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Conserved domains on  [gi|635575886|pdb|4NNJ|A]
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Chain A, Ubiquitin-activating enzyme E1 1

Protein Classification

ubiquitin-activating E1 family protein( domain architecture ID 1000537)

Ube1 (ubiquitin-activating E1) family protein similar to ubiquitin-activating enzyme E1 (UBA1) that catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation through the ubiquitin-proteasome system

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ube1 super family cl36897
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 29-1039 0e+00

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.


The actual alignment was detected with superfamily member TIGR01408:

Pssm-ID: 273603 [Multi-domain]  Cd Length: 1006  Bit Score: 1314.11  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A          29 EIDESLYSRQLYVLGKEAMLKMQTSNVLILGLKGLGVEIAKNVVLAGVKSMTVFDPEPVQLADLSTQFFLTEKDIGQKRG 108
Cdd:TIGR01408    1 EIDEALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         109 DVTRAKLAELNAYVPVNVLDSLDDVTQLSQFQVVVATDTvSLEDKVKINEFCHSS--GIRFISSETRGLFGNTFVDLGDE 186
Cdd:TIGR01408   81 EAVVKKLAELNPYVHVSSSSVPFNEEFLDKFQCVVLTEM-SLPLQKEINDFCHSQcpPIAFISADVRGLFGSLFCDFGDE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         187 FTVLDPTGEEPRTGMVSDI--EPDGTVTMLDDNRHGLEDGNFVRFSEVEGLDKLNDGTLFKVEVLGPFAFRIGSVKEYGE 264
Cdd:TIGR01408  160 FEVLDTDGEEPKTGFIASItqANPGIVTCLENHRHKLETGDFVTFREVNGMTGLNDGSPRKITVISPYSFSIGDTTELGP 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         265 YKKGGIFTEVKVPRKISFKSLKQQLSNPEFVFSDFAKFDRAAQLHLGFQALHQFAVRHnGELPRTMNDEDANELIKLVTD 344
Cdd:TIGR01408  240 YLHGGIATQVKTPKTVFFKSLREQLKDPKCLIVDFSKPERPPEIHTAFQALDQFQEKY-SRKPNVGCQQDAEELLKLATS 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         345 LSVQQPEvlgEGVDVNEDLIKELSYQARGDIPGVVAFFGGLVAQEVLKACSGKFTPLKQFMYFDSLESLPdpKNFPRNEK 424
Cdd:TIGR01408  319 ISETLEE---KVPDVDAKLVHWLSWTAQGFLSPMAAAVGGVVSQEVLKAVTGKFSPLCQWFYFDSAESLP--SLGKPECE 393

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         425 TTQPVNSRYDNQIAVFGLDFQKKIANSKVFLVGSGAIGCEMLKNWALLGLGSGSDGYIVVTDNDSIEKSNLNRQFLFRPK 504
Cdd:TIGR01408  394 EFLPRGDRYDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVGTGKKGMITVTDPDLIEKSNLNRQFLFRPH 473

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         505 DVGKNKSEVAAEAVCAMNPDLKgkINAKIDKVGPETEEIFNDSFWESLDFVTNALDNVDARTYVDRRCVFYRKPLLESGT 584
Cdd:TIGR01408  474 HIGKPKSYTAADATLKINPQIK--IDAHQNRVGPETETIFNDEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGT 551

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         585 LGTKGNTQVIIPRLTESYSSSRDPPEKSIPLCTLRSFPNKIDHTIAWAKSLFQGYFTDSAENVNMYLTQPNFVEQTLK-- 662
Cdd:TIGR01408  552 LGTKGNTQVVVPHLTESYGSSRDPPEKEIPFCTLKSFPAAIEHTIQWARDKFEGLFSHKPSLVNKYLSSPSSAEEVLQki 631

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         663 QSGDVKGVLESISDSLSS-KPHNFEDCIKWARLEFEKKFNHDIKQLLFNFPKDAKTSNGEPFWSGAKRAPTPLEFDIYNN 741
Cdd:TIGR01408  632 QSGHSREGLEQIIKLLSKeKPRNFSQCVEWARLKFEKYFNNKALQLLHCFPLDIRTSTGSPFWSSPKRPPSPLKFDLNEP 711

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         742 DHFHFVVAGASLRAYNYGIKSDDSNskPNVDEYKSVIDHMIIPEFTPNANLKIQVNDDDPDPNANAANGSDEIDQLVSSL 821
Cdd:TIGR01408  712 LHLSFIQAAAKLYATVYGIPFAEED--LSADALLNILSEVKIPEFKPRSNKKIQTDETARKPDTAPIDDRNAIFQLEKAI 789

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         822 PDP-STLAGFKLEPVDFEKDDDTNHHIEFITACSNCRAQNYFIETADRQKTKFIAGRIIPAIATTTSLVTGLVNLELYKL 900
Cdd:TIGR01408  790 LSNeATKSDFRMAPLSFEKDDDHNGHIDFITAASNLRAKNYSIEPADRFKTKFIAGKIIPAIATSTATVSGLVCLELIKV 869

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         901 IDNKTDIEQYKNGFVNLALPFFGFSEPIASPKGEYNNKKYDKIWDRFDIKGDIKLSDLIEHFEKDEGLEITMLSYGVSLL 980
Cdd:TIGR01408  870 TDGGYKFEVYKNCFLNLAIPLFVFTEPTEVRKTKIRNGISFTIWDRWTLHGDFTLLEFINAVKEKYGLEPTMVSQGVKLL 949

                          970       980       990      1000      1010
                   ....*....|....*....|....*....|....*....|....*....|....*....
4NNJ_A         981 YASFFPpkKLKERLNLPITQLVKLVTKKDIPAHVSTMILEICADDKEGEDVEVPFITIH 1039
Cdd:TIGR01408  950 YVPVMP--GHAERLKLKMHKLVKPTTKKKLPPYRVHLTVSFACDDDGDEDVPGPPVRIY 1006
 
Name Accession Description Interval E-value
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 29-1039 0e+00

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: 1314.11  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A          29 EIDESLYSRQLYVLGKEAMLKMQTSNVLILGLKGLGVEIAKNVVLAGVKSMTVFDPEPVQLADLSTQFFLTEKDIGQKRG 108
Cdd:TIGR01408    1 EIDEALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         109 DVTRAKLAELNAYVPVNVLDSLDDVTQLSQFQVVVATDTvSLEDKVKINEFCHSS--GIRFISSETRGLFGNTFVDLGDE 186
Cdd:TIGR01408   81 EAVVKKLAELNPYVHVSSSSVPFNEEFLDKFQCVVLTEM-SLPLQKEINDFCHSQcpPIAFISADVRGLFGSLFCDFGDE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         187 FTVLDPTGEEPRTGMVSDI--EPDGTVTMLDDNRHGLEDGNFVRFSEVEGLDKLNDGTLFKVEVLGPFAFRIGSVKEYGE 264
Cdd:TIGR01408  160 FEVLDTDGEEPKTGFIASItqANPGIVTCLENHRHKLETGDFVTFREVNGMTGLNDGSPRKITVISPYSFSIGDTTELGP 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         265 YKKGGIFTEVKVPRKISFKSLKQQLSNPEFVFSDFAKFDRAAQLHLGFQALHQFAVRHnGELPRTMNDEDANELIKLVTD 344
Cdd:TIGR01408  240 YLHGGIATQVKTPKTVFFKSLREQLKDPKCLIVDFSKPERPPEIHTAFQALDQFQEKY-SRKPNVGCQQDAEELLKLATS 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         345 LSVQQPEvlgEGVDVNEDLIKELSYQARGDIPGVVAFFGGLVAQEVLKACSGKFTPLKQFMYFDSLESLPdpKNFPRNEK 424
Cdd:TIGR01408  319 ISETLEE---KVPDVDAKLVHWLSWTAQGFLSPMAAAVGGVVSQEVLKAVTGKFSPLCQWFYFDSAESLP--SLGKPECE 393

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         425 TTQPVNSRYDNQIAVFGLDFQKKIANSKVFLVGSGAIGCEMLKNWALLGLGSGSDGYIVVTDNDSIEKSNLNRQFLFRPK 504
Cdd:TIGR01408  394 EFLPRGDRYDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVGTGKKGMITVTDPDLIEKSNLNRQFLFRPH 473

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         505 DVGKNKSEVAAEAVCAMNPDLKgkINAKIDKVGPETEEIFNDSFWESLDFVTNALDNVDARTYVDRRCVFYRKPLLESGT 584
Cdd:TIGR01408  474 HIGKPKSYTAADATLKINPQIK--IDAHQNRVGPETETIFNDEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGT 551

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         585 LGTKGNTQVIIPRLTESYSSSRDPPEKSIPLCTLRSFPNKIDHTIAWAKSLFQGYFTDSAENVNMYLTQPNFVEQTLK-- 662
Cdd:TIGR01408  552 LGTKGNTQVVVPHLTESYGSSRDPPEKEIPFCTLKSFPAAIEHTIQWARDKFEGLFSHKPSLVNKYLSSPSSAEEVLQki 631

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         663 QSGDVKGVLESISDSLSS-KPHNFEDCIKWARLEFEKKFNHDIKQLLFNFPKDAKTSNGEPFWSGAKRAPTPLEFDIYNN 741
Cdd:TIGR01408  632 QSGHSREGLEQIIKLLSKeKPRNFSQCVEWARLKFEKYFNNKALQLLHCFPLDIRTSTGSPFWSSPKRPPSPLKFDLNEP 711

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         742 DHFHFVVAGASLRAYNYGIKSDDSNskPNVDEYKSVIDHMIIPEFTPNANLKIQVNDDDPDPNANAANGSDEIDQLVSSL 821
Cdd:TIGR01408  712 LHLSFIQAAAKLYATVYGIPFAEED--LSADALLNILSEVKIPEFKPRSNKKIQTDETARKPDTAPIDDRNAIFQLEKAI 789

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         822 PDP-STLAGFKLEPVDFEKDDDTNHHIEFITACSNCRAQNYFIETADRQKTKFIAGRIIPAIATTTSLVTGLVNLELYKL 900
Cdd:TIGR01408  790 LSNeATKSDFRMAPLSFEKDDDHNGHIDFITAASNLRAKNYSIEPADRFKTKFIAGKIIPAIATSTATVSGLVCLELIKV 869

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         901 IDNKTDIEQYKNGFVNLALPFFGFSEPIASPKGEYNNKKYDKIWDRFDIKGDIKLSDLIEHFEKDEGLEITMLSYGVSLL 980
Cdd:TIGR01408  870 TDGGYKFEVYKNCFLNLAIPLFVFTEPTEVRKTKIRNGISFTIWDRWTLHGDFTLLEFINAVKEKYGLEPTMVSQGVKLL 949

                          970       980       990      1000      1010
                   ....*....|....*....|....*....|....*....|....*....|....*....
4NNJ_A         981 YASFFPpkKLKERLNLPITQLVKLVTKKDIPAHVSTMILEICADDKEGEDVEVPFITIH 1039
Cdd:TIGR01408  950 YVPVMP--GHAERLKLKMHKLVKPTTKKKLPPYRVHLTVSFACDDDGDEDVPGPPVRIY 1006
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 452-994 0e+00

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: 803.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A       452 KVFLVGSGAIGCEMLKNWALLGLGSGSDGYIVVTDNDSIEKSNLNRQFLFRPKDVGKNKSEVAAEAVCAMNPDLKgkINA 531
Cdd:cd01490    1 KVFLVGAGAIGCELLKNFALMGVGTGESGEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLK--ITA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A       532 KIDKVGPETEEIFNDSFWESLDFVTNALDNVDARTYVDRRCVFYRKPLLESGTLGTKGNTQVIIPRLTESYSSSRDPPEK 611
Cdd:cd01490   79 LQNRVGPETEHIFNDEFWEKLDGVANALDNVDARMYVDRRCVYYRKPLLESGTLGTKGNTQVVIPHLTESYSSSRDPPEK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A       612 SIPLCTLRSFPNKIDHTIAWAKSLFQGYFTDSAENVNMYLtqpnfveqtlkqsgdvkgvlesisdslsskphnFEDCIKW 691
Cdd:cd01490  159 SIPLCTLKNFPNAIEHTIQWARDEFEGLFKQPPENVNQYL---------------------------------FEDCVRW 205

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A       692 ARLEFEKKFNHDIKQLLFNFPKDAKTSNGEPFWSGAKRAPTPLEFDIYNNDHFHFVVAGASLRAYNYGIKSddsnskpnv 771
Cdd:cd01490  206 ARLLFEKYFNNNIKQLLHNFPPDAVTSDGAPFWSGPKRCPTPLEFDVNNPLHLDFVLAAANLYAEVYGIPG--------- 276

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A       772 deyksvidhmiipeftpnanlkiqvndddpdpnanaangsdeidqlvsslpdpstlagfklepvdFEKDDDTNHHIEFIT 851
Cdd:cd01490  277 -----------------------------------------------------------------FEKDDDTNFHMDFIT 291

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A       852 ACSNCRAQNYFIETADRQKTKFIAGRIIPAIATTTSLVTGLVNLELYKLIDNKTDIEQYKNGFVNLALPFFGFSEPIASP 931
Cdd:cd01490  292 AASNLRARNYSIPPADRHKTKRIAGKIIPAIATTTAAVTGLVCLELYKVVDGKRPLEAYKNAFLNLALPFFAFSEPIPAP 371

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
4NNJ_A       932 KGEYNNKKYDKIWDRFDIKGDIKLSDLI-EHFEKDEGLEITMLSYGVSLLYASFFPPKKLKERL 994
Cdd:cd01490  372 KVKYAYDEEWTIWDRFEVKGKQTLQELLiDYFKEKYGLEVTMLSQGVSMLYSSFMPPAKLKERL 435
UBA_E1_SCCH pfam10585
Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ...
 622-872 8.82e-128

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: 388.13  E-value: 8.82e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         622 PNKIDHTIAWAKSLFQGYFTDSAENVNMYLTQP-NFVEQTLKQSGDVKG-VLESISDSL-SSKPHNFEDCIKWARLEFEK 698
Cdd:pfam10585    1 PNAIEHTIQWARDEFEGLFVQPPEEVNKYLQPPqNFIESLLKQGGGQKLeTLESVRKSLvTERPKTFEDCVAWARLKFEK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         699 KFNHDIKQLLFNFPKDAKTSNGEPFWSGAKRAPTPLEFDIYNNDHFHFVVAGASLRAYNYGIKSDdsnskPNVDEYKSVI 778
Cdd:pfam10585   81 LFNNDIKQLLYNFPPDHKTSSGAPFWSGPKRPPTPLEFDPNNPLHLDFVVAAANLRAQVYGIPGS-----RDREAIAKVL 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         779 DHMIIPEFTPNANLKIQVNDDD-PDPNANAANGSDEIDQLVSSLPD----PSTLAGFKLEPVDFEKDDDTNHHIEFITAC 853
Cdd:pfam10585  156 SKVKVPEFKPKSGVKIQVNDEEaADPNAESEDDEDELDELLEELPKlavsPSSLAGFRLNPIEFEKDDDTNFHIDFITAA 235

                          250
                   ....*....|....*....
4NNJ_A         854 SNCRAQNYFIETADRQKTK 872
Cdd:pfam10585  236 SNLRARNYGIPPADRHKTK 254
UBA_e1_C smart00985
Ubiquitin-activating enzyme e1 C-terminal domain; This presumed domain found at the C terminus ...
 910-1036 2.80e-62

Ubiquitin-activating enzyme e1 C-terminal domain; This presumed domain found at the C terminus of Ubiquitin-activating enzyme e1 proteins is functionally uncharacterised.


Pssm-ID: 214955  Cd Length: 128  Bit Score: 207.11  E-value: 2.80e-62
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A          910 YKNGFVNLALPFFGFSEPIASPKGEYNNKKYDKIWDRFDIKG-DIKLSDLIEHFEKDEGLEITMLSYGVSLLYASFFPPK 988
Cdd:smart00985    1 YKNAFLNLALPFFAFSEPIAAPKTKYRDKDKWTLWDRLEVPGgDITLKELLDYFEEKYGLEVTMLSQGVSLLYSSFMPPK 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*...
4NNJ_A          989 KLKERLNLPITQLVKLVTKKDIPAHVSTMILEICADDKEGEDVEVPFI 1036
Cdd:smart00985   81 KHKERLDLPVTELVEQVTKKKLPPHVKYLVLEVSCEDEDDEDVEVPYI 128
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 432-611 1.22e-34

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: 132.95  E-value: 1.22e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A       432 RYDNQIAV--FGLDFQKKIANSKVFLVGSGAIGCEMLKNWALLGLGSgsdgyIVVTDNDSIEKSNLNRQFLFRPKDVGKN 509
Cdd:COG0476    7 RYSRQILLpeIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGT-----LTLVDDDVVELSNLQRQILYTEADVGRP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A       510 KSEVAAEAVCAMNPDLkgKINAKIDKVGPET-EEIFNDSfweslDFVTNALDNVDARTYVDRRCVFYRKPLLESGTLGTK 588
Cdd:COG0476   82 KVEAAAERLRALNPDV--EVEAIPERLTEENaLELLAGA-----DLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFE 154

                        170       180
                 ....*....|....*....|....
4NNJ_A       589 GNTQVIIPRLTESYSS-SRDPPEK 611
Cdd:COG0476  155 GQVTVFIPGDTPCYRClFPEPPEP 178
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 412-616 2.25e-17

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 85.32  E-value: 2.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A        412 SLPDPKNFPRNEKttqpvnSRYDNQIAV--FGLDFQKKIANSKVFLVGSGAIGCEMLKNWALLGLGSgsdgyIVVTDNDS 489
Cdd:PRK05600    7 TLSPFMQLPTSEL------RRTARQLALpgFGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVGT-----ITLIDDDT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A        490 IEKSNLNRQFLFRPKDVGKNKSEVAAEAVCAMNPDLkgKINAKIDKVGPETE-EIFNdsfweSLDFVTNALDNVDARTYV 568
Cdd:PRK05600   76 VDVSNIHRQILFGASDVGRPKVEVAAERLKEIQPDI--RVNALRERLTAENAvELLN-----GVDLVLDGSDSFATKFLV 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
4NNJ_A        569 DRRCVFYRKPLLESGTLGTKGNTQVIIPRLTESYSSSRD-----PPEKSIPLC 616
Cdd:PRK05600  149 ADAAEITGTPLVWGTVLRFHGELAVFNSGPDHRGVGLRDlfpeqPSGDSIPDC 201
 
Name Accession Description Interval E-value
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 29-1039 0e+00

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: 1314.11  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A          29 EIDESLYSRQLYVLGKEAMLKMQTSNVLILGLKGLGVEIAKNVVLAGVKSMTVFDPEPVQLADLSTQFFLTEKDIGQKRG 108
Cdd:TIGR01408    1 EIDEALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         109 DVTRAKLAELNAYVPVNVLDSLDDVTQLSQFQVVVATDTvSLEDKVKINEFCHSS--GIRFISSETRGLFGNTFVDLGDE 186
Cdd:TIGR01408   81 EAVVKKLAELNPYVHVSSSSVPFNEEFLDKFQCVVLTEM-SLPLQKEINDFCHSQcpPIAFISADVRGLFGSLFCDFGDE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         187 FTVLDPTGEEPRTGMVSDI--EPDGTVTMLDDNRHGLEDGNFVRFSEVEGLDKLNDGTLFKVEVLGPFAFRIGSVKEYGE 264
Cdd:TIGR01408  160 FEVLDTDGEEPKTGFIASItqANPGIVTCLENHRHKLETGDFVTFREVNGMTGLNDGSPRKITVISPYSFSIGDTTELGP 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         265 YKKGGIFTEVKVPRKISFKSLKQQLSNPEFVFSDFAKFDRAAQLHLGFQALHQFAVRHnGELPRTMNDEDANELIKLVTD 344
Cdd:TIGR01408  240 YLHGGIATQVKTPKTVFFKSLREQLKDPKCLIVDFSKPERPPEIHTAFQALDQFQEKY-SRKPNVGCQQDAEELLKLATS 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         345 LSVQQPEvlgEGVDVNEDLIKELSYQARGDIPGVVAFFGGLVAQEVLKACSGKFTPLKQFMYFDSLESLPdpKNFPRNEK 424
Cdd:TIGR01408  319 ISETLEE---KVPDVDAKLVHWLSWTAQGFLSPMAAAVGGVVSQEVLKAVTGKFSPLCQWFYFDSAESLP--SLGKPECE 393

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         425 TTQPVNSRYDNQIAVFGLDFQKKIANSKVFLVGSGAIGCEMLKNWALLGLGSGSDGYIVVTDNDSIEKSNLNRQFLFRPK 504
Cdd:TIGR01408  394 EFLPRGDRYDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVGTGKKGMITVTDPDLIEKSNLNRQFLFRPH 473

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         505 DVGKNKSEVAAEAVCAMNPDLKgkINAKIDKVGPETEEIFNDSFWESLDFVTNALDNVDARTYVDRRCVFYRKPLLESGT 584
Cdd:TIGR01408  474 HIGKPKSYTAADATLKINPQIK--IDAHQNRVGPETETIFNDEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGT 551

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         585 LGTKGNTQVIIPRLTESYSSSRDPPEKSIPLCTLRSFPNKIDHTIAWAKSLFQGYFTDSAENVNMYLTQPNFVEQTLK-- 662
Cdd:TIGR01408  552 LGTKGNTQVVVPHLTESYGSSRDPPEKEIPFCTLKSFPAAIEHTIQWARDKFEGLFSHKPSLVNKYLSSPSSAEEVLQki 631

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         663 QSGDVKGVLESISDSLSS-KPHNFEDCIKWARLEFEKKFNHDIKQLLFNFPKDAKTSNGEPFWSGAKRAPTPLEFDIYNN 741
Cdd:TIGR01408  632 QSGHSREGLEQIIKLLSKeKPRNFSQCVEWARLKFEKYFNNKALQLLHCFPLDIRTSTGSPFWSSPKRPPSPLKFDLNEP 711

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         742 DHFHFVVAGASLRAYNYGIKSDDSNskPNVDEYKSVIDHMIIPEFTPNANLKIQVNDDDPDPNANAANGSDEIDQLVSSL 821
Cdd:TIGR01408  712 LHLSFIQAAAKLYATVYGIPFAEED--LSADALLNILSEVKIPEFKPRSNKKIQTDETARKPDTAPIDDRNAIFQLEKAI 789

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         822 PDP-STLAGFKLEPVDFEKDDDTNHHIEFITACSNCRAQNYFIETADRQKTKFIAGRIIPAIATTTSLVTGLVNLELYKL 900
Cdd:TIGR01408  790 LSNeATKSDFRMAPLSFEKDDDHNGHIDFITAASNLRAKNYSIEPADRFKTKFIAGKIIPAIATSTATVSGLVCLELIKV 869

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         901 IDNKTDIEQYKNGFVNLALPFFGFSEPIASPKGEYNNKKYDKIWDRFDIKGDIKLSDLIEHFEKDEGLEITMLSYGVSLL 980
Cdd:TIGR01408  870 TDGGYKFEVYKNCFLNLAIPLFVFTEPTEVRKTKIRNGISFTIWDRWTLHGDFTLLEFINAVKEKYGLEPTMVSQGVKLL 949

                          970       980       990      1000      1010
                   ....*....|....*....|....*....|....*....|....*....|....*....
4NNJ_A         981 YASFFPpkKLKERLNLPITQLVKLVTKKDIPAHVSTMILEICADDKEGEDVEVPFITIH 1039
Cdd:TIGR01408  950 YVPVMP--GHAERLKLKMHKLVKPTTKKKLPPYRVHLTVSFACDDDGDEDVPGPPVRIY 1006
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 452-994 0e+00

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: 803.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A       452 KVFLVGSGAIGCEMLKNWALLGLGSGSDGYIVVTDNDSIEKSNLNRQFLFRPKDVGKNKSEVAAEAVCAMNPDLKgkINA 531
Cdd:cd01490    1 KVFLVGAGAIGCELLKNFALMGVGTGESGEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLK--ITA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A       532 KIDKVGPETEEIFNDSFWESLDFVTNALDNVDARTYVDRRCVFYRKPLLESGTLGTKGNTQVIIPRLTESYSSSRDPPEK 611
Cdd:cd01490   79 LQNRVGPETEHIFNDEFWEKLDGVANALDNVDARMYVDRRCVYYRKPLLESGTLGTKGNTQVVIPHLTESYSSSRDPPEK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A       612 SIPLCTLRSFPNKIDHTIAWAKSLFQGYFTDSAENVNMYLtqpnfveqtlkqsgdvkgvlesisdslsskphnFEDCIKW 691
Cdd:cd01490  159 SIPLCTLKNFPNAIEHTIQWARDEFEGLFKQPPENVNQYL---------------------------------FEDCVRW 205

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A       692 ARLEFEKKFNHDIKQLLFNFPKDAKTSNGEPFWSGAKRAPTPLEFDIYNNDHFHFVVAGASLRAYNYGIKSddsnskpnv 771
Cdd:cd01490  206 ARLLFEKYFNNNIKQLLHNFPPDAVTSDGAPFWSGPKRCPTPLEFDVNNPLHLDFVLAAANLYAEVYGIPG--------- 276

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A       772 deyksvidhmiipeftpnanlkiqvndddpdpnanaangsdeidqlvsslpdpstlagfklepvdFEKDDDTNHHIEFIT 851
Cdd:cd01490  277 -----------------------------------------------------------------FEKDDDTNFHMDFIT 291

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A       852 ACSNCRAQNYFIETADRQKTKFIAGRIIPAIATTTSLVTGLVNLELYKLIDNKTDIEQYKNGFVNLALPFFGFSEPIASP 931
Cdd:cd01490  292 AASNLRARNYSIPPADRHKTKRIAGKIIPAIATTTAAVTGLVCLELYKVVDGKRPLEAYKNAFLNLALPFFAFSEPIPAP 371

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
4NNJ_A       932 KGEYNNKKYDKIWDRFDIKGDIKLSDLI-EHFEKDEGLEITMLSYGVSLLYASFFPPKKLKERL 994
Cdd:cd01490  372 KVKYAYDEEWTIWDRFEVKGKQTLQELLiDYFKEKYGLEVTMLSQGVSMLYSSFMPPAKLKERL 435
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 34-417 2.48e-151

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: 450.95  E-value: 2.48e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A        34 LYSRQLYVLGKEAMLKMQTSNVLILGLKGLGVEIAKNVVLAGVKSMTVFDPEPVQLADLSTQFFLTEKDIGQKRGDVTRA 113
Cdd:cd01491    1 LYSRQLYVLGHEAMKKLQKSNVLISGLGGLGVEIAKNLILAGVKSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAEASQA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A       114 KLAELNAYVPVNVLDSLDDVTQLSQFQVVVATDTvSLEDKVKINEFCHSSGIRFISSETRGLFGNTFVDLGDEFTVLDPT 193
Cdd:cd01491   81 RLAELNPYVPVTVSTGPLTTDELLKFQVVVLTDA-SLEDQLKINEFCHSPGIKFISADTRGLFGSIFCDFGDEFTVYDPN 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A       194 GEEPRTGMVSDI--EPDGTVTMLDDNRHGLEDGNFVRFSEVEGLDKLNDGTLFKVEVLGPFAFRIGSVKEYGEYKKGGIF 271
Cdd:cd01491  160 GEEPKSGMISSIskDNPGVVTCLDETRHGFEDGDYVTFSEVEGMTELNGCEPRKIKVKGPYTFSIGDTSSFSEYIRGGIV 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A       272 TEVKvprkisfkslkqqlsnpefvfsdfakfdraaqlhlgfqalhqfavrhngelprtmndedaneliklvtdlsvqqpe 351
Cdd:cd01491  240 TQVK---------------------------------------------------------------------------- 243

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
4NNJ_A       352 vlgegvdvnedlikelsyqargdIPGVVAFFGGLVAQEVLKACSGKFTPLKQFMYFDSLESLPDPK 417
Cdd:cd01491  244 -----------------------LSPMAAFFGGLAAQEVLKACSGKFTPLKQWLYFDALECLPEDE 286
UBA_E1_SCCH pfam10585
Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ...
 622-872 8.82e-128

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: 388.13  E-value: 8.82e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         622 PNKIDHTIAWAKSLFQGYFTDSAENVNMYLTQP-NFVEQTLKQSGDVKG-VLESISDSL-SSKPHNFEDCIKWARLEFEK 698
Cdd:pfam10585    1 PNAIEHTIQWARDEFEGLFVQPPEEVNKYLQPPqNFIESLLKQGGGQKLeTLESVRKSLvTERPKTFEDCVAWARLKFEK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         699 KFNHDIKQLLFNFPKDAKTSNGEPFWSGAKRAPTPLEFDIYNNDHFHFVVAGASLRAYNYGIKSDdsnskPNVDEYKSVI 778
Cdd:pfam10585   81 LFNNDIKQLLYNFPPDHKTSSGAPFWSGPKRPPTPLEFDPNNPLHLDFVVAAANLRAQVYGIPGS-----RDREAIAKVL 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         779 DHMIIPEFTPNANLKIQVNDDD-PDPNANAANGSDEIDQLVSSLPD----PSTLAGFKLEPVDFEKDDDTNHHIEFITAC 853
Cdd:pfam10585  156 SKVKVPEFKPKSGVKIQVNDEEaADPNAESEDDEDELDELLEELPKlavsPSSLAGFRLNPIEFEKDDDTNFHIDFITAA 235

                          250
                   ....*....|....*....
4NNJ_A         854 SNCRAQNYFIETADRQKTK 872
Cdd:pfam10585  236 SNLRARNYGIPPADRHKTK 254
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 452-655 1.91e-79

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: 259.05  E-value: 1.91e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A       452 KVFLVGSGAIGCEMLKNWALLGLGsgsdgYIVVTDNDSIEKSNLNRQFLFRPKDVGKNKSEVAAEAVCAMNPDlkGKINA 531
Cdd:cd01484    1 KVLLVGAGGIGCELLKNLALMGFG-----QIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPN--CKVVP 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A       532 KIDKVGPEteEIFNDSFWESLDFVTNALDNVDARTYVDRRCVFYRKPLLESGTLGTKGNTQVIIPRLTESYSSSRDPPEK 611
Cdd:cd01484   74 YQNKVGPE--QDFNDTFFEQFHIIVNALDNIIARRYVNGMLIFLIVPLIESGTEGFKGNAQVILPGMTECIECTLYPPQK 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
4NNJ_A       612 SIPLCTLRSFPNKIDHTIAWAKSLFQgyftDSAENVNMYLTQPN 655
Cdd:cd01484  152 NFPMCTIASMPRLPEHCIEWARMLQW----DDPEHIQFIFQASN 191
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 433-621 1.02e-68

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: 229.45  E-value: 1.02e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         433 YDNQIA--VFGLDFQKKIANSKVFLVGSGAIGCEMLKNWALLGLGSgsdgyIVVTDNDSIEKSNLNRQFLFRPKDVGKNK 510
Cdd:pfam00899    1 YSRQLAlpLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGK-----ITLVDFDTVELSNLNRQFLFREADIGKPK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         511 SEVAAEAVCAMNPDLkgKINAKIDKVGPETeeifNDSFWESLDFVTNALDNVDARTYVDRRCVFYRKPLLESGTLGTKGN 590
Cdd:pfam00899   76 AEVAAERLREINPDV--EVEAYTERLTPEN----AEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQ 149

                          170       180       190
                   ....*....|....*....|....*....|...
4NNJ_A         591 TQVIIPRLTESYS--SSRDPPEKSIPLCTLRSF 621
Cdd:pfam00899  150 VTVVIPGKTPCYRclFPEDPPPKLVPSCTVAGV 182
UBA_e1_C smart00985
Ubiquitin-activating enzyme e1 C-terminal domain; This presumed domain found at the C terminus ...
 910-1036 2.80e-62

Ubiquitin-activating enzyme e1 C-terminal domain; This presumed domain found at the C terminus of Ubiquitin-activating enzyme e1 proteins is functionally uncharacterised.


Pssm-ID: 214955  Cd Length: 128  Bit Score: 207.11  E-value: 2.80e-62
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A          910 YKNGFVNLALPFFGFSEPIASPKGEYNNKKYDKIWDRFDIKG-DIKLSDLIEHFEKDEGLEITMLSYGVSLLYASFFPPK 988
Cdd:smart00985    1 YKNAFLNLALPFFAFSEPIAAPKTKYRDKDKWTLWDRLEVPGgDITLKELLDYFEEKYGLEVTMLSQGVSLLYSSFMPPK 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*...
4NNJ_A          989 KLKERLNLPITQLVKLVTKKDIPAHVSTMILEICADDKEGEDVEVPFI 1036
Cdd:smart00985   81 KHKERLDLPVTELVEQVTKKKLPPHVKYLVLEVSCEDEDDEDVEVPYI 128
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 452-917 6.72e-60

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: 207.62  E-value: 6.72e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A       452 KVFLVGSGAIGCEMLKNWALLGLGSgsdgyIVVTDNDSIEKSNLNRQFLFRPKDVGKNKSEVAAEAVCAMNPDLKgkINA 531
Cdd:cd01489    1 KVLVVGAGGIGCELLKNLVLTGFGE-----IHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVK--IVA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A       532 KIDKVgpeTEEIFNDSFWESLDFVTNALDNVDARTYVDRRCVFYRKPLLESGTLGTKGNTQVIIPRLTESYSSSRDPPEK 611
Cdd:cd01489   74 YHANI---KDPDFNVEFFKQFDLVFNALDNLAARRHVNKMCLAADVPLIESGTTGFLGQVQVIKKGKTECYECQPKETPK 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A       612 SIPLCTLRSFPNKIDHTIAWAKSLFqgyftdsaenvnmyltqpnFVeqtlkqsgdvkgvlesisdslsskphnfedcikw 691
Cdd:cd01489  151 TFPVCTIRSTPSQPIHCIVWAKSLF-------------------FL---------------------------------- 177

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A       692 arleFEKKFNHDIKQLLFNfpkdaktsngEPFWSgAKRAPTPLEFdiynndhfhfvvagaslraynygiksddsnskpnv 771
Cdd:cd01489  178 ----FNKVFKDDIERLLSM----------EELWK-TRKPPVPLSW----------------------------------- 207

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A       772 deyksvidhmiipeftpnanlkiqvndddpdpnanaangsdeiDQLVsslpdpstlagfklepvdFEKDDDTNhhIEFIT 851
Cdd:cd01489  208 -------------------------------------------KELT------------------FDKDDQDA--LDFVA 224

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
4NNJ_A       852 ACSNCRAQNYFIETADRQKTKFIAGRIIPAIATTTSLVTGLVNLELYKLIdnKTDIEQYKNGFVNL 917
Cdd:cd01489  225 AAANLRSHVFGIPMKSRFDIKQMAGNIIPAIATTNAIIAGLIVLEALKVL--SGDKEQCRTVFLNL 288
E1_UFD pfam09358
Ubiquitin fold domain; The ubiquitin fold domain is found at the C-terminus of ...
 944-1036 7.22e-48

Ubiquitin fold domain; The ubiquitin fold domain is found at the C-terminus of ubiquitin-activating E1 family enzymes. This domain binds to E2 enzymes.


Pssm-ID: 462768  Cd Length: 93  Bit Score: 165.02  E-value: 7.22e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         944 WDRFDIKGDIKLSDLIEHFEKDEGLEITMLSYGVSLLYASFFPPKKLKERLNLPITQLVKLVTKKDIPAHVSTMILEICA 1023
Cdd:pfam09358    1 WDRFEVEGDMTLQELLDYFKEKYGLEVTMLSYGVSLLYSSFMPPKKHKERLPMKISELVEEVSKKPIPPHQKYLVLEVSC 80

                           90
                   ....*....|...
4NNJ_A        1024 DDKEGEDVEVPFI 1036
Cdd:pfam09358   81 EDEDGEDVEVPYV 93
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 34-183 1.12e-40

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: 148.59  E-value: 1.12e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A        34 LYSRQLYVLGKEAMLKMQTSNVLILGLKGLGVEIAKNVVLAGVKSMTVFDPEPVQLADLSTQFFLTEKDIGQKRGDVTRA 113
Cdd:cd01492    3 LYDRQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEASLE 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
4NNJ_A       114 KLAELNAYVPVNVldSLDDVTQL-----SQFQVVVATDtVSLEDKVKINEFCHSSGIRFISSETRGLFGNTFVDL 183
Cdd:cd01492   83 RLRALNPRVKVSV--DTDDISEKpeeffSQFDVVVATE-LSRAELVKINELCRKLGVKFYATGVHGLFGFVFADL 154
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 34-183 1.47e-39

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: 145.26  E-value: 1.47e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A        34 LYSRQLYVLGKEAMLKMQTSNVLILGLKGLGVEIAKNVVLAGVKSMTVFDPEPVQLADLSTQFFL--TEKDIGQKRGDVT 111
Cdd:cd01485    1 LYDRQIRLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFLdaEVSNSGMNRAAAS 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
4NNJ_A       112 RAKLAELNAYVPVNVLD----SLDDVTQ--LSQFQVVVATDtVSLEDKVKINEFCHSSGIRFISSETRGLFGNTFVDL 183
Cdd:cd01485   81 YEFLQELNPNVKLSIVEedslSNDSNIEeyLQKFTLVIATE-ENYERTAKVNDVCRKHHIPFISCATYGLIGYAFFDF 157
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 452-635 7.26e-39

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: 146.73  E-value: 7.26e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A       452 KVFLVGSGAIGCEMLKNWALLGLGSgsdgyIVVTDNDSIEKSNLNRQFLFRPKDVGKNKSEVAAEAVCAMNPDLkgkina 531
Cdd:cd01488    1 KILVIGAGGLGCELLKNLALSGFRN-----IHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGV------ 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A       532 kidKVGPETEEI--FNDSFWESLDFVTNALDNVDARTYVDR---RCVFYR-----KPLLESGTLGTKGNTQVIIPRLTES 601
Cdd:cd01488   70 ---NVTPHFGKIqdKDEEFYRQFNIIICGLDSIEARRWINGtlvSLLLYEdpesiIPLIDGGTEGFKGHARVILPGITAC 146

                        170       180       190
                 ....*....|....*....|....*....|....*.
4NNJ_A       602 YSSSRD--PPEKSIPLCTLRSFPNKIDHTIAWAKSL 635
Cdd:cd01488  147 IECSLDlfPPQVTFPLCTIANTPRLPEHCIEYASLI 182
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 432-616 6.22e-35

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: 132.99  E-value: 6.22e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A       432 RYDNQIAV--FGLDFQKKIANSKVFLVGSGAIGC---EMLknwALLGLGsgsdgYIVVTDNDSIEKSNLNRQFLFRPKDV 506
Cdd:cd00757    1 RYSRQILLpeIGEEGQEKLKNARVLVVGAGGLGSpaaEYL---AAAGVG-----KLGLVDDDVVELSNLQRQILHTEADV 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A       507 GKNKSEVAAEAVCAMNPDLkgKINAKIDKVGPET-EEIFNDSfweslDFVTNALDNVDARTYVDRRCVFYRKPLLESGTL 585
Cdd:cd00757   73 GQPKAEAAAERLRAINPDV--EIEAYNERLDAENaEELIAGY-----DLVLDCTDNFATRYLINDACVKLGKPLVSGAVL 145

                        170       180       190
                 ....*....|....*....|....*....|..
4NNJ_A       586 GTKGNTQVIIPRLTESYSSS-RDPPEKSIPLC 616
Cdd:cd00757  146 GFEGQVTVFIPGEGPCYRCLfPEPPPPGVPSC 177
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 452-595 8.69e-35

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: 129.70  E-value: 8.69e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A       452 KVFLVGSGAIGCEMLKNWALLGLGSgsdgyIVVTDNDSIEKSNLNRQFLFRPKDVGKNKSEVAAEAVCAMNPDLkgKINA 531
Cdd:cd01483    1 RVLLVGLGGLGSEIALNLARSGVGK-----ITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGV--NVTA 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
4NNJ_A       532 KIDKVGPETEeifnDSFWESLDFVTNALDNVDARTYVDRRCVFYRKPLLESGTLGTKGNTQVII 595
Cdd:cd01483   74 VPEGISEDNL----DDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQVID 133
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 432-611 1.22e-34

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: 132.95  E-value: 1.22e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A       432 RYDNQIAV--FGLDFQKKIANSKVFLVGSGAIGCEMLKNWALLGLGSgsdgyIVVTDNDSIEKSNLNRQFLFRPKDVGKN 509
Cdd:COG0476    7 RYSRQILLpeIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGT-----LTLVDDDVVELSNLQRQILYTEADVGRP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A       510 KSEVAAEAVCAMNPDLkgKINAKIDKVGPET-EEIFNDSfweslDFVTNALDNVDARTYVDRRCVFYRKPLLESGTLGTK 588
Cdd:COG0476   82 KVEAAAERLRALNPDV--EVEAIPERLTEENaLELLAGA-----DLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFE 154

                        170       180
                 ....*....|....*....|....
4NNJ_A       589 GNTQVIIPRLTESYSS-SRDPPEK 611
Cdd:COG0476  155 GQVTVFIPGDTPCYRClFPEPPEP 178
E1_4HB pfam16191
Ubiquitin-activating enzyme E1 four-helix bundle; This domain is found in the ...
 276-346 2.06e-33

Ubiquitin-activating enzyme E1 four-helix bundle; This domain is found in the ubiquitin-activating E1 family enzymes.


Pssm-ID: 465055  Cd Length: 70  Bit Score: 122.95  E-value: 2.06e-33
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
4NNJ_A         276 VPRKISFKSLKQQLSNPEFVFSDFAKFDRAAQLHLGFQALHQFAVRHnGELPRTMNDEDANELIKLVTDLS 346
Cdd:pfam16191    1 MPKTLSFKSLEESLKEPEFLISDFAKFDRPAQLHLAFQALHAFQEKH-GRLPRPWNEEDAEEVVKLAKELN 70
E1_FCCH pfam16190
Ubiquitin-activating enzyme E1 FCCH domain; This domain is found in the ubiquitin-activating ...
 206-275 1.04e-32

Ubiquitin-activating enzyme E1 FCCH domain; This domain is found in the ubiquitin-activating E1 family enzymes.


Pssm-ID: 465054 [Multi-domain]  Cd Length: 70  Bit Score: 121.05  E-value: 1.04e-32
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         206 EPDGTVTMLDDNRHGLEDGNFVRFSEVEGLDKLNDGTLFKVEVLGPFAFRIGSVKEYGEYKKGGIFTEVK 275
Cdd:pfam16190    1 DNPGVVTCLDDTRHGLEDGDYVTFSEVEGMTELNGCEPRKIKVLGPYTFSIGDTSSFSPYLRGGIVTQVK 70
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 35-181 1.83e-31

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: 123.52  E-value: 1.83e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A          35 YSRQLY--VLGKEAMLKMQTSNVLILGLKGLGVEIAKNVVLAGVKSMTVFDPEPVQLADLSTQFFLTEKDIGQKRGDVTR 112
Cdd:pfam00899    1 YSRQLAlpLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
4NNJ_A         113 AKLAELNAYVPVNVL------DSLDDVtqLSQFQVVV-ATDtvSLEDKVKINEFCHSSGIRFISSETRGLFGNTFV 181
Cdd:pfam00899   81 ERLREINPDVEVEAYterltpENAEEL--IKSFDIVVdATD--NFAARYLVNDACVKLGKPLIEAGVLGFKGQVTV 152
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 55-183 1.15e-18

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: 83.47  E-value: 1.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A        55 VLILGLKGLGVEIAKNVVLAGVKSMTVFDPEPVQLADLSTQFFLTEKDIGQKRGDVTRAKLAELNAYVPVNV--LDSLDD 132
Cdd:cd01483    2 VLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAvpEGISED 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
4NNJ_A       133 VTQLSQFQVVVATDTV-SLEDKVKINEFCHSSGIRFISSETRGLFGNTFVDL 183
Cdd:cd01483   82 NLDDFLDGVDLVIDAIdNIAVRRALNRACKELGIPVIDAGGLGLGGDIQVID 133
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 35-177 3.20e-18

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: 88.52  E-value: 3.20e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A        35 YSRQLYVLGKEAMLKMQTSNVLILGLKGLGVEIAKNVVLAGVKSMTVFDPEPVQLADLSTQFFLTEKDIGQKRGDVTRAK 114
Cdd:cd01493    3 YDRQLRLWGEHGQAALESAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAEATCEL 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
4NNJ_A       115 LAELNAYV--------PVNVLDSldDVTQLSQFQVVVATD--TVSLEdkvKINEFCHSSGIRFISSETRGLFG 177
Cdd:cd01493   83 LQELNPDVngsaveesPEALLDN--DPSFFSQFTVVIATNlpESTLL---RLADVLWSANIPLLYVRSYGLYG 150
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 412-616 2.25e-17

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 85.32  E-value: 2.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A        412 SLPDPKNFPRNEKttqpvnSRYDNQIAV--FGLDFQKKIANSKVFLVGSGAIGCEMLKNWALLGLGSgsdgyIVVTDNDS 489
Cdd:PRK05600    7 TLSPFMQLPTSEL------RRTARQLALpgFGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVGT-----ITLIDDDT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A        490 IEKSNLNRQFLFRPKDVGKNKSEVAAEAVCAMNPDLkgKINAKIDKVGPETE-EIFNdsfweSLDFVTNALDNVDARTYV 568
Cdd:PRK05600   76 VDVSNIHRQILFGASDVGRPKVEVAAERLKEIQPDI--RVNALRERLTAENAvELLN-----GVDLVLDGSDSFATKFLV 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
4NNJ_A        569 DRRCVFYRKPLLESGTLGTKGNTQVIIPRLTESYSSSRD-----PPEKSIPLC 616
Cdd:PRK05600  149 ADAAEITGTPLVWGTVLRFHGELAVFNSGPDHRGVGLRDlfpeqPSGDSIPDC 201
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 432-583 2.30e-17

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 82.59  E-value: 2.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A        432 RYDNQIAVFGLDF--QKKIANSKVFLVGSGAIGCEmlknwALLGLGSGSDGYIVVTDNDSIEKSNLNRQFLFRPKDVGKN 509
Cdd:PRK05690   12 RYNRQIILRGFDFdgQEKLKAARVLVVGLGGLGCA-----ASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIGQP 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
4NNJ_A        510 KSEVAAEAVCAMNPDLK-GKINAKIDKvgpetEEIfnDSFWESLDFVTNALDNVDARTYVDRRCVFYRKPLLeSG 583
Cdd:PRK05690   87 KVESARAALARINPHIAiETINARLDD-----DEL--AALIAGHDLVLDCTDNVATRNQLNRACFAAKKPLV-SG 153
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 433-589 9.98e-17

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: 79.64  E-value: 9.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A       433 YDNQIAVFGLDFQKKIANSKVFLVGSGAIGCEMLKNWALLGLGSgsdgyIVVTDNDSIEKSNLNRQFLFRPKDVGKNKSE 512
Cdd:cd01492    4 YDRQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGS-----LTILDDRTVTEEDLGAQFLIPAEDLGQNRAE 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
4NNJ_A       513 VAAEAVCAMNPdlkgKINAKIDKVGPETEeifNDSFWESLDFVTNALDNVDARTYVDRRCVFYRKPLLESGTLGTKG 589
Cdd:cd01492   79 ASLERLRALNP----RVKVSVDTDDISEK---PEEFFSQFDVVVATELSRAELVKINELCRKLGVKFYATGVHGLFG 148
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 35-169 4.25e-16

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: 79.02  E-value: 4.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A        35 YSRQ--LYVLGKEAMLKMQTSNVLILGLKGLGVEIAKNVVLAGVKSMTVFDPEPVQLADLSTQFFLTEKDIGQKRGDVTR 112
Cdd:COG0476    8 YSRQilLPEIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGRPKVEAAA 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
4NNJ_A       113 AKLAELNAYVPVNVL------DSLDDVtqLSQFQVVV-ATDtvSLEDKVKINEFCHSSGIRFIS 169
Cdd:COG0476   88 ERLRALNPDVEVEAIperlteENALEL--LAGADLVLdCTD--NFATRYLLNDACVKLGIPLVS 147
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
441-579 5.09e-16

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 81.21  E-value: 5.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A        441 GLDFQKKIANSKVFLVGSGAIGCEmlknwALLGLGSGSDGYIVVTDNDSIEKSNLNRQFLFRPKDVGKNKSEVAAEAVCA 520
Cdd:PRK08762  126 GEEGQRRLLEARVLLIGAGGLGSP-----AALYLAAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVGQPKVDSAAQRLAA 200

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A        521 MNPDLkgKINAKIDKVGPET-EEIFNDsfwesLDFVTNALDNVDARTYVDRRCVFYRKPL 579
Cdd:PRK08762  201 LNPDV--QVEAVQERVTSDNvEALLQD-----VDVVVDGADNFPTRYLLNDACVKLGKPL 253
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 440-602 2.05e-15

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: 76.87  E-value: 2.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A       440 FGLDFQKKIANSKVFLVGSGAIG---CEMLknwALLGLGsgsdgYIVVTDNDSIEKSNLNRQFLFRPKDVGKNKSEVAAE 516
Cdd:cd00755    1 YGEEGLEKLRNAHVAVVGLGGVGswaAEAL---ARSGVG-----KLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A       517 AVCAMNPDLkgKINAKIDKVGPETEEIFNDsfwESLDFVTNALDNVDARTYVDRRCVFYRKPLLESGTLGTKGN-TQVII 595
Cdd:cd00755   73 RIRDINPEC--EVDAVEEFLTPDNSEDLLG---GDPDFVVDAIDSIRAKVALIAYCRKRKIPVISSMGAGGKLDpTRIRV 147


                 ....*..
4NNJ_A       596 PRLTESY 602
Cdd:cd00755  148 ADISKTS 154
PRK08328 PRK08328
hypothetical protein; Provisional
 432-601 2.35e-15

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 76.37  E-value: 2.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A        432 RYDNQIAVFGLDFQKKIANSKVFLVGSGAIGCEMLKNWALLGLGSgsdgyIVVTDNDSIEKSNLNRQFLFRPKDVGKNKS 511
Cdd:PRK08328    9 RYDRQIMIFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGR-----ILLIDEQTPELSNLNRQILHWEEDLGKNPK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A        512 EVAAE-AVCAMNPDLkgKINAKIDKVGPET-EEIFNDsfwesLDFVTNALDNVDARTYVDRRCVFYRKPLLESGTLGTKG 589
Cdd:PRK08328   84 PLSAKwKLERFNSDI--KIETFVGRLSEENiDEVLKG-----VDVIVDCLDNFETRYLLDDYAHKKGIPLVHGAVEGTYG 156

                         170
                  ....*....|..
4NNJ_A        590 NTQVIIPRLTES 601
Cdd:PRK08328  157 QVTTIVPGKTKR 168
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 35-170 2.18e-14

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: 73.67  E-value: 2.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A        35 YSRQLYV--LGKEAMLKMQTSNVLILGLKGLGVEIAKNVVLAGVKSMTVFDPEPVQLADLSTQFFLTEKDIGQKRGDVTR 112
Cdd:cd00757    2 YSRQILLpeIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAAA 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
4NNJ_A       113 AKLAELNAYVPVNVLD---SLDDVTQL-SQFQVVV-ATDtvSLEDKVKINEFCHSSGIRFISS 170
Cdd:cd00757   82 ERLRAINPDVEIEAYNerlDAENAEELiAGYDLVLdCTD--NFATRYLINDACVKLGKPLVSG 142
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 433-530 6.66e-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: 71.30  E-value: 6.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A       433 YDNQIAVFGLDFQKKIANSKVFLVGSGAIGCEMLKNWALLGLGSgsdgyIVVTDNDSIEKSNLNRQFLFRPKDV--GKNK 510
Cdd:cd01485    2 YDRQIRLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDS-----ITIVDHRLVSTEDLGSNFFLDAEVSnsGMNR 76

                         90       100
                 ....*....|....*....|
4NNJ_A       511 SEVAAEAVCAMNPDLKGKIN 530
Cdd:cd01485   77 AAASYEFLQELNPNVKLSIV 96
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 432-528 8.94e-14

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: 74.65  E-value: 8.94e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A       432 RYDNQIAVFGLDFQKKIANSKVFLVGSGAIGCEMLKNWALLGLGSgsdgyIVVTDNDSIEKSNLNRQFLFRPKDVGKNKS 511
Cdd:cd01493    2 KYDRQLRLWGEHGQAALESAHVCLLNATATGTEILKNLVLPGIGS-----FTIVDGSKVDEEDLGNNFFLDASSLGKSRA 76

                         90
                 ....*....|....*..
4NNJ_A       512 EVAAEAVCAMNPDLKGK 528
Cdd:cd01493   77 EATCELLQELNPDVNGS 93
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 431-565 9.03e-14

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 74.14  E-value: 9.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A        431 SRYDNQIAV--FGLDFQKKIANSKVFLVGSGAIGCEmlknwALLGLGSGSDGYIVVTDNDSIEKSNLNRQFLFRPKDVGK 508
Cdd:PRK05597    7 ARYRRQIMLgeIGQQGQQSLFDAKVAVIGAGGLGSP-----ALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVGQ 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
4NNJ_A        509 NKSEVAAEAVCAMNPDLkgKINAKIDKVGPETEEifndSFWESLDFVTNALDNVDAR 565
Cdd:PRK05597   82 PKAESAREAMLALNPDV--KVTVSVRRLTWSNAL----DELRDADVILDGSDNFDTR 132
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 430-599 3.24e-13

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 71.95  E-value: 3.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A        430 NSRYDNQI--AVFGLDFQKKIANSKVFLVGSGAIG---CEMLknwallgLGSGSdGYIVVTDNDSIEKSNLNRQFLFRPK 504
Cdd:PRK07688    2 NERYSRQElfSPIGEEGQQKLREKHVLIIGAGALGtanAEML-------VRAGV-GKVTIVDRDYVEWSNLQRQQLYTES 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A        505 DVGKN--KSEVAAEAVCAMNPDLkgKINAKIDKVGPetEEIfnDSFWESLDFVTNALDNVDARTYVDRRCVFYRKPLLES 582
Cdd:PRK07688   74 DVKNNlpKAVAAKKRLEEINSDV--RVEAIVQDVTA--EEL--EELVTGVDLIIDATDNFETRFIVNDAAQKYGIPWIYG 147

                         170
                  ....*....|....*..
4NNJ_A        583 GTLGTKGNTQVIIPRLT 599
Cdd:PRK07688  148 ACVGSYGLSYTIIPGKT 164
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 440-583 1.37e-12

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: 68.57  E-value: 1.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A       440 FGLDFQKKIANSKVFLVGSGAIGcemlkNWALLGLG-SGSdGYIVVTDNDSIEKSNLNRQFLFRPKDVGKNKSEVAAEAV 518
Cdd:COG1179   14 YGEEGLERLANAHVAVVGLGGVG-----SWAAEALArSGV-GRLTLVDLDDVCESNINRQLHALDSTVGRPKVEVMAERI 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
4NNJ_A       519 CAMNPDLkgKINAKIDKVGPET-EEIFNDSFweslDFVTNALDNVDARTYVDRRCVFYRKPLLESG 583
Cdd:COG1179   88 RDINPDC--EVTAIDEFVTPENaDELLSEDY----DYVIDAIDSVSAKAALIAWCRRRGIPIISSM 147
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 432-599 1.58e-12

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 70.14  E-value: 1.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A        432 RYDNQIAV--FGLDFQKKIANSKVFLVGSGAIGCEMLKNWALLGLGSgsdgyIVVTDNDSIEKSNLNRQFLFRPKDVG-- 507
Cdd:PRK12475    4 RYSRQILFsgIGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIGK-----LTIADRDYVEWSNLQRQQLYTEEDAKqk 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A        508 KNKSEVAAEAVCAMNPDLkgKINAKIDKVGPETEEifndSFWESLDFVTNALDNVDARTYVDRRCVFYRKPLLESGTLGT 587
Cdd:PRK12475   79 KPKAIAAKEHLRKINSEV--EIVPVVTDVTVEELE----ELVKEVDLIIDATDNFDTRLLINDLSQKYNIPWIYGGCVGS 152

                         170
                  ....*....|..
4NNJ_A        588 KGNTQVIIPRLT 599
Cdd:PRK12475  153 YGVTYTIIPGKT 164
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 412-578 2.50e-12

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 70.12  E-value: 2.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A        412 SLPdPKNFPRNEKTTQPVnSRYDNQ--IAVFGLDFQKKIANSKVFLVGSGAIGCEmlknwALLGLGSGSDGYIVVTDNDS 489
Cdd:PRK07878    4 SLP-PLVEPAAELTRDEV-ARYSRHliIPDVGVDGQKRLKNARVLVIGAGGLGSP-----TLLYLAAAGVGTLGIVEFDV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A        490 IEKSNLNRQFLFRPKDVGKNKSEVAAEAVCAMNPdlkgKINAKIDKVGPETE---EIFNDsfwesLDFVTNALDNVDART 566
Cdd:PRK07878   77 VDESNLQRQVIHGQSDVGRSKAQSARDSIVEINP----LVNVRLHEFRLDPSnavELFSQ-----YDLILDGTDNFATRY 147

                         170
                  ....*....|..
4NNJ_A        567 YVDRRCVFYRKP 578
Cdd:PRK07878  148 LVNDAAVLAGKP 159
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 433-523 3.49e-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: 65.37  E-value: 3.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A       433 YDNQIAVFGLDFQKKIANSKVFLVGSGAIGCEMLKNWALLGLGSgsdgyIVVTDNDSIEKSNLNRQFLFRPKDVGKNKSE 512
Cdd:cd01491    2 YSRQLYVLGHEAMKKLQKSNVLISGLGGLGVEIAKNLILAGVKS-----VTLHDTKPCSWSDLSSQFYLREEDIGKNRAE 76

                         90
                 ....*....|.
4NNJ_A       513 VAAEAVCAMNP 523
Cdd:cd01491   77 ASQARLAELNP 87
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 35-169 5.96e-11

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 63.71  E-value: 5.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         35 YSRQ--LYVLGKEAMLKMQTSNVLILGLKGLGVEIAKNVVLAGVKSMTVFDPEPVQLADLSTQFFLTEKDIGQKRGDVTR 112
Cdd:PRK05690   13 YNRQiiLRGFDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIGQPKVESAR 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
4NNJ_A        113 AKLAELNAYVPVNVLDS-LDDV---TQLSQFQVVV-ATDTVSLEDKVkiNEFCHSSGIRFIS 169
Cdd:PRK05690   93 AALARINPHIAIETINArLDDDelaALIAGHDLVLdCTDNVATRNQL--NRACFAAKKPLVS 152
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 42-170 1.15e-10

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


Pssm-ID: 238384 [Multi-domain]  Cd Length: 231  Bit Score: 62.62  E-value: 1.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A        42 LGKEAMLKMQTSNVLILGLKGLGVEIAKNVVLAGVKSMTVFDPEPVQLADLSTQFFLTEKDIGQKRGDVTRAKLAELNAY 121
Cdd:cd00755    1 YGEEGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
4NNJ_A       122 VPVNVLDSL---DDVTQL--SQFQVVV-ATDTVSLedKVKINEFCHSSGIRFISS 170
Cdd:cd00755   81 CEVDAVEEFltpDNSEDLlgGDPDFVVdAIDSIRA--KVALIAYCRKRKIPVISS 133
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 452-566 1.29e-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: 58.55  E-value: 1.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A       452 KVFLVGSGAIGcemlKNWALLGLGSGSdGYIVVTDNDSIEKSNLNRQFlFRPKDVGKNKSEVAAEAVCAMNPDLK-GKIN 530
Cdd:cd01487    1 KVGIAGAGGLG----SNIAVLLARSGV-GNLKLVDFDVVEPSNLNRQQ-YFLSQIGEPKVEALKENLREINPFVKiEAIN 74

                         90       100       110
                 ....*....|....*....|....*....|....*.
4NNJ_A       531 AKIDkvGPETEEIFNDSfweslDFVTNALDNVDART 566
Cdd:cd01487   75 IKID--ENNLEGLFGDC-----DIVVEAFDNAETKA 103
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
424-566 1.81e-09

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 58.71  E-value: 1.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A        424 KTTQPVNSRYDNQIAV-FGLDFQKKIANSKVFLVGSGAIGcemlKNWALLGLGSGSdGYIVVTDNDSIEKSNLNRQFLFr 502
Cdd:PRK08644    1 RGEIPSMEEFEAMLASrHTPKLLEKLKKAKVGIAGAGGLG----SNIAVALARSGV-GNLKLVDFDVVEPSNLNRQQYF- 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
4NNJ_A        503 PKDVGKNKSEVAAEAVCAMNPDLkgKINAKIDKVGPET-EEIFNDSfweslDFVTNALDNVDART 566
Cdd:PRK08644   75 ISQIGMPKVEALKENLLEINPFV--EIEAHNEKIDEDNiEELFKDC-----DIVVEAFDNAETKA 132
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 449-586 1.83e-08

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 56.74  E-value: 1.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A        449 ANSKVFLVGSGAIGcemlkNWALLGLGSGSDGYIVVTDNDSIEKSNLNRQFLFRPKDVGKNKSEVAAEAVCAMNPDLkgK 528
Cdd:PRK15116   29 ADAHICVVGIGGVG-----SWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMAERIRQINPEC--R 101

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
4NNJ_A        529 INAKIDKVGPE-TEEIFNDSFweslDFVTNALDNVDARTYVDRRCVFYRKPLLESGTLG 586
Cdd:PRK15116  102 VTVVDDFITPDnVAEYMSAGF----SYVIDAIDSVRPKAALIAYCRRNKIPLVTTGGAG 156
PTZ00245 PTZ00245
ubiquitin activating enzyme; Provisional
 35-154 2.21e-08

ubiquitin activating enzyme; Provisional


Pssm-ID: 140272  Cd Length: 287  Bit Score: 56.60  E-value: 2.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         35 YSRQLYVLGKEAMLKMQTSNVLILGLKGLGVEIAKNVVLAGVKSMTVFDPEPVQLADLSTQfFLTEKDIGQKRGDVTRAK 114
Cdd:PTZ00245    9 YDRQIRLWGKSTQQQLMHTSVALHGVAGAAAEAAKNLVLAGVRAVAVADEGLVTDADVCTN-YLMQGEAGGTRGARALGA 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
4NNJ_A        115 LAELNAYvpVNVLDSLDDVTQLSQFQVVVATdTVSLEDKV 154
Cdd:PTZ00245   88 LQRLNPH--VSVYDAVTKLDGSSGTRVTMAA-VITEEDAV 124
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 55-177 2.71e-08

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: 56.62  E-value: 2.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A        55 VLILGLKGLGVEIAKNVVLAGVKSMTVFDPEPVQLADLSTQFFLTEKDIGQKRGDVTRAKLAELNAYVPV-----NVLDS 129
Cdd:cd01489    2 VLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIvayhaNIKDP 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
4NNJ_A       130 LDDVTQLSQFQVVV-ATDtvSLEDKVKINEFCHSSGIRFISSETRGLFG 177
Cdd:cd01489   82 DFNVEFFKQFDLVFnALD--NLAARRHVNKMCLAADVPLIESGTTGFLG 128
PRK08328 PRK08328
hypothetical protein; Provisional
 35-177 4.89e-08

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 54.80  E-value: 4.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         35 YSRQLYVLGKEAMLKMQTSNVLILGLKGLGVEIAKNVVLAGVKSMTVFDPEPVQLADLSTQFFLTEKDIGQKRGDVT-RA 113
Cdd:PRK08328   10 YDRQIMIFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEDLGKNPKPLSaKW 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
4NNJ_A        114 KLAELNAYVPVNVL------DSLDDVtqLSQFQVVVatDTV-SLEDKVKINEFCHSSGIRFISSETRGLFG 177
Cdd:PRK08328   90 KLERFNSDIKIETFvgrlseENIDEV--LKGVDVIV--DCLdNFETRYLLDDYAHKKGIPLVHGAVEGTYG 156
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 55-144 7.22e-08

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


Pssm-ID: 238765 [Multi-domain]  Cd Length: 291  Bit Score: 55.05  E-value: 7.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A        55 VLILGLKGLGVEIAKNVVLAGVKSMTVFDPEPVQLADLSTQFFLTEKDIGQKRGDVTrAKLaeLNAYVP-VNVLDSLDDV 133
Cdd:cd01488    2 ILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVA-AKF--VNDRVPgVNVTPHFGKI 78

                         90
                 ....*....|....*.
4NNJ_A       134 TQL-----SQFQVVVA 144
Cdd:cd01488   79 QDKdeefyRQFNIIIC 94
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
35-133 1.11e-07

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 55.40  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         35 YSRQLYV--LGKEAMLKMQTSNVLILGLKGLGVEIAKNVVLAGVKSMTVFDPEPVQLADLSTQFFLTEKDIGQKRGDVTR 112
Cdd:PRK08762  116 YSRHLRLpeVGEEGQRRLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVGQPKVDSAA 195

                          90       100       110
                  ....*....|....*....|....*....|.
4NNJ_A        113 AKLAELNAYVPV----------NVLDSLDDV 133
Cdd:PRK08762  196 QRLAALNPDVQVeavqervtsdNVEALLQDV 226
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 55-181 1.28e-07

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: 53.74  E-value: 1.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A        55 VLILGLKGLGVEIAKNVVLAGVKSMTVFDPEPVQLADLSTQFFLTEKDIGQKRGDVTRAKLAELNAYVPV-----NVLDS 129
Cdd:cd01484    2 VLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCKVvpyqnKVGPE 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
4NNJ_A       130 LD-DVTQLSQFQVVV-ATDtvSLEDKVKINEFCHSSGIRFISSETRGLFGNTFV 181
Cdd:cd01484   82 QDfNDTFFEQFHIIVnALD--NIIARRYVNGMLIFLIVPLIESGTEGFKGNAQV 133
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
441-578 3.45e-07

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 53.59  E-value: 3.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A        441 GLDFQKKIANSKVFLVGSGAIGCEMLKNWALLGLGSgsdgyIVVTDNDSIEKSNLNRQFLFRPKDVGKNKSEVAAEAVCA 520
Cdd:PRK07411   29 GLEGQKRLKAASVLCIGTGGLGSPLLLYLAAAGIGR-----IGIVDFDVVDSSNLQRQVIHGTSWVGKPKIESAKNRILE 103

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
4NNJ_A        521 MNPdlkgkiNAKID----KVGPETE-EIFndsfwESLDFVTNALDNVDARTYVDRRCVFYRKP 578
Cdd:PRK07411  104 INP------YCQVDlyetRLSSENAlDIL-----APYDVVVDGTDNFPTRYLVNDACVLLNKP 155
PRK08223 PRK08223
hypothetical protein; Validated
 445-596 1.07e-06

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 51.61  E-value: 1.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A        445 QKKIANSKVFLVGSGAIGCEMLKNWALLGLGSGSdgyivVTDNDSIEKSNLNRQFLFRPKDVGKNKSEVAAEAVCAMNPD 524
Cdd:PRK08223   22 QQRLRNSRVAIAGLGGVGGIHLLTLARLGIGKFT-----IADFDVFELRNFNRQAGAMMSTLGRPKAEVLAEMVRDINPE 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
4NNJ_A        525 LkgKINAKIDKVGPETEeifnDSFWESLDFVTNALD--NVDARTYVDRRCVFYRKPLLESGTLGTKGNTQVIIP 596
Cdd:PRK08223   97 L--EIRAFPEGIGKENA----DAFLDGVDVYVDGLDffEFDARRLVFAACQQRGIPALTAAPLGMGTALLVFDP 164
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 35-168 2.54e-06

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 50.76  E-value: 2.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         35 YSRQLYV--LGKEAMLKMQTSNVLILGLKGLGVEIAKNVVLAGVKSMTVFDPEPVQLADLSTQFFLTEKDIGQKRGDVTR 112
Cdd:PRK07688    5 YSRQELFspIGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDVKNNLPKAVA 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
4NNJ_A        113 AK--LAELNAYVPVNVLdsLDDVT--QLSQFQ-----VVVATDtvSLEDKVKINEFCHSSGIRFI 168
Cdd:PRK07688   85 AKkrLEEINSDVRVEAI--VQDVTaeELEELVtgvdlIIDATD--NFETRFIVNDAAQKYGIPWI 145
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 30-126 2.75e-06

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 50.64  E-value: 2.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         30 IDESLYSRQ--LYVLGKEAMLKMQTSNVLILGLKGLGVEIAKNVVLAGVKSMTVFDPEPVQLADLSTQFFLTEKDIGQKR 107
Cdd:PRK05597    4 LDIARYRRQimLGEIGQQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVGQPK 83

                          90
                  ....*....|....*....
4NNJ_A        108 GDVTRAKLAELNAYVPVNV 126
Cdd:PRK05597   84 AESAREAMLALNPDVKVTV 102
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 55-128 3.77e-06

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: 48.15  E-value: 3.77e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
4NNJ_A        55 VLILGLKGLGVEIAKNVVLAGVKSMTVFDPEPVQLADLSTQFFLTEkDIGQKRGDVTRAKLAELNAYVPVNVLD 128
Cdd:cd01487    2 VGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQYFLS-QIGEPKVEALKENLREINPFVKIEAIN 74
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 35-180 7.04e-06

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 49.34  E-value: 7.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         35 YSRQLYV--LGKEAMLKMQTSNVLILGLKGLGVEIAKNVVLAGVKSMTVFDPEPVQLADLSTQFFLTEKDIGQKRGDVTR 112
Cdd:PRK12475    5 YSRQILFsgIGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTEEDAKQKKPKAIA 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
4NNJ_A        113 AK--LAELNAYVPVN--VLD----SLDDVTQlsQFQVVV-ATDtvSLEDKVKINEFCHSSGIRFISSETRGLFGNTF 180
Cdd:PRK12475   85 AKehLRKINSEVEIVpvVTDvtveELEELVK--EVDLIIdATD--NFDTRLLINDLSQKYNIPWIYGGCVGSYGVTY 157
PRK14851 PRK14851
hypothetical protein; Provisional
 433-596 9.58e-06

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 49.47  E-value: 9.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A        433 YDNQIAVFGLDFQKKIANSKVFLVGSGAIGCEMLKNWALLGLGSgsdgyIVVTDNDSIEKSNLNRQFLFRPKDVGKNKSE 512
Cdd:PRK14851   26 FSRNIGLFTPGEQERLAEAKVAIPGMGGVGGVHLITMVRTGIGR-----FHIADFDQFEPVNVNRQFGARVPSFGRPKLA 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A        513 VAAEAVCAMNPDLkgKINAKIDKVGPETEEIFndsfwesLDFVTNALDNVDARTYVDRRCVFYRK-----PLLESGTLGT 587
Cdd:PRK14851  101 VMKEQALSINPFL--EITPFPAGINADNMDAF-------LDGVDVVLDGLDFFQFEIRRTLFNMArekgiPVITAGPLGY 171


                  ....*....
4NNJ_A        588 KGNTQVIIP 596
Cdd:PRK14851  172 SSAMLVFTP 180
PRK14852 PRK14852
hypothetical protein; Provisional
 445-596 3.85e-05

hypothetical protein; Provisional


Pssm-ID: 184854 [Multi-domain]  Cd Length: 989  Bit Score: 47.77  E-value: 3.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A        445 QKKIANSKVFLVGSGAIGCEMLKNWALLGLGSGSdgyivVTDNDSIEKSNLNRQFLFRPKDVGKNKSEVAAEAVCAMNPD 524
Cdd:PRK14852  327 QRRLLRSRVAIAGLGGVGGIHLMTLARTGIGNFN-----LADFDAYSPVNLNRQYGASIASFGRGKLDVMTERALSVNPF 401

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
4NNJ_A        525 LkgKINAKIDKVGPETEeifnDSFWESLDFVTNALD--NVDARTYVDRRCVFYRKPLLESGTLGTKGNTQVIIP 596
Cdd:PRK14852  402 L--DIRSFPEGVAAETI----DAFLKDVDLLVDGIDffALDIRRRLFNRALELGIPVITAGPLGYSCALLVFMP 469
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 35-146 1.21e-04

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 45.85  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         35 YSRQLYV--LGKEAMLKMQTSNVLILGLKGLGVEIAKNVVLAGVKSMTVFDPEPVQLADLSTQFFLTEKDIGQKRGDVTR 112
Cdd:PRK07878   23 YSRHLIIpdVGVDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRQVIHGQSDVGRSKAQSAR 102

                          90       100       110
                  ....*....|....*....|....*....|....*....
4NNJ_A        113 AKLAELNAYVPVNV----LDSLDDVTQLSQFQVVV-ATD 146
Cdd:PRK07878  103 DSIVEINPLVNVRLhefrLDPSNAVELFSQYDLILdGTD 141
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
 452-524 1.39e-04

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: 45.06  E-value: 1.39e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
4NNJ_A       452 KVFLVGSGAIGCEMLKNwaLLGLGSgsdGYIVVTDNDSIEKSNLNRQFLFRPKDV--GKNKSEVAAEAVCAMNPD 524
Cdd:cd01486    1 KCLLLGAGTLGCNVARN--LLGWGV---RHITFVDSGKVSYSNPVRQSLFTFEDCkgGKPKAEAAAERLKEIFPS 70
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 36-127 1.56e-04

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 45.26  E-value: 1.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         36 SRQLYV--LGKEAMLKMQTSNVLILGLKGLGVEIAKNVVLAGVKSMTVFDPEPVQLADLSTQFFLTEKDIGQKRGDVTRA 113
Cdd:PRK05600   23 ARQLALpgFGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDVGRPKVEVAAE 102

                          90
                  ....*....|....
4NNJ_A        114 KLAELNAYVPVNVL 127
Cdd:PRK05600  103 RLKEIQPDIRVNAL 116
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 847-932 1.00e-03

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: 41.86  E-value: 1.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         847 IEFITACSNCraqnYFIETADRQKTKF--IAGriipAIATTTSLVTGLVNLELYKLIDNKTDIeQYKNGFVNLALPFFGF 924
Cdd:pfam00899  154 IPGKTPCYRC----LFPEDPPPKLVPSctVAG----VLGPTTAVVAGLQALEALKLLLGKGEP-NLAGRLLQFDALTMTF 224


                   ....*...
4NNJ_A         925 SEPIASPK 932
Cdd:pfam00899  225 RELRLALK 232
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
29-128 1.41e-03

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 41.38  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NNJ_A         29 EIDESLYSRqlyvLGKEAMLKMQTSNVLILGLKGLGVEIAKNVVLAGVKSMTVFDPEPVQLADLSTQFFLTEkDIGQKRG 108
Cdd:PRK08644    9 EFEAMLASR----HTPKLLEKLKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVVEPSNLNRQQYFIS-QIGMPKV 83

                          90       100
                  ....*....|....*....|
4NNJ_A        109 DVTRAKLAELNAYVPVNVLD 128
Cdd:PRK08644   84 EALKENLLEINPFVEIEAHN 103
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 54-127 1.95e-03

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: 41.89  E-value: 1.95e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
4NNJ_A        54 NVLILGLKGLGVEIAKNVVLAGVKS-----MTVFDPEPVQLADLSTQFFLTEKDIGQKRGDVTRAKLAELNAYVPVNVL 127
Cdd:cd01490    1 KVFLVGAGAIGCELLKNFALMGVGTgesgeITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITAL 79
 
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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