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Conserved domains on  [gi|1474260443|ref|WP_118666610|]
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MULTISPECIES: ATP-binding protein [unclassified Blautia]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TilS COG0037
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ...
 123-355 1.80e-74

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: 231.65  E-value: 1.80e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443 123 KFTKAINTYELVKPGDRIAVCISGGKDSMLMAKCFQELKLHNKFDFEVkfVVMDPG---YSPENRKVIEDNAKSLHIPIT 199
Cdd:COG0037     1 KVRKAIRDYRLLEPGDRILVAVSGGKDSLALLHLLAKLRRRLGFELVA--VHVDHGlreESDEDAEFVAELCEELGIPLH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443 200 IFETDIFDSVYHVENSPCYLCARMRRGHLYHFAQQLGCNKIALGHHYDDVIETILMGMLYGAQVQTMMPKLHSIHFeGME 279
Cdd:COG0037    79 VVRVDVPAIAKKEGKSPEAAARRARYGALYELARELGADKIATGHHLDDQAETFLLNLLRGSGLAGLAGMPPSRGG-GVR 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1474260443 280 LIRPLYLVREDDIKAWRDYNGLHFIQCACkftdtcttcnNEENRSKRVEIK-ELIKNLKKVNPFVESNIFRSVENVN 355
Cdd:COG0037   158 LIRPLLYVSRKEIEAYAKENGLPWIEDPC----------NYDPRYTRNRIRhLVLPELEERNPGFKENLARSAENLA 224
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 3-91 2.36e-16

Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle


:

Pssm-ID: 440372 [Multi-domain]  Cd Length: 106  Bit Score: 74.23  E-value: 2.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443   3 TSISIKELKE-LDPSSYQIVDIRDAVEISHGAIPGALGMKTEEIETS-DAIDRSKKTIICCSRGRFSVAAAEELQEKGWD 80
Cdd:COG0607     4 KEISPAELAElLESEDAVLLDVREPEEFAAGHIPGAINIPLGELAERlDELPKDKPIVVYCASGGRSAQAAALLRRAGYT 83

                          90
                  ....*....|..
gi 1474260443  81 AV-SLEGGYIAW 91
Cdd:COG0607    84 NVyNLAGGIEAW 95
 
Name Accession Description Interval E-value
TilS COG0037
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ...
 123-355 1.80e-74

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: 231.65  E-value: 1.80e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443 123 KFTKAINTYELVKPGDRIAVCISGGKDSMLMAKCFQELKLHNKFDFEVkfVVMDPG---YSPENRKVIEDNAKSLHIPIT 199
Cdd:COG0037     1 KVRKAIRDYRLLEPGDRILVAVSGGKDSLALLHLLAKLRRRLGFELVA--VHVDHGlreESDEDAEFVAELCEELGIPLH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443 200 IFETDIFDSVYHVENSPCYLCARMRRGHLYHFAQQLGCNKIALGHHYDDVIETILMGMLYGAQVQTMMPKLHSIHFeGME 279
Cdd:COG0037    79 VVRVDVPAIAKKEGKSPEAAARRARYGALYELARELGADKIATGHHLDDQAETFLLNLLRGSGLAGLAGMPPSRGG-GVR 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1474260443 280 LIRPLYLVREDDIKAWRDYNGLHFIQCACkftdtcttcnNEENRSKRVEIK-ELIKNLKKVNPFVESNIFRSVENVN 355
Cdd:COG0037   158 LIRPLLYVSRKEIEAYAKENGLPWIEDPC----------NYDPRYTRNRIRhLVLPELEERNPGFKENLARSAENLA 224
TtcA-like cd24138
tRNA-cytidine(32) 2-sulfurtransferase and similar proteins; tRNA-cytidine(32) ...
 130-310 2.84e-72

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: 224.08  E-value: 2.84e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443 130 TYELVKPGDRIAVCISGGKDSMLMAKCFQELKLHNKFDFEVKFVVMDPGYSP--ENRKVIEDNAKSLHIPITIFETDIFD 207
Cdd:cd24138     1 DFKMIEPGDRILVGLSGGKDSLTLLHLLEELKRRAPIKFELVAVTVDPGYPGyrPPREELAEILEELGEILEDEESEIII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443 208 SV-YHVENSPCYLCARMRRGHLYHFAQQLGCNKIALGHHYDDVIETILMGMLYGAQVQTMMPKLHSiHFEGMELIRPLYL 286
Cdd:cd24138    81 IEkEREEKSPCSLCSRLRRGILYSLAKELGCNKLALGHHLDDAVETLLMNLLYGGRLKTMPPKVTM-DRGGLTVIRPLIY 159

                         170       180
                  ....*....|....*....|....
gi 1474260443 287 VREDDIKAWRDYNGLHFIQCACKF 310
Cdd:cd24138   160 VREKDIRAFAEENGLPKIECPCPY 183
PRK10696 PRK10696
tRNA 2-thiocytidine biosynthesis protein TtcA; Provisional
 108-354 5.30e-61

tRNA 2-thiocytidine biosynthesis protein TtcA; Provisional


Pssm-ID: 236737 [Multi-domain]  Cd Length: 258  Bit Score: 197.77  E-value: 5.30e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443 108 VEKSLRKKFKKAIwskfTKAINTYELVKPGDRIAVCISGGKDSMLMAKCFQELKLHNKFDFEVKFVVMD---PGYsPENr 184
Cdd:PRK10696    4 EFNKLQKRLRRQV----GQAIADFNMIEEGDRVMVCLSGGKDSYTLLDILLNLQKRAPINFELVAVNLDqkqPGF-PEH- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443 185 kVIEDNAKSLHIPITIFETDIFDSVYHV--ENSP-CYLCARMRRGHLYHFAQQLGCNKIALGHHYDDVIETILMGMLYGA 261
Cdd:PRK10696   78 -VLPEYLESLGVPYHIEEQDTYSIVKEKipEGKTtCSLCSRLRRGILYRTARELGATKIALGHHRDDILETLFLNMFYGG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443 262 QVQTMMPKLHS---IHFegmeLIRPLYLVREDDIKAWRDYNGLHFIQCACkftdtcttCNNEENRsKRVEIKELIKNLKK 338
Cdd:PRK10696  157 KLKAMPPKLLSddgKHI----VIRPLAYVAEKDIIKFAEAKEFPIIPCNL--------CGSQENL-QRQVVKEMLRDWEK 223

                         250
                  ....*....|....*.
gi 1474260443 339 VNPFVESNIFRSVENV 354
Cdd:PRK10696  224 EYPGRIETMFRALQNV 239
lysidine_TilS_N TIGR02432
tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble ...
 139-305 7.73e-20

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: 86.53  E-value: 7.73e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443 139 RIAVCISGGKDSMLMAKCFQELKLHNKFDFEVkfVVMDPGYSPENR---KVIEDNAKSLHIPITIFETDIFDSVYHVENS 215
Cdd:TIGR02432   1 RILVAVSGGVDSMALLHLLLKLQPKIKIKLIA--AHVDHGLRPESDeeaEFVQQFCRKLNIPLEIKKVDVKALAKGKKKN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443 216 pcyLCARMRRgHLYHF----AQQLGCNKIALGHHYDDVIETILMGMLYGAqvqtmmpklHSIHFEGM----------ELI 281
Cdd:TIGR02432  79 ---LEEAARE-ARYDFfeeiAKKHGADYILTAHHADDQAETILMRLLRGS---------GLRGLSGMkpirilgsgiQII 145

                         170       180
                  ....*....|....*....|....
gi 1474260443 282 RPLYLVREDDIKAWRDYNGLHFIQ 305
Cdd:TIGR02432 146 RPLLGISKSEIEEYLKENGLPWFE 169
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 3-91 2.36e-16

Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440372 [Multi-domain]  Cd Length: 106  Bit Score: 74.23  E-value: 2.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443   3 TSISIKELKE-LDPSSYQIVDIRDAVEISHGAIPGALGMKTEEIETS-DAIDRSKKTIICCSRGRFSVAAAEELQEKGWD 80
Cdd:COG0607     4 KEISPAELAElLESEDAVLLDVREPEEFAAGHIPGAINIPLGELAERlDELPKDKPIVVYCASGGRSAQAAALLRRAGYT 83

                          90
                  ....*....|..
gi 1474260443  81 AV-SLEGGYIAW 91
Cdd:COG0607    84 NVyNLAGGIEAW 95
ATP_bind_3 pfam01171
PP-loop family; This family of proteins belongs to the PP-loop superfamily.
 140-305 3.55e-15

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


Pssm-ID: 426097 [Multi-domain]  Cd Length: 178  Bit Score: 73.04  E-value: 3.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443 140 IAVciSGGKDSMLMAKCFQELKLHNKFDFEVkfVVMDPGYSPENR---KVIEDNAKSLHIPITIFETDifdsVYHVENSP 216
Cdd:pfam01171   1 VAV--SGGPDSMALLYLLAKLKIKLGIELTA--AHVNHGLREESDreaEHVQALCRQLGIPLEILRVD----VAKKSGEN 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443 217 CYLCAR-MRRGHLYHFAQQLGCNKIALGHHYDDVIETILM--------GMLYGAQVQTMmpklhsihFEGMELIRPLYLV 287
Cdd:pfam01171  73 LEAAAReARYDFFEEALKKHGADVLLTAHHLDDQLETFLMrlkrgsglAGLAGIPPVRE--------FAGGRIIRPLLKV 144

                         170
                  ....*....|....*...
gi 1474260443 288 REDDIKAWRDYNGLHFIQ 305
Cdd:pfam01171 145 SKAEIEAYAKEHKIPWFE 162
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 9-91 2.81e-13

Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.


Pssm-ID: 238089 [Multi-domain]  Cd Length: 89  Bit Score: 65.01  E-value: 2.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443   9 ELKEL-DPSSYQIVDIRDAVEISHGAIPGALGMKTEEIETS---DAIDRSKKTIICCSRGRFSVAAAEELQEKG-WDAVS 83
Cdd:cd00158     1 ELKELlDDEDAVLLDVREPEEYAAGHIPGAINIPLSELEERaalLELDKDKPIVVYCRSGNRSARAAKLLRKAGgTNVYN 80


                  ....*...
gi 1474260443  84 LEGGYIAW 91
Cdd:cd00158    81 LEGGMLAW 88
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 18-95 2.81e-10

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 56.70  E-value: 2.81e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443   18 YQIVDIRDAVEISHGAIPGAL---------------GMKTEEIETSDAIDRSKKTIICCSRGRFSVAAAEELQEKGWDAV 82
Cdd:smart00450   5 VVLLDVRSPEEYEGGHIPGAVniplselldrrgeldILEFEELLKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELGFKNV 84

                           90
                   ....*....|....
gi 1474260443   83 S-LEGGYIAWLMDV 95
Cdd:smart00450  85 YlLDGGYKEWSAAG 98
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
1-91 3.63e-10

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 61.18  E-value: 3.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443   1 MSTSISIKELKELDPSSYQIVDIRDAVEISHGAIPGALGMKTEEIET---SDAIDRSKKTIICCSRGRFSVAAAEELQEK 77
Cdd:PRK08762    1 SIREISPAEARARAAQGAVLIDVREAHERASGQAEGALRIPRGFLELrieTHLPDRDREIVLICASGTRSAHAAATLREL 80

                          90
                  ....*....|....*
gi 1474260443  78 GW-DAVSLEGGYIAW 91
Cdd:PRK08762   81 GYtRVASVAGGFSAW 95
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 13-91 2.31e-08

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 51.33  E-value: 2.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443  13 LDPSSYQIVDIRDAVEISHGAIPGAL-----------GMKTEEIETSDAIDRSKKTIICCSRGRFSVAAAEELQEKGWDA 81
Cdd:pfam00581   1 LEDGKVVLIDVRPPEEYAKGHIPGAVnvplsslslppLPLLELLEKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYKN 80

                          90
                  ....*....|.
gi 1474260443  82 VS-LEGGYIAW 91
Cdd:pfam00581  81 VYvLDGGFEAW 91
 
Name Accession Description Interval E-value
TilS COG0037
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ...
 123-355 1.80e-74

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: 231.65  E-value: 1.80e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443 123 KFTKAINTYELVKPGDRIAVCISGGKDSMLMAKCFQELKLHNKFDFEVkfVVMDPG---YSPENRKVIEDNAKSLHIPIT 199
Cdd:COG0037     1 KVRKAIRDYRLLEPGDRILVAVSGGKDSLALLHLLAKLRRRLGFELVA--VHVDHGlreESDEDAEFVAELCEELGIPLH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443 200 IFETDIFDSVYHVENSPCYLCARMRRGHLYHFAQQLGCNKIALGHHYDDVIETILMGMLYGAQVQTMMPKLHSIHFeGME 279
Cdd:COG0037    79 VVRVDVPAIAKKEGKSPEAAARRARYGALYELARELGADKIATGHHLDDQAETFLLNLLRGSGLAGLAGMPPSRGG-GVR 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1474260443 280 LIRPLYLVREDDIKAWRDYNGLHFIQCACkftdtcttcnNEENRSKRVEIK-ELIKNLKKVNPFVESNIFRSVENVN 355
Cdd:COG0037   158 LIRPLLYVSRKEIEAYAKENGLPWIEDPC----------NYDPRYTRNRIRhLVLPELEERNPGFKENLARSAENLA 224
TtcA-like cd24138
tRNA-cytidine(32) 2-sulfurtransferase and similar proteins; tRNA-cytidine(32) ...
 130-310 2.84e-72

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: 224.08  E-value: 2.84e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443 130 TYELVKPGDRIAVCISGGKDSMLMAKCFQELKLHNKFDFEVKFVVMDPGYSP--ENRKVIEDNAKSLHIPITIFETDIFD 207
Cdd:cd24138     1 DFKMIEPGDRILVGLSGGKDSLTLLHLLEELKRRAPIKFELVAVTVDPGYPGyrPPREELAEILEELGEILEDEESEIII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443 208 SV-YHVENSPCYLCARMRRGHLYHFAQQLGCNKIALGHHYDDVIETILMGMLYGAQVQTMMPKLHSiHFEGMELIRPLYL 286
Cdd:cd24138    81 IEkEREEKSPCSLCSRLRRGILYSLAKELGCNKLALGHHLDDAVETLLMNLLYGGRLKTMPPKVTM-DRGGLTVIRPLIY 159

                         170       180
                  ....*....|....*....|....
gi 1474260443 287 VREDDIKAWRDYNGLHFIQCACKF 310
Cdd:cd24138   160 VREKDIRAFAEENGLPKIECPCPY 183
PRK10696 PRK10696
tRNA 2-thiocytidine biosynthesis protein TtcA; Provisional
 108-354 5.30e-61

tRNA 2-thiocytidine biosynthesis protein TtcA; Provisional


Pssm-ID: 236737 [Multi-domain]  Cd Length: 258  Bit Score: 197.77  E-value: 5.30e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443 108 VEKSLRKKFKKAIwskfTKAINTYELVKPGDRIAVCISGGKDSMLMAKCFQELKLHNKFDFEVKFVVMD---PGYsPENr 184
Cdd:PRK10696    4 EFNKLQKRLRRQV----GQAIADFNMIEEGDRVMVCLSGGKDSYTLLDILLNLQKRAPINFELVAVNLDqkqPGF-PEH- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443 185 kVIEDNAKSLHIPITIFETDIFDSVYHV--ENSP-CYLCARMRRGHLYHFAQQLGCNKIALGHHYDDVIETILMGMLYGA 261
Cdd:PRK10696   78 -VLPEYLESLGVPYHIEEQDTYSIVKEKipEGKTtCSLCSRLRRGILYRTARELGATKIALGHHRDDILETLFLNMFYGG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443 262 QVQTMMPKLHS---IHFegmeLIRPLYLVREDDIKAWRDYNGLHFIQCACkftdtcttCNNEENRsKRVEIKELIKNLKK 338
Cdd:PRK10696  157 KLKAMPPKLLSddgKHI----VIRPLAYVAEKDIIKFAEAKEFPIIPCNL--------CGSQENL-QRQVVKEMLRDWEK 223

                         250
                  ....*....|....*.
gi 1474260443 339 VNPFVESNIFRSVENV 354
Cdd:PRK10696  224 EYPGRIETMFRALQNV 239
CTU1-like cd01713
cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human ...
 126-306 5.28e-29

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: 111.91  E-value: 5.28e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443 126 KAINTYELVKPGDRIAVCISGGKDSMLMAKCFQELKLHNKFDFEVKFVVMD---PGYSPENRKVIEDNAKSLHIPITI-- 200
Cdd:cd01713     7 RTIRKYRLIKPGDRVAVGLSGGKDSTVLLYVLKELNKRHDYGVELIAVTIDegiKGYRDDSLEAARKLAEEYGIPLEIvs 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443 201 FEtDIF----DSVYHVEN---SPCYLCARMRRGHLYHFAQQLGCNKIALGHHYDDVIETILMGMLYG--AQVQTMMPKLH 271
Cdd:cd01713    87 FE-DEFgftlDELIVGKGgkkNACTYCGVFRRRALNRGARELGADKLATGHNLDDEAETILMNLLRGdvARLLRTGPEPR 165

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1474260443 272 SIHFEGMELIRPLYLVREDDIKAWRDYNGL--HFIQC 306
Cdd:cd01713   166 SEGEGLVPRIKPLRYIPEKEIVLYAHLNGLpyFSTEC 202
TtuA-like cd01993
tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins; tRNA-5-methyluridine(54) ...
 131-310 1.02e-20

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: 88.92  E-value: 1.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443 131 YELVKPGDRIAVCISGGKDSMLMAKCFQELklhnkfDFEVKFVVMDPG---YSPENRKVIEDNAKSLHIPITIFE--TDI 205
Cdd:cd01993     2 YKMFEKDDKILVAVSGGKDSLALLAVLKKL------GYNVEALYINLGigeYSEKSEEVVKKLAEKLNLPLHVVDlkEEY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443 206 FDSVYHVEN----SPCYLCARMRRGHLYHFAQQLGCNKIALGHHYDDvIETILMGMLYGAQVQTM---MPKLHSIHFEGM 278
Cdd:cd01993    76 GLGIPELAKksrrPPCSVCGLVKRYIMNKFAVENGFDVVATGHNLDD-EAAFLLGNILNWNEEYLakqGPFLLPEHGGLV 154

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1474260443 279 ELIRPLYLVREDDIKAWRDYNGLHFIQCACKF 310
Cdd:cd01993   155 TRVKPLYEITEEEIALYALLNGIPYLEEECPY 186
TilS_N cd01992
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine ...
 139-333 1.89e-20

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: 88.03  E-value: 1.89e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443 139 RIAVCISGGKDSMLMAKCFQELKLHNKFDFEVkfVVMDPGYSPENRKVIE---DNAKSLHIPITIFE-TDIFDSVYHVEN 214
Cdd:cd01992     1 KILVAVSGGPDSMALLHLLKELRPKLGLKLVA--VHVDHGLREESAEEAQfvaKLCKKLGIPLHILTvTEAPKSGGNLEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443 215 SpcylcARMRRghlYHF----AQQLGCNKIALGHHYDDVIETILMGMLYGAQVQTMMPKLHSIHFEGMELIRPLYLVRED 290
Cdd:cd01992    79 A-----AREAR---YAFleraAKEHGIDVLLTAHHLDDQAETVLMRLLRGSGLSGLAGMAARSKAGGIRLIRPLLGISKA 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1474260443 291 DIKAWRDYNGLHFIQcackftDTcttcNNEENRSKRVEI-KELI 333
Cdd:cd01992   151 ELLAYCRENGLPWVE------DP----SNADLKYTRNRIrHELL 184
lysidine_TilS_N TIGR02432
tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble ...
 139-305 7.73e-20

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: 86.53  E-value: 7.73e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443 139 RIAVCISGGKDSMLMAKCFQELKLHNKFDFEVkfVVMDPGYSPENR---KVIEDNAKSLHIPITIFETDIFDSVYHVENS 215
Cdd:TIGR02432   1 RILVAVSGGVDSMALLHLLLKLQPKIKIKLIA--AHVDHGLRPESDeeaEFVQQFCRKLNIPLEIKKVDVKALAKGKKKN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443 216 pcyLCARMRRgHLYHF----AQQLGCNKIALGHHYDDVIETILMGMLYGAqvqtmmpklHSIHFEGM----------ELI 281
Cdd:TIGR02432  79 ---LEEAARE-ARYDFfeeiAKKHGADYILTAHHADDQAETILMRLLRGS---------GLRGLSGMkpirilgsgiQII 145

                         170       180
                  ....*....|....*....|....
gi 1474260443 282 RPLYLVREDDIKAWRDYNGLHFIQ 305
Cdd:TIGR02432 146 RPLLGISKSEIEEYLKENGLPWFE 169
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 3-91 2.36e-16

Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440372 [Multi-domain]  Cd Length: 106  Bit Score: 74.23  E-value: 2.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443   3 TSISIKELKE-LDPSSYQIVDIRDAVEISHGAIPGALGMKTEEIETS-DAIDRSKKTIICCSRGRFSVAAAEELQEKGWD 80
Cdd:COG0607     4 KEISPAELAElLESEDAVLLDVREPEEFAAGHIPGAINIPLGELAERlDELPKDKPIVVYCASGGRSAQAAALLRRAGYT 83

                          90
                  ....*....|..
gi 1474260443  81 AV-SLEGGYIAW 91
Cdd:COG0607    84 NVyNLAGGIEAW 95
ATP_bind_3 pfam01171
PP-loop family; This family of proteins belongs to the PP-loop superfamily.
 140-305 3.55e-15

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


Pssm-ID: 426097 [Multi-domain]  Cd Length: 178  Bit Score: 73.04  E-value: 3.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443 140 IAVciSGGKDSMLMAKCFQELKLHNKFDFEVkfVVMDPGYSPENR---KVIEDNAKSLHIPITIFETDifdsVYHVENSP 216
Cdd:pfam01171   1 VAV--SGGPDSMALLYLLAKLKIKLGIELTA--AHVNHGLREESDreaEHVQALCRQLGIPLEILRVD----VAKKSGEN 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443 217 CYLCAR-MRRGHLYHFAQQLGCNKIALGHHYDDVIETILM--------GMLYGAQVQTMmpklhsihFEGMELIRPLYLV 287
Cdd:pfam01171  73 LEAAAReARYDFFEEALKKHGADVLLTAHHLDDQLETFLMrlkrgsglAGLAGIPPVRE--------FAGGRIIRPLLKV 144

                         170
                  ....*....|....*...
gi 1474260443 288 REDDIKAWRDYNGLHFIQ 305
Cdd:pfam01171 145 SKAEIEAYAKEHKIPWFE 162
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 9-91 2.81e-13

Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.


Pssm-ID: 238089 [Multi-domain]  Cd Length: 89  Bit Score: 65.01  E-value: 2.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443   9 ELKEL-DPSSYQIVDIRDAVEISHGAIPGALGMKTEEIETS---DAIDRSKKTIICCSRGRFSVAAAEELQEKG-WDAVS 83
Cdd:cd00158     1 ELKELlDDEDAVLLDVREPEEYAAGHIPGAINIPLSELEERaalLELDKDKPIVVYCRSGNRSARAAKLLRKAGgTNVYN 80


                  ....*...
gi 1474260443  84 LEGGYIAW 91
Cdd:cd00158    81 LEGGMLAW 88
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 5-88 5.89e-11

Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus lactis NADH oxidase, Bacillus cereus NADH dehydrogenase, and Bacteroides thetaiotaomicron pyridine nucleotide-disulphide oxidoreductase, and similar rhodanese-like domains found C-terminal of the pyridine nucleotide-disulphide oxidoreductase (Pyr-redox) domain and the Pyr-redox dimerization domain.


Pssm-ID: 238782 [Multi-domain]  Cd Length: 90  Bit Score: 58.43  E-value: 5.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443   5 ISIKELKELDPSSYQIVDIRDAVEISHGAIPGALGMKTEEI-ETSDAIDRSKKTIICCSRGRFSVAAAEELQEKGWDAVS 83
Cdd:cd01524     1 VQWHELDNYRADGVTLIDVRTPQEFEKGHIKGAINIPLDELrDRLNELPKDKEIIVYCAVGLRGYIAARILTQNGFKVKN 80


                  ....*
gi 1474260443  84 LEGGY 88
Cdd:cd01524    81 LDGGY 85
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 18-95 2.81e-10

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 56.70  E-value: 2.81e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443   18 YQIVDIRDAVEISHGAIPGAL---------------GMKTEEIETSDAIDRSKKTIICCSRGRFSVAAAEELQEKGWDAV 82
Cdd:smart00450   5 VVLLDVRSPEEYEGGHIPGAVniplselldrrgeldILEFEELLKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELGFKNV 84

                           90
                   ....*....|....
gi 1474260443   83 S-LEGGYIAWLMDV 95
Cdd:smart00450  85 YlLDGGYKEWSAAG 98
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
1-91 3.63e-10

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 61.18  E-value: 3.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443   1 MSTSISIKELKELDPSSYQIVDIRDAVEISHGAIPGALGMKTEEIET---SDAIDRSKKTIICCSRGRFSVAAAEELQEK 77
Cdd:PRK08762    1 SIREISPAEARARAAQGAVLIDVREAHERASGQAEGALRIPRGFLELrieTHLPDRDREIVLICASGTRSAHAAATLREL 80

                          90
                  ....*....|....*
gi 1474260443  78 GW-DAVSLEGGYIAW 91
Cdd:PRK08762   81 GYtRVASVAGGFSAW 95
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 3-92 3.56e-09

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 57.96  E-value: 3.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443   3 TSISIKELKELdPSSYQIVDIRDAVEISHGAIPGALGMKTEEIE---TSDAIDRSKKTIICCSRGRFSVAAAEELQEKGW 79
Cdd:PRK05597  261 EVLDVPRVSAL-PDGVTLIDVREPSEFAAYSIPGAHNVPLSAIRegaNPPSVSAGDEVVVYCAAGVRSAQAVAILERAGY 339

                          90
                  ....*....|....
gi 1474260443  80 -DAVSLEGGYIAWL 92
Cdd:PRK05597  340 tGMSSLDGGIEGWL 353
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 5-91 2.01e-08

GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain superfamily. Unlike other rhodanese sulfurtransferases, GlpE is a single domain protein but indications are that it functions as a dimer. The active site contains a catalytically active cysteine.


Pssm-ID: 238721 [Multi-domain]  Cd Length: 96  Bit Score: 51.49  E-value: 2.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443   5 ISIKELKEL--DPSSYQIVDIRD----AVEISHgaIPGALGMKTEEIET-SDAIDRSKKTIICCSRGRFSVAAAEELQEK 77
Cdd:cd01444     2 ISVDELAELlaAGEAPVLLDVRDpasyAALPDH--IPGAIHLDEDSLDDwLGDLDRDRPVVVYCYHGNSSAQLAQALREA 79

                          90
                  ....*....|....*
gi 1474260443  78 GWDAV-SLEGGYIAW 91
Cdd:cd01444    80 GFTDVrSLAGGFEAW 94
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 13-91 2.31e-08

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 51.33  E-value: 2.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443  13 LDPSSYQIVDIRDAVEISHGAIPGAL-----------GMKTEEIETSDAIDRSKKTIICCSRGRFSVAAAEELQEKGWDA 81
Cdd:pfam00581   1 LEDGKVVLIDVRPPEEYAKGHIPGAVnvplsslslppLPLLELLEKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYKN 80

                          90
                  ....*....|.
gi 1474260443  82 VS-LEGGYIAW 91
Cdd:pfam00581  81 VYvLDGGFEAW 91
LarE-like cd01990
Lactate racemization operon protein LarE and similar proteins; This subfamily includes ...
 139-248 4.59e-07

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: 50.33  E-value: 4.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443 139 RIAVCISGGKDSMLMAKCfqelkLHNKFDFEVKFVVMDPGYSPenRKVIED---NAKSLHIPITIFETDIFDSVYHVENS 215
Cdd:cd01990     1 KVVVAFSGGVDSSLLAKL-----AKEVLGDNVVAVTADSPLVP--REELEEakrIAEEIGIRHEIIKTDELDDEEYVAND 73

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1474260443 216 P--CYLCARMRRGHLYHFAQQLGCNKIALGHHYDD 248
Cdd:cd01990    74 PdrCYHCKKALYSTLKEIAKERGYDVVLDGTNADD 108
Polysulfide_ST cd01447
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ...
 5-92 8.67e-07

Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as a polysulfide binding and transferase domain in anaerobic gram-negative bacteria, functioning in oxidative phosphorylation with polysulfide-sulfur as a terminal electron acceptor. The active site contains the same conserved cysteine that is the catalytic residue in other Rhodanese Homology Domain proteins.


Pssm-ID: 238724 [Multi-domain]  Cd Length: 103  Bit Score: 47.04  E-value: 8.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443   5 ISIKELKEL-DPSSYQIVDIRDAVEISH-GAIPGALGMKTEEIE---------TSDAIDRSKKTIICCSRGRFSVAAAEE 73
Cdd:cd01447     1 LSPEDARALlGSPGVLLVDVRDPRELERtGMIPGAFHAPRGMLEfwadpdspyHKPAFAEDKPFVFYCASGWRSALAGKT 80

                          90       100
                  ....*....|....*....|
gi 1474260443  74 LQEKGWDAV-SLEGGYIAWL 92
Cdd:cd01447    81 LQDMGLKPVyNIEGGFKDWK 100
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 5-95 3.38e-06

Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes uncharacterized putative rhodanese-related domains.


Pssm-ID: 238786 [Multi-domain]  Cd Length: 101  Bit Score: 45.46  E-value: 3.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443   5 ISIKELKEL---DPSSYQIVDIRDAVEISHGAIPGALGMKTEEI----ETSDAIDRSKKTIICCSRGRFSVAAAEELQEK 77
Cdd:cd01528     2 ISVAELAEWladEREEPVLIDVREPEELEIAFLPGFLHLPMSEIpersKELDSDNPDKDIVVLCHHGGRSMQVAQWLLRQ 81

                          90
                  ....*....|....*....
gi 1474260443  78 GWDAV-SLEGGYIAWLMDV 95
Cdd:cd01528    82 GFENVyNLQGGIDAWSLEV 100
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
5-100 6.05e-06

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 47.81  E-value: 6.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443   5 ISIKELKELDPS---SYQIVDIRDAVEISHGAIPGALGMKTEEIETSDAIDRSK------KTIICCSRGRFSVAAAEELQ 75
Cdd:PRK07411  284 MTVTELKALLDSgadDFVLIDVRNPNEYEIARIPGSVLVPLPDIENGPGVEKVKellnghRLIAHCKMGGRSAKALGILK 363

                          90       100
                  ....*....|....*....|....*.
gi 1474260443  76 EKGWDAVSLEGGYIAWLMDV-MSAPE 100
Cdd:PRK07411  364 EAGIEGTNVKGGITAWSREVdPSVPQ 389
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 3-91 2.96e-05

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 45.85  E-value: 2.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443   3 TSISIKELKELDPS--SYQIVDIRDAVEISHGAIPGALGMKTEEIETSDA---IDRSKKTIICCSRGRFSVAAAEELQEK 77
Cdd:PRK07878  287 STITPRELKEWLDSgkKIALIDVREPVEWDIVHIPGAQLIPKSEILSGEAlakLPQDRTIVLYCKTGVRSAEALAALKKA 366

                          90
                  ....*....|....*
gi 1474260443  78 GW-DAVSLEGGYIAW 91
Cdd:PRK07878  367 GFsDAVHLQGGVVAW 381
4RHOD_Repeats cd01529
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ...
 8-91 4.63e-05

Member of the Rhodanese Homology Domain superfamily. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. Only the second and most of the fourth repeats contain the putative catalytic Cys residue. This CD aligns the 1st , 2nd, 3rd, and 4th repeats.


Pssm-ID: 238787 [Multi-domain]  Cd Length: 96  Bit Score: 41.89  E-value: 4.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443   8 KELKELDPSSYqIVDIRDAVEISHGAIPGA-------LGMKTEEIETSDAIDRSKKTIICCSRGRFSVAAAEELQEKGWD 80
Cdd:cd01529     4 DWLGEHEPGTA-LLDVRAEDEYAAGHLPGKrsipgaaLVLRSQELQALEAPGRATRYVLTCDGSLLARFAAQELLALGGK 82

                          90
                  ....*....|..
gi 1474260443  81 AVS-LEGGYIAW 91
Cdd:cd01529    83 PVAlLDGGTSAW 94
RHOD_Lact_B cd01523
Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with ...
 20-92 1.19e-04

Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with rhodanese-like domains found N-terminal of the metallo-beta-lactamase domain.


Pssm-ID: 238781 [Multi-domain]  Cd Length: 100  Bit Score: 40.94  E-value: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443  20 IVDIRDAVEISHGAIPGALGMKT-----EEIETSDAIDRSKKT----IICCSRGRFSVAAAEELQEKGWDAVSLEGGYIA 90
Cdd:cd01523    18 ILDVRNESDYERWKIDGENNTPYfdpyfDFLEIEEDILDQLPDdqevTVICAKEGSSQFVAELLAERGYDVDYLAGGMKA 97


                  ..
gi 1474260443  91 WL 92
Cdd:cd01523    98 WS 99
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 5-95 1.95e-04

Member of the Rhodanese Homology Domain superfamily. This CD includes several putative molybdopterin synthase sulfurylases including the molybdenum cofactor biosynthetic protein (CnxF) of Aspergillus nidulans and the molybdenum cofactor synthesis protein 3 (MOCS3) of Homo sapiens. These rhodanese-like domains are found C-terminal of the ThiF and MoeZ_MoeB domains.


Pssm-ID: 238784 [Multi-domain]  Cd Length: 122  Bit Score: 40.76  E-value: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443   5 ISIKELKELDPSSYQIV--DIRDAVEISHGAIPGALGMKTEEIETSDA-----------IDRSKKTIICCSRGRFSVAAA 71
Cdd:cd01526    10 VSVKDYKNILQAGKKHVllDVRPKVHFEICRLPEAINIPLSELLSKAAelkslqelpldNDKDSPIYVVCRRGNDSQTAV 89

                          90       100
                  ....*....|....*....|....*.
gi 1474260443  72 EELQEKGWDA--VSLEGGYIAWLMDV 95
Cdd:cd01526    90 RKLKELGLERfvRDIIGGLKAWADKV 115
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
20-91 2.35e-04

thiosulfate sulfurtransferase GlpE;


Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 40.39  E-value: 2.35e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1474260443  20 IVDIRDAVEISHGAIPGALGMKTEEIET-SDAIDRSKKTIICCSRGRFSVAAAEELQEKGWDAV-SLEGGYIAW 91
Cdd:PRK00162   23 LVDIRDPQSFAMGHAPGAFHLTNDSLGAfMRQADFDTPVMVMCYHGNSSQGAAQYLLQQGFDVVySIDGGFEAW 96
PRK11784 PRK11784
tRNA 2-selenouridine synthase; Provisional
 7-102 3.67e-04

tRNA 2-selenouridine synthase; Provisional


Pssm-ID: 236982 [Multi-domain]  Cd Length: 345  Bit Score: 42.12  E-value: 3.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443   7 IKELKELDPSSYQIVDIRDAVEISHGAIPGALG---MKTEE-------------------------------IET--SDA 50
Cdd:PRK11784    5 AQDFRALFLNDTPLIDVRSPIEFAEGHIPGAINlplLNDEEraevgtcykqqgqfaaialghalvagniaahREEawADF 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1474260443  51 IDRSKKTIICCSRG--RfSVAAAEELQEKGWDAVSLEGGYIA---WLMDVMSAPEEQ 102
Cdd:PRK11784   85 PRANPRGLLYCWRGglR-SGSVQQWLKEAGIDVPRLEGGYKAyrrFVIDTLEEAPAQ 140
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 7-92 4.64e-04

Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein 67B2 of Drosophila melanogaster and other similar proteins, many of which are uncharacterized.


Pssm-ID: 238777 [Multi-domain]  Cd Length: 106  Bit Score: 39.18  E-value: 4.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443   7 IKELKELDPSSYqIVDIRDAVEISHGAIPG-----------ALGMKTEEIETSDAIDR---SKKTIICCSRGRFSVAAAE 72
Cdd:cd01519     6 VKNLPNPHPNKV-LIDVREPEELKTGKIPGainiplsslpdALALSEEEFEKKYGFPKpskDKELIFYCKAGVRSKAAAE 84

                          90       100
                  ....*....|....*....|.
gi 1474260443  73 ELQEKGWDAVSL-EGGYIAWL 92
Cdd:cd01519    85 LARSLGYENVGNyPGSWLDWA 105
RHOD_YgaP cd01527
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YgaP, ...
 3-91 1.10e-03

Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YgaP, and similar uncharacterized putative rhodanese-related sulfurtransferases.


Pssm-ID: 238785 [Multi-domain]  Cd Length: 99  Bit Score: 38.24  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443   3 TSISIKELKELDPSSYQIVDIRDAVEISHGAIPGALGMKTEEIETSD-AIDRSKKTIICCSRGRFSVAAAEEL-QEKGWD 80
Cdd:cd01527     2 TTISPNDACELLAQGAVLVDIREPDEYLRERIPGARLVPLSQLESEGlPLVGANAIIFHCRSGMRTQQNAERLaAISAGE 81

                          90
                  ....*....|.
gi 1474260443  81 AVSLEGGYIAW 91
Cdd:cd01527    82 AYVLEGGLDAW 92
MnmA_TRMU-like cd01998
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ...
 139-244 2.78e-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: 39.41  E-value: 2.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443 139 RIAVCISGGKDS----MLMAKCFQE-----LKLHNKFDFEVkfvvmDPGYSPENRKVIEDNAKSLHIPITI------FET 203
Cdd:cd01998     1 KVAVAMSGGVDSsvaaALLKEQGYDvigvfMKNWDDEDNEK-----GGCCSEEDIEDARRVADQLGIPLYVvdfseeYWE 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1474260443 204 DIFDsvYHVE--------NsPCYLC-ARMRRGHLYHFAQQLGCNKIALGH 244
Cdd:cd01998    76 RVFD--PFLEeykagrtpN-PDVLCnREIKFGALLDAAKKLGADYIATGH 122
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
 17-94 8.86e-03

Member of the Rhodanese Homology Domain superfamily. This CD includes the putative rhodanese-like protein, Psp2, of Yersinia pestis biovar Medievalis and other similar uncharacterized proteins.


Pssm-ID: 238779 [Multi-domain]  Cd Length: 110  Bit Score: 35.79  E-value: 8.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260443  17 SYQIVDIRDAVEISHGAIPGALGMKTEEIETSDAIDRSK-KTIICCSRG---RFSVAAAEELQEKGWDAVSLEGGYIAWL 92
Cdd:cd01521    25 DFVLVDVRSAEAYARGHVPGAINLPHREICENATAKLDKeKLFVVYCDGpgcNGATKAALKLAELGFPVKEMIGGLDWWK 104


                  ..
gi 1474260443  93 MD 94
Cdd:cd01521   105 RE 106
 
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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