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Conserved domains on  [gi|446922510|ref|WP_000999766|]
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MULTISPECIES: HesA/MoeB/ThiF family protein [Salmonella]

Protein Classification

HesA/MoeB/ThiF family protein( domain architecture ID 11422192)

HesA/MoeB/ThiF family protein is an E1-like enzyme containing an NAD/FAD-binding fold that is involved in molybdopterin and thiamine biosynthesis

CATH:  3.40.50.720
EC:  2.7.7.-
Gene Ontology:  GO:0016779
PubMed:  12660720|11713534|12504674

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 2-245 9.07e-126

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: 356.75  E-value: 9.07e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510   2 NDRDFMRYSRQILLGDIAIEGQQKLLASHVLIVGLGGLGSPAALYLTGAGIGKLTLVDDDDIHLSNLQRQILFTTDDIAG 81
Cdd:COG0476    1 TDEELERYSRQILLPEIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510  82 SKSQVARQRLTRLNPDIELVSLQQRLQGEALRHAVARADVVLDCTDNMATRQEINAACVALNTPLISASAVGFGGQLMVL 161
Cdd:COG0476   81 PKVEAAAERLRALNPDVEVEAIPERLTEENALELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQVTVF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510 162 TPPwEQGCYRCLWPDDVEPERNCRTAGIVGPVVGVMGTLQALEAIKLLSGMETP-SGELRLFDGKTSQWRSLALRRASGC 240
Cdd:COG0476  161 IPG-DTPCYRCLFPEPPEPGPSCAEAGVLGPLVGVIGSLQATEAIKLLTGIGEPlAGRLLLFDALTMEFRTIKLPRDPDC 239


                 ....*
gi 446922510 241 PVCGG 245
Cdd:COG0476  240 PVCGE 244
 
Name Accession Description Interval E-value
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 2-245 9.07e-126

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: 356.75  E-value: 9.07e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510   2 NDRDFMRYSRQILLGDIAIEGQQKLLASHVLIVGLGGLGSPAALYLTGAGIGKLTLVDDDDIHLSNLQRQILFTTDDIAG 81
Cdd:COG0476    1 TDEELERYSRQILLPEIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510  82 SKSQVARQRLTRLNPDIELVSLQQRLQGEALRHAVARADVVLDCTDNMATRQEINAACVALNTPLISASAVGFGGQLMVL 161
Cdd:COG0476   81 PKVEAAAERLRALNPDVEVEAIPERLTEENALELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQVTVF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510 162 TPPwEQGCYRCLWPDDVEPERNCRTAGIVGPVVGVMGTLQALEAIKLLSGMETP-SGELRLFDGKTSQWRSLALRRASGC 240
Cdd:COG0476  161 IPG-DTPCYRCLFPEPPEPGPSCAEAGVLGPLVGVIGSLQATEAIKLLTGIGEPlAGRLLLFDALTMEFRTIKLPRDPDC 239


                 ....*
gi 446922510 241 PVCGG 245
Cdd:COG0476  240 PVCGE 244
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 8-234 6.83e-112

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: 320.96  E-value: 6.83e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510   8 RYSRQILLGDIAIEGQQKLLASHVLIVGLGGLGSPAALYLTGAGIGKLTLVDDDDIHLSNLQRQILFTTDDIAGSKSQVA 87
Cdd:cd00757    1 RYSRQILLPEIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510  88 RQRLTRLNPDIELVSLQQRLQGEALRHAVARADVVLDCTDNMATRQEINAACVALNTPLISASAVGFGGQLMVLTpPWEQ 167
Cdd:cd00757   81 AERLRAINPDVEIEAYNERLDAENAEELIAGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLGFEGQVTVFI-PGEG 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446922510 168 GCYRCLWPDDVEPE-RNCRTAGIVGPVVGVMGTLQALEAIKLLSGMETP-SGELRLFDGKTSQWRSLAL 234
Cdd:cd00757  160 PCYRCLFPEPPPPGvPSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPlAGRLLLFDALSMSFRTLKL 228
adenyl_thiF TIGR02356
thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB ...
 8-209 1.12e-104

thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB/ThiF family of proteins (pfam00899) include a number of members encoded in the midst of thiamine biosynthetic operons. This mix of known and putative ThiF proteins shows a deep split in phylogenetic trees, with the Escherichia. coli ThiF and the E. coli MoeB proteins seemingly more closely related than E. coli ThiF and Campylobacter (for example) ThiF. This model represents the more widely distributed clade of ThiF proteins such found in E. coli. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 274094  Cd Length: 202  Bit Score: 301.58  E-value: 1.12e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510    8 RYSRQILLGDIAIEGQQKLLASHVLIVGLGGLGSPAALYLTGAGIGKLTLVDDDDIHLSNLQRQILFTTDDIAGSKSQVA 87
Cdd:TIGR02356   1 RYARQLLLPDIGEEGQQRLLNSHVLIIGAGGLGSPAALYLAGAGVGTIVIVDDDHVDLSNLQRQILFTEEDVGRPKVEVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510   88 RQRLTRLNPDIELVSLQQRLQGEALRHAVARADVVLDCTDNMATRQEINAACVALNTPLISASAVGFGGQLMVLTPPWEQ 167
Cdd:TIGR02356  81 AQRLRELNSDIQVTALKERVTAENLELLINNVDLVLDCTDNFATRYLINDACVALGTPLISAAVVGFGGQLMVFDPGGEG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 446922510  168 GCYRCLWPDDVEPERNCRTAGIVGPVVGVMGTLQALEAIKLL 209
Cdd:TIGR02356 161 PCLRCLFPDIADTGPSCATAGVIGPVVGVIGSLQALEALKLL 202
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 1-240 3.16e-100

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 292.13  E-value: 3.16e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510   1 MNDRDFMRYSRQILLGDIAIEGQQKLLASHVLIVGLGGLGSPAALYLTGAGIGKLTLVDDDDIHLSNLQRQILFTTDDIA 80
Cdd:PRK05690   5 LSDEEMLRYNRQIILRGFDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510  81 GSKSQVARQRLTRLNPDIELVSLQQRLQGEALRHAVARADVVLDCTDNMATRQEINAACVALNTPLISASAVGFGGQLMV 160
Cdd:PRK05690  85 QPKVESARAALARINPHIAIETINARLDDDELAALIAGHDLVLDCTDNVATRNQLNRACFAAKKPLVSGAAIRMEGQVTV 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510 161 LTPPWEQGCYRCLWPDDVEPERNCRTAGIVGPVVGVMGTLQALEAIKLLSGMETP-SGELRLFDGKTSQWRSLALRRASG 239
Cdd:PRK05690 165 FTYQDDEPCYRCLSRLFGENALTCVEAGVMAPLVGVIGSLQAMEAIKLLTGYGEPlSGRLLLYDAMTMQFREMKLKRDPG 244


                 .
gi 446922510 240 C 240
Cdd:PRK05690 245 C 245
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 9-242 7.96e-98

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: 285.69  E-value: 7.96e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510    9 YSRQILLGDIAIEGQQKLLASHVLIVGLGGLGSPAALYLTGAGIGKLTLVDDDDIHLSNLQRQILFTTDDIAGSKSQVAR 88
Cdd:pfam00899   1 YSRQLALPLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510   89 QRLTRLNPDIELVSLQQRLQGEALRHAVARADVVLDCTDNMATRQEINAACVALNTPLISASAVGFGGQLMVLTPPwEQG 168
Cdd:pfam00899  81 ERLREINPDVEVEAYTERLTPENAEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVVIPG-KTP 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446922510  169 CYRCLWPDDVEPE--RNCRTAGIVGPVVGVMGTLQALEAIKLLSG--METPSGELRLFDGKTSQWRSLALR-RASGCPV 242
Cdd:pfam00899 160 CYRCLFPEDPPPKlvPSCTVAGVLGPTTAVVAGLQALEALKLLLGkgEPNLAGRLLQFDALTMTFRELRLAlKNPNCPV 238
 
Name Accession Description Interval E-value
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 2-245 9.07e-126

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: 356.75  E-value: 9.07e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510   2 NDRDFMRYSRQILLGDIAIEGQQKLLASHVLIVGLGGLGSPAALYLTGAGIGKLTLVDDDDIHLSNLQRQILFTTDDIAG 81
Cdd:COG0476    1 TDEELERYSRQILLPEIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510  82 SKSQVARQRLTRLNPDIELVSLQQRLQGEALRHAVARADVVLDCTDNMATRQEINAACVALNTPLISASAVGFGGQLMVL 161
Cdd:COG0476   81 PKVEAAAERLRALNPDVEVEAIPERLTEENALELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQVTVF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510 162 TPPwEQGCYRCLWPDDVEPERNCRTAGIVGPVVGVMGTLQALEAIKLLSGMETP-SGELRLFDGKTSQWRSLALRRASGC 240
Cdd:COG0476  161 IPG-DTPCYRCLFPEPPEPGPSCAEAGVLGPLVGVIGSLQATEAIKLLTGIGEPlAGRLLLFDALTMEFRTIKLPRDPDC 239


                 ....*
gi 446922510 241 PVCGG 245
Cdd:COG0476  240 PVCGE 244
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 8-234 6.83e-112

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: 320.96  E-value: 6.83e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510   8 RYSRQILLGDIAIEGQQKLLASHVLIVGLGGLGSPAALYLTGAGIGKLTLVDDDDIHLSNLQRQILFTTDDIAGSKSQVA 87
Cdd:cd00757    1 RYSRQILLPEIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510  88 RQRLTRLNPDIELVSLQQRLQGEALRHAVARADVVLDCTDNMATRQEINAACVALNTPLISASAVGFGGQLMVLTpPWEQ 167
Cdd:cd00757   81 AERLRAINPDVEIEAYNERLDAENAEELIAGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLGFEGQVTVFI-PGEG 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446922510 168 GCYRCLWPDDVEPE-RNCRTAGIVGPVVGVMGTLQALEAIKLLSGMETP-SGELRLFDGKTSQWRSLAL 234
Cdd:cd00757  160 PCYRCLFPEPPPPGvPSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPlAGRLLLFDALSMSFRTLKL 228
adenyl_thiF TIGR02356
thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB ...
 8-209 1.12e-104

thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB/ThiF family of proteins (pfam00899) include a number of members encoded in the midst of thiamine biosynthetic operons. This mix of known and putative ThiF proteins shows a deep split in phylogenetic trees, with the Escherichia. coli ThiF and the E. coli MoeB proteins seemingly more closely related than E. coli ThiF and Campylobacter (for example) ThiF. This model represents the more widely distributed clade of ThiF proteins such found in E. coli. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 274094  Cd Length: 202  Bit Score: 301.58  E-value: 1.12e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510    8 RYSRQILLGDIAIEGQQKLLASHVLIVGLGGLGSPAALYLTGAGIGKLTLVDDDDIHLSNLQRQILFTTDDIAGSKSQVA 87
Cdd:TIGR02356   1 RYARQLLLPDIGEEGQQRLLNSHVLIIGAGGLGSPAALYLAGAGVGTIVIVDDDHVDLSNLQRQILFTEEDVGRPKVEVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510   88 RQRLTRLNPDIELVSLQQRLQGEALRHAVARADVVLDCTDNMATRQEINAACVALNTPLISASAVGFGGQLMVLTPPWEQ 167
Cdd:TIGR02356  81 AQRLRELNSDIQVTALKERVTAENLELLINNVDLVLDCTDNFATRYLINDACVALGTPLISAAVVGFGGQLMVFDPGGEG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 446922510  168 GCYRCLWPDDVEPERNCRTAGIVGPVVGVMGTLQALEAIKLL 209
Cdd:TIGR02356 161 PCLRCLFPDIADTGPSCATAGVIGPVVGVIGSLQALEALKLL 202
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 1-240 3.16e-100

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 292.13  E-value: 3.16e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510   1 MNDRDFMRYSRQILLGDIAIEGQQKLLASHVLIVGLGGLGSPAALYLTGAGIGKLTLVDDDDIHLSNLQRQILFTTDDIA 80
Cdd:PRK05690   5 LSDEEMLRYNRQIILRGFDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510  81 GSKSQVARQRLTRLNPDIELVSLQQRLQGEALRHAVARADVVLDCTDNMATRQEINAACVALNTPLISASAVGFGGQLMV 160
Cdd:PRK05690  85 QPKVESARAALARINPHIAIETINARLDDDELAALIAGHDLVLDCTDNVATRNQLNRACFAAKKPLVSGAAIRMEGQVTV 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510 161 LTPPWEQGCYRCLWPDDVEPERNCRTAGIVGPVVGVMGTLQALEAIKLLSGMETP-SGELRLFDGKTSQWRSLALRRASG 239
Cdd:PRK05690 165 FTYQDDEPCYRCLSRLFGENALTCVEAGVMAPLVGVIGSLQAMEAIKLLTGYGEPlSGRLLLYDAMTMQFREMKLKRDPG 244


                 .
gi 446922510 240 C 240
Cdd:PRK05690 245 C 245
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 9-242 7.96e-98

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: 285.69  E-value: 7.96e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510    9 YSRQILLGDIAIEGQQKLLASHVLIVGLGGLGSPAALYLTGAGIGKLTLVDDDDIHLSNLQRQILFTTDDIAGSKSQVAR 88
Cdd:pfam00899   1 YSRQLALPLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510   89 QRLTRLNPDIELVSLQQRLQGEALRHAVARADVVLDCTDNMATRQEINAACVALNTPLISASAVGFGGQLMVLTPPwEQG 168
Cdd:pfam00899  81 ERLREINPDVEVEAYTERLTPENAEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVVIPG-KTP 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446922510  169 CYRCLWPDDVEPE--RNCRTAGIVGPVVGVMGTLQALEAIKLLSG--METPSGELRLFDGKTSQWRSLALR-RASGCPV 242
Cdd:pfam00899 160 CYRCLFPEDPPPKlvPSCTVAGVLGPTTAVVAGLQALEALKLLLGkgEPNLAGRLLQFDALTMTFRELRLAlKNPNCPV 238
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
1-244 4.04e-82

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 250.70  E-value: 4.04e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510   1 MNDRDFMRYSRQILLGDIAIEGQQKLLASHVLIVGLGGLGSPAALYLTGAGIGKLTLVDDDDIHLSNLQRQILFTTDDIA 80
Cdd:PRK08762 108 LTDEQDERYSRHLRLPEVGEEGQRRLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVG 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510  81 GSKSQVARQRLTRLNPDIELVSLQQRLQGEALRHAVARADVVLDCTDNMATRQEINAACVALNTPLISASAVGFGGQLMV 160
Cdd:PRK08762 188 QPKVDSAAQRLAALNPDVQVEAVQERVTSDNVEALLQDVDVVVDGADNFPTRYLLNDACVKLGKPLVYGAVFRFEGQVSV 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510 161 LTP--PWEQG-CYRCLWPDDVEPE--RNCRTAGIVGPVVGVMGTLQALEAIKLLSGMETP-SGELRLFDGKTSQWRSLAL 234
Cdd:PRK08762 268 FDAgrQRGQApCYRCLFPEPPPPElaPSCAEAGVLGVLPGVIGLLQATEAIKLLLGIGDPlTGRLLTFDALAMRFRELRL 347

                        250
                 ....*....|
gi 446922510 235 RRASGCPVCG 244
Cdd:PRK08762 348 PPDPHCPVCA 357
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 5-229 3.62e-64

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 203.95  E-value: 3.62e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510   5 DFMRYSRQILLGDIAIEGQQKLLASHVLIVGLGGLGSPAALYLTGAGIGKLTLVDDDDIHLSNLQRQILFTTDDIAGSKS 84
Cdd:PRK05597   5 DIARYRRQIMLGEIGQQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVGQPKA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510  85 QVARQRLTRLNPDIELVSLQQRLQGEALRHAVARADVVLDCTDNMATRQEINAACVALNTPLISASAVGFGGQLMVLTPp 164
Cdd:PRK05597  85 ESAREAMLALNPDVKVTVSVRRLTWSNALDELRDADVILDGSDNFDTRHLASWAAARLGIPHVWASILGFDAQLSVFHA- 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446922510 165 wEQG-CYRCLWPDDVEPER--NCRTAGIVGPVVGVMGTLQALEAIKLLSGMETP-SGELRLFDGKTSQW 229
Cdd:PRK05597 164 -GHGpIYEDLFPTPPPPGSvpSCSQAGVLGPVVGVVGSAMAMEALKLITGVGTPlIGKLGYYDSLDGTW 231
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 1-244 4.16e-56

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 182.50  E-value: 4.16e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510   1 MNDRdfmrYSRQILLGDIAIEGQQKLLASHVLIVGLGGLGSPAALYLTGAGIGKLTLVDDDDIHLSNLQRQILFTTDDIA 80
Cdd:PRK07688   1 MNER----YSRQELFSPIGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDVK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510  81 GS--KSQVARQRLTRLNPDIELVSLQQRLQGEALRHAVARADVVLDCTDNMATRQEINAACVALNTPLISASAVG-FGGQ 157
Cdd:PRK07688  77 NNlpKAVAAKKRLEEINSDVRVEAIVQDVTAEELEELVTGVDLIIDATDNFETRFIVNDAAQKYGIPWIYGACVGsYGLS 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510 158 LMVLtpPWEQGCYRCLWPDDVEPERNCRTAGIVGPVVGVMGTLQALEAIKLLSG-METPSGELRLFD---GKTSQWRSLA 233
Cdd:PRK07688 157 YTII--PGKTPCLRCLLQSIPLGGATCDTAGIISPAVQIVASYQVTEALKLLVGdYEALRDGLVSFDvwkNEYSCMNVQK 234

                        250
                 ....*....|.
gi 446922510 234 LRRaSGCPVCG 244
Cdd:PRK07688 235 LKK-DNCPSCG 244
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
1-242 1.79e-54

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 179.93  E-value: 1.79e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510   1 MNDRDFMRYSRQILLGDIAIEGQQKLLASHVLIVGLGGLGSPAALYLTGAGIGKLTLVDDDDIHLSNLQRQILFTTDDIA 80
Cdd:PRK07411  11 LSKDEYERYSRHLILPEVGLEGQKRLKAASVLCIGTGGLGSPLLLYLAAAGIGRIGIVDFDVVDSSNLQRQVIHGTSWVG 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510  81 GSKSQVARQRLTRLNPDIELVSLQQRLQGEALRHAVARADVVLDCTDNMATRQEINAACVALNTPLISASAVGFGGQLMV 160
Cdd:PRK07411  91 KPKIESAKNRILEINPYCQVDLYETRLSSENALDILAPYDVVVDGTDNFPTRYLVNDACVLLNKPNVYGSIFRFEGQATV 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510 161 LTppWEQG-CYRCLWPDDVEPER--NCRTAGIVGPVVGVMGTLQALEAIKLLSGME-TPSGELRLFDGKTSQWRSLALRR 236
Cdd:PRK07411 171 FN--YEGGpNYRDLYPEPPPPGMvpSCAEGGVLGILPGIIGVIQATETIKIILGAGnTLSGRLLLYNALDMKFRELKLRP 248


                 ....*.
gi 446922510 237 ASGCPV 242
Cdd:PRK07411 249 NPERPV 254
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 8-241 7.49e-54

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 178.36  E-value: 7.49e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510   8 RYSRQILLGDIAIEGQQKLLASHVLIVGLGGLGSPAALYLTGAGIGKLTLVDDDDIHLSNLQRQILFTTDDIAGSKSQVA 87
Cdd:PRK07878  22 RYSRHLIIPDVGVDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRQVIHGQSDVGRSKAQSA 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510  88 RQRLTRLNPDIELVSLQQRLQGEALRHAVARADVVLDCTDNMATRQEINAACVALNTPLISASAVGFGGQLMVL--TPPW 165
Cdd:PRK07878 102 RDSIVEINPLVNVRLHEFRLDPSNAVELFSQYDLILDGTDNFATRYLVNDAAVLAGKPYVWGSIYRFEGQASVFweDAPD 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510 166 EQG-CYRCLWPDDVEPER--NCRTAGIVGPVVGVMGTLQALEAIKLLSGM-ETPSGELRLFDGKTSQWRSLALRRASGCP 241
Cdd:PRK07878 182 GLGlNYRDLYPEPPPPGMvpSCAEGGVLGVLCASIGSIMGTEAIKLITGIgEPLLGRLMVYDALEMTYRTIKIRKDPSTP 261
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 8-244 7.37e-48

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 161.44  E-value: 7.37e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510   8 RYSRQILLGDIAIEGQQKLLASHVLIVGLGGLGSPAALYLTGAGIGKLTLVDDDDIHLSNLQRQILFTTDDIAGS--KSQ 85
Cdd:PRK12475   4 RYSRQILFSGIGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTEEDAKQKkpKAI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510  86 VARQRLTRLNPDIELVSLQQRLQGEALRHAVARADVVLDCTDNMATRQEINAACVALNTPLISASAVGFGGQLMVLTPPw 165
Cdd:PRK12475  84 AAKEHLRKINSEVEIVPVVTDVTVEELEELVKEVDLIIDATDNFDTRLLINDLSQKYNIPWIYGGCVGSYGVTYTIIPG- 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510 166 EQGCYRCLWPDDVEPERNCRTAGIVGPVVGVMGTLQALEAIKLLSG-METPSGELRLFDGKTSQWRSLALRR--ASGCPV 242
Cdd:PRK12475 163 KTPCLRCLMEHVPVGGATCDTAGIIQPAVQIVVAYQVTEALKILVEdFEALRETFLSFDIWNNQNMSIKVNKqkKDTCPS 242


                 ..
gi 446922510 243 CG 244
Cdd:PRK12475 243 CG 244
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 1-231 2.78e-47

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 160.82  E-value: 2.78e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510   1 MNDRDFMRYSRQILLGDIAIEGQQKLLASHVLIVGLGGLGSPAALYLTGAGIGKLTLVDDDDIHLSNLQRQILFTTDDIA 80
Cdd:PRK05600  14 LPTSELRRTARQLALPGFGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDVG 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510  81 GSKSQVARQRLTRLNPDIELVSLQQRLQGEALRHAVARADVVLDCTDNMATRQEINAACVALNTPLISASAVGFGGQLMV 160
Cdd:PRK05600  94 RPKVEVAAERLKEIQPDIRVNALRERLTAENAVELLNGVDLVLDGSDSFATKFLVADAAEITGTPLVWGTVLRFHGELAV 173

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446922510 161 LT-PPWEQGC-YRCLWPD----DVEPerNCRTAGIVGPVVGVMGTLQALEAIKLLSGMETPS-GELRLFDGKTSQWRS 231
Cdd:PRK05600 174 FNsGPDHRGVgLRDLFPEqpsgDSIP--DCATAGVLGATTAVIGALMATEAIKFLTGIGDVQpGTVLSYDALTATTRS 249
PRK08328 PRK08328
hypothetical protein; Provisional
 1-215 7.01e-44

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 148.02  E-value: 7.01e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510   1 MNDRDFMRYSRQILLgdIAIEGQQKLLASHVLIVGLGGLGSPAALYLTGAGIGKLTLVDDDDIHLSNLQRQILFTTDDI- 79
Cdd:PRK08328   2 LSERELERYDRQIMI--FGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEDLg 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510  80 AGSKSQVARQRLTRLNPDIELVSLQQRLQGEALRHAVARADVVLDCTDNMATRQEINAACVALNTPLISASAVGFGGQLM 159
Cdd:PRK08328  80 KNPKPLSAKWKLERFNSDIKIETFVGRLSEENIDEVLKGVDVIVDCLDNFETRYLLDDYAHKKGIPLVHGAVEGTYGQVT 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446922510 160 VLTPPWEQGcYRCLWPddvEPERNCRTAGIVGPVVGVMGTLQALEAIKLLSGMETP 215
Cdd:PRK08328 160 TIVPGKTKR-LREIFP---KVKKKKGKFPILGATAGVIGSIQAMEVIKLITGYGEP 211
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 30-164 4.95e-36

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: 124.69  E-value: 4.95e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510  30 HVLIVGLGGLGSPAALYLTGAGIGKLTLVDDDDIHLSNLQRQILFTTDDIAGSKSQVARQRLTRLNPDIELVSLQQRLQG 109
Cdd:cd01483    1 RVLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEGISE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446922510 110 EALRHAVARADVVLDCTDNMATRQEINAACVALNTPLISASAVGFGGQLMVLTPP 164
Cdd:cd01483   81 DNLDDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQVIDIG 135
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 8-158 2.20e-33

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: 120.96  E-value: 2.20e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510   8 RYSR-QILLGDiaiEGQQKLLASHVLIVGLGGLGSPAALYLTGAGIGKLTLVDDDDIHLSNLQRQILFTTDDIAGSKSQV 86
Cdd:COG1179    6 RFSRtERLYGE---EGLERLANAHVAVVGLGGVGSWAAEALARSGVGRLTLVDLDDVCESNINRQLHALDSTVGRPKVEV 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446922510  87 ARQRLTRLNPDIELVSLQQRLQGEALRHAV-ARADVVLDCTDNMATRQEINAACVALNTPLIsaSAVGFGGQL 158
Cdd:COG1179   83 MAERIRDINPDCEVTAIDEFVTPENADELLsEDYDYVIDAIDSVSAKAALIAWCRRRGIPII--SSMGAGGKL 153
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 21-206 2.60e-30

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: 112.70  E-value: 2.60e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510  21 EGQQKLLASHVLIVGLGGLGSPAALYLTGAGIGKLTLVDDDDIHLSNLQRQILFTTDDIAGSKSQVARQRLTRLNPDIEL 100
Cdd:cd00755    4 EGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPECEV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510 101 VSLQQRLQGEALRHAVARA-DVVLDCTDNMATRQEINAACVALNTPLISASAVG-------------------------- 153
Cdd:cd00755   84 DAVEEFLTPDNSEDLLGGDpDFVVDAIDSIRAKVALIAYCRKRKIPVISSMGAGgkldptrirvadisktsgdplarkvr 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446922510 154 --------FGG-------QLMVLTPPWEQGCYRCLWPDDVEPERNCRTAGIVGPVVGVMGTLQALEAI 206
Cdd:cd00755  164 krlrkrgiFFGvpvvystEPPDPPKADELVCGDEVGADAALQGLRRAGLGSASTVPAVFGLAIASEVI 231
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 31-172 5.42e-24

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: 97.84  E-value: 5.42e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510  31 VLIVGLGGLGSPAALYLTGAGIGKLTLVDDDDIHLSNLQRQILFTTDDIAGSKSQVARQRLTRLNPDIELVSLQQRLQGE 110
Cdd:cd01489    2 VLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKDP 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446922510 111 alRHAVA---RADVVLDCTDNMATRQEINAACVALNTPLISASAVGFGGQLMVLTPPWEQgCYRC 172
Cdd:cd01489   82 --DFNVEffkQFDLVFNALDNLAARRHVNKMCLAADVPLIESGTTGFLGQVQVIKKGKTE-CYEC 143
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
23-156 9.47e-24

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 94.92  E-value: 9.47e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510  23 QQKLLASHVLIVGLGGLGSPAALYLTGAGIGKLTLVDDDDIHLSNLQRQILFtTDDIAGSKSQVARQRLTRLNPDIELVS 102
Cdd:PRK08644  23 LEKLKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVVEPSNLNRQQYF-ISQIGMPKVEALKENLLEINPFVEIEA 101

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446922510 103 LQQRLQGEALRHAVARADVVLDCTDNMATRQEI-NAACVALNTPLISASAV-GFGG 156
Cdd:PRK08644 102 HNEKIDEDNIEELFKDCDIVVEAFDNAETKAMLvETVLEHPGKKLVAASGMaGYGD 157
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 30-156 1.27e-22

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: 90.90  E-value: 1.27e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510  30 HVLIVGLGGLGSPAALYLTGAGIGKLTLVDDDDIHLSNLQRQILFtTDDIAGSKSQVARQRLTRLNPDIELVSLQQRLQG 109
Cdd:cd01487    1 KVGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQYF-LSQIGEPKVEALKENLREINPFVKIEAINIKIDE 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 446922510 110 EALRHAVARADVVLDCTDNMATRQEI-NAACVALNTPLISASAVGFGG 156
Cdd:cd01487   80 NNLEGLFGDCDIVVEAFDNAETKAMLaESLLGNKNKPVVCASGMAGFG 127
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 9-227 2.05e-22

Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 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. Aos1 contains part of the adenylation domain.


Pssm-ID: 238769 [Multi-domain]  Cd Length: 197  Bit Score: 91.20  E-value: 2.05e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510   9 YSRQILLGdiAIEGQQKLLASHVLIVGLGGLGSPAALYLTGAGIGKLTLVDDDDIHLSNLQRQILFTTDDIAGSKSQVAR 88
Cdd:cd01492    4 YDRQIRLW--GLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEASL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510  89 QRLTRLNPDIElVSLQQRLQGEALRHAVARADVVLDCTDNMATRQEINAACVALNTPLISASAVGFGGQLMVltppweqg 168
Cdd:cd01492   82 ERLRALNPRVK-VSVDTDDISEKPEEFFSQFDVVVATELSRAELVKINELCRKLGVKFYATGVHGLFGFVFA-------- 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446922510 169 cyrCLWPddveperncrtagivgPVVGVMGTLQALEAIKLLSGMETPSGELRLFDGKTS 227
Cdd:cd01492  153 ---DLLA----------------PVAAVVGGILAQDVINALSKRESPLNNFFVFDGETS 192
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 31-172 8.07e-21

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: 87.63  E-value: 8.07e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510  31 VLIVGLGGLGSPAALYLTGAGIGKLTLVDDDDIHLSNLQRQILFTTDDIAGSKSQVARQRLTRLNPDIELVSLQQRLQGE 110
Cdd:cd01484    2 VLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQNKVGPE 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446922510 111 AL--RHAVARADVVLDCTDNMATRQEINAACVALNTPLISASAVGFGGQLMVLTPPWEQgCYRC 172
Cdd:cd01484   82 QDfnDTFFEQFHIIVNALDNIIARRYVNGMLIFLIVPLIESGTEGFKGNAQVILPGMTE-CIEC 144
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 9-160 3.88e-18

Ubiquitin activating enzyme (E1), repeat 1. 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 first repeat of Ub-E1.


Pssm-ID: 238768 [Multi-domain]  Cd Length: 286  Bit Score: 81.54  E-value: 3.88e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510   9 YSRQI-LLGDIAIegqQKLLASHVLIVGLGGLGSPAALYLTGAGIGKLTLVDDDDIHLSNLQRQILFTTDDIAGSKSQVA 87
Cdd:cd01491    2 YSRQLyVLGHEAM---KKLQKSNVLISGLGGLGVEIAKNLILAGVKSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAEAS 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446922510  88 RQRLTRLNPDIELVSLQQRLQGEALrhavARADVVLDCTDNMATRQEINAACVALNTPLISASAVGFGGQLMV 160
Cdd:cd01491   79 QARLAELNPYVPVTVSTGPLTTDEL----LKFQVVVLTDASLEDQLKINEFCHSPGIKFISADTRGLFGSIFC 147
thiF_fam2 TIGR02354
thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins ...
 24-132 5.82e-17

thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins (pfam00899) include a number of members encoded in the midst of thiamine biosynthetic operons. This mix of known and putative ThiF proteins shows a deep split in phylogenetic trees, with one the E. coli ThiF and the E. coli MoeB proteins seemingly more closely related than E. coli ThiF and Campylobacter (for example) ThiF. This model represents the divergent clade of putative ThiF proteins such found in Campylobacter. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 162819  Cd Length: 200  Bit Score: 76.45  E-value: 5.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510   24 QKLLASHVLIVGLGGLGSPAALYLTGAGIGKLTLVDDDDIHLSNLQRQILFTTdDIAGSKSQVARQRLTRLNPDIELVSL 103
Cdd:TIGR02354  17 QKLEQATVAICGLGGLGSNVAINLARAGIGKLILVDFDVVEPSNLNRQQYKAS-QVGEPKTEALKENISEINPYTEIEAY 95

                          90       100
                  ....*....|....*....|....*....
gi 446922510  104 QQRLQGEALRHAVARADVVLDCTDNMATR 132
Cdd:TIGR02354  96 DEKITEENIDKFFKDADIVCEAFDNAEAK 124
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 30-163 2.89e-16

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: 77.33  E-value: 2.89e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510  30 HVLIVGLGGLG-----SPAALYLTGAGIGKLTLVDDDDIHLSNLQRQILFTTDDIAGSKSQVARQRLTRLNPDIELVSLQ 104
Cdd:cd01490    1 KVFLVGAGAIGcellkNFALMGVGTGESGEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITALQ 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446922510 105 QRLqGEALRHAV-----ARADVVLDCTDNMATRQEINAACVALNTPLISASAVGFGGQLMVLTP 163
Cdd:cd01490   81 NRV-GPETEHIFndefwEKLDGVANALDNVDARMYVDRRCVYYRKPLLESGTLGTKGNTQVVIP 143
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 8-163 4.42e-16

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: 77.24  E-value: 4.42e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510     8 RYSRQI-LLGDiaiEGQQKLLASHVLIVGLGGLGSP--AALYLTGAGI---GKLTLVDDDDIHLSNLQRQILFTTDDIAG 81
Cdd:TIGR01408  401 RYDAQIaVFGD---TFQQKLQNLNIFLVGCGAIGCEmlKNFALMGVGTgkkGMITVTDPDLIEKSNLNRQFLFRPHHIGK 477

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510    82 SKSQVARQRLTRLNPDIELVSLQQRLQGEALR----HAVARADVVLDCTDNMATRQEINAACVALNTPLISASAVGFGGQ 157
Cdd:TIGR01408  478 PKSYTAADATLKINPQIKIDAHQNRVGPETETifndEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGTLGTKGN 557


                   ....*.
gi 446922510   158 LMVLTP 163
Cdd:TIGR01408  558 TQVVVP 563
PRK08223 PRK08223
hypothetical protein; Validated
 15-163 8.11e-16

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 75.10  E-value: 8.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510  15 LGDIAIEGQQKLLASHVLIVGLGGLGSPAALYLTGAGIGKLTLVDDDDIHLSNLQRQILFTTDDIAGSKSQVARQRLTRL 94
Cdd:PRK08223  14 LGWITPTEQQRLRNSRVAIAGLGGVGGIHLLTLARLGIGKFTIADFDVFELRNFNRQAGAMMSTLGRPKAEVLAEMVRDI 93

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446922510  95 NPDIELVSLQQRLQGEALRHAVARADVVLDCTDNMA--TRQEINAACVALNTPLISASAVGFGGQLMVLTP 163
Cdd:PRK08223  94 NPELEIRAFPEGIGKENADAFLDGVDVYVDGLDFFEfdARRLVFAACQQRGIPALTAAPLGMGTALLVFDP 164
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 11-158 6.90e-15

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 72.14  E-value: 6.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510  11 RQILLGDIAIEGQQKL---LASHVLIVGLGGLGSPAALYLTGAGIGKLTLVDDDDIHLSNLQRQILFTTDDIAGSKSQVA 87
Cdd:PRK15116  10 RQRFGGTARLYGEKALqlfADAHICVVGIGGVGSWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVM 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446922510  88 RQRLTRLNPDIELVSLQQRLQGEALRHAV-ARADVVLDCTDNMATRQEINAACVALNTPLISASavGFGGQL 158
Cdd:PRK15116  90 AERIRQINPECRVTVVDDFITPDNVAEYMsAGFSYVIDAIDSVRPKAALIAYCRRNKIPLVTTG--GAGGQI 159
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 9-227 2.96e-14

Ubiquitin activating enzyme (E1), repeat 1-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. The 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 first repeat of Ub-E1.


Pssm-ID: 238762 [Multi-domain]  Cd Length: 198  Bit Score: 68.99  E-value: 2.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510   9 YSRQI-LLGDiaiEGQQKLLASHVLIVGLGGLGSPAALYLTGAGIGKLTLVDDDDIHLSNLQRQILF--TTDDIAGSKSQ 85
Cdd:cd01485    2 YDRQIrLWGD---EAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFLdaEVSNSGMNRAA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510  86 VARQRLTRLNPDI------ELVSLQQRLQGEALRhavaRADVVLDCTDNMATRQEINAACVALNTPLISasavgfggqlm 159
Cdd:cd01485   79 ASYEFLQELNPNVklsiveEDSLSNDSNIEEYLQ----KFTLVIATEENYERTAKVNDVCRKHHIPFIS----------- 143

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446922510 160 vltppweqgcyrclwpddvepernCRTAGIVG------PVVGVMGTLQALEAIKLLSGMETPSGELRLFDGKTS 227
Cdd:cd01485  144 ------------------------CATYGLIGyaffdfPIAAFLGGVVAQEAIKSISGKFTPLNNLYIYDGFES 193
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 9-158 5.71e-14

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: 71.07  E-value: 5.71e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510     9 YSRQI-LLGDiaiEGQQKLLASHVLIVGLGGLGSPAALYLTGAGIGKLTLVDDDDIHLSNLQRQILFTTDDIAGSKSQVA 87
Cdd:TIGR01408    7 YSRQLyVLGD---EAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRAEAV 83

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446922510    88 RQRLTRLNPDIELVSLQQRLQGEALRHAVAradVVLdcTDNMATRQ-EINAACVALNTPL--ISASAVGFGGQL 158
Cdd:TIGR01408   84 VKKLAELNPYVHVSSSSVPFNEEFLDKFQC---VVL--TEMSLPLQkEINDFCHSQCPPIafISADVRGLFGSL 152
PRK14852 PRK14852
hypothetical protein; Provisional
 9-163 2.31e-13

hypothetical protein; Provisional


Pssm-ID: 184854 [Multi-domain]  Cd Length: 989  Bit Score: 69.34  E-value: 2.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510   9 YSRQILLGDIAieGQQKLLASHVLIVGLGGLGSPAALYLTGAGIGKLTLVDDDDIHLSNLQRQILFTTDDIAGSKSQVAR 88
Cdd:PRK14852 315 FSRNLGLVDYA--GQRRLLRSRVAIAGLGGVGGIHLMTLARTGIGNFNLADFDAYSPVNLNRQYGASIASFGRGKLDVMT 392

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446922510  89 QRLTRLNPDIELVSLQQRLQGEALRHAVARADVVLDCTDNMA--TRQEINAACVALNTPLISASAVGFGGQLMVLTP 163
Cdd:PRK14852 393 ERALSVNPFLDIRSFPEGVAAETIDAFLKDVDLLVDGIDFFAldIRRRLFNRALELGIPVITAGPLGYSCALLVFMP 469
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 30-172 4.36e-13

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: 67.38  E-value: 4.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510  30 HVLIVGLGGLGSPAALYLTGAGIGKLTLVDDDDIHLSNLQRQILFTTDDIAGSKSQVARQRLTRLNPDIELVSLQQRLQ- 108
Cdd:cd01488    1 KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQd 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446922510 109 -GEALRHAVaraDVVLDCTDNMATRQEINAACVAL----NT----PLISASAVGFGGQLMVLTPPWeQGCYRC 172
Cdd:cd01488   81 kDEEFYRQF---NIIICGLDSIEARRWINGTLVSLllyeDPesiiPLIDGGTEGFKGHARVILPGI-TACIEC 149
PRK14851 PRK14851
hypothetical protein; Provisional
 9-163 3.40e-10

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 59.87  E-value: 3.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510   9 YSRQI-LLGDiaieGQQKLLA-SHVLIVGLGGLGSPAALYLTGAGIGKLTLVDDDDIHLSNLQRQILFTTDDIAGSKSQV 86
Cdd:PRK14851  26 FSRNIgLFTP----GEQERLAeAKVAIPGMGGVGGVHLITMVRTGIGRFHIADFDQFEPVNVNRQFGARVPSFGRPKLAV 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510  87 ARQRLTRLNPDIELVSLQQRLQGEALRHAVARADVVLDCTDNMA---TRQEINAAcVALNTPLISASAVGFGGQLMVLTP 163
Cdd:PRK14851 102 MKEQALSINPFLEITPFPAGINADNMDAFLDGVDVVLDGLDFFQfeiRRTLFNMA-REKGIPVITAGPLGYSSAMLVFTP 180
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
 31-99 1.27e-09

Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and Apg8, and assigns them to specific E2 enzymes, Apg10 and Apg3, respectively. This leads to the covalent conjugation of Apg8 with phosphatidylethanolamine, an important step in autophagy. Autophagy is a dynamic membrane phenomenon for bulk protein degradation in the lysosome/vacuole.


Pssm-ID: 238763 [Multi-domain]  Cd Length: 307  Bit Score: 57.38  E-value: 1.27e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446922510  31 VLIVGLGGLGSPAALYLTGAGIGKLTLVDDDDIHLSNLQRQILFTTDDIAGS--KSQVARQRLTRLNPDIE 99
Cdd:cd01486    2 CLLLGAGTLGCNVARNLLGWGVRHITFVDSGKVSYSNPVRQSLFTFEDCKGGkpKAEAAAERLKEIFPSID 72
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 8-156 1.29e-09

Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 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. ABPP1 contains part of the adenylation domain.


Pssm-ID: 238770 [Multi-domain]  Cd Length: 425  Bit Score: 57.70  E-value: 1.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510   8 RYSRQI-LLGDiaiEGQQKLLASHVLIVGLGGLGSPAALYLTGAGIGKLTLVDDDDIHLSNLQRQILFTTDDIAGSKSQV 86
Cdd:cd01493    2 KYDRQLrLWGE---HGQAALESAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAEA 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446922510  87 ARQRLTRLNPDIE----LVSLQQRLQGEAlrHAVARADVVLDCTDNMATRQEINAACVALNTPLISASAVGFGG 156
Cdd:cd01493   79 TCELLQELNPDVNgsavEESPEALLDNDP--SFFSQFTVVIATNLPESTLLRLADVLWSANIPLLYVRSYGLYG 150
cyclo_dehyd_2 TIGR03882
bacteriocin biosynthesis cyclodehydratase domain; This model describes a ThiF-like domain of a ...
 152-252 1.88e-05

bacteriocin biosynthesis cyclodehydratase domain; This model describes a ThiF-like domain of a fusion protein found in clusters associated with the production of TOMMs (thiazole/oxazole-modified microcins), small bacteriocins with characteristic heterocycle modifications. This domain is presumed to act as a cyclodehydratase, as do members of the SagC family modeled by TIGR03603.


Pssm-ID: 274832  Cd Length: 164  Bit Score: 43.88  E-value: 1.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510  152 VGFGGQLMVLTP---PWEQGCYRCL---W----PDDVEPER--NCRTAGIVGPVVGVMGTLQ-----ALEAIKLLSGMET 214
Cdd:TIGR03882   6 VRPSGGEAWIGPlfrPGKPGCWHCLatrLranrPDEAFLARlqGTPLAGPRPPWLTPAALAAvaalaAAELAKWLAGERP 85

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 446922510  215 P-SGELRLFDGKTSQWRSLALRRASGCPVCGGQHADSVQ 252
Cdd:TIGR03882  86 RlEGAVLTLDLATLTVSRHPLLPRPQCPVCGDLPDDTPE 124
E1_like_apg7 TIGR01381
E1-like protein-activating enzyme Gsa7p/Apg7p; This model represents a family of eukaryotic ...
 29-172 4.04e-05

E1-like protein-activating enzyme Gsa7p/Apg7p; This model represents a family of eukaryotic proteins found in animals, plants, and yeasts, including Apg7p (YHR171W) from Saccharomyces cerevisiae and GSA7 from Pichia pastoris. Members are about 650 to 700 residues in length and include a central domain of about 150 residues shared with the ThiF/MoeB/HesA family of proteins. A low level of similarity to ubiquitin-activating enzyme E1 is described in a paper on peroxisome autophagy mediated by GSA7, and is the basis of the name ubiquitin activating enzyme E1-like protein. Members of the family appear to be involved in protein lipidation events analogous to ubiquitination and required for membrane fusion events during autophagy.


Pssm-ID: 273590 [Multi-domain]  Cd Length: 664  Bit Score: 44.55  E-value: 4.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510   29 SHVLIVGLGGLGSPAALYLTGAGIGKLTLVDDDDIHLSNLQRQILFTTDDIAGS---KSQVARQRLTRLNPDIEL----- 100
Cdd:TIGR01381 339 LKVLLLGAGTLGCNVARCLIGWGVRHITFVDNGKVSYSNPVRQSLSNFEDCLLGgrgKAETAQKALKRIFPSIQAtghrl 418

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510  101 --------VSLQQ--RLQGEA--LRHAVARADVVLDCTDNMATRQEINAACVALNTPLISAsAVGFGGQLMV-------- 160
Cdd:TIGR01381 419 tvpmpghpIDEKDvpELEKDIarLEQLIKDHDVVFLLLDSREARWLPTVLCSRHKKIAISA-ALGFDSYVVMrhgigrse 497

                         170       180
                  ....*....|....*....|.
gi 446922510  161 ---------LTPPWEQGCYRC 172
Cdd:TIGR01381 498 svsdvsssdSVPYSRLGCYFC 518
PRK07877 PRK07877
Rv1355c family protein;
18-96 9.95e-03

Rv1355c family protein;


Pssm-ID: 236122 [Multi-domain]  Cd Length: 722  Bit Score: 36.89  E-value: 9.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922510  18 IAIEGQQKLLASHVLIVGLGgLGSPAALYLTGAGI-GKLTLVDDDDIHLSNLQRqILFTTDDIAGSKSQVARQRLTRLNP 96
Cdd:PRK07877  97 ITAEEQERLGRLRIGVVGLS-VGHAIAHTLAAEGLcGELRLADFDTLELSNLNR-VPAGVFDLGVNKAVVAARRIAELDP 174
 
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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