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Conserved domains on  [gi|1845970063|ref|NP_001370592|]
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Ubiquitin-like modifier-activating enzyme 5 [Caenorhabditis elegans]

Protein Classification

HesA/MoeB/ThiF family protein( domain architecture ID 10091534)

HesA/MoeB/ThiF family protein similar to eukaryotic ubiquitin-activating enzyme 5 (UBA5), a UFM1 (ubiquitin-fold modifier 1) E1-activating enzyme, and to bacterial protein HesA that may be required for efficient nitrogen fixation

CATH:  3.40.50.720
Gene Ontology:  GO:0008641
PubMed:  12660720

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 63-307 6.97e-67

ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis family. The common reaction mechanism catalyzed by MoeB and ThiF, like other E1 enzymes, begins with a nucleophilic attack of the C-terminal carboxylate of MoaD and ThiS, respectively, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD and ThiS. MoeB, as the MPT synthase (MoaE/MoaD complex) sulfurase, is involved in the biosynthesis of the molybdenum cofactor, a derivative of the tricyclic pterin, molybdopterin (MPT). ThiF catalyzes the adenylation of ThiS, as part of the biosynthesis pathway of thiamin pyrophosphate (vitamin B1).


:

Pssm-ID: 238386 [Multi-domain]  Cd Length: 228  Bit Score: 212.34  E-value: 6.97e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063  63 PYSRLMALQRMGIVNEyERIREKTVAVVGVGGVGSVVAEMLTRCGIGKLILFDYDKVEIANMNR-LFYQPNQAGLSKVEA 141
Cdd:cd00757     1 RYSRQILLPEIGEEGQ-EKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRqILHTEADVGQPKAEA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063 142 ARDTLIHVNPDVQIEVHNFNItTMDNFDTFVNRirkgsltdgkIDLVLSCVDNFEARMAVNMACNEENQIWMESGVSEna 221
Cdd:cd00757    80 AAERLRAINPDVEIEAYNERL-DAENAEELIAG----------YDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLG-- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063 222 VSGHIQYIEPGKTACFACVPPLVVASGIdertlkRDGVCAASLPTTMAVVAGFLVMNTLKYLLNFGEV--SQYVGYNALS 299
Cdd:cd00757   147 FEGQVTVFIPGEGPCYRCLFPEPPPPGV------PSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPlaGRLLLFDALS 220


                  ....*...
gi 1845970063 300 DFFPRDSI 307
Cdd:cd00757   221 MSFRTLKL 228
 
Name Accession Description Interval E-value
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 63-307 6.97e-67

ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis family. The common reaction mechanism catalyzed by MoeB and ThiF, like other E1 enzymes, begins with a nucleophilic attack of the C-terminal carboxylate of MoaD and ThiS, respectively, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD and ThiS. MoeB, as the MPT synthase (MoaE/MoaD complex) sulfurase, is involved in the biosynthesis of the molybdenum cofactor, a derivative of the tricyclic pterin, molybdopterin (MPT). ThiF catalyzes the adenylation of ThiS, as part of the biosynthesis pathway of thiamin pyrophosphate (vitamin B1).


Pssm-ID: 238386 [Multi-domain]  Cd Length: 228  Bit Score: 212.34  E-value: 6.97e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063  63 PYSRLMALQRMGIVNEyERIREKTVAVVGVGGVGSVVAEMLTRCGIGKLILFDYDKVEIANMNR-LFYQPNQAGLSKVEA 141
Cdd:cd00757     1 RYSRQILLPEIGEEGQ-EKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRqILHTEADVGQPKAEA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063 142 ARDTLIHVNPDVQIEVHNFNItTMDNFDTFVNRirkgsltdgkIDLVLSCVDNFEARMAVNMACNEENQIWMESGVSEna 221
Cdd:cd00757    80 AAERLRAINPDVEIEAYNERL-DAENAEELIAG----------YDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLG-- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063 222 VSGHIQYIEPGKTACFACVPPLVVASGIdertlkRDGVCAASLPTTMAVVAGFLVMNTLKYLLNFGEV--SQYVGYNALS 299
Cdd:cd00757   147 FEGQVTVFIPGEGPCYRCLFPEPPPPGV------PSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPlaGRLLLFDALS 220


                  ....*...
gi 1845970063 300 DFFPRDSI 307
Cdd:cd00757   221 MSFRTLKL 228
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 64-313 1.83e-45

ThiF family; This domain is found in ubiquitin activating E1 family and members of the bacterial ThiF/MoeB/HesA family. It is repeated in Ubiquitin-activating enzyme E1.


Pssm-ID: 459987 [Multi-domain]  Cd Length: 238  Bit Score: 157.03  E-value: 1.83e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063  64 YSRLMALQRMGiVNEYERIREKTVAVVGVGGVGSVVAEMLTRCGIGKLILFDYDKVEIANMNRLF-YQPNQAGLSKVEAA 142
Cdd:pfam00899   1 YSRQLALPLIG-EDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFlFREADIGKPKAEVA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063 143 RDTLIHVNPDVQIEVHNFNITTmDNFDTFVNrirkgsltdgKIDLVLSCVDNFEARMAVNMACNEENQIWMESGVSenAV 222
Cdd:pfam00899  80 AERLREINPDVEVEAYTERLTP-ENAEELIK----------SFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVL--GF 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063 223 SGHIQYIEPGKTACFACvpplvVASGIDERTLKRDGVCAASLPTTMAVVAGFLVMNTLKYLLNFGEVS---QYVGYNALS 299
Cdd:pfam00899 147 KGQVTVVIPGKTPCYRC-----LFPEDPPPKLVPSCTVAGVLGPTTAVVAGLQALEALKLLLGKGEPNlagRLLQFDALT 221

                         250
                  ....*....|....*
gi 1845970063 300 DFFPRDSIK-PNPYC 313
Cdd:pfam00899 222 MTFRELRLAlKNPNC 236
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 101-313 1.05e-35

Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; Molybdopterin or thiamine biosynthesis adenylyltransferase is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440244 [Multi-domain]  Cd Length: 244  Bit Score: 131.40  E-value: 1.05e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063 101 EMLTRCGIGKLILFDYDKVEIANMNR-LFYQPNQAGLSKVEAARDTLIHVNPDVQIEVHNFNITTmDNFDTFVnrirkgs 179
Cdd:COG0476    44 LYLAAAGVGTLTLVDDDVVELSNLQRqILYTEADVGRPKVEAAAERLRALNPDVEVEAIPERLTE-ENALELL------- 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063 180 ltdGKIDLVLSCVDNFEARMAVNMACNEENQIWMESGVSEnaVSGHIQYIEPGKTACFACVPPLVVASGIDERTlkrdgv 259
Cdd:COG0476   116 ---AGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIG--FEGQVTVFIPGDTPCYRCLFPEPPEPGPSCAE------ 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1845970063 260 cAASLPTTMAVVAGFLVMNTLKYLLNFGE--VSQYVGYNALSDFFPRDSIKPNPYC 313
Cdd:COG0476   185 -AGVLGPLVGVIGSLQATEAIKLLTGIGEplAGRLLLFDALTMEFRTIKLPRDPDC 239
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
102-202 5.00e-21

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 90.69  E-value: 5.00e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063 102 MLTRCGIGKLILFDYDKVEIANMNRLFYQPNQAGLSKVEAARDTLIHVNPDVQIEVHNFNITTmDNFDTFVnrirkgslt 181
Cdd:PRK08644   46 ALARSGVGNLKLVDFDVVEPSNLNRQQYFISQIGMPKVEALKENLLEINPFVEIEAHNEKIDE-DNIEELF--------- 115

                          90       100
                  ....*....|....*....|..
gi 1845970063 182 dGKIDLVLSCVDNFEA-RMAVN 202
Cdd:PRK08644  116 -KDCDIVVEAFDNAETkAMLVE 136
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 109-234 1.33e-06

ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino acids, of a multicopy family of eukaryotic proteins, many of which are designated ubiquitin-activating enzyme E1. Members have two copies of the ThiF family domain (pfam00899), a repeat found in ubiquitin-activating proteins (pfam02134), and other regions.


Pssm-ID: 273603 [Multi-domain]  Cd Length: 1006  Bit Score: 50.66  E-value: 1.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063  109 GKLILFDYDKVEIANMNRLF-YQPNQAGLSKVEAARDTLIHVNPDVQIEVHNfnittmdnfdtfvNRIrkGSLTDG---- 183
Cdd:TIGR01408  449 GMITVTDPDLIEKSNLNRQFlFRPHHIGKPKSYTAADATLKINPQIKIDAHQ-------------NRV--GPETETifnd 513

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1845970063  184 ----KIDLVLSCVDNFEARMAVNMACNEENQIWMESGVSenAVSGHIQYIEPGKT 234
Cdd:TIGR01408  514 efyeKLDVVINALDNVEARRYVDSRCLAFLKPLLESGTL--GTKGNTQVVVPHLT 566
 
Name Accession Description Interval E-value
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 63-307 6.97e-67

ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis family. The common reaction mechanism catalyzed by MoeB and ThiF, like other E1 enzymes, begins with a nucleophilic attack of the C-terminal carboxylate of MoaD and ThiS, respectively, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD and ThiS. MoeB, as the MPT synthase (MoaE/MoaD complex) sulfurase, is involved in the biosynthesis of the molybdenum cofactor, a derivative of the tricyclic pterin, molybdopterin (MPT). ThiF catalyzes the adenylation of ThiS, as part of the biosynthesis pathway of thiamin pyrophosphate (vitamin B1).


Pssm-ID: 238386 [Multi-domain]  Cd Length: 228  Bit Score: 212.34  E-value: 6.97e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063  63 PYSRLMALQRMGIVNEyERIREKTVAVVGVGGVGSVVAEMLTRCGIGKLILFDYDKVEIANMNR-LFYQPNQAGLSKVEA 141
Cdd:cd00757     1 RYSRQILLPEIGEEGQ-EKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRqILHTEADVGQPKAEA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063 142 ARDTLIHVNPDVQIEVHNFNItTMDNFDTFVNRirkgsltdgkIDLVLSCVDNFEARMAVNMACNEENQIWMESGVSEna 221
Cdd:cd00757    80 AAERLRAINPDVEIEAYNERL-DAENAEELIAG----------YDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLG-- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063 222 VSGHIQYIEPGKTACFACVPPLVVASGIdertlkRDGVCAASLPTTMAVVAGFLVMNTLKYLLNFGEV--SQYVGYNALS 299
Cdd:cd00757   147 FEGQVTVFIPGEGPCYRCLFPEPPPPGV------PSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPlaGRLLLFDALS 220


                  ....*...
gi 1845970063 300 DFFPRDSI 307
Cdd:cd00757   221 MSFRTLKL 228
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 64-313 1.83e-45

ThiF family; This domain is found in ubiquitin activating E1 family and members of the bacterial ThiF/MoeB/HesA family. It is repeated in Ubiquitin-activating enzyme E1.


Pssm-ID: 459987 [Multi-domain]  Cd Length: 238  Bit Score: 157.03  E-value: 1.83e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063  64 YSRLMALQRMGiVNEYERIREKTVAVVGVGGVGSVVAEMLTRCGIGKLILFDYDKVEIANMNRLF-YQPNQAGLSKVEAA 142
Cdd:pfam00899   1 YSRQLALPLIG-EDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFlFREADIGKPKAEVA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063 143 RDTLIHVNPDVQIEVHNFNITTmDNFDTFVNrirkgsltdgKIDLVLSCVDNFEARMAVNMACNEENQIWMESGVSenAV 222
Cdd:pfam00899  80 AERLREINPDVEVEAYTERLTP-ENAEELIK----------SFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVL--GF 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063 223 SGHIQYIEPGKTACFACvpplvVASGIDERTLKRDGVCAASLPTTMAVVAGFLVMNTLKYLLNFGEVS---QYVGYNALS 299
Cdd:pfam00899 147 KGQVTVVIPGKTPCYRC-----LFPEDPPPKLVPSCTVAGVLGPTTAVVAGLQALEALKLLLGKGEPNlagRLLQFDALT 221

                         250
                  ....*....|....*
gi 1845970063 300 DFFPRDSIK-PNPYC 313
Cdd:pfam00899 222 MTFRELRLAlKNPNC 236
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 101-313 1.05e-35

Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; Molybdopterin or thiamine biosynthesis adenylyltransferase is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440244 [Multi-domain]  Cd Length: 244  Bit Score: 131.40  E-value: 1.05e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063 101 EMLTRCGIGKLILFDYDKVEIANMNR-LFYQPNQAGLSKVEAARDTLIHVNPDVQIEVHNFNITTmDNFDTFVnrirkgs 179
Cdd:COG0476    44 LYLAAAGVGTLTLVDDDVVELSNLQRqILYTEADVGRPKVEAAAERLRALNPDVEVEAIPERLTE-ENALELL------- 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063 180 ltdGKIDLVLSCVDNFEARMAVNMACNEENQIWMESGVSEnaVSGHIQYIEPGKTACFACVPPLVVASGIDERTlkrdgv 259
Cdd:COG0476   116 ---AGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIG--FEGQVTVFIPGDTPCYRCLFPEPPEPGPSCAE------ 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1845970063 260 cAASLPTTMAVVAGFLVMNTLKYLLNFGE--VSQYVGYNALSDFFPRDSIKPNPYC 313
Cdd:COG0476   185 -AGVLGPLVGVIGSLQATEAIKLLTGIGEplAGRLLLFDALTMEFRTIKLPRDPDC 239
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
102-202 5.00e-21

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 90.69  E-value: 5.00e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063 102 MLTRCGIGKLILFDYDKVEIANMNRLFYQPNQAGLSKVEAARDTLIHVNPDVQIEVHNFNITTmDNFDTFVnrirkgslt 181
Cdd:PRK08644   46 ALARSGVGNLKLVDFDVVEPSNLNRQQYFISQIGMPKVEALKENLLEINPFVEIEAHNEKIDE-DNIEELF--------- 115

                          90       100
                  ....*....|....*....|..
gi 1845970063 182 dGKIDLVLSCVDNFEA-RMAVN 202
Cdd:PRK08644  116 -KDCDIVVEAFDNAETkAMLVE 136
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 101-283 2.97e-16

thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 79.27  E-value: 2.97e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063 101 EMLTRCGIGKLILFDYDKVEIANMNR--LFYQPN-QAGLSKVEAARDTLIHVNPDVQIEVHNFNITTmDNFDTFVnrirk 177
Cdd:PRK07688   41 EMLVRAGVGKVTIVDRDYVEWSNLQRqqLYTESDvKNNLPKAVAAKKRLEEINSDVRVEAIVQDVTA-EELEELV----- 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063 178 gsltdGKIDLVLSCVDNFEARMAVNMACNEENQIWMESGvsenAVSGH-IQY-IEPGKTACFACVPPLVVASGIderTLK 255
Cdd:PRK07688  115 -----TGVDLIIDATDNFETRFIVNDAAQKYGIPWIYGA----CVGSYgLSYtIIPGKTPCLRCLLQSIPLGGA---TCD 182

                         170       180       190
                  ....*....|....*....|....*....|
gi 1845970063 256 RDGVCAaslpttMAV--VAGFLVMNTLKYL 283
Cdd:PRK07688  183 TAGIIS------PAVqiVASYQVTEALKLL 206
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 102-217 7.52e-15

E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. The common reaction mechanism catalyzed by E1-like enzymes begins with a nucleophilic attack of the C-terminal carboxylate of the ubiquitin-like substrate, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of the substrate. The exact function of this family is unknown.


Pssm-ID: 238764 [Multi-domain]  Cd Length: 174  Bit Score: 72.03  E-value: 7.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063 102 MLTRCGIGKLILFDYDKVEIANMNRLFYQPNQAGLSKVEAARDTLIHVNPDVQIEVHNFNITTMDNFDTFvnrirkgslt 181
Cdd:cd01487    17 LLARSGVGNLKLVDFDVVEPSNLNRQQYFLSQIGEPKVEALKENLREINPFVKIEAINIKIDENNLEGLF---------- 86

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1845970063 182 dGKIDLVLSCVDNFEAR--MAVNMACNEENQIWMESGV 217
Cdd:cd01487    87 -GDCDIVVEAFDNAETKamLAESLLGNKNKPVVCASGM 123
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 64-285 1.55e-14

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 74.38  E-value: 1.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063  64 YSRLMALQRMGIVNEyERIREKTVAVVGVGGVGSVVAEMLTRCGIGKLILFDYDKVEIANMNR--LFYQPN-QAGLSKVE 140
Cdd:PRK12475    5 YSRQILFSGIGEEGQ-RKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRqqLYTEEDaKQKKPKAI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063 141 AARDTLIHVNPDVQIEVHNFNItTMDNFDTFVNrirkgsltdgKIDLVLSCVDNFEARMAVNMACNEENQIWMESG-VSE 219
Cdd:PRK12475   84 AAKEHLRKINSEVEIVPVVTDV-TVEELEELVK----------EVDLIIDATDNFDTRLLINDLSQKYNIPWIYGGcVGS 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1845970063 220 NAVSghiQYIEPGKTACFACVPPLVVASGIDERTlkrdgvcAASLPTTMAVVAGFLVMNTLKYLLN 285
Cdd:PRK12475  153 YGVT---YTIIPGKTPCLRCLMEHVPVGGATCDT-------AGIIQPAVQIVVAYQVTEALKILVE 208
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 93-218 2.33e-14

Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes classical ubiquitin-activating enzymes E1, ubiquitin-like (ubl) activating enzymes and other mechanistic homologes, like MoeB, Thif1 and others. The common reaction mechanism catalyzed by MoeB, ThiF and the E1 enzymes begins with a nucleophilic attack of the C-terminal carboxylate of MoaD, ThiS and ubiquitin, respectively, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD and ThiS.


Pssm-ID: 238760 [Multi-domain]  Cd Length: 143  Bit Score: 69.99  E-value: 2.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063  93 GGVGSVVAEMLTRCGIGKLILFDYDKVEIANMNR-LFYQPNQAGLSKVEAARDTLIHVNPDVQIEVHNFNITTMDNFDTF 171
Cdd:cd01483     8 GGLGSEIALNLARSGVGKITLIDFDTVELSNLNRqFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEGISEDNLDDFL 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1845970063 172 vnrirkgsltdGKIDLVLSCVDNFEARMAVNMACNEENQIWMESGVS 218
Cdd:cd01483    88 -----------DGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGL 123
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 101-209 8.88e-14

tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and biogenesis]; tRNA A37 threonylcarbamoyladenosine dehydratase is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440792  Cd Length: 247  Bit Score: 70.50  E-value: 8.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063 101 EMLTRCGIGKLILFDYDKVEIANMNRlfyqpnQA-------GLSKVEAARDTLIHVNPDVQIEVHNFNITTmDNFDTFVn 173
Cdd:COG1179    41 EALARSGVGRLTLVDLDDVCESNINR------QLhaldstvGRPKVEVMAERIRDINPDCEVTAIDEFVTP-ENADELL- 112

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1845970063 174 rirkgsltDGKIDLVLSCVDNFEARMAVNMACNEEN 209
Cdd:COG1179   113 --------SEDYDYVIDAIDSVSAKAALIAWCRRRG 140
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 93-241 2.87e-13

Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating enzyme (E1), specific for the SUMO family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. The E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by SUMO family of ubiquitin-like proteins (Ublps) is involved in cell division, nuclear transport, the stress response and signal transduction. UBA2 contains both the nucleotide-binding motif involved in adenylation and the catalytic cysteine involved in the thioester intermediate and Ublp transfer to E2.


Pssm-ID: 238766 [Multi-domain]  Cd Length: 312  Bit Score: 70.10  E-value: 2.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063  93 GGVGSVVAEMLTRCGIGKLILFDYDKVEIANMNRLF-YQPNQAGLSKVEAARDTLIHVNPDVQIEVHNFNITTMD-NFDT 170
Cdd:cd01489     8 GGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFlFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKDPDfNVEF 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1845970063 171 FvnrirkgsltdGKIDLVLSCVDNFEARMAVNMACNEENQIWMESGVSenAVSGHIQYIEPGKTACFACVP 241
Cdd:cd01489    88 F-----------KQFDLVFNALDNLAARRHVNKMCLAADVPLIESGTT--GFLGQVQVIKKGKTECYECQP 145
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 93-313 7.19e-12

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 64.87  E-value: 7.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063  93 GGVGSVVAEMLTRCGIGKLILFDYDKVEIANMNR-LFYQPNQAGLSKVEAARDTLIHVNPDVQIEVHNFNITTmDNFDTF 171
Cdd:PRK05690   41 GGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRqVLHDDATIGQPKVESARAALARINPHIAIETINARLDD-DELAAL 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063 172 VNRirkgsltdgkIDLVLSCVDNFEARMAVNMACNEENQ-------IWMEsgvsenavsGHIQYIEPGKTA-CFACVPPL 243
Cdd:PRK05690  120 IAG----------HDLVLDCTDNVATRNQLNRACFAAKKplvsgaaIRME---------GQVTVFTYQDDEpCYRCLSRL 180

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1845970063 244 VVASGIderTLKRDGVcaaslpttMAVVAGFL----VMNTLKYLLNFGEVSqyVG----YNALSDFFPRDSIKPNPYC 313
Cdd:PRK05690  181 FGENAL---TCVEAGV--------MAPLVGVIgslqAMEAIKLLTGYGEPL--SGrlllYDAMTMQFREMKLKRDPGC 245
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 93-242 4.10e-10

Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present universally in eukaryotic cells, is part of cascade to attach ubiquitin (Ub) covalently to substrate proteins. This cascade consists of activating (E1), conjugating (E2), and/or ligating (E3) enzymes and then targets them for degradation by the 26S proteasome. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and ubiquitin's C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. A set of novel molecules with a structural similarity to Ub, called Ub-like proteins (Ubls), have similar conjugation cascades. In contrast to ubiquitin-E1, which is a single-chain protein with a weakly conserved two-fold repeat, many of the Ubls-E1are a heterodimer where each subunit corresponds to one half of a single-chain E1. This CD represents the family homologous to the second repeat of Ub-E1.


Pssm-ID: 238761 [Multi-domain]  Cd Length: 234  Bit Score: 59.51  E-value: 4.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063  93 GGVGSVVAEMLTRCGIGKLILFDYDKVEIANMNRLF-YQPNQAGLSKVEAARDTLIHVNPDVQIEVHNFNITTMDNF-DT 170
Cdd:cd01484     8 GGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFlFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQNKVGPEQDFnDT 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1845970063 171 FVNrirkgsltdgKIDLVLSCVDNFEARMAVNMACNEENQIWMESGVSenAVSGHIQYIEPGKTACFACV--PP 242
Cdd:cd01484    88 FFE----------QFHIIVNALDNIIARRYVNGMLIFLIVPLIESGTE--GFKGNAQVILPGMTECIECTlyPP 149
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 93-200 9.74e-10

Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli hypothetical protein ygdL. The common reaction mechanism catalyzed by E1-like enzymes begins with a nucleophilic attack of the C-terminal carboxylate of the ubiquitin-like substrate, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of the substrate. The exact function of this family is unknown.


Pssm-ID: 238384 [Multi-domain]  Cd Length: 231  Bit Score: 58.39  E-value: 9.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063  93 GGVGSVVAEMLTRCGIGKLILFDYDKVEIANMNR-LFYQPNQAGLSKVEAARDTLIHVNPDVQIEVHNFNITTmDNFDtf 171
Cdd:cd00755    20 GGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRqIHALLSTVGKPKVEVMAERIRDINPECEVDAVEEFLTP-DNSE-- 96

                          90       100
                  ....*....|....*....|....*....
gi 1845970063 172 vnrirkgSLTDGKIDLVLSCVDNFEARMA 200
Cdd:cd00755    97 -------DLLGGDPDFVVDAIDSIRAKVA 118
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 103-239 1.24e-08

Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating enzyme (E1), specific for the Rub family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins. consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin(-like) by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by Rub family of ubiquitin-like proteins (Ublps) activates SCF ubiquitin ligases and is involved in cell cycle control, signaling and embryogenesis. UBA3 contains both the nucleotide-binding motif involved in adenylation and the catalytic cysteine involved in the thioester intermediate and Ublp transfer to E2.


Pssm-ID: 238765 [Multi-domain]  Cd Length: 291  Bit Score: 55.82  E-value: 1.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063 103 LTRCGIGKLILFDYDKVEIANMNRLF-YQPNQAGLSKVEAARDTLIHVNPDVQIEVHNFNITTMDnfDTFVNrirkgslt 181
Cdd:cd01488    18 LALSGFRNIHVIDMDTIDVSNLNRQFlFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQDKD--EEFYR-------- 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1845970063 182 dgKIDLVLSCVDNFEAR-----MAVNMA--CNEENQIWMESGVSEnAVSGHIQYIEPGKTACFAC 239
Cdd:cd01488    88 --QFNIIICGLDSIEARrwingTLVSLLlyEDPESIIPLIDGGTE-GFKGHARVILPGITACIEC 149
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
64-313 1.93e-08

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 55.79  E-value: 1.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063  64 YSRLMALQRMGIVNEyERIREKTVAVVGVGGVGSVVAEMLTRCGIGKLILFDYDKVEIANMNR-LFYQPNQAGLSKVEAA 142
Cdd:PRK08762  116 YSRHLRLPEVGEEGQ-RRLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRqILHTEDRVGQPKVDSA 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063 143 RDTLIHVNPDVQIEVHNFNITTmDNfdtfVNRIRKGsltdgkIDLVLSCVDNFEARMAVNMACneenqIWMESGVSENAV 222
Cdd:PRK08762  195 AQRLAALNPDVQVEAVQERVTS-DN----VEALLQD------VDVVVDGADNFPTRYLLNDAC-----VKLGKPLVYGAV 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063 223 ---SGHIQYIEPGKTA----CFACV----PPLVVASGIDErtlkrDGVCAAsLPTTMavvaGFLVMN-TLKYLLNFGE-- 288
Cdd:PRK08762  259 frfEGQVSVFDAGRQRgqapCYRCLfpepPPPELAPSCAE-----AGVLGV-LPGVI----GLLQATeAIKLLLGIGDpl 328

                         250       260
                  ....*....|....*....|....*
gi 1845970063 289 VSQYVGYNALSDFFPRDSIKPNPYC 313
Cdd:PRK08762  329 TGRLLTFDALAMRFRELRLPPDPHC 353
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 109-234 7.34e-08

Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present universally in eukaryotic cells, is part of cascade to attach ubiquitin (Ub) covalently to substrate proteins. This cascade consists of activating (E1), conjugating (E2), and/or ligating (E3) enzymes and then targets them for degradation by the 26S proteasome. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and ubiquitin's C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Ubiquitin-E1 is a single-chain protein with a weakly conserved two-fold repeat. This CD represents the second repeat of Ub-E1.


Pssm-ID: 238767 [Multi-domain]  Cd Length: 435  Bit Score: 54.22  E-value: 7.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063 109 GKLILFDYDKVEIANMNRLF-YQPNQAGLSKVEAARDTLIHVNPDVQIEVHNFNI--TTMDNF-DTFVNrirkgsltdgK 184
Cdd:cd01490    29 GEITVTDMDNIEKSNLNRQFlFRPHDVGKPKSEVAAAAVKAMNPDLKITALQNRVgpETEHIFnDEFWE----------K 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1845970063 185 IDLVLSCVDNFEARMAVNMACNEENQIWMESGVSenAVSGHIQYIEPGKT 234
Cdd:cd01490    99 LDGVANALDNVDARMYVDRRCVYYRKPLLESGTL--GTKGNTQVVIPHLT 146
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 59-198 1.24e-06

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 50.26  E-value: 1.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063  59 VDSNPYSRLMALQRMGIVNEyERIREKTVAVVGVGGVGSVVAEMLTRCGIGKLILFDYDKVEIANMNRLFYQPNQA-GLS 137
Cdd:PRK05597    4 LDIARYRRQIMLGEIGQQGQ-QSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGvGQP 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1845970063 138 KVEAARDTLIHVNPDVQIEVHNFNITtmdnFDTFVNRIRKGsltdgkiDLVLSCVDNFEAR 198
Cdd:PRK05597   83 KAESAREAMLALNPDVKVTVSVRRLT----WSNALDELRDA-------DVILDGSDNFDTR 132
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 109-234 1.33e-06

ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino acids, of a multicopy family of eukaryotic proteins, many of which are designated ubiquitin-activating enzyme E1. Members have two copies of the ThiF family domain (pfam00899), a repeat found in ubiquitin-activating proteins (pfam02134), and other regions.


Pssm-ID: 273603 [Multi-domain]  Cd Length: 1006  Bit Score: 50.66  E-value: 1.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063  109 GKLILFDYDKVEIANMNRLF-YQPNQAGLSKVEAARDTLIHVNPDVQIEVHNfnittmdnfdtfvNRIrkGSLTDG---- 183
Cdd:TIGR01408  449 GMITVTDPDLIEKSNLNRQFlFRPHHIGKPKSYTAADATLKINPQIKIDAHQ-------------NRV--GPETETifnd 513

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1845970063  184 ----KIDLVLSCVDNFEARMAVNMACNEENQIWMESGVSenAVSGHIQYIEPGKT 234
Cdd:TIGR01408  514 efyeKLDVVINALDNVEARRYVDSRCLAFLKPLLESGTL--GTKGNTQVVVPHLT 566
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 64-313 1.94e-06

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 49.71  E-value: 1.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063  64 YSRLMALQRMGiVNEYERIREKTVAVVGVGGVGSVVAEMLTRCGIGKLILFDYDKVEIANMNR-LFYQPNQAGLSKVEAA 142
Cdd:PRK07878   23 YSRHLIIPDVG-VDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRqVIHGQSDVGRSKAQSA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063 143 RDTLIHVNPDVQIEVHNFNITTMDNFDTFvnrirkgsltdGKIDLVLSCVDNFEARMAVNMACNEENQ--IW-----MES 215
Cdd:PRK07878  102 RDSIVEINPLVNVRLHEFRLDPSNAVELF-----------SQYDLILDGTDNFATRYLVNDAAVLAGKpyVWgsiyrFEG 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063 216 GVS---ENAVSGH-----IQYIEPGktacfacvPPLVVASGIDERTLkrdGVCAASLPTTMAVVAgflvmntLKYLLNFG 287
Cdd:PRK07878  171 QASvfwEDAPDGLglnyrDLYPEPP--------PPGMVPSCAEGGVL---GVLCASIGSIMGTEA-------IKLITGIG 232

                         250       260
                  ....*....|....*....|....*...
gi 1845970063 288 E--VSQYVGYNALSDFFPRDSIKPNPYC 313
Cdd:PRK07878  233 EplLGRLMVYDALEMTYRTIKIRKDPST 260
PRK08223 PRK08223
hypothetical protein; Validated
 103-205 2.18e-06

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 48.91  E-value: 2.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063 103 LTRCGIGKLILFDYDKVEIANMNRLFyqpnQAGLS-----KVEAARDTLIHVNPDVQIEVHNFNITTmDNFDTFVnrirk 177
Cdd:PRK08223   46 LARLGIGKFTIADFDVFELRNFNRQA----GAMMStlgrpKAEVLAEMVRDINPELEIRAFPEGIGK-ENADAFL----- 115

                          90       100       110
                  ....*....|....*....|....*....|
gi 1845970063 178 gsltDGkIDLVLSCVDNFE--ARMAVNMAC 205
Cdd:PRK08223  116 ----DG-VDVYVDGLDFFEfdARRLVFAAC 140
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 65-311 3.15e-06

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 48.72  E-value: 3.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063  65 SRLMALQRMGIvNEYERIREKTVAVVGVGGVGSVVAEMLTRCGIGKLILFDYDKVEIANMNR-LFYQPNQAGLSKVEAAR 143
Cdd:PRK05600   23 ARQLALPGFGI-EQQERLHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRqILFGASDVGRPKVEVAA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063 144 DTLIHVNPDVQIEVHNFNITTMDNFDTFvnrirkgsltdGKIDLVLSCVDNFearmAVNMACNEENQIwmeSGVSenAVS 223
Cdd:PRK05600  102 ERLKEIQPDIRVNALRERLTAENAVELL-----------NGVDLVLDGSDSF----ATKFLVADAAEI---TGTP--LVW 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063 224 GHIQYIEpGKTACFACVPPlvvASGIDERTL---------KRDGVCAASLPTTMAVVAGFLVMNTLKYLLNFGEV--SQY 292
Cdd:PRK05600  162 GTVLRFH-GELAVFNSGPD---HRGVGLRDLfpeqpsgdsIPDCATAGVLGATTAVIGALMATEAIKFLTGIGDVqpGTV 237

                         250
                  ....*....|....*....
gi 1845970063 293 VGYNALSDFFPRDSIKPNP 311
Cdd:PRK05600  238 LSYDALTATTRSFRVGADP 256
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
64-205 1.66e-05

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 46.65  E-value: 1.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063  64 YSRLMALQRMGIVNEyERIREKTVAVVGVGGVGSVVAEMLTRCGIGKLILFDYDKVEIANMNR-LFYQPNQAGLSKVEAA 142
Cdd:PRK07411   19 YSRHLILPEVGLEGQ-KRLKAASVLCIGTGGLGSPLLLYLAAAGIGRIGIVDFDVVDSSNLQRqVIHGTSWVGKPKIESA 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1845970063 143 RDTLIHVNPDVQIEVHNFNITTMDNFDTFVNrirkgsltdgkIDLVLSCVDNFEARMAVNMAC 205
Cdd:PRK07411   98 KNRILEINPYCQVDLYETRLSSENALDILAP-----------YDVVVDGTDNFPTRYLVNDAC 149
PRK08328 PRK08328
hypothetical protein; Provisional
 80-288 2.27e-04

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 42.48  E-value: 2.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063  80 ERIREKTVAVVGVGGVGSVVAEMLTRCGIGKLILFDYDKVEIANMNR--LFYQPNQAGLSKVEAARDTLIHVNPDVQIEv 157
Cdd:PRK08328   23 EKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRqiLHWEEDLGKNPKPLSAKWKLERFNSDIKIE- 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063 158 hnfnittmdnfdTFVNRIRKGSLTD--GKIDLVLSCVDNFEARMAVNMACNEENqIWMESGVSEnAVSGHIQYIEPGKTA 235
Cdd:PRK08328  102 ------------TFVGRLSEENIDEvlKGVDVIVDCLDNFETRYLLDDYAHKKG-IPLVHGAVE-GTYGQVTTIVPGKTK 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1845970063 236 CFACVPPlvvasgideRTLKRDGVCAAsLPTTMAVVAGFLVMNTLKYLLNFGE 288
Cdd:PRK08328  168 RLREIFP---------KVKKKKGKFPI-LGATAGVIGSIQAMEVIKLITGYGE 210
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 93-205 1.55e-03

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 40.17  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970063  93 GGVGSVVAEMLTRCGIGKLILFDYDKVEIANMNRLFYQPNQ-AGLSKVEAARDTLIHVNPDVQievhnfnITTMDNFDTF 171
Cdd:PRK15116   39 GGVGSWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDnVGLAKAEVMAERIRQINPECR-------VTVVDDFITP 111

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1845970063 172 VNrirKGSLTDGKIDLVLSCVDNFEARMAVNMAC 205
Cdd:PRK15116  112 DN---VAEYMSAGFSYVIDAIDSVRPKAALIAYC 142
 
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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