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Conserved domains on  [gi|294659774|ref|XP_462198|]
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DEHA2G15114p [Debaryomyces hansenii CBS767]

Protein Classification

E1_enzyme_family and UBA_E1_SCCH superfamily-containing protein( domain architecture ID 1563435)

protein containing superfamilies E1_enzyme_family, UBA_E1_SCCH, and UAE_UbL

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
E1_enzyme_family super family cl22428
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 24-459 8.64e-161

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.


The actual alignment was detected with superfamily member cd01489:

Pssm-ID: 451392 [Multi-domain]  Cd Length: 312  Bit Score: 463.00  E-value: 8.64e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774  24 VLMVGAGGIGCELLKNLVLSQYGEIHIVDLDTITLSNLNRQFLFRPTDIDKSKSLTVVKAVEAFNYhNTKLVPHHGNIMD 103
Cdd:cd01489    2 VLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNP-NVKIVAYHANIKD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774 104 TnQFPIAWWDQFSYVFNALDNLEARRYVNKMCLFLKKPLMESGTTGYDGQVQPIFPYYSECFECQAKATPKTYPVCTIRS 183
Cdd:cd01489   81 P-DFNVEFFKQFDLVFNALDNLAARRHVNKMCLAADVPLIESGTTGFLGQVQVIKKGKTECYECQPKETPKTFPVCTIRS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774 184 TPSQPVHCITWAKEFLFhqLFDessstvtteqskeqqrkklqeetddkqeienmlkesnelselrqlikapnledrnqfi 263
Cdd:cd01489  160 TPSQPIHCIVWAKSLFF--LFN---------------------------------------------------------- 179

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774 264 hrtiiKIFKVDIERLLRIDSLWKTRVKPVPLQFDELyvndvnnllsdkrneviisrdtsvwsllenlyvfykasenlqkr 343
Cdd:cd01489  180 -----KVFKDDIERLLSMEELWKTRKPPVPLSWKEL-------------------------------------------- 210

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774 344 ldesesfvSFDKDDEDTLNFVVAAANIRCSIFNIEVKSKFDIKQIAGNIIPAIATTNAIISGFSSLGALSYYKSTAennd 423
Cdd:cd01489  211 --------TFDKDDQDALDFVAAAANLRSHVFGIPMKSRFDIKQMAGNIIPAIATTNAIIAGLIVLEALKVLSGDK---- 278

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 294659774 424 fgDMSKDSSTVFVSIRPNKYITSASLVGPGDQCPSC 459
Cdd:cd01489  279 --EQCRTVFLNLQPNRRKRLLVPCKLDPPNPNCYVC 312
UAE_UbL super family cl39046
Ubiquitin/SUMO-activating enzyme ubiquitin-like domain; This is the C-terminal domain of ...
 473-547 5.81e-08

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


The actual alignment was detected with superfamily member pfam14732:

Pssm-ID: 476859  Cd Length: 88  Bit Score: 50.65  E-value: 5.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774  473 LKTWTLKDLVDK-LIQTYGYEDDVSIILGQSKLIYDF-----DFDDNLEKKLSEInGFRNGELLLVqdeDDMLENLELYI 546
Cdd:pfam14732   5 TEKATLGDLVEDvLKKKLGMVAPDVSLSGGGTILYLSseedeTEDDNLPKKLSEL-GIKNGSILTV---DDFLQDFEVNL 80


                  .
gi 294659774  547 N 547
Cdd:pfam14732  81 V 81
UBA_E1_SCCH super family cl10464
Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ...
 185-386 2.99e-07

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


The actual alignment was detected with superfamily member pfam10585:

Pssm-ID: 463157  Cd Length: 254  Bit Score: 52.23  E-value: 2.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774  185 PSQPVHCITWAKEfLFHQLFDESSSTVtteqskeqqrKKLQEetDDKQEIENMLKES--NELSELRQLIKA------PNL 256
Cdd:pfam10585   1 PNAIEHTIQWARD-EFEGLFVQPPEEV----------NKYLQ--PPQNFIESLLKQGggQKLETLESVRKSlvterpKTF 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774  257 ED-----RNQFihrtiIKIFKVDIERLLR---IDSL-------WK-TRVKPVPLQFDE--------------LY------ 300
Cdd:pfam10585  68 EDcvawaRLKF-----EKLFNNDIKQLLYnfpPDHKtssgapfWSgPKRPPTPLEFDPnnplhldfvvaaanLRaqvygi 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774  301 -----VNDVNNLLSD-------KRNEVIISRDTSVWSLLENLYVFYKAS-----ENLQKRLDESESF-------VSFDKD 356
Cdd:pfam10585 143 pgsrdREAIAKVLSKvkvpefkPKSGVKIQVNDEEAADPNAESEDDEDEldellEELPKLAVSPSSLagfrlnpIEFEKD 222

                         250       260       270
                  ....*....|....*....|....*....|..
gi 294659774  357 DEDT--LNFVVAAANIRCSIFNIEVKSKFDIK 386
Cdd:pfam10585 223 DDTNfhIDFITAASNLRARNYGIPPADRHKTK 254
 
Name Accession Description Interval E-value
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 24-459 8.64e-161

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: 463.00  E-value: 8.64e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774  24 VLMVGAGGIGCELLKNLVLSQYGEIHIVDLDTITLSNLNRQFLFRPTDIDKSKSLTVVKAVEAFNYhNTKLVPHHGNIMD 103
Cdd:cd01489    2 VLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNP-NVKIVAYHANIKD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774 104 TnQFPIAWWDQFSYVFNALDNLEARRYVNKMCLFLKKPLMESGTTGYDGQVQPIFPYYSECFECQAKATPKTYPVCTIRS 183
Cdd:cd01489   81 P-DFNVEFFKQFDLVFNALDNLAARRHVNKMCLAADVPLIESGTTGFLGQVQVIKKGKTECYECQPKETPKTFPVCTIRS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774 184 TPSQPVHCITWAKEFLFhqLFDessstvtteqskeqqrkklqeetddkqeienmlkesnelselrqlikapnledrnqfi 263
Cdd:cd01489  160 TPSQPIHCIVWAKSLFF--LFN---------------------------------------------------------- 179

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774 264 hrtiiKIFKVDIERLLRIDSLWKTRVKPVPLQFDELyvndvnnllsdkrneviisrdtsvwsllenlyvfykasenlqkr 343
Cdd:cd01489  180 -----KVFKDDIERLLSMEELWKTRKPPVPLSWKEL-------------------------------------------- 210

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774 344 ldesesfvSFDKDDEDTLNFVVAAANIRCSIFNIEVKSKFDIKQIAGNIIPAIATTNAIISGFSSLGALSYYKSTAennd 423
Cdd:cd01489  211 --------TFDKDDQDALDFVAAAANLRSHVFGIPMKSRFDIKQMAGNIIPAIATTNAIIAGLIVLEALKVLSGDK---- 278

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 294659774 424 fgDMSKDSSTVFVSIRPNKYITSASLVGPGDQCPSC 459
Cdd:cd01489  279 --EQCRTVFLNLQPNRRKRLLVPCKLDPPNPNCYVC 312
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 7-418 7.38e-58

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: 210.13  E-value: 7.38e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774     7 LRKILGEDRCNNIRKANVLMVGAGGIGCELLKNLVL-----SQYGEIHIVDLDTITLSNLNRQFLFRPTDIDKSKSLTVV 81
Cdd:TIGR01408  405 QIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALmgvgtGKKGMITVTDPDLIEKSNLNRQFLFRPHHIGKPKSYTAA 484

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774    82 KAVEAFN------YHNTKLVPHHGNIMDTnqfpiAWWDQFSYVFNALDNLEARRYVNKMCLFLKKPLMESGTTGYDGQVQ 155
Cdd:TIGR01408  485 DATLKINpqikidAHQNRVGPETETIFND-----EFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGTLGTKGNTQ 559

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774   156 PIFPYYSECFECQAKATPKTYPVCTIRSTPSQPVHCITWAKEfLFHQLFDESSSTVTTEQSKEQQRKKLQEETDDKQEIE 235
Cdd:TIGR01408  560 VVVPHLTESYGSSRDPPEKEIPFCTLKSFPAAIEHTIQWARD-KFEGLFSHKPSLVNKYLSSPSSAEEVLQKIQSGHSRE 638

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774   236 NMLKESNELSELR-----QLIKAPNLEDRNQFIHRTIIKIFKVDIERLLRIDSLWKTRVK--PVPLQFD----------- 297
Cdd:TIGR01408  639 GLEQIIKLLSKEKprnfsQCVEWARLKFEKYFNNKALQLLHCFPLDIRTSTGSPFWSSPKrpPSPLKFDlneplhlsfiq 718

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774   298 ---------------------ELYVNDVNNL----LSDKRNEVIISRDTSvwSLLENLYVFYKAS-ENLQKRLDESESFV 351
Cdd:TIGR01408  719 aaaklyatvygipfaeedlsaDALLNILSEVkipeFKPRSNKKIQTDETA--RKPDTAPIDDRNAiFQLEKAILSNEATK 796

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 294659774   352 S--------FDKDDEDT--LNFVVAAANIRCSIFNIEVKSKFDIKQIAGNIIPAIATTNAIISGfssLGALSYYKST 418
Cdd:TIGR01408  797 SdfrmaplsFEKDDDHNghIDFITAASNLRAKNYSIEPADRFKTKFIAGKIIPAIATSTATVSG---LVCLELIKVT 870
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 6-184 2.33e-55

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: 187.85  E-value: 2.33e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774    6 YLRKI----LGEDRCNNIRKANVLMVGAGGIGCELLKNLVLSQYGEIHIVDLDTITLSNLNRQFLFRPTDIDKSKSLTVV 81
Cdd:pfam00899   1 YSRQLalplIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774   82 KAVEAFNYHnTKLVPHHGNIMDTNqfPIAWWDQFSYVFNALDNLEARRYVNKMCLFLKKPLMESGTTGYDGQVQPIFPYY 161
Cdd:pfam00899  81 ERLREINPD-VEVEAYTERLTPEN--AEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVVIPGK 157

                         170       180
                  ....*....|....*....|....*
gi 294659774  162 SECFEC--QAKATPKTYPVCTIRST 184
Cdd:pfam00899 158 TPCYRClfPEDPPPKLVPSCTVAGV 182
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 6-179 1.29e-33

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: 128.71  E-value: 1.29e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774   6 YLRKIL----GEDRCNNIRKANVLMVGAGGIGCELLKNLVLSQYGEIHIVDLDTITLSNLNRQFLFRPTDIDKSKSLTVV 81
Cdd:COG0476    8 YSRQILlpeiGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGRPKVEAAA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774  82 KAVEAFNyHNTKLVPHHGNIMDTNQFPIAwwDQFSYVFNALDNLEARRYVNKMCLFLKKPLMESGTTGYDGQVQPIFPYY 161
Cdd:COG0476   88 ERLRALN-PDVEVEAIPERLTEENALELL--AGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQVTVFIPGD 164

                        170
                 ....*....|....*...
gi 294659774 162 SECFECQAKATPKTYPVC 179
Cdd:COG0476  165 TPCYRCLFPEPPEPGPSC 182
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 20-167 6.42e-19

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 86.44  E-value: 6.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774  20 RKANVLMVGAGGIGCELLKNLVLSQYGEIHIVDLDTITLSNLNRQFLFRPTDIDKSKSLTVVKAVEAFNYHnTKLVPHHG 99
Cdd:PRK05690  31 KAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIGQPKVESARAALARINPH-IAIETINA 109

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 294659774 100 NIMDTNQFP-IAwwdQFSYVFNALDNLEARRYVNKMCLFLKKPLMeSGTTG-YDGQVQpIFPYYSE--CFEC 167
Cdd:PRK05690 110 RLDDDELAAlIA---GHDLVLDCTDNVATRNQLNRACFAAKKPLV-SGAAIrMEGQVT-VFTYQDDepCYRC 176
UAE_UbL pfam14732
Ubiquitin/SUMO-activating enzyme ubiquitin-like domain; This is the C-terminal domain of ...
 473-547 5.81e-08

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


Pssm-ID: 464286  Cd Length: 88  Bit Score: 50.65  E-value: 5.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774  473 LKTWTLKDLVDK-LIQTYGYEDDVSIILGQSKLIYDF-----DFDDNLEKKLSEInGFRNGELLLVqdeDDMLENLELYI 546
Cdd:pfam14732   5 TEKATLGDLVEDvLKKKLGMVAPDVSLSGGGTILYLSseedeTEDDNLPKKLSEL-GIKNGSILTV---DDFLQDFEVNL 80


                  .
gi 294659774  547 N 547
Cdd:pfam14732  81 V 81
UBA_E1_SCCH pfam10585
Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ...
 185-386 2.99e-07

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: 52.23  E-value: 2.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774  185 PSQPVHCITWAKEfLFHQLFDESSSTVtteqskeqqrKKLQEetDDKQEIENMLKES--NELSELRQLIKA------PNL 256
Cdd:pfam10585   1 PNAIEHTIQWARD-EFEGLFVQPPEEV----------NKYLQ--PPQNFIESLLKQGggQKLETLESVRKSlvterpKTF 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774  257 ED-----RNQFihrtiIKIFKVDIERLLR---IDSL-------WK-TRVKPVPLQFDE--------------LY------ 300
Cdd:pfam10585  68 EDcvawaRLKF-----EKLFNNDIKQLLYnfpPDHKtssgapfWSgPKRPPTPLEFDPnnplhldfvvaaanLRaqvygi 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774  301 -----VNDVNNLLSD-------KRNEVIISRDTSVWSLLENLYVFYKAS-----ENLQKRLDESESF-------VSFDKD 356
Cdd:pfam10585 143 pgsrdREAIAKVLSKvkvpefkPKSGVKIQVNDEEAADPNAESEDDEDEldellEELPKLAVSPSSLagfrlnpIEFEKD 222

                         250       260       270
                  ....*....|....*....|....*....|..
gi 294659774  357 DEDT--LNFVVAAANIRCSIFNIEVKSKFDIK 386
Cdd:pfam10585 223 DDTNfhIDFITAASNLRARNYGIPPADRHKTK 254
 
Name Accession Description Interval E-value
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 24-459 8.64e-161

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: 463.00  E-value: 8.64e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774  24 VLMVGAGGIGCELLKNLVLSQYGEIHIVDLDTITLSNLNRQFLFRPTDIDKSKSLTVVKAVEAFNYhNTKLVPHHGNIMD 103
Cdd:cd01489    2 VLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNP-NVKIVAYHANIKD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774 104 TnQFPIAWWDQFSYVFNALDNLEARRYVNKMCLFLKKPLMESGTTGYDGQVQPIFPYYSECFECQAKATPKTYPVCTIRS 183
Cdd:cd01489   81 P-DFNVEFFKQFDLVFNALDNLAARRHVNKMCLAADVPLIESGTTGFLGQVQVIKKGKTECYECQPKETPKTFPVCTIRS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774 184 TPSQPVHCITWAKEFLFhqLFDessstvtteqskeqqrkklqeetddkqeienmlkesnelselrqlikapnledrnqfi 263
Cdd:cd01489  160 TPSQPIHCIVWAKSLFF--LFN---------------------------------------------------------- 179

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774 264 hrtiiKIFKVDIERLLRIDSLWKTRVKPVPLQFDELyvndvnnllsdkrneviisrdtsvwsllenlyvfykasenlqkr 343
Cdd:cd01489  180 -----KVFKDDIERLLSMEELWKTRKPPVPLSWKEL-------------------------------------------- 210

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774 344 ldesesfvSFDKDDEDTLNFVVAAANIRCSIFNIEVKSKFDIKQIAGNIIPAIATTNAIISGFSSLGALSYYKSTAennd 423
Cdd:cd01489  211 --------TFDKDDQDALDFVAAAANLRSHVFGIPMKSRFDIKQMAGNIIPAIATTNAIIAGLIVLEALKVLSGDK---- 278

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 294659774 424 fgDMSKDSSTVFVSIRPNKYITSASLVGPGDQCPSC 459
Cdd:cd01489  279 --EQCRTVFLNLQPNRRKRLLVPCKLDPPNPNCYVC 312
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 24-409 1.26e-89

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: 277.54  E-value: 1.26e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774  24 VLMVGAGGIGCELLKNLVLSQYGEIHIVDLDTITLSNLNRQFLFRPTDIDKSKSLTVVKAVEAFNyHNTKLVPHHGNIMD 103
Cdd:cd01484    2 VLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRN-PNCKVVPYQNKVGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774 104 TNQFPIAWWDQFSYVFNALDNLEARRYVNKMCLFLKKPLMESGTTGYDGQVQPIFPYYSECFECQAKATPKTYPVCTIRS 183
Cdd:cd01484   81 EQDFNDTFFEQFHIIVNALDNIIARRYVNGMLIFLIVPLIESGTEGFKGNAQVILPGMTECIECTLYPPQKNFPMCTIAS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774 184 TPSQPVHCITWAKEFLFhqlfdessstvtteqskeqqrkklqeetddkqeienmlkesnelselrqlikapnledrnqfi 263
Cdd:cd01484  161 MPRLPEHCIEWARMLQW--------------------------------------------------------------- 177

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774 264 hrtiikifkvdierllridslwktrvkpvplqfdelyvndvnnllsdkrneviisrdtsvwsllenlyvfykasenlqkr 343
Cdd:cd01484      --------------------------------------------------------------------------------

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 294659774 344 ldesesfvsfdkDDEDTLNFVVAAANIRCSIFNIEVKSKFDIKQIAGNIIPAIATTNAIISGFSSL 409
Cdd:cd01484  178 ------------DDPEHIQFIFQASNERASQYNIRGVTYFLTKGVAGRIIPAVATTNAVVAGVCAL 231
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 23-424 9.79e-70

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: 232.56  E-value: 9.79e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774  23 NVLMVGAGGIGCELLKNLVL-----SQYGEIHIVDLDTITLSNLNRQFLFRPTDIDKSKSLTVVKAVEAFN------YHN 91
Cdd:cd01490    1 KVFLVGAGAIGCELLKNFALmgvgtGESGEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNpdlkitALQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774  92 TKLVPHHGNIMDTNqfpiaWWDQFSYVFNALDNLEARRYVNKMCLFLKKPLMESGTTGYDGQVQPIFPYYSECFECQAKA 171
Cdd:cd01490   81 NRVGPETEHIFNDE-----FWEKLDGVANALDNVDARMYVDRRCVYYRKPLLESGTLGTKGNTQVVIPHLTESYSSSRDP 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774 172 TPKTYPVCTIRSTPSQPVHCITWAKEfLFHQLFDESSSTVtteqskeqqrkklqeetddkqeieNMLKEsnelselRQLI 251
Cdd:cd01490  156 PEKSIPLCTLKNFPNAIEHTIQWARD-EFEGLFKQPPENV------------------------NQYLF-------EDCV 203

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774 252 KAPNLEDRNQFIHRtiikifkvdIERLLR---IDSLWKTRVK--------PVPLQFdelyvnDVNNllsdkrneviisrd 320
Cdd:cd01490  204 RWARLLFEKYFNNN---------IKQLLHnfpPDAVTSDGAPfwsgpkrcPTPLEF------DVNN-------------- 254

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774 321 tsvwsllENLYVFYKASENLqkrLDESESFVSFDKDDeDT---LNFVVAAANIRCSIFNIEVKSKFDIKQIAGNIIPAIA 397
Cdd:cd01490  255 -------PLHLDFVLAAANL---YAEVYGIPGFEKDD-DTnfhMDFITAASNLRARNYSIPPADRHKTKRIAGKIIPAIA 323

                        410       420
                 ....*....|....*....|....*..
gi 294659774 398 TTNAIISGfssLGALSYYKSTAENNDF 424
Cdd:cd01490  324 TTTAAVTG---LVCLELYKVVDGKRPL 347
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 24-247 1.45e-58

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: 198.35  E-value: 1.45e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774  24 VLMVGAGGIGCELLKNLVLSQYGEIHIVDLDTITLSNLNRQFLFRPTDIDKSKSLTVVKAVEAfNYHNTKLVPHHGNIMD 103
Cdd:cd01488    2 ILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVND-RVPGVNVTPHFGKIQD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774 104 tnqFPIAWWDQFSYVFNALDNLEARRYVNKM-CLFLK-------KPLMESGTTGYDGQVQPIFPYYSECFECQAKATPK- 174
Cdd:cd01488   81 ---KDEEFYRQFNIIICGLDSIEARRWINGTlVSLLLyedpesiIPLIDGGTEGFKGHARVILPGITACIECSLDLFPPq 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 294659774 175 -TYPVCTIRSTPSQPVHCITWAKeflfhqlfdessstvTTEQSKEQQRKKLqeETDDKQEIENMLKESNELSEL 247
Cdd:cd01488  158 vTFPLCTIANTPRLPEHCIEYAS---------------LIQWPKEFPFVPL--DGDDPEHIEWLYQKALERAAQ 214
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 7-418 7.38e-58

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: 210.13  E-value: 7.38e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774     7 LRKILGEDRCNNIRKANVLMVGAGGIGCELLKNLVL-----SQYGEIHIVDLDTITLSNLNRQFLFRPTDIDKSKSLTVV 81
Cdd:TIGR01408  405 QIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALmgvgtGKKGMITVTDPDLIEKSNLNRQFLFRPHHIGKPKSYTAA 484

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774    82 KAVEAFN------YHNTKLVPHHGNIMDTnqfpiAWWDQFSYVFNALDNLEARRYVNKMCLFLKKPLMESGTTGYDGQVQ 155
Cdd:TIGR01408  485 DATLKINpqikidAHQNRVGPETETIFND-----EFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGTLGTKGNTQ 559

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774   156 PIFPYYSECFECQAKATPKTYPVCTIRSTPSQPVHCITWAKEfLFHQLFDESSSTVTTEQSKEQQRKKLQEETDDKQEIE 235
Cdd:TIGR01408  560 VVVPHLTESYGSSRDPPEKEIPFCTLKSFPAAIEHTIQWARD-KFEGLFSHKPSLVNKYLSSPSSAEEVLQKIQSGHSRE 638

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774   236 NMLKESNELSELR-----QLIKAPNLEDRNQFIHRTIIKIFKVDIERLLRIDSLWKTRVK--PVPLQFD----------- 297
Cdd:TIGR01408  639 GLEQIIKLLSKEKprnfsQCVEWARLKFEKYFNNKALQLLHCFPLDIRTSTGSPFWSSPKrpPSPLKFDlneplhlsfiq 718

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774   298 ---------------------ELYVNDVNNL----LSDKRNEVIISRDTSvwSLLENLYVFYKAS-ENLQKRLDESESFV 351
Cdd:TIGR01408  719 aaaklyatvygipfaeedlsaDALLNILSEVkipeFKPRSNKKIQTDETA--RKPDTAPIDDRNAiFQLEKAILSNEATK 796

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 294659774   352 S--------FDKDDEDT--LNFVVAAANIRCSIFNIEVKSKFDIKQIAGNIIPAIATTNAIISGfssLGALSYYKST 418
Cdd:TIGR01408  797 SdfrmaplsFEKDDDHNghIDFITAASNLRAKNYSIEPADRFKTKFIAGKIIPAIATSTATVSG---LVCLELIKVT 870
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 6-184 2.33e-55

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: 187.85  E-value: 2.33e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774    6 YLRKI----LGEDRCNNIRKANVLMVGAGGIGCELLKNLVLSQYGEIHIVDLDTITLSNLNRQFLFRPTDIDKSKSLTVV 81
Cdd:pfam00899   1 YSRQLalplIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774   82 KAVEAFNYHnTKLVPHHGNIMDTNqfPIAWWDQFSYVFNALDNLEARRYVNKMCLFLKKPLMESGTTGYDGQVQPIFPYY 161
Cdd:pfam00899  81 ERLREINPD-VEVEAYTERLTPEN--AEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVVIPGK 157

                         170       180
                  ....*....|....*....|....*
gi 294659774  162 SECFEC--QAKATPKTYPVCTIRST 184
Cdd:pfam00899 158 TPCYRClfPEDPPPKLVPSCTVAGV 182
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 6-179 1.29e-33

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: 128.71  E-value: 1.29e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774   6 YLRKIL----GEDRCNNIRKANVLMVGAGGIGCELLKNLVLSQYGEIHIVDLDTITLSNLNRQFLFRPTDIDKSKSLTVV 81
Cdd:COG0476    8 YSRQILlpeiGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGRPKVEAAA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774  82 KAVEAFNyHNTKLVPHHGNIMDTNQFPIAwwDQFSYVFNALDNLEARRYVNKMCLFLKKPLMESGTTGYDGQVQPIFPYY 161
Cdd:COG0476   88 ERLRALN-PDVEVEAIPERLTEENALELL--AGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQVTVFIPGD 164

                        170
                 ....*....|....*...
gi 294659774 162 SECFECQAKATPKTYPVC 179
Cdd:COG0476  165 TPCYRCLFPEPPEPGPSC 182
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 24-158 7.86e-32

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: 120.07  E-value: 7.86e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774  24 VLMVGAGGIGCELLKNLVLSQYGEIHIVDLDTITLSNLNRQFLFRPTDIDKSKSLTVVKAVEAFNyHNTKLVPHHGNIMD 103
Cdd:cd01483    2 VLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELN-PGVNVTAVPEGISE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 294659774 104 TNQfpIAWWDQFSYVFNALDNLEARRYVNKMCLFLKKPLMESGTTGYDGQVQPIF 158
Cdd:cd01483   81 DNL--DDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQVID 133
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 6-167 5.71e-31

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: 120.66  E-value: 5.71e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774   6 YLRKIL----GEDRCNNIRKANVLMVGAGGIGCELLKNLVLSQYGEIHIVDLDTITLSNLNRQFLFRPTDIDKSKSLTVV 81
Cdd:cd00757    2 YSRQILlpeiGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774  82 KAVEAFNyHNTKLVPHHGNIMDTNQFPIAwwDQFSYVFNALDNLEARRYVNKMCLFLKKPLMESGTTGYDGQVQPIFPYY 161
Cdd:cd00757   82 ERLRAIN-PDVEIEAYNERLDAENAEELI--AGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLGFEGQVTVFIPGE 158


                 ....*.
gi 294659774 162 SECFEC 167
Cdd:cd00757  159 GPCYRC 164
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 20-167 6.42e-19

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 86.44  E-value: 6.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774  20 RKANVLMVGAGGIGCELLKNLVLSQYGEIHIVDLDTITLSNLNRQFLFRPTDIDKSKSLTVVKAVEAFNYHnTKLVPHHG 99
Cdd:PRK05690  31 KAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIGQPKVESARAALARINPH-IAIETINA 109

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 294659774 100 NIMDTNQFP-IAwwdQFSYVFNALDNLEARRYVNKMCLFLKKPLMeSGTTG-YDGQVQpIFPYYSE--CFEC 167
Cdd:PRK05690 110 RLDDDELAAlIA---GHDLVLDCTDNVATRNQLNRACFAAKKPLV-SGAAIrMEGQVT-VFTYQDDepCYRC 176
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 18-154 1.88e-14

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: 72.32  E-value: 1.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774  18 NIRKANVLMVGAGGIGCELLKNLVLSQYGEIHIVDLDTITLSNLNRQFLFRPTDIDKSKSLTVVKAVEAFNyhntKLVPH 97
Cdd:cd01492   18 RLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEASLERLRALN----PRVKV 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 294659774  98 HGNIMDTNQFPIAWWDQFSYVF-NALDNLEARRyVNKMCLFLKKPLMESGTTGYDGQV 154
Cdd:cd01492   94 SVDTDDISEKPEEFFSQFDVVVaTELSRAELVK-INELCRKLGVKFYATGVHGLFGFV 150
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
3-167 1.22e-13

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 72.74  E-value: 1.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774   3 KDTYLRKIL----GEDRCNNIRKANVLMVGAGGIGCELLKNLVLSQYGEIHIVDLDTITLSNLNRQFLFRPTDIDKSKSL 78
Cdd:PRK08762 113 DERYSRHLRlpevGEEGQRRLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVGQPKVD 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774  79 TVVKAVEAFN------YHNTKLVPHhgNIMDTNQfpiawwdQFSYVFNALDNLEARRYVNKMCLFLKKPLMESGTTGYDG 152
Cdd:PRK08762 193 SAAQRLAALNpdvqveAVQERVTSD--NVEALLQ-------DVDVVVDGADNFPTRYLLNDACVKLGKPLVYGAVFRFEG 263

                        170
                 ....*....|....*....
gi 294659774 153 QVQPIFPYYSE----CFEC 167
Cdd:PRK08762 264 QVSVFDAGRQRgqapCYRC 282
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 12-154 3.41e-12

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 68.58  E-value: 3.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774  12 GEDRCNNirkANVLMVGAGGIGCELLKNLVLSQYGEIHIVDLDTITLSNLNRQFLFRPTDIDKSKSLTVVKAVEAFN--- 88
Cdd:PRK07878  36 GQKRLKN---ARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRQVIHGQSDVGRSKAQSARDSIVEINplv 112

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 294659774  89 ---YHNTKLVPHhgNIMDTnqfpiawWDQFSYVFNALDNLEARRYVNKMCLFLKKPLMESGTTGYDGQV 154
Cdd:PRK07878 113 nvrLHEFRLDPS--NAVEL-------FSQYDLILDGTDNFATRYLVNDAAVLAGKPYVWGSIYRFEGQA 172
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 6-135 3.06e-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: 64.60  E-value: 3.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774   6 YLRKI--LGEDRCNNIRKANVLMVGAGGIGCELLKNLVLSQYGEIHIVDLDTITLSNLNRQFLFRPTDIDKSKSLTVVKA 83
Cdd:cd01491    2 YSRQLyvLGHEAMKKLQKSNVLISGLGGLGVEIAKNLILAGVKSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAEASQAR 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 294659774  84 VEAFNyHNTKLVPHHGNIMDTnqfpiaWWDQFSYVFNALDNLEARRYVNKMC 135
Cdd:cd01491   82 LAELN-PYVPVTVSTGPLTTD------ELLKFQVVVLTDASLEDQLKINEFC 126
PRK08328 PRK08328
hypothetical protein; Provisional
 10-159 8.41e-11

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 62.51  E-value: 8.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774  10 ILGEDRCNNIRKANVLMVGAGGIGCELLKNLVLSQYGEIHIVDLDTITLSNLNRQFLFRPTDIDK-SKSLTVVKAVEAFN 88
Cdd:PRK08328  16 IFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEDLGKnPKPLSAKWKLERFN 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 294659774  89 yHNTKLVPHHGNIMDTNQFPIAwwDQFSYVFNALDNLEARRYVNKMCLFLKKPLMESGTTGYDGQVQPIFP 159
Cdd:PRK08328  96 -SDIKIETFVGRLSEENIDEVL--KGVDVIVDCLDNFETRYLLDDYAHKKGIPLVHGAVEGTYGQVTTIVP 163
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 11-156 1.15e-09

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


Pssm-ID: 238384 [Multi-domain]  Cd Length: 231  Bit Score: 58.77  E-value: 1.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774  11 LGEDRCNNIRKANVLMVGAGGIGCELLKNLVLSQYGEIHIVDLDTITLSNLNRQFLFRPTDIDKSKSLTVVKAVEAFNYH 90
Cdd:cd00755    1 YGEEGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPE 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 294659774  91 NtKLVPHH-----GNIMDTNQFpiawwdQFSYVFNALDNLEARRYVNKMCLFLKKPLMESGTTGydGQVQP 156
Cdd:cd00755   81 C-EVDAVEefltpDNSEDLLGG------DPDFVVDAIDSIRAKVALIAYCRKRKIPVISSMGAG--GKLDP 142
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 13-76 3.02e-09

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 59.12  E-value: 3.02e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 294659774  13 EDRCNNirkANVLMVGAGGIGCELLKNLVLSQYGEIHIVDLDTITLSNLNRQFLFRPTDIDKSK 76
Cdd:PRK05600  36 QERLHN---ARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDVGRPK 96
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 4-179 3.39e-09

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 58.97  E-value: 3.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774   4 DTYLRKIL----GEDRCNNIRKANVLMVGAGGIGCELLKNLVLSQYGEIHIVDLDTITLSNLNRQFLFRPTDID--KSKS 77
Cdd:PRK12475   3 ERYSRQILfsgiGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTEEDAKqkKPKA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774  78 LTVVKAVEAFNyHNTKLVPHhgnIMD-TNQFPIAWWDQFSYVFNALDNLEARRYVNKMCLFLKKPLMESGTTGYDGQVQP 156
Cdd:PRK12475  83 IAAKEHLRKIN-SEVEIVPV---VTDvTVEELEELVKEVDLIIDATDNFDTRLLINDLSQKYNIPWIYGGCVGSYGVTYT 158

                        170       180
                 ....*....|....*....|...
gi 294659774 157 IFPYYSECFECQAKATPKTYPVC 179
Cdd:PRK12475 159 IIPGKTPCLRCLMEHVPVGGATC 181
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 8-73 4.39e-09

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: 56.66  E-value: 4.39e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 294659774   8 RKILGEDRCNNIRKANVLMVGAGGIGCELLKNLVLSQYGEIHIVDLDTITLSNLNRQFLFRPTDID 73
Cdd:cd01485    6 IRLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFLDAEVSN 71
UAE_UbL pfam14732
Ubiquitin/SUMO-activating enzyme ubiquitin-like domain; This is the C-terminal domain of ...
 473-547 5.81e-08

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


Pssm-ID: 464286  Cd Length: 88  Bit Score: 50.65  E-value: 5.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774  473 LKTWTLKDLVDK-LIQTYGYEDDVSIILGQSKLIYDF-----DFDDNLEKKLSEInGFRNGELLLVqdeDDMLENLELYI 546
Cdd:pfam14732   5 TEKATLGDLVEDvLKKKLGMVAPDVSLSGGGTILYLSseedeTEDDNLPKKLSEL-GIKNGSILTV---DDFLQDFEVNL 80


                  .
gi 294659774  547 N 547
Cdd:pfam14732  81 V 81
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
7-76 6.57e-08

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 53.32  E-value: 6.57e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774   7 LRKILGEDRCNNIRKANVLMVGAGGIGCELLKNLVLSQYGEIHIVDLDTITLSNLNRQFLFrPTDIDKSK 76
Cdd:PRK08644  14 LASRHTPKLLEKLKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVVEPSNLNRQQYF-ISQIGMPK 82
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 24-150 2.56e-07

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: 50.84  E-value: 2.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774  24 VLMVGAGGIGCELLKNLVLSQYGEIHIVDLDTITLSNLNRQFlFRPTDIDKSKSLTVVKAVEAFNYHnTKLVPHHGNIMD 103
Cdd:cd01487    2 VGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQ-YFLSQIGEPKVEALKENLREINPF-VKIEAINIKIDE 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 294659774 104 TNQFPIawWDQFSYVFNALDNLEARRYV-NKMCLFLKKPL-MESGTTGY 150
Cdd:cd01487   80 NNLEGL--FGDCDIVVEAFDNAETKAMLaESLLGNKNKPVvCASGMAGF 126
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 4-179 2.80e-07

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 52.69  E-value: 2.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774   4 DTYLRKIL----GEDRCNNIRKANVLMVGAGGIGCELLKNLVLSQYGEIHIVDLDTITLSNLNRQFLFRPTDIDKS--KS 77
Cdd:PRK07688   3 ERYSRQELfspiGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDVKNNlpKA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774  78 LTVVKAVEAFNYHntklVPHHGNIMDT---NQFPIAwwDQFSYVFNALDNLEARRYVNKMCLFLKKPLMESGTTGYDGQV 154
Cdd:PRK07688  83 VAAKKRLEEINSD----VRVEAIVQDVtaeELEELV--TGVDLIIDATDNFETRFIVNDAAQKYGIPWIYGACVGSYGLS 156

                        170       180
                 ....*....|....*....|....*
gi 294659774 155 QPIFPYYSECFECQAKATPKTYPVC 179
Cdd:PRK07688 157 YTIIPGKTPCLRCLLQSIPLGGATC 181
UBA_E1_SCCH pfam10585
Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ...
 185-386 2.99e-07

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: 52.23  E-value: 2.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774  185 PSQPVHCITWAKEfLFHQLFDESSSTVtteqskeqqrKKLQEetDDKQEIENMLKES--NELSELRQLIKA------PNL 256
Cdd:pfam10585   1 PNAIEHTIQWARD-EFEGLFVQPPEEV----------NKYLQ--PPQNFIESLLKQGggQKLETLESVRKSlvterpKTF 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774  257 ED-----RNQFihrtiIKIFKVDIERLLR---IDSL-------WK-TRVKPVPLQFDE--------------LY------ 300
Cdd:pfam10585  68 EDcvawaRLKF-----EKLFNNDIKQLLYnfpPDHKtssgapfWSgPKRPPTPLEFDPnnplhldfvvaaanLRaqvygi 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774  301 -----VNDVNNLLSD-------KRNEVIISRDTSVWSLLENLYVFYKAS-----ENLQKRLDESESF-------VSFDKD 356
Cdd:pfam10585 143 pgsrdREAIAKVLSKvkvpefkPKSGVKIQVNDEEAADPNAESEDDEDEldellEELPKLAVSPSSLagfrlnpIEFEKD 222

                         250       260       270
                  ....*....|....*....|....*....|..
gi 294659774  357 DEDT--LNFVVAAANIRCSIFNIEVKSKFDIK 386
Cdd:pfam10585 223 DDTNfhIDFITAASNLRARNYGIPPADRHKTK 254
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
19-160 3.71e-07

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 52.81  E-value: 3.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774  19 IRKANVLMVGAGGIGCELLKNLVLSQYGEIHIVDLDTITLSNLNRQFLFRPTDIDKSKSLTVVKAVEAFN------YHNT 92
Cdd:PRK07411  36 LKAASVLCIGTGGLGSPLLLYLAAAGIGRIGIVDFDVVDSSNLQRQVIHGTSWVGKPKIESAKNRILEINpycqvdLYET 115

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 294659774  93 KLVPHhgNIMDTNQfpiawwdQFSYVFNALDNLEARRYVNKMCLFLKKPLMESGTTGYDGQVQpIFPY 160
Cdd:PRK07411 116 RLSSE--NALDILA-------PYDVVVDGTDNFPTRYLVNDACVLLNKPNVYGSIFRFEGQAT-VFNY 173
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 7-64 1.11e-06

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: 50.08  E-value: 1.11e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 294659774   7 LRKILGEDRCNNIRKANVLMVGAGGIG---CEllkNLVLSQYGEIHIVDLDTITLSNLNRQ 64
Cdd:COG1179   10 TERLYGEEGLERLANAHVAVVGLGGVGswaAE---ALARSGVGRLTLVDLDDVCESNINRQ 67
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 17-82 3.60e-06

Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric activating enzyme (E1), specific for the Rub family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin(-like) by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by Rub family of ubiquitin-like proteins (Ublps) activates SCF ubiquitin ligases and is involved in cell cycle control, signaling and embryogenesis. ABPP1 contains part of the adenylation domain.


Pssm-ID: 238770 [Multi-domain]  Cd Length: 425  Bit Score: 49.61  E-value: 3.60e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 294659774  17 NNIRKANVLMVGAGGIGCELLKNLVLSQYGEIHIVDLDTITLSNLNRQFLFRPTDIDKSKSLTVVK 82
Cdd:cd01493   16 AALESAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAEATCE 81
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 6-88 4.94e-06

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 49.10  E-value: 4.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774   6 YLRKI----LGEDRCNNIRKANVLMVGAGGIGCELLKNLVLSQYGEIHIVDLDTITLSNLNRQFLFRPTDIDKSKSLTVV 81
Cdd:PRK05597   9 YRRQImlgeIGQQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVGQPKAESAR 88


                 ....*..
gi 294659774  82 KAVEAFN 88
Cdd:PRK05597  89 EAMLALN 95
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 8-88 1.54e-05

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: 48.35  E-value: 1.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774     8 RKILGEDRCNNIRKANVLMVGAGGIGCELLKNLVLSQYGEIHIVDLDTITLSNLNRQFLFRPTDIDKSKSLTVVKAVEAF 87
Cdd:TIGR01408   11 LYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRAEAVVKKLAEL 90


                   .
gi 294659774    88 N 88
Cdd:TIGR01408   91 N 91
PRK14851 PRK14851
hypothetical protein; Provisional
 21-150 6.70e-04

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 42.93  E-value: 6.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294659774  21 KANVLMVGAGGIGCELLKNLVLSQYGEIHIVDLDTITLSNLNRQFLFRPTDIDKSKSLTVVKAVEAFN-YHNTKLVPHHG 99
Cdd:PRK14851  43 EAKVAIPGMGGVGGVHLITMVRTGIGRFHIADFDQFEPVNVNRQFGARVPSFGRPKLAVMKEQALSINpFLEITPFPAGI 122

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 294659774 100 NIMDTNQFpiawWDQFSYVFNALD--NLEARRYVNKMCLFLKKPLMESGTTGY 150
Cdd:PRK14851 123 NADNMDAF----LDGVDVVLDGLDffQFEIRRTLFNMAREKGIPVITAGPLGY 171
 
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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