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Conserved domains on  [gi|398366555|ref|NP_010678|]
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E1 ubiquitin-activating protein UBA2 [Saccharomyces cerevisiae S288C]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 23-438 0e+00

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: 520.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  23 RCLLVGAGGIGSELLKDIILMEFGEIHIVDLDTIDLSNLNRQFLFRQKDIKQPKSTTAVKAVQHFN-NSKLVPYQGNVMD 101
Cdd:cd01489    1 KVLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNpNVKIVAYHANIKD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555 102 IsTFPLHWFEQFDIIFNALDNLAARRYVNKISQFLSLPLIESGTAGFDGYMQPIIPGKTECFECTKKETPKTFPVCTIRS 181
Cdd:cd01489   81 P-DFNVEFFKQFDLVFNALDNLAARRHVNKMCLAADVPLIESGTTGFLGQVQVIKKGKTECYECQPKETPKTFPVCTIRS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555 182 TPSQPIHCIVWAKNFLFnqlfasetsgneddnnqdwgtddaeeikrikqetnelyelqkiiisrdasripeILNKLFIQD 261
Cdd:cd01489  160 TPSQPIHCIVWAKSLFF------------------------------------------------------LFNKVFKDD 185

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555 262 INKLLAIENLWKTRTKPVPLSDSQintptktaqsasnsvgtiqeqisnfinitqklmdrypkeqnhIEFDKDDADTLEFV 341
Cdd:cd01489  186 IERLLSMEELWKTRKPPVPLSWKE------------------------------------------LTFDKDDQDALDFV 223

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555 342 ATAANIRSHIFNIPMKSVFDIKQIAGNIIPAIATTNAIVAGASSLISLRVLNLLKYAPTTKYtdlnmaftAKASNLSQNR 421
Cdd:cd01489  224 AAAANLRSHVFGIPMKSRFDIKQMAGNIIPAIATTNAIIAGLIVLEALKVLSGDKEQCRTVF--------LNLQPNRRKR 295

                        410
                 ....*....|....*..
gi 398366555 422 YLSNPKLAPPNKNCPVC 438
Cdd:cd01489  296 LLVPCKLDPPNPNCYVC 312
UBA_E1_SCCH super family cl10464
Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ...
 183-370 1.34e-03

Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ubiquitin by first adenylating with ATP its C-terminal glycine residue and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding an ubiquitin-E1 thiolester and free AMP. Later the ubiquitin moiety is transferred to a cysteine residue on one of the many forms of ubiquitin-conjugating enzymes (E2). This domain carries the last of five conserved cysteines that is part of the active site of the enzyme, responsible for ubiquitin thiolester complex formation, the active site being represented by the sequence motif PICTLKNFP. The catalytic cysteine domain contains the E1 active site cysteine, and is divided in two half-domains, FCCH and SCCH, for 'first' and 'second' catalytic cysteine half-domain, respectively. This is the SCCH domain in which resides the catalytic cysteine.


The actual alignment was detected with superfamily member pfam10585:

Pssm-ID: 463157  Cd Length: 254  Bit Score: 41.06  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  183 PSQPIHCIVWAKNfLFNQLFasetsgneddnnqdwgTDDAEEIKRIKQETNELYE-LQKIIISRDASRIPEILN------ 255
Cdd:pfam10585   1 PNAIEHTIQWARD-EFEGLF----------------VQPPEEVNKYLQPPQNFIEsLLKQGGGQKLETLESVRKslvter 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  256 ----------------KLFIQDINKLLaienlwktRTKPvplsdsqINTPTKTAQ---SASnsvgtiqeqisnfinitqK 316
Cdd:pfam10585  64 pktfedcvawarlkfeKLFNNDIKQLL--------YNFP-------PDHKTSSGApfwSGP------------------K 110

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 398366555  317 lmdRYPKEqnhIEFDKDDADTLEFVATAANIRSHIFNIP-MKSVFDIKQIAGNII 370
Cdd:pfam10585 111 ---RPPTP---LEFDPNNPLHLDFVVAAANLRAQVYGIPgSRDREAIAKVLSKVK 159
UAE_UbL super family cl39046
Ubiquitin/SUMO-activating enzyme ubiquitin-like domain; This is the C-terminal domain of ...
 453-518 2.41e-03

Ubiquitin/SUMO-activating enzyme ubiquitin-like domain; This is the C-terminal domain of ubiquitin-activating enzyme and SUMO-activating enzyme 2. It is structurally similar to ubiquitin. This domain is involved in E1-SUMO-thioester transfer to the SUMO E2 conjugating protein.


The actual alignment was detected with superfamily member pfam14732:

Pssm-ID: 476859  Cd Length: 88  Bit Score: 37.56  E-value: 2.41e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398366555  453 LNKMKLSDFV--VLIRE-KYSYPqDISLLdaSNQRLLF-----DYDFEDLNDRTLSEINLGNGSIILFSDEEGD 518
Cdd:pfam14732   5 TEKATLGDLVedVLKKKlGMVAP-DVSLS--GGGTILYlsseeDETEDDNLPKKLSELGIKNGSILTVDDFLQD 75
 
Name Accession Description Interval E-value
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 23-438 0e+00

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: 520.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  23 RCLLVGAGGIGSELLKDIILMEFGEIHIVDLDTIDLSNLNRQFLFRQKDIKQPKSTTAVKAVQHFN-NSKLVPYQGNVMD 101
Cdd:cd01489    1 KVLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNpNVKIVAYHANIKD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555 102 IsTFPLHWFEQFDIIFNALDNLAARRYVNKISQFLSLPLIESGTAGFDGYMQPIIPGKTECFECTKKETPKTFPVCTIRS 181
Cdd:cd01489   81 P-DFNVEFFKQFDLVFNALDNLAARRHVNKMCLAADVPLIESGTTGFLGQVQVIKKGKTECYECQPKETPKTFPVCTIRS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555 182 TPSQPIHCIVWAKNFLFnqlfasetsgneddnnqdwgtddaeeikrikqetnelyelqkiiisrdasripeILNKLFIQD 261
Cdd:cd01489  160 TPSQPIHCIVWAKSLFF------------------------------------------------------LFNKVFKDD 185

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555 262 INKLLAIENLWKTRTKPVPLSDSQintptktaqsasnsvgtiqeqisnfinitqklmdrypkeqnhIEFDKDDADTLEFV 341
Cdd:cd01489  186 IERLLSMEELWKTRKPPVPLSWKE------------------------------------------LTFDKDDQDALDFV 223

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555 342 ATAANIRSHIFNIPMKSVFDIKQIAGNIIPAIATTNAIVAGASSLISLRVLNLLKYAPTTKYtdlnmaftAKASNLSQNR 421
Cdd:cd01489  224 AAAANLRSHVFGIPMKSRFDIKQMAGNIIPAIATTNAIIAGLIVLEALKVLSGDKEQCRTVF--------LNLQPNRRKR 295

                        410
                 ....*....|....*..
gi 398366555 422 YLSNPKLAPPNKNCPVC 438
Cdd:cd01489  296 LLVPCKLDPPNPNCYVC 312
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 10-182 8.04e-69

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: 223.67  E-value: 8.04e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555   10 IIGEDSYKKLRSSRCLLVGAGGIGSELLKDIILMEFGEIHIVDLDTIDLSNLNRQFLFRQKDIKQPKSTTAVKAVQHFNN 89
Cdd:pfam00899   9 LIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAAERLREINP 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555   90 S-KLVPYQGNVMDisTFPLHWFEQFDIIFNALDNLAARRYVNKISQFLSLPLIESGTAGFDGYMQPIIPGKTECFEC--T 166
Cdd:pfam00899  89 DvEVEAYTERLTP--ENAEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVVIPGKTPCYRClfP 166

                         170
                  ....*....|....*.
gi 398366555  167 KKETPKTFPVCTIRST 182
Cdd:pfam00899 167 EDPPPKLVPSCTVAGV 182
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 3-409 7.59e-49

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: 183.94  E-value: 7.59e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555     3 RETSLVTIIGEDSYKKLRSSRCLLVGAGGIGSELLKDIILM-----EFGEIHIVDLDTIDLSNLNRQFLFRQKDIKQPKS 77
Cdd:TIGR01408  401 RYDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMgvgtgKKGMITVTDPDLIEKSNLNRQFLFRPHHIGKPKS 480

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555    78 TTAVKAVQHFNNS-KLVPYQGNVMDIS--TFPLHWFEQFDIIFNALDNLAARRYVNKISQFLSLPLIESGTAGFDGYMQP 154
Cdd:TIGR01408  481 YTAADATLKINPQiKIDAHQNRVGPETetIFNDEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGTLGTKGNTQV 560

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555   155 IIPGKTECFECTKKETPKTFPVCTIRSTPSQPIHCIVWAKNfLFNQLFasetSGNEDDNNQDWGT-DDAEEIKRIKQETN 233
Cdd:TIGR01408  561 VVPHLTESYGSSRDPPEKEIPFCTLKSFPAAIEHTIQWARD-KFEGLF----SHKPSLVNKYLSSpSSAEEVLQKIQSGH 635

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555   234 ELYELQKII-----------------------------------------------------------ISRDASRiPEIL 254
Cdd:TIGR01408  636 SREGLEQIIkllskekprnfsqcvewarlkfekyfnnkalqllhcfpldirtstgspfwsspkrppspLKFDLNE-PLHL 714

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555   255 NklFIQ-----------------DINKLLAIENLWKTRTKPV-PLSDSQINTPTKTAQSASNSVGTIQEQISNFINITQK 316
Cdd:TIGR01408  715 S--FIQaaaklyatvygipfaeeDLSADALLNILSEVKIPEFkPRSNKKIQTDETARKPDTAPIDDRNAIFQLEKAILSN 792

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555   317 LMDRYPKEQNHIEFDKDDaDT---LEFVATAANIRSHIFNIPMKSVFDIKQIAGNIIPAIATTNAIVAGASSLISLRVLN 393
Cdd:TIGR01408  793 EATKSDFRMAPLSFEKDD-DHnghIDFITAASNLRAKNYSIEPADRFKTKFIAGKIIPAIATSTATVSGLVCLELIKVTD 871

                          490
                   ....*....|....*.
gi 398366555   394 LLKYAPTTKYTDLNMA 409
Cdd:TIGR01408  872 GGYKFEVYKNCFLNLA 887
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 11-177 1.96e-38

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: 142.19  E-value: 1.96e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  11 IGEDSYKKLRSSRCLLVGAGGIGSELLKDIILMEFGEIHIVDLDTIDLSNLNRQFLFRQKDIKQPKSTTAVKAVQHFN-N 89
Cdd:COG0476   17 IGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGRPKVEAAAERLRALNpD 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  90 SKLVPYQG-----NVMDIstfplhwFEQFDIIFNALDNLAARRYVNKISQFLSLPLIESGTAGFDGYMQPIIPGKTECFE 164
Cdd:COG0476   97 VEVEAIPErlteeNALEL-------LAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQVTVFIPGDTPCYR 169

                        170
                 ....*....|...
gi 398366555 165 CTKKETPKTFPVC 177
Cdd:COG0476  170 CLFPEPPEPGPSC 182
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 11-177 3.70e-24

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 104.04  E-value: 3.70e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  11 IGEDSYKKLRSSRCLLVGAGGIGSELLKDIILMEFGEIHIVDLDTIDLSNLNRQFLFRQKDIKQ--PKSTTAVKAVQHFN 88
Cdd:PRK12475  14 IGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTEEDAKQkkPKAIAAKEHLRKIN 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  89 NS-KLVPYqgnVMDISTFPLHWF-EQFDIIFNALDNLAARRYVNKISQFLSLPLIESGTAGFDGYMQPIIPGKTECFECT 166
Cdd:PRK12475  94 SEvEIVPV---VTDVTVEELEELvKEVDLIIDATDNFDTRLLINDLSQKYNIPWIYGGCVGSYGVTYTIIPGKTPCLRCL 170

                        170
                 ....*....|.
gi 398366555 167 KKETPKTFPVC 177
Cdd:PRK12475 171 MEHVPVGGATC 181
UBA_E1_SCCH pfam10585
Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ...
 183-370 1.34e-03

Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ubiquitin by first adenylating with ATP its C-terminal glycine residue and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding an ubiquitin-E1 thiolester and free AMP. Later the ubiquitin moiety is transferred to a cysteine residue on one of the many forms of ubiquitin-conjugating enzymes (E2). This domain carries the last of five conserved cysteines that is part of the active site of the enzyme, responsible for ubiquitin thiolester complex formation, the active site being represented by the sequence motif PICTLKNFP. The catalytic cysteine domain contains the E1 active site cysteine, and is divided in two half-domains, FCCH and SCCH, for 'first' and 'second' catalytic cysteine half-domain, respectively. This is the SCCH domain in which resides the catalytic cysteine.


Pssm-ID: 463157  Cd Length: 254  Bit Score: 41.06  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  183 PSQPIHCIVWAKNfLFNQLFasetsgneddnnqdwgTDDAEEIKRIKQETNELYE-LQKIIISRDASRIPEILN------ 255
Cdd:pfam10585   1 PNAIEHTIQWARD-EFEGLF----------------VQPPEEVNKYLQPPQNFIEsLLKQGGGQKLETLESVRKslvter 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  256 ----------------KLFIQDINKLLaienlwktRTKPvplsdsqINTPTKTAQ---SASnsvgtiqeqisnfinitqK 316
Cdd:pfam10585  64 pktfedcvawarlkfeKLFNNDIKQLL--------YNFP-------PDHKTSSGApfwSGP------------------K 110

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 398366555  317 lmdRYPKEqnhIEFDKDDADTLEFVATAANIRSHIFNIP-MKSVFDIKQIAGNII 370
Cdd:pfam10585 111 ---RPPTP---LEFDPNNPLHLDFVVAAANLRAQVYGIPgSRDREAIAKVLSKVK 159
UAE_UbL pfam14732
Ubiquitin/SUMO-activating enzyme ubiquitin-like domain; This is the C-terminal domain of ...
 453-518 2.41e-03

Ubiquitin/SUMO-activating enzyme ubiquitin-like domain; This is the C-terminal domain of ubiquitin-activating enzyme and SUMO-activating enzyme 2. It is structurally similar to ubiquitin. This domain is involved in E1-SUMO-thioester transfer to the SUMO E2 conjugating protein.


Pssm-ID: 464286  Cd Length: 88  Bit Score: 37.56  E-value: 2.41e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398366555  453 LNKMKLSDFV--VLIRE-KYSYPqDISLLdaSNQRLLF-----DYDFEDLNDRTLSEINLGNGSIILFSDEEGD 518
Cdd:pfam14732   5 TEKATLGDLVedVLKKKlGMVAP-DVSLS--GGGTILYlsseeDETEDDNLPKKLSELGIKNGSILTVDDFLQD 75
 
Name Accession Description Interval E-value
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 23-438 0e+00

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: 520.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  23 RCLLVGAGGIGSELLKDIILMEFGEIHIVDLDTIDLSNLNRQFLFRQKDIKQPKSTTAVKAVQHFN-NSKLVPYQGNVMD 101
Cdd:cd01489    1 KVLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNpNVKIVAYHANIKD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555 102 IsTFPLHWFEQFDIIFNALDNLAARRYVNKISQFLSLPLIESGTAGFDGYMQPIIPGKTECFECTKKETPKTFPVCTIRS 181
Cdd:cd01489   81 P-DFNVEFFKQFDLVFNALDNLAARRHVNKMCLAADVPLIESGTTGFLGQVQVIKKGKTECYECQPKETPKTFPVCTIRS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555 182 TPSQPIHCIVWAKNFLFnqlfasetsgneddnnqdwgtddaeeikrikqetnelyelqkiiisrdasripeILNKLFIQD 261
Cdd:cd01489  160 TPSQPIHCIVWAKSLFF------------------------------------------------------LFNKVFKDD 185

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555 262 INKLLAIENLWKTRTKPVPLSDSQintptktaqsasnsvgtiqeqisnfinitqklmdrypkeqnhIEFDKDDADTLEFV 341
Cdd:cd01489  186 IERLLSMEELWKTRKPPVPLSWKE------------------------------------------LTFDKDDQDALDFV 223

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555 342 ATAANIRSHIFNIPMKSVFDIKQIAGNIIPAIATTNAIVAGASSLISLRVLNLLKYAPTTKYtdlnmaftAKASNLSQNR 421
Cdd:cd01489  224 AAAANLRSHVFGIPMKSRFDIKQMAGNIIPAIATTNAIIAGLIVLEALKVLSGDKEQCRTVF--------LNLQPNRRKR 295

                        410
                 ....*....|....*..
gi 398366555 422 YLSNPKLAPPNKNCPVC 438
Cdd:cd01489  296 LLVPCKLDPPNPNCYVC 312
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 23-389 6.32e-125

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: 368.83  E-value: 6.32e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  23 RCLLVGAGGIGSELLKDIILMEFGEIHIVDLDTIDLSNLNRQFLFRQKDIKQPKSTTAVKAVQHFN-NSKLVPYQGNVMD 101
Cdd:cd01484    1 KVLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNpNCKVVPYQNKVGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555 102 ISTFPLHWFEQFDIIFNALDNLAARRYVNKISQFLSLPLIESGTAGFDGYMQPIIPGKTECFECTKKETPKTFPVCTIRS 181
Cdd:cd01484   81 EQDFNDTFFEQFHIIVNALDNIIARRYVNGMLIFLIVPLIESGTEGFKGNAQVILPGMTECIECTLYPPQKNFPMCTIAS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555 182 TPSQPIHCIVWAKNFLFnqlfasetsgneddnnqdwgtddaeeikrikqetnelyelqkiiisrdasripeilnklfiqd 261
Cdd:cd01484  161 MPRLPEHCIEWARMLQW--------------------------------------------------------------- 177

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555 262 inkllaienlwktrtkpvplsdsqintptktaqsasnsvgtiqeqisnfinitqklmdrypkeqnhiefdkDDADTLEFV 341
Cdd:cd01484  178 -----------------------------------------------------------------------DDPEHIQFI 186

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 398366555 342 ATAANIRSHIFNIPMKSVFDIKQIAGNIIPAIATTNAIVAGASSLISL 389
Cdd:cd01484  187 FQASNERASQYNIRGVTYFLTKGVAGRIIPAVATTNAVVAGVCALEVF 234
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 10-182 8.04e-69

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: 223.67  E-value: 8.04e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555   10 IIGEDSYKKLRSSRCLLVGAGGIGSELLKDIILMEFGEIHIVDLDTIDLSNLNRQFLFRQKDIKQPKSTTAVKAVQHFNN 89
Cdd:pfam00899   9 LIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAAERLREINP 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555   90 S-KLVPYQGNVMDisTFPLHWFEQFDIIFNALDNLAARRYVNKISQFLSLPLIESGTAGFDGYMQPIIPGKTECFEC--T 166
Cdd:pfam00899  89 DvEVEAYTERLTP--ENAEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVVIPGKTPCYRClfP 166

                         170
                  ....*....|....*.
gi 398366555  167 KKETPKTFPVCTIRST 182
Cdd:pfam00899 167 EDPPPKLVPSCTVAGV 182
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 23-409 6.24e-62

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: 212.15  E-value: 6.24e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  23 RCLLVGAGGIGSELLKDIILM-----EFGEIHIVDLDTIDLSNLNRQFLFRQKDIKQPKSTTAVKAVQHFNNS-KLVPYQ 96
Cdd:cd01490    1 KVFLVGAGAIGCELLKNFALMgvgtgESGEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDlKITALQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  97 gNVMDIST---FPLHWFEQFDIIFNALDNLAARRYVNKISQFLSLPLIESGTAGFDGYMQPIIPGKTECFECTKKETPKT 173
Cdd:cd01490   81 -NRVGPETehiFNDEFWEKLDGVANALDNVDARMYVDRRCVYYRKPLLESGTLGTKGNTQVVIPHLTESYSSSRDPPEKS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555 174 FPVCTIRSTPSQPIHCIVWAKNfLFNQLFaseTSGNEDDNNQDWgtDDAEEIKRIKQEtnelyelqkiiisrdasripei 253
Cdd:cd01490  160 IPLCTLKNFPNAIEHTIQWARD-EFEGLF---KQPPENVNQYLF--EDCVRWARLLFE---------------------- 211

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555 254 lnKLFIQDINKLL------AI----ENLWKTRTKPvplsdsqintPTKTAQSASNsvgtiqEQISNFINITQKLmdrYPK 323
Cdd:cd01490  212 --KYFNNNIKQLLhnfppdAVtsdgAPFWSGPKRC----------PTPLEFDVNN------PLHLDFVLAAANL---YAE 270

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555 324 EQNHIEFDKDDaDT---LEFVATAANIRSHIFNIPMKSVFDIKQIAGNIIPAIATTNAIVAGASSLISLRVLNLLKYAPT 400
Cdd:cd01490  271 VYGIPGFEKDD-DTnfhMDFITAASNLRARNYSIPPADRHKTKRIAGKIIPAIATTTAAVTGLVCLELYKVVDGKRPLEA 349


                 ....*....
gi 398366555 401 TKYTDLNMA 409
Cdd:cd01490  350 YKNAFLNLA 358
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 23-439 1.09e-57

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: 196.04  E-value: 1.09e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  23 RCLLVGAGGIGSELLKDIILMEFGEIHIVDLDTIDLSNLNRQFLFRQKDIKQPKSTTAVKAV-QHFNNSKLVPYQGnvmD 101
Cdd:cd01488    1 KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVnDRVPGVNVTPHFG---K 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555 102 ISTFPLHWFEQFDIIFNALDNLAARRYVNKISQFLSL--------PLIESGTAGFDGYMQPIIPGKTECFECTKKETPK- 172
Cdd:cd01488   78 IQDKDEEFYRQFNIIICGLDSIEARRWINGTLVSLLLyedpesiiPLIDGGTEGFKGHARVILPGITACIECSLDLFPPq 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555 173 -TFPVCTIRSTPSQPIHCIVWAKnflfnqlfasetsgneddnnqdwgtddaeeikrikqetnelyelqkiiisrdasrip 251
Cdd:cd01488  158 vTFPLCTIANTPRLPEHCIEYAS--------------------------------------------------------- 180

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555 252 eilnklfiqdinkllaienlwktrtkpvplsdsqintptktaqsasnsvgTIQeqisnfinitqklmdrYPKEQNHIEFD 331
Cdd:cd01488  181 --------------------------------------------------LIQ----------------WPKEFPFVPLD 194

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555 332 KDDADTLEFVATAANIRSHIFNIPMKSVFDIKQIAGNIIPAIATTNAIVAGASSLISLRVL-----NLLKYaptTKYTDL 406
Cdd:cd01488  195 GDDPEHIEWLYQKALERAAQFNISGVTYSLTQGVVKRIIPAVASTNAIIAAACCLEALKIAtdcyeNLNNY---LMYNGV 271

                        410       420       430
                 ....*....|....*....|....*....|...
gi 398366555 407 NMAFTakasnlsqnrYLSNpklAPPNKNCPVCS 439
Cdd:cd01488  272 DGCYT----------YTFE---HERKEDCPVCS 291
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 3-409 7.59e-49

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: 183.94  E-value: 7.59e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555     3 RETSLVTIIGEDSYKKLRSSRCLLVGAGGIGSELLKDIILM-----EFGEIHIVDLDTIDLSNLNRQFLFRQKDIKQPKS 77
Cdd:TIGR01408  401 RYDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMgvgtgKKGMITVTDPDLIEKSNLNRQFLFRPHHIGKPKS 480

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555    78 TTAVKAVQHFNNS-KLVPYQGNVMDIS--TFPLHWFEQFDIIFNALDNLAARRYVNKISQFLSLPLIESGTAGFDGYMQP 154
Cdd:TIGR01408  481 YTAADATLKINPQiKIDAHQNRVGPETetIFNDEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGTLGTKGNTQV 560

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555   155 IIPGKTECFECTKKETPKTFPVCTIRSTPSQPIHCIVWAKNfLFNQLFasetSGNEDDNNQDWGT-DDAEEIKRIKQETN 233
Cdd:TIGR01408  561 VVPHLTESYGSSRDPPEKEIPFCTLKSFPAAIEHTIQWARD-KFEGLF----SHKPSLVNKYLSSpSSAEEVLQKIQSGH 635

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555   234 ELYELQKII-----------------------------------------------------------ISRDASRiPEIL 254
Cdd:TIGR01408  636 SREGLEQIIkllskekprnfsqcvewarlkfekyfnnkalqllhcfpldirtstgspfwsspkrppspLKFDLNE-PLHL 714

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555   255 NklFIQ-----------------DINKLLAIENLWKTRTKPV-PLSDSQINTPTKTAQSASNSVGTIQEQISNFINITQK 316
Cdd:TIGR01408  715 S--FIQaaaklyatvygipfaeeDLSADALLNILSEVKIPEFkPRSNKKIQTDETARKPDTAPIDDRNAIFQLEKAILSN 792

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555   317 LMDRYPKEQNHIEFDKDDaDT---LEFVATAANIRSHIFNIPMKSVFDIKQIAGNIIPAIATTNAIVAGASSLISLRVLN 393
Cdd:TIGR01408  793 EATKSDFRMAPLSFEKDD-DHnghIDFITAASNLRAKNYSIEPADRFKTKFIAGKIIPAIATSTATVSGLVCLELIKVTD 871

                          490
                   ....*....|....*.
gi 398366555   394 LLKYAPTTKYTDLNMA 409
Cdd:TIGR01408  872 GGYKFEVYKNCFLNLA 887
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 23-165 6.18e-40

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: 142.79  E-value: 6.18e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  23 RCLLVGAGGIGSELLKDIILMEFGEIHIVDLDTIDLSNLNRQFLFRQKDIKQPKSTTAVKAVQHFN-NSKLVPYQGNVMD 101
Cdd:cd01483    1 RVLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNpGVNVTAVPEGISE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398366555 102 ISTfpLHWFEQFDIIFNALDNLAARRYVNKISQFLSLPLIESGTAGFDGYMQPIIPGKTECFEC 165
Cdd:cd01483   81 DNL--DDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQVIDIGSLSAAEA 142
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 11-177 1.96e-38

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: 142.19  E-value: 1.96e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  11 IGEDSYKKLRSSRCLLVGAGGIGSELLKDIILMEFGEIHIVDLDTIDLSNLNRQFLFRQKDIKQPKSTTAVKAVQHFN-N 89
Cdd:COG0476   17 IGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGRPKVEAAAERLRALNpD 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  90 SKLVPYQG-----NVMDIstfplhwFEQFDIIFNALDNLAARRYVNKISQFLSLPLIESGTAGFDGYMQPIIPGKTECFE 164
Cdd:COG0476   97 VEVEAIPErlteeNALEL-------LAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQVTVFIPGDTPCYR 169

                        170
                 ....*....|...
gi 398366555 165 CTKKETPKTFPVC 177
Cdd:COG0476  170 CLFPEPPEPGPSC 182
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 11-165 3.56e-36

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: 135.30  E-value: 3.56e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  11 IGEDSYKKLRSSRCLLVGAGGIGSELLKDIILMEFGEIHIVDLDTIDLSNLNRQFLFRQKDIKQPKSTTAVKAVQHFNNS 90
Cdd:cd00757   11 IGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAAAERLRAINPD 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  91 -KLVPYQ-----GNVMDIstfplhwFEQFDIIFNALDNLAARRYVNKISQFLSLPLIESGTAGFDGYMQPIIPGKTECFE 164
Cdd:cd00757   91 vEIEAYNerldaENAEEL-------IAGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLGFEGQVTVFIPGEGPCYR 163


                 .
gi 398366555 165 C 165
Cdd:cd00757  164 C 164
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 11-177 3.70e-24

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 104.04  E-value: 3.70e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  11 IGEDSYKKLRSSRCLLVGAGGIGSELLKDIILMEFGEIHIVDLDTIDLSNLNRQFLFRQKDIKQ--PKSTTAVKAVQHFN 88
Cdd:PRK12475  14 IGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTEEDAKQkkPKAIAAKEHLRKIN 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  89 NS-KLVPYqgnVMDISTFPLHWF-EQFDIIFNALDNLAARRYVNKISQFLSLPLIESGTAGFDGYMQPIIPGKTECFECT 166
Cdd:PRK12475  94 SEvEIVPV---VTDVTVEELEELvKEVDLIIDATDNFDTRLLINDLSQKYNIPWIYGGCVGSYGVTYTIIPGKTPCLRCL 170

                        170
                 ....*....|.
gi 398366555 167 KKETPKTFPVC 177
Cdd:PRK12475 171 MEHVPVGGATC 181
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
11-171 8.00e-22

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 97.77  E-value: 8.00e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  11 IGEDSYKKLRSSRCLLVGAGGIGSELLKDIILMEFGEIHIVDLDTIDLSNLNRQFLFRQKDIKQPKSTTAVKAVQHFNNS 90
Cdd:PRK08762 125 VGEEGQRRLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVGQPKVDSAAQRLAALNPD 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  91 -KLVPYQ-----GNVMDIstfplhwFEQFDIIFNALDNLAARRYVNKISQFLSLPLIESGTAGFDGYMQPIIPGKTE--- 161
Cdd:PRK08762 205 vQVEAVQervtsDNVEAL-------LQDVDVVVDGADNFPTRYLLNDACVKLGKPLVYGAVFRFEGQVSVFDAGRQRgqa 277

                        170
                 ....*....|.
gi 398366555 162 -CFECTKKETP 171
Cdd:PRK08762 278 pCYRCLFPEPP 288
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 11-177 1.58e-21

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 96.22  E-value: 1.58e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  11 IGEDSYKKLRSSRCLLVGAGGIGSELLKDIILMEFGEIHIVDLDTIDLSNLNRQFLFRQKDIKQ--PKSTTAVKAVQHFN 88
Cdd:PRK07688  14 IGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDVKNnlPKAVAAKKRLEEIN 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  89 NSklVPYQGNVMDISTFPLH-WFEQFDIIFNALDNLAARRYVNKISQFLSLPLIESGTAGFDGYMQPIIPGKTECFECTK 167
Cdd:PRK07688  94 SD--VRVEAIVQDVTAEELEeLVTGVDLIIDATDNFETRFIVNDAAQKYGIPWIYGACVGSYGLSYTIIPGKTPCLRCLL 171

                        170
                 ....*....|
gi 398366555 168 KETPKTFPVC 177
Cdd:PRK07688 172 QSIPLGGATC 181
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 12-152 3.70e-19

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: 85.81  E-value: 3.70e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  12 GEDSYKKLRSSRCLLVGAGGIGSELLKDIILMEFGEIHIVDLDTIDLSNLNRQFLFRQKDIKQPKSTTAVKAVQHFNNsk 91
Cdd:cd01492   12 GLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEASLERLRALNP-- 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398366555  92 LVPYQGNVMDISTFPLHWFEQFDIIFNALDNLAARRYVNKISQFLSLPLIESGTAGFDGYM 152
Cdd:cd01492   90 RVKVSVDTDDISEKPEEFFSQFDVVVATELSRAELVKINELCRKLGVKFYATGVHGLFGFV 150
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 11-165 1.70e-17

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 82.20  E-value: 1.70e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  11 IGEDSYKKLRSSRCLLVGAGGIGSELLKDIILMEFGEIHIVDLDTIDLSNLNRQFLFRQKDIKQPKSTTAVKAVQHFN-N 89
Cdd:PRK05690  22 FDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIGQPKVESARAALARINpH 101

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398366555  90 SKLVPYQGNVMDISTFPLhwFEQFDIIFNALDNLAARRYVNKISQFLSLPLIeSGTAG-FDGYMQPIIPGKTE-CFEC 165
Cdd:PRK05690 102 IAIETINARLDDDELAAL--IAGHDLVLDCTDNVATRNQLNRACFAAKKPLV-SGAAIrMEGQVTVFTYQDDEpCYRC 176
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 11-171 4.32e-17

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 83.60  E-value: 4.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  11 IGEDSYKKLRSSRCLLVGAGGIGSELLKDIILMEFGEIHIVDLDTIDLSNLNRQFLFRQKDIKQPKSTTAVKAVQHFN-- 88
Cdd:PRK07878  32 VGVDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRQVIHGQSDVGRSKAQSARDSIVEINpl 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  89 ------NSKLVPyqGNVMDIstfplhwFEQFDIIFNALDNLAARRYVNKISQFLSLPLIESGTAGFDG----YMQPIIPG 158
Cdd:PRK07878 112 vnvrlhEFRLDP--SNAVEL-------FSQYDLILDGTDNFATRYLVNDAAVLAGKPYVWGSIYRFEGqasvFWEDAPDG 182

                        170
                 ....*....|...
gi 398366555 159 KTECFECTKKETP 171
Cdd:PRK07878 183 LGLNYRDLYPEPP 195
PRK08328 PRK08328
hypothetical protein; Provisional
 8-176 3.06e-16

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 78.30  E-value: 3.06e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555   8 VTIIGEDSYKKLRSSRCLLVGAGGIGSELLKDIILMEFGEIHIVDLDTIDLSNLNRQFLFRQKDI-KQPKSTTAVKAVQH 86
Cdd:PRK08328  14 IMIFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEDLgKNPKPLSAKWKLER 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  87 FN-NSKLVPYQG-----NVMDIstfplhwFEQFDIIFNALDNLAARRYVNKISQFLSLPLIESGTAGFDGYMQPIIPGKT 160
Cdd:PRK08328  94 FNsDIKIETFVGrlseeNIDEV-------LKGVDVIVDCLDNFETRYLLDDYAHKKGIPLVHGAVEGTYGQVTTIVPGKT 166

                        170       180
                 ....*....|....*....|
gi 398366555 161 ----ECFECTKKETPKtFPV 176
Cdd:PRK08328 167 krlrEIFPKVKKKKGK-FPI 185
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 12-171 2.08e-13

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: 69.37  E-value: 2.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  12 GEDSYKKLRSSRCLLVGAGGIGSELLKDIILMEFGEIHIVDLDTIDLSNLNRQFLFRQK--DIKQPKSTTAVKAVQHFNN 89
Cdd:cd01485   10 GDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFLDAEvsNSGMNRAAASYEFLQELNP 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  90 SKLVPYQGNvMDISTFPL--HWFEQFDIIFNALDNLAARRYVNKISQFLSLPLIESGTAGFDGYMQPIIP--------GK 159
Cdd:cd01485   90 NVKLSIVEE-DSLSNDSNieEYLQKFTLVIATEENYERTAKVNDVCRKHHIPFISCATYGLIGYAFFDFPiaaflggvVA 168

                        170
                 ....*....|...
gi 398366555 160 TECFEC-TKKETP 171
Cdd:cd01485  169 QEAIKSiSGKFTP 181
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 11-147 2.29e-13

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: 69.94  E-value: 2.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  11 IGEDSYKKLRSSRCLLVGAGGIGSELLKDIILMEFGEIHIVDLDTIDLSNLNRQFLFRQKDIKQPKSTTAVKAVQHFN-N 89
Cdd:cd00755    1 YGEEGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINpE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398366555  90 SKLVPYQ-----GNVMDIstfplhWFEQFDIIFNALDN------LAARRYVNKIsqflslPLIESGTAG 147
Cdd:cd00755   81 CEVDAVEefltpDNSEDL------LGGDPDFVVDAIDSirakvaLIAYCRKRKI------PVISSMGAG 137
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 11-149 3.13e-12

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 68.36  E-value: 3.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  11 IGEDSYKKLRSSRCLLVGAGGIGSELLKDIILMEFGEIHIVDLDTIDLSNLNRQFLFRQKDIKQPKSTTAVKAVQHFNNS 90
Cdd:PRK05597  18 IGQQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVGQPKAESAREAMLALNPD 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 398366555  91 KLVPYQGNVMDISTfPLHWFEQFDIIFNALDNLAARRYVNKISQFLSLPLIESGTAGFD 149
Cdd:PRK05597  98 VKVTVSVRRLTWSN-ALDELRDADVILDGSDNFDTRHLASWAAARLGIPHVWASILGFD 155
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
4-150 3.43e-12

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 66.03  E-value: 3.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555   4 ETSLVTIIGEDSYKKLRSSRCLLVGAGGIGSELLKDIILMEFGEIHIVDLDTIDLSNLNRQFLFrQKDIKQPKsTTAVKA 83
Cdd:PRK08644  11 EAMLASRHTPKLLEKLKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVVEPSNLNRQQYF-ISQIGMPK-VEALKE 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  84 vqhfNNSKLVPY-----------QGNVMDIstfplhwFEQFDIIFNALDNLAARR-YVNKISQFLSLPLI-ESGTAGFDG 150
Cdd:PRK08644  89 ----NLLEINPFveieahnekidEDNIEEL-------FKDCDIVVEAFDNAETKAmLVETVLEHPGKKLVaASGMAGYGD 157
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 12-152 2.62e-11

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 65.67  E-value: 2.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  12 GEDSYKKLRSSRCLLVGAGGIGSELLKDIILMEFGEIHIVDLDTIDLSNLNRQFLFRQKDIKQPKSTTAVKAVQhfnnsK 91
Cdd:PRK05600  32 GIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDVGRPKVEVAAERLK-----E 106

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398366555  92 LVPyqgnvmDISTFPLHW----------FEQFDIIFNALDNLAARRYVNKISQFLSLPLIESGTAGFDGYM 152
Cdd:PRK05600 107 IQP------DIRVNALRErltaenavelLNGVDLVLDGSDSFATKFLVADAAEITGTPLVWGTVLRFHGEL 171
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 10-116 7.11e-11

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: 63.44  E-value: 7.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  10 IIGEDSYKKLRSSRCLLVGAGGIGSELLKDIILMEFGEIHIVDLDTIDLSNLNRQFLFRQKDIKQPKSTTAVKAVQHFNN 89
Cdd:cd01491    8 VLGHEAMKKLQKSNVLISGLGGLGVEIAKNLILAGVKSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAEASQARLAELNP 87

                         90       100
                 ....*....|....*....|....*....
gi 398366555  90 SKLVpyqgnvmDISTFPL--HWFEQFDII 116
Cdd:cd01491   88 YVPV-------TVSTGPLttDELLKFQVV 109
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
11-150 3.21e-10

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 62.44  E-value: 3.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  11 IGEDSYKKLRSSRCLLVGAGGIGSELLKDIILMEFGEIHIVDLDTIDLSNLNRQFLFRQKDIKQPKSTTAVKAVQHFNns 90
Cdd:PRK07411  28 VGLEGQKRLKAASVLCIGTGGLGSPLLLYLAAAGIGRIGIVDFDVVDSSNLQRQVIHGTSWVGKPKIESAKNRILEIN-- 105

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398366555  91 klvPY-QGNVMDI---STFPLHWFEQFDIIFNALDNLAARRYVNKISQFLSLPLIESGTAGFDG 150
Cdd:PRK07411 106 ---PYcQVDLYETrlsSENALDILAPYDVVVDGTDNFPTRYLVNDACVLLNKPNVYGSIFRFEG 166
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 10-147 1.65e-09

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: 58.94  E-value: 1.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  10 IIGEDSYKKLRSSRCLLVGAGGIGSellkdiILMEF------GEIHIVDLDTIDLSNLNRQFLFRQKDIKQPKsTTAVKA 83
Cdd:COG1179   13 LYGEEGLERLANAHVAVVGLGGVGS------WAAEAlarsgvGRLTLVDLDDVCESNINRQLHALDSTVGRPK-VEVMAE 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398366555  84 -VQHFN-NSKLVPYQGNVMDiSTFPLHWFEQFDIIFNALDNLAARRYVNKISQFLSLPLIESGTAG 147
Cdd:COG1179   86 rIRDINpDCEVTAIDEFVTP-ENADELLSEDYDYVIDAIDSVSAKAALIAWCRRRGIPIISSMGAG 150
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 23-148 7.86e-09

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: 55.47  E-value: 7.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  23 RCLLVGAGGIGSELLKDIILMEFGEIHIVDLDTIDLSNLNRQFlFRQKDIKQPKsTTAVKAvqhfNNSKLVPY------- 95
Cdd:cd01487    1 KVGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQ-YFLSQIGEPK-VEALKE----NLREINPFvkieain 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 398366555  96 ----QGNVMDIstfplhwFEQFDIIFNALDNLAARRYV-NKISQFLSLPLI-ESGTAGF 148
Cdd:cd01487   75 ikidENNLEGL-------FGDCDIVVEAFDNAETKAMLaESLLGNKNKPVVcASGMAGF 126
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 19-157 4.84e-06

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: 49.23  E-value: 4.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  19 LRSSRCLLVGAGGIGSELLKDIILMEFGEIHIVDLDTIDLSNLNRQFLFRQKDIKQPKSTTAVKAVQHFNNSklvpYQGN 98
Cdd:cd01493   18 LESAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAEATCELLQELNPD----VNGS 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398366555  99 VMDIS-TFPLHW----FEQFDIIFNAldNLAAR--RYVNKISQFLSLPLIESGTAGFDGYMQPIIP 157
Cdd:cd01493   94 AVEESpEALLDNdpsfFSQFTVVIAT--NLPEStlLRLADVLWSANIPLLYVRSYGLYGYIRIQLK 157
PRK14851 PRK14851
hypothetical protein; Provisional
 17-172 5.82e-06

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 49.47  E-value: 5.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  17 KKLRSSRCLLVGAGGIGSELLKDIILMEFGEIHIVDLDTIDLSNLNRQFLFRQKDIKQPKSTTAVKAVQHFNnsklvPYq 96
Cdd:PRK14851  39 ERLAEAKVAIPGMGGVGGVHLITMVRTGIGRFHIADFDQFEPVNVNRQFGARVPSFGRPKLAVMKEQALSIN-----PF- 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  97 gnvMDISTFP-------LHWF-EQFDIIFNALDNLA--ARRYVNKISQFLSLPLIESGTAGFDGYMQPIIPGKT---ECF 163
Cdd:PRK14851 113 ---LEITPFPaginadnMDAFlDGVDVVLDGLDFFQfeIRRTLFNMAREKGIPVITAGPLGYSSAMLVFTPQGMgfdDYF 189


                 ....*....
gi 398366555 164 ECTKKETPK 172
Cdd:PRK14851 190 NIGGKMPEE 198
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 10-89 6.25e-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: 49.50  E-value: 6.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555    10 IIGEDSYKKLRSSRCLLVGAGGIGSELLKDIILMEFGEIHIVDLDTIDLSNLNRQFLFRQKDIKQPKSTTAVKAVQHFNN 89
Cdd:TIGR01408   13 VLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRAEAVVKKLAELNP 92
PRK08223 PRK08223
hypothetical protein; Validated
 3-158 1.16e-05

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 47.37  E-value: 1.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555   3 RETSLVTiigEDSYKKLRSSRCLLVGAGGIGSELLKDIILMEFGEIHIVDLDTIDLSNLNRQFLFRQKDIKQPKSTTAVK 82
Cdd:PRK08223  12 RNLGWIT---PTEQQRLRNSRVAIAGLGGVGGIHLLTLARLGIGKFTIADFDVFELRNFNRQAGAMMSTLGRPKAEVLAE 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  83 AVQHFNNSklvpyqgnvMDISTFP----LHWFEQF----DIIFNALDNLA--ARRYVNKISQFLSLPLIESGTAGFDGYM 152
Cdd:PRK08223  89 MVRDINPE---------LEIRAFPegigKENADAFldgvDVYVDGLDFFEfdARRLVFAACQQRGIPALTAAPLGMGTAL 159


                 ....*.
gi 398366555 153 QPIIPG 158
Cdd:PRK08223 160 LVFDPG 165
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
 23-85 2.06e-05

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: 46.98  E-value: 2.06e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398366555  23 RCLLVGAGGIGSELLKdiILMEFGEIHI--VDLDTIDLSNLNRQFLFRQKDIK--QPKSTTAVKAVQ 85
Cdd:cd01486    1 KCLLLGAGTLGCNVAR--NLLGWGVRHItfVDSGKVSYSNPVRQSLFTFEDCKggKPKAEAAAERLK 65
E1_like_apg7 TIGR01381
E1-like protein-activating enzyme Gsa7p/Apg7p; This model represents a family of eukaryotic ...
 19-152 1.58e-04

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: 44.93  E-value: 1.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555   19 LRSSRCLLVGAGGIGSELLKdiILMEFGEIHI--VDLDTIDLSNLNRQFLFRQKDIK---QPKSTTAVKAVQ-------- 85
Cdd:TIGR01381 336 YSQLKVLLLGAGTLGCNVAR--CLIGWGVRHItfVDNGKVSYSNPVRQSLSNFEDCLlggRGKAETAQKALKrifpsiqa 413

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555   86 -----------HFNNSKLVPYQ-GNVMDISTFplhwFEQFDIIFNALDNLAAR-------RYVNKISQFLSLpliesgta 146
Cdd:TIGR01381 414 tghrltvpmpgHPIDEKDVPELeKDIARLEQL----IKDHDVVFLLLDSREARwlptvlcSRHKKIAISAAL-------- 481


                  ....*.
gi 398366555  147 GFDGYM 152
Cdd:TIGR01381 482 GFDSYV 487
UDP_invert_4-6DH_SDR_e cd05237
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ...
 22-119 3.42e-04

UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; UDP-Glcnac inverting 4,6-dehydratase was identified in Helicobacter pylori as the hexameric flaA1 gene product (FlaA1). FlaA1 is hexameric, possesses UDP-GlcNAc-inverting 4,6-dehydratase activity, and catalyzes the first step in the creation of a pseudaminic acid derivative in protein glycosylation. Although this subgroup has the NADP-binding motif characteristic of extended SDRs, its members tend to have a Met substituted for the active site Tyr found in most SDR families. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187548 [Multi-domain]  Cd Length: 287  Bit Score: 42.99  E-value: 3.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  22 SRCLLVGAGG-IGSELLKDIILMEFGEIHIVDLDTIDLSNLNRQFLfrqkdikqpksttavkavQHFNNSKLVPYQGNVM 100
Cdd:cd05237    3 KTILVTGGAGsIGSELVRQILKFGPKKLIVFDRDENKLHELVRELR------------------SRFPHDKLRFIIGDVR 64

                         90       100
                 ....*....|....*....|
gi 398366555 101 D-ISTFPLHWFEQFDIIFNA 119
Cdd:cd05237   65 DkERLRRAFKERGPDIVFHA 84
PRK14852 PRK14852
hypothetical protein; Provisional
 3-158 1.25e-03

hypothetical protein; Provisional


Pssm-ID: 184854 [Multi-domain]  Cd Length: 989  Bit Score: 41.99  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555   3 RETSLVTIIGEdsyKKLRSSRCLLVGAGGIGSELLKDIILMEFGEIHIVDLDTIDLSNLNRQFLFRQKDIKQPKSTTAVK 82
Cdd:PRK14852 317 RNLGLVDYAGQ---RRLLRSRVAIAGLGGVGGIHLMTLARTGIGNFNLADFDAYSPVNLNRQYGASIASFGRGKLDVMTE 393

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  83 AVQHFNnsklvPYqgnvMDISTFPL--------HWFEQFDIIFNALDNLA---ARRYVNKISQfLSLPLIESGTAGFDGY 151
Cdd:PRK14852 394 RALSVN-----PF----LDIRSFPEgvaaetidAFLKDVDLLVDGIDFFAldiRRRLFNRALE-LGIPVITAGPLGYSCA 463


                 ....*..
gi 398366555 152 MQPIIPG 158
Cdd:PRK14852 464 LLVFMPG 470
UBA_E1_SCCH pfam10585
Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ...
 183-370 1.34e-03

Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ubiquitin by first adenylating with ATP its C-terminal glycine residue and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding an ubiquitin-E1 thiolester and free AMP. Later the ubiquitin moiety is transferred to a cysteine residue on one of the many forms of ubiquitin-conjugating enzymes (E2). This domain carries the last of five conserved cysteines that is part of the active site of the enzyme, responsible for ubiquitin thiolester complex formation, the active site being represented by the sequence motif PICTLKNFP. The catalytic cysteine domain contains the E1 active site cysteine, and is divided in two half-domains, FCCH and SCCH, for 'first' and 'second' catalytic cysteine half-domain, respectively. This is the SCCH domain in which resides the catalytic cysteine.


Pssm-ID: 463157  Cd Length: 254  Bit Score: 41.06  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  183 PSQPIHCIVWAKNfLFNQLFasetsgneddnnqdwgTDDAEEIKRIKQETNELYE-LQKIIISRDASRIPEILN------ 255
Cdd:pfam10585   1 PNAIEHTIQWARD-EFEGLF----------------VQPPEEVNKYLQPPQNFIEsLLKQGGGQKLETLESVRKslvter 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366555  256 ----------------KLFIQDINKLLaienlwktRTKPvplsdsqINTPTKTAQ---SASnsvgtiqeqisnfinitqK 316
Cdd:pfam10585  64 pktfedcvawarlkfeKLFNNDIKQLL--------YNFP-------PDHKTSSGApfwSGP------------------K 110

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 398366555  317 lmdRYPKEqnhIEFDKDDADTLEFVATAANIRSHIFNIP-MKSVFDIKQIAGNII 370
Cdd:pfam10585 111 ---RPPTP---LEFDPNNPLHLDFVVAAANLRAQVYGIPgSRDREAIAKVLSKVK 159
UAE_UbL pfam14732
Ubiquitin/SUMO-activating enzyme ubiquitin-like domain; This is the C-terminal domain of ...
 453-518 2.41e-03

Ubiquitin/SUMO-activating enzyme ubiquitin-like domain; This is the C-terminal domain of ubiquitin-activating enzyme and SUMO-activating enzyme 2. It is structurally similar to ubiquitin. This domain is involved in E1-SUMO-thioester transfer to the SUMO E2 conjugating protein.


Pssm-ID: 464286  Cd Length: 88  Bit Score: 37.56  E-value: 2.41e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398366555  453 LNKMKLSDFV--VLIRE-KYSYPqDISLLdaSNQRLLF-----DYDFEDLNDRTLSEINLGNGSIILFSDEEGD 518
Cdd:pfam14732   5 TEKATLGDLVedVLKKKlGMVAP-DVSLS--GGGTILYlsseeDETEDDNLPKKLSELGIKNGSILTVDDFLQD 75
 
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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