYRGEI-QQLLYDLEENHPGTRHSILAGYEDLAAIAA 283
Cdd:COG0037  156 -VRLIRPLLYVSRKEIEAYAKENGLPWIEDPCNYDPRYTRNRIrHLVLPELEERNPGFKENLARSAENLAEEED 228
TtuA-like cd01993
tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins; tRNA-5-methyluridine(54) ...
 58-248 1.66e-38

tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins; tRNA-5-methyluridine(54) 2-sulfurtransferase, also called tRNA thiouridine synthetase TtuA, catalyzes the ATP-dependent 2-thiolation of 5-methyluridine residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2-thiouridine (m(5)s(2)U or s(2)T). TtuA belongs to the adenine nucleotide alpha hydrolase superfamily (AANH) that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. This domain has a strongly conserved motif SGGKD at the N-terminus.


Pssm-ID: 467497 [Multi-domain]  Cd Length: 190  Bit Score: 134.76  E-value: 1.66e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496169756  58 IGLSGGKDSVVLTQILHDTFaedprIELVGLTIHEGIEGYRDKSIDACVELADDLGIRHELVSYEEEFGVRMDDVVEDdp 137
Cdd:cd01993   13 VAVSGGKDSLALLAVLKKLG-----YNVEALYINLGIGEYSEKSEEVVKKLAEKLNLPLHVVDLKEEYGLGIPELAKK-- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496169756 138 ENMAACAYCGVFRRDLLEKYAEKLEADLLLTGHNLDDEAQTALMNFLEGDVEQIAKHFDASLgalserEEQGEFVPRAKP 217
Cdd:cd01993   86 SRRPPCSVCGLVKRYIMNKFAVENGFDVVATGHNLDDEAAFLLGNILNWNEEYLAKQGPFLL------PEHGGLVTRVKP 159

                        170       180       190
                 ....*....|....*....|....*....|.
gi 496169756 218 LRDVPEKEVALYAHVNDLPAHITECPHASEA 248
Cdd:cd01993  160 LYEITEEEIALYALLNGIPYLEEECPYAEGA 190
TIGR00269 TIGR00269
TIGR00269 family protein; [Hypothetical proteins, Conserved]
 212-318 2.08e-28

TIGR00269 family protein; [Hypothetical proteins, Conserved]


Pssm-ID: 129370 [Multi-domain]  Cd Length: 104  Bit Score: 105.66  E-value: 2.08e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496169756  212 VPRAKPLRDVPEKEVALYAHVNDLPAHITECPHASEAYRGEIQQLLYDLEENHPGTRHSILAGYEDLAAIAADEFsgdDG 291
Cdd:TIGR00269   1 VPRIKPLRYIPEKEVVLYAFLNELKVHLDECPYSSLSVRARIRDFLYDLENKKPGVKFSVLRGFEKLIPLLKELS---EQ 77

                          90       100
                  ....*....|....*....|....*..
gi 496169756  292 ADLRECAECGSTTTREICRKCSLLESL 318
Cdd:TIGR00269  78 EDLRRCERCGEPTSGRICKACKFLEEL 104
TtcA-like cd24138
tRNA-cytidine(32) 2-sulfurtransferase and similar proteins; tRNA-cytidine(32) ...
 58-247 2.51e-25

tRNA-cytidine(32) 2-sulfurtransferase and similar proteins; tRNA-cytidine(32) 2-sulfurtransferase, also called two-thiocytidine biosynthesis protein A or tRNA 2-thiocytidine biosynthesis protein TtcA, catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). TtcA belongs to the adenine nucleotide alpha hydrolase superfamily (AANH) that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. This domain has a strongly conserved motif SGGKD at the N-terminus.


Pssm-ID: 467514 [Multi-domain]  Cd Length: 187  Bit Score: 100.04  E-value: 2.51e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496169756  58 IGLSGGKDSVVLTQILHD-TFAEDPRIELVGLTIHEGIEGYRDKSiDACVELADDLGIRHELVSYEeefgvrmDDVVEDD 136
Cdd:cd24138   13 VGLSGGKDSLTLLHLLEElKRRAPIKFELVAVTVDPGYPGYRPPR-EELAEILEELGEILEDEESE-------IIIIEKE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496169756 137 PENMAACAYCGVFRRDLLEKYAEKLEADLLLTGHNLDDEAQTALMNFLEGdvEQIakhfdASLGALSEREEQGEFVPRak 216
Cdd:cd24138   85 REEKSPCSLCSRLRRGILYSLAKELGCNKLALGHHLDDAVETLLMNLLYG--GRL-----KTMPPKVTMDRGGLTVIR-- 155

                        170       180       190
                 ....*....|....*....|....*....|.
gi 496169756 217 PLRDVPEKEVALYAHVNDLPAHITECPHASE 247
Cdd:cd24138  156 PLIYVREKDIRAFAEENGLPKIECPCPYCGD 186
lysidine_TilS_N TIGR02432
tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble ...
 57-236 1.82e-18

tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble position of a tRNA must discriminate between G and A of mRNA are AUA (Ile) vs. AUG (Met) and UGA (stop) vs. UGG (Trp). In all bacteria, the wobble position of the tRNA(Ile) recognizing AUA is lysidine, a lysine derivative of cytidine. This family describes a protein domain found, apparently, in all bacteria in a single copy. Eukaryotic sequences appear to be organellar. The domain archictecture of this protein family is variable; some, including characterized proteins of E. coli and B. subtilis known to be tRNA(Ile)-lysidine synthetase, include a conserved 50-residue domain that many other members lack. This protein belongs to the ATP-binding PP-loop family ( pfam01171). It appears in the literature and protein databases as TilS, YacA, and putative cell cycle protein MesJ (a misnomer). [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274129 [Multi-domain]  Cd Length: 189  Bit Score: 81.52  E-value: 1.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496169756   57 VIGLSGGKDSVVLTQILHDtFAEDPRIELVGLTIHEGIEGYRDKSIDACVELADDLGIRHELVSYeeefgvrmdDVVEDD 136
Cdd:TIGR02432   3 LVAVSGGVDSMALLHLLLK-LQPKIKIKLIAAHVDHGLRPESDEEAEFVQQFCRKLNIPLEIKKV---------DVKALA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496169756  137 PEN-----MAACAycgvFRRDLLEKYAEKLEADLLLTGHNLDDEAQTALMNFLEGdveqiaKHFD--ASLGALSEREEQG 209
Cdd:TIGR02432  73 KGKkknleEAARE----ARYDFFEEIAKKHGADYILTAHHADDQAETILMRLLRG------SGLRglSGMKPIRILGSGI 142

                         170       180
                  ....*....|....*....|....*..
gi 496169756  210 EFVpraKPLRDVPEKEVALYAHVNDLP 236
Cdd:TIGR02432 143 QII---RPLLGISKSEIEEYLKENGLP 166
PRK10696 PRK10696
tRNA 2-thiocytidine biosynthesis protein TtcA; Provisional
 55-272 9.56e-17

tRNA 2-thiocytidine biosynthesis protein TtcA; Provisional


Pssm-ID: 236737 [Multi-domain]  Cd Length: 258  Bit Score: 78.36  E-value: 9.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496169756  55 TWVIGLSGGKDSVVLTQILHDTFAEDP-RIELVGLTIHEGIEGYRDKSIDACVEladDLGIRHELVsYEEEFGVrmddVV 133
Cdd:PRK10696  31 RVMVCLSGGKDSYTLLDILLNLQKRAPiNFELVAVNLDQKQPGFPEHVLPEYLE---SLGVPYHIE-EQDTYSI----VK 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496169756 134 EDDPENMAACAYCGVFRRDLLEKYAEKLEADLLLTGHNLDDEAQTALMNFLegdveqiakhFDASLGALSE--REEQGE- 210
Cdd:PRK10696 103 EKIPEGKTTCSLCSRLRRGILYRTARELGATKIALGHHRDDILETLFLNMF----------YGGKLKAMPPklLSDDGKh 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496169756 211 FVPRakPLRDVPEKEVALYAHVNDLPAHITECPHASE-AYRGEIQQLLYDLEENHPGTRHSIL 272
Cdd:PRK10696 173 IVIR--PLAYVAEKDIIKFAEAKEFPIIPCNLCGSQEnLQRQVVKEMLRDWEKEYPGRIETMF 233
TilS_N cd01992
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine ...
 55-236 5.32e-15

N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine synthase (EC 6.3.4.19), also called tRNA(Ile)-2-lysyl-cytidine synthase or tRNA(Ile)-lysidine synthetase, catalyzes the ligation of lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. This subfamily belongs to the adenine nucleotide alpha hydrolase superfamily that also includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to adenosine group. This domain has a strongly conserved motif SGGXD at the N-terminus.


Pssm-ID: 467496 [Multi-domain]  Cd Length: 185  Bit Score: 71.86  E-value: 5.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496169756  55 TWVIGLSGGKDSVVLTQILHDtFAEDPRIELVGLTIHEGIegyRDKSID---ACVELADDLGIRHElvsyeeefgVRMDD 131
Cdd:cd01992    1 KILVAVSGGPDSMALLHLLKE-LRPKLGLKLVAVHVDHGL---REESAEeaqFVAKLCKKLGIPLH---------ILTVT 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496169756 132 VVEDDPENMAACAYcgVFRRDLLEKYAEKLEADLLLTGHNLDDEAQTALMNFLEGdveqiakHFDASLGALSEREEQGEf 211
Cdd:cd01992   68 EAPKSGGNLEAAAR--EARYAFLERAAKEHGIDVLLTAHHLDDQAETVLMRLLRG-------SGLSGLAGMAARSKAGG- 137

                        170       180
                 ....*....|....*....|....*
gi 496169756 212 VPRAKPLRDVPEKEVALYAHVNDLP 236
Cdd:cd01992  138 IRLIRPLLGISKAELLAYCRENGLP 162
ATP_bind_3 pfam01171
PP-loop family; This family of proteins belongs to the PP-loop superfamily.
 58-236 4.11e-13

PP-loop family; This family of proteins belongs to the PP-loop superfamily.


Pssm-ID: 426097 [Multi-domain]  Cd Length: 178  Bit Score: 66.50  E-value: 4.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496169756   58 IGLSGGKDSVVLTQILHDtFAEDPRIELVGLTIHEGIEGYRDKSIDACVELADDLGIRHELVSYeeefgvrmdDVVEDDP 137
Cdd:pfam01171   1 VAVSGGPDSMALLYLLAK-LKIKLGIELTAAHVNHGLREESDREAEHVQALCRQLGIPLEILRV---------DVAKKSG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496169756  138 ENMAACAYcgVFRRDLLEKYAEKLEADLLLTGHNLDDEAQTALMNFLEGDveqiakhFDASLGALSEREEQGEfVPRAKP 217
Cdd:pfam01171  71 ENLEAAAR--EARYDFFEEALKKHGADVLLTAHHLDDQLETFLMRLKRGS-------GLAGLAGIPPVREFAG-GRIIRP 140

                         170
                  ....*....|....*....
gi 496169756  218 LRDVPEKEVALYAHVNDLP 236
Cdd:pfam01171 141 LLKVSKAEIEAYAKEHKIP 159
tRNA_Me_trans pfam03054
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ...
 57-170 1.23e-05

tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA(5-methylaminomethyl-2-thiouridine)-methyltransferase which is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine present in the wobble position of some tRNAs.


Pssm-ID: 460787 [Multi-domain]  Cd Length: 202  Bit Score: 45.32  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496169756   57 VIGLSGGKDSVVLTQILHDTFAEdprieLVGLTIHEGIEGYRDKSIDACV---------ELADDLGIRHELVSYEEEFgv 127
Cdd:pfam03054   4 VVAMSGGVDSSVAAYLLKEQGHN-----VIGVFMKNWDEEQSLDEEGKCCseedladaqRVCEQLGIPLYVVNFEKEY-- 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 496169756  128 rMDDVVEDDPENMAA------CAYCG--VFRRDLLEKYAEKLEADLLLTGH 170
Cdd:pfam03054  77 -WEDVFEPFLDEYKNgrtpnpDVLCNkeIKFGALLDYALENLGADYVATGH 126
LarE-like cd01990
Lactate racemization operon protein LarE and similar proteins; This subfamily includes ...
 57-174 9.45e-05

Lactate racemization operon protein LarE and similar proteins; This subfamily includes Lactiplantibacillus plantarum LarE, a sacrificial sulfur insertase of the N-type ATP pyrophosphatase family. LarE is part of the lar operon, encoding five Lar proteins (LarA-E) that collaboratively synthesize and incorporate a niacin-derived Ni-containing cofactor into LarA, an Ni-dependent lactate racemase. It catalyzes successive thiolation reactions by donating the sulfur atom of their exclusive cysteine residues to the substrate. The LarE-like subfamily belongs to the nucleotide alpha hydrolase (AANH) superfamily that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. Proteins from this subfamily probably binds ATP. This domain is about 200 amino acids long with a strongly conserved motif SGGxDS at the N-terminus.


Pssm-ID: 467494 [Multi-domain]  Cd Length: 222  Bit Score: 43.02  E-value: 9.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496169756  57 VIGLSGGKDSVVLTQILHDTFAEdpriELVGLTIHEGIegYRDKSIDACVELADDLGIRHELVSYEEefgVRMDDVVEDD 136
Cdd:cd01990    3 VVAFSGGVDSSLLAKLAKEVLGD----NVVAVTADSPL--VPREELEEAKRIAEEIGIRHEIIKTDE---LDDEEYVAND 73

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 496169756 137 PEnmaACAYCGVFRRDLLEKYAEKLEADLLLTGHNLDD 174
Cdd:cd01990   74 PD---RCYHCKKALYSTLKEIAKERGYDVVLDGTNADD 108
mnmA PRK00143
tRNA-specific 2-thiouridylase MnmA; Reviewed
 57-170 1.22e-04

tRNA-specific 2-thiouridylase MnmA; Reviewed


Pssm-ID: 234664 [Multi-domain]  Cd Length: 346  Bit Score: 43.14  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496169756  57 VIGLSGGKDSVVLTQILHDTFAEdprieLVGLT--IHEGIEGYRDK-------SIDAcVELADDLGIRHELVSYEEEFGv 127
Cdd:PRK00143   4 VVGMSGGVDSSVAAALLKEQGYE-----VIGVFmkLWDDDDETGKGgccaeedIADA-RRVADKLGIPHYVVDFEKEFW- 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 496169756 128 rmDDVVEDdpenMAA----------CAYC--GV-FrRDLLEkYAEKLEADLLLTGH 170
Cdd:PRK00143  77 --DRVIDY----FLDeykagrtpnpCVLCnkEIkF-KAFLE-YARELGADYIATGH 124
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 46-238 1.20e-03

3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; 3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 439945 [Multi-domain]  Cd Length: 232  Bit Score: 39.83  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496169756  46 RDATPENPQTWVIGLSGGKDSVVLTQILHDtfaEDPRIELVglTIHEGIE-----GYRDksidacvELADDLGIRHELVS 120
Cdd:COG0175   26 REAAAEFGGRVVVSSSGGKDSTVLLHLAAK---FKPPIPVL--FLDTGYEfpetyEFRD-------RLAERLGLDLIVVR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496169756 121 YEEEFGVRMD----DVVEDDPEnmaacAYCGVFRRDLLEKYAEKLEADLLLTGhnL-DDEAQT-ALMNFLegdveqiakh 194
Cdd:COG0175   94 PEDAFAEQLAefgpPLFYRDPR-----WCCKIRKVEPLKRALAGYDFDAWITG--LrRDESPTrAKEPVV---------- 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 496169756 195 fdaslgalsEREEQGEFVpRAKPLRDVPEKEVALYAHVNDLPAH 238
Cdd:COG0175  157 ---------EWDPVGGLI-KVNPLADWTELDVWAYIRREDLPYN 190
MnmA COG0482
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ...
 57-170 1.86e-03

tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ribosomal structure and biogenesis]; tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440250 [Multi-domain]  Cd Length: 353  Bit Score: 39.65  E-value: 1.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496169756  57 VIGLSGGKDSVVLTQILHDT-FaedpriELVGLTIHEGIEGYRDKSiDACVEL---------ADDLGIRHELVSYEEEFG 126
Cdd:COG0482    4 VVGMSGGVDSSVAAALLKEQgY------EVIGVTMKLWDDDDASGS-GGCCSLediedarrvADKLGIPHYVVDFEEEFK 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 496169756 127 vrmDDVVEDdpenMAA----------CAYC--GV-FrRDLLEkYAEKLEADLLLTGH 170
Cdd:COG0482   77 ---DRVIDY----FLDeylagrtpnpCVLCnrEIkF-GALLE-KALELGADYIATGH 124
MnmA_TRMU-like cd01998
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ...
 57-170 3.19e-03

MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial tRNA-specific 2-thiouridylase MnmA (EC 2.8.1.13) and mitochondrial tRNA-specific 2-thiouridylase 1 (TRMU or MTU1, EC 2.8.1.14). MnmA catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. TRMU/MTU1 catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln); this is required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. This family belongs to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.


Pssm-ID: 467502 [Multi-domain]  Cd Length: 349  Bit Score: 38.64  E-value: 3.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496169756  57 VIGLSGGKDSVV----LTQILHDtfaedprieLVGLT--IHEGIEGYRD-----KSIDACVELADDLGIRHELVSYEEEF 125
Cdd:cd01998    3 AVAMSGGVDSSVaaalLKEQGYD---------VIGVFmkNWDDEDNEKGgccseEDIEDARRVADQLGIPLYVVDFSEEY 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 496169756 126 gvrMDDVVeddpENMAA----------CAYCGvfRR---DLLEKYAEKLEADLLLTGH 170
Cdd:cd01998   74 ---WERVF----DPFLEeykagrtpnpDVLCN--REikfGALLDAAKKLGADYIATGH 122
PRK14664 PRK14664
tRNA-specific 2-thiouridylase MnmA; Provisional
 57-187 5.71e-03

tRNA-specific 2-thiouridylase MnmA; Provisional


Pssm-ID: 173127 [Multi-domain]  Cd Length: 362  Bit Score: 38.01  E-value: 5.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496169756  57 VIGLSGGKDSVVLTQILhdtfaEDPRIELVGLTIHEgiegYRDKSIDAcVELADDLGIRHELVSYEEEFG---VR--MDD 131
Cdd:PRK14664   9 LVGMSGGIDSTATCLML-----QEQGYEIVGVTMRV----WGDEPQDA-RELAARMGIEHYVADERVPFKdtiVKnfIDE 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 496169756 132 VVEDDPENmaACAYCG-VFRRDLLEKYAEKLEADLLLTGHNLDDEAQTALMNFLEGD 187
Cdd:PRK14664  79 YRQGRTPN--PCVMCNpLFKFRMLIEWADKLGCAWIATGHYSRLEERNGHIYIVAGD 133
QueC-like cd01995
7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC ...
 57-176 7.61e-03

7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC 6.3.4.20) is also called 7-cyano-7-carbaguanine synthase, preQ(0) synthase, or queuosine biosynthesis protein QueC. It catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)), as part of the biosynthesis pathway of queuosine (Q). Q is one of the most complex modifications occurring at the wobble position of tRNAs with GUN anticodons, and is implicated in a number of biological activities, including accuracy of decoding, virulence, and cellular differentiation. This subfamily belongs to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.


Pssm-ID: 467499 [Multi-domain]  Cd Length: 208  Bit Score: 37.21  E-value: 7.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496169756  57 VIGLSGGKDSVVLTQILHDTFAedpriELVGLTIHegiEGYR--DKSIDACVELADDLGIRHELV---SYEEEFGVRMDD 131
Cdd:cd01995    4 VVLLSGGLDSTTLLYWALKEGY-----EVHALTFD---YGQRhaKEELEAAKLIAKLLGIEHKVIdlsFLGELGGSSLTD 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496169756 132 VVEDDPE---------------------NMAACaycgvfrrdllekYAEKLEADLLLTGHNLDDEA 176
Cdd:cd01995   76 EGEEVPDgeydeesipstwvpnrnliflSIAAA-------------YAESLGASAIVIGVNAEDAS 128
NadE COG0171
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ...
 57-142 9.07e-03

NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ synthetase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 439941 [Multi-domain]  Cd Length: 542  Bit Score: 37.52  E-value: 9.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496169756  57 VIGLSGGKDS-VVLTqILHDTFAEDPrieLVGLTIheGIEGYRDKSIDACVELADDLGIRHELVS-----------YEEE 124
Cdd:COG0171  290 VLGLSGGIDSaLVAA-LAVDALGPEN---VLGVTM--PSRYTSDESLEDAEELAENLGIEYEEIDitpaveafleaLPHA 363

                         90
                 ....*....|....*...
gi 496169756 125 FGVRMDDVVEddpENMAA 142
Cdd:COG0171  364 FGGELDDVAE---ENLQA 378
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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