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Conserved domains on  [gi|4885649|ref|NP_005490|]
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SUMO-activating enzyme subunit 2 isoform 1 [Homo sapiens]

Protein Classification

ubiquitin-activating E1 family protein( domain architecture ID 10845023)

ubiquitin-activating E1 family protein similar to Caenorhabditis elegans SUMO-activating enzyme subunit uba-2 that acts as an E1 ligase for smo-1, mediating ATP-dependent activation of smo-1 and formation of a thioester with a conserved cysteine residue on uba-2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 19-444 0e+00

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


:

Pssm-ID: 238766 [Multi-domain]  Cd Length: 312  Bit Score: 615.93  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649   19 RVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAYHDSIMN 98
Cdd:cd01489   1 KVLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649   99 PDYNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTECYECHPKPTQRTFPGCTIRNT 178
Cdd:cd01489  81 PDFNVEFFKQFDLVFNALDNLAARRHVNKMCLAADVPLIESGTTGFLGQVQVIKKGKTECYECQPKETPKTFPVCTIRST 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649  179 PSEPIHCIVWAKYLFNqlfgeedadqevspdradpeaawepteaeararasnedgdikristkewakstgydpvkLFTKL 258
Cdd:cd01489 161 PSQPIHCIVWAKSLFF-----------------------------------------------------------LFNKV 181

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649  259 FKDDIRYLLTMDKLWRKRKPPVPLDWaevqsqgeetnasdqqnepqlglkdqqvldvksyarlfsksietlrvhlaekgd 338
Cdd:cd01489 182 FKDDIERLLSMEELWKTRKPPVPLSW------------------------------------------------------ 207

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649  339 gAELIWDKDDPSAMDFVTSAANLRMHIFSMNMKSRFDIKSMAGNIIPAIATTNAVIAGLIVLEGLKILSGKIDQCRTIFL 418
Cdd:cd01489 208 -KELTFDKDDQDALDFVAAAANLRSHVFGIPMKSRFDIKQMAGNIIPAIATTNAIIAGLIVLEALKVLSGDKEQCRTVFL 286

                       410       420
                ....*....|....*....|....*.
gi 4885649  419 NKQPNPRKKLLVPCALDPPNPNCYVC 444
Cdd:cd01489 287 NLQPNRRKRLLVPCKLDPPNPNCYVC 312
UBA2_C pfam16195
SUMO-activating enzyme subunit 2 C-terminus;
549-635 3.49e-33

SUMO-activating enzyme subunit 2 C-terminus;


:

Pssm-ID: 465058  Cd Length: 93  Bit Score: 122.33  E-value: 3.49e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649    549 DAPEKVGPKQA-EDAAKSITNGSDDGAQPSTST--AQEQDDVLIVDSDEEDSSNNADVSEEERSRKRKLD-EKENLSAKR 624
Cdd:pfam16195   1 DAPEKAPPKQAnPEEVNSIANGNKDSAQPSTSTkaAPEQDDVLIVDSDEEGPSSSADVATEGSGRKRKLDaDTEEASTKR 80

                          90
                  ....*....|.
gi 4885649    625 SRIEQKEELDD 635
Cdd:pfam16195  81 SRTEQSAADDD 91
UAE_UbL pfam14732
Ubiquitin/SUMO-activating enzyme ubiquitin-like domain; This is the C-terminal domain of ...
 452-538 2.59e-31

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: 116.91  E-value: 2.59e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649    452 VRLNVHKVTVLTLQDKIVKEKFAMVAPDVQIEDGKGTILISSEEGETEA-NNHKKLSEFGIRNGSRLQADDFLQDYTLLI 530
Cdd:pfam14732   1 LKVDTEKATLGDLVEDVLKKKLGMVAPDVSLSGGGTILYLSSEEDETEDdNLPKKLSELGIKNGSILTVDDFLQDFEVNL 80


                  ....*...
gi 4885649    531 NILHSEDL 538
Cdd:pfam14732  81 VILHREEL 88
UBA_E1_SCCH super family cl10464
Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ...
 179-362 4.09e-05

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: 45.68  E-value: 4.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649    179 PSEPIHCIVWAKYLFNQLFGE--EDADQEVSPdradPEAAWEPTEAEararASNEDGDI----------KRISTKE---- 242
Cdd:pfam10585   1 PNAIEHTIQWARDEFEGLFVQppEEVNKYLQP----PQNFIESLLKQ----GGGQKLETlesvrkslvtERPKTFEdcva 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649    243 WAkstgydpVKLFTKLFKDDIRYLLT---MDKL-------WR--KRkPPVPLDW------------------AEVQSQGE 292
Cdd:pfam10585  73 WA-------RLKFEKLFNNDIKQLLYnfpPDHKtssgapfWSgpKR-PPTPLEFdpnnplhldfvvaaanlrAQVYGIPG 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649    293 ETNASDQQN----------EPQLGLK----DQQVLDVKSYARLFSKSIETLRVHLAEKGDGAE---------LIWDKDDP 349
Cdd:pfam10585 145 SRDREAIAKvlskvkvpefKPKSGVKiqvnDEEAADPNAESEDDEDELDELLEELPKLAVSPSslagfrlnpIEFEKDDD 224

                         250
                  ....*....|....*
gi 4885649    350 SA--MDFVTSAANLR 362
Cdd:pfam10585 225 TNfhIDFITAASNLR 239
 
Name Accession Description Interval E-value
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 19-444 0e+00

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


Pssm-ID: 238766 [Multi-domain]  Cd Length: 312  Bit Score: 615.93  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649   19 RVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAYHDSIMN 98
Cdd:cd01489   1 KVLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649   99 PDYNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTECYECHPKPTQRTFPGCTIRNT 178
Cdd:cd01489  81 PDFNVEFFKQFDLVFNALDNLAARRHVNKMCLAADVPLIESGTTGFLGQVQVIKKGKTECYECQPKETPKTFPVCTIRST 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649  179 PSEPIHCIVWAKYLFNqlfgeedadqevspdradpeaawepteaeararasnedgdikristkewakstgydpvkLFTKL 258
Cdd:cd01489 161 PSQPIHCIVWAKSLFF-----------------------------------------------------------LFNKV 181

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649  259 FKDDIRYLLTMDKLWRKRKPPVPLDWaevqsqgeetnasdqqnepqlglkdqqvldvksyarlfsksietlrvhlaekgd 338
Cdd:cd01489 182 FKDDIERLLSMEELWKTRKPPVPLSW------------------------------------------------------ 207

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649  339 gAELIWDKDDPSAMDFVTSAANLRMHIFSMNMKSRFDIKSMAGNIIPAIATTNAVIAGLIVLEGLKILSGKIDQCRTIFL 418
Cdd:cd01489 208 -KELTFDKDDQDALDFVAAAANLRSHVFGIPMKSRFDIKQMAGNIIPAIATTNAIIAGLIVLEALKVLSGDKEQCRTVFL 286

                       410       420
                ....*....|....*....|....*.
gi 4885649  419 NKQPNPRKKLLVPCALDPPNPNCYVC 444
Cdd:cd01489 287 NLQPNRRKRLLVPCKLDPPNPNCYVC 312
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 3-178 1.09e-66

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: 218.28  E-value: 1.09e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649      3 LSRGLPRELAEAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQ 82
Cdd:pfam00899   6 ALPLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAAERLRE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649     83 FYPKANIVAYHDSIMNPDyNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTECYECH 162
Cdd:pfam00899  86 INPDVEVEAYTERLTPEN-AEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVVIPGKTPCYRCL 164

                         170
                  ....*....|....*...
gi 4885649    163 P--KPTQRTFPGCTIRNT 178
Cdd:pfam00899 165 FpeDPPPKLVPSCTVAGV 182
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 10-419 1.72e-56

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: 206.66  E-value: 1.72e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649      10 ELAEAVAGGRVLVVGAGGIGCELLKNLVLTGFS-----HIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFY 84
Cdd:TIGR01408  412 TFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVGtgkkgMITVTDPDLIEKSNLNRQFLFRPHHIGKPKSYTAADATLKIN 491

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649      85 PKANIVAYHDSImNPD----YNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTECYE 160
Cdd:TIGR01408  492 PQIKIDAHQNRV-GPEtetiFNDEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGTLGTKGNTQVVVPHLTESYG 570

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649     161 CHPKPTQRTFPGCTIRNTPSEPIHCIVWAKYLFNQLFGEEDAdqEVSPDRADPEAAWEPTEAEARARASNEDGDIKRIST 240
Cdd:TIGR01408  571 SSRDPPEKEIPFCTLKSFPAAIEHTIQWARDKFEGLFSHKPS--LVNKYLSSPSSAEEVLQKIQSGHSREGLEQIIKLLS 648

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649     241 KE----WAKSTGYDPVKlFTKLFKDDIRYLL----------TMDKLWRK-RKPPVPLDW------------------AEV 287
Cdd:TIGR01408  649 KEkprnFSQCVEWARLK-FEKYFNNKALQLLhcfpldirtsTGSPFWSSpKRPPSPLKFdlneplhlsfiqaaaklyATV 727

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649     288 QS--QGEETNASD-----------QQNEPQLGLKDQ--------QVLDVKSYARLFS--KSIETLRvHLAEKGDGAELIW 344
Cdd:TIGR01408  728 YGipFAEEDLSADallnilsevkiPEFKPRSNKKIQtdetarkpDTAPIDDRNAIFQleKAILSNE-ATKSDFRMAPLSF 806

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4885649     345 DKDDPSA--MDFVTSAANLRMHIFSMNMKSRFDIKSMAGNIIPAIATTNAVIAGLIVLEGLKILSG--KIDQCRTIFLN 419
Cdd:TIGR01408  807 EKDDDHNghIDFITAASNLRAKNYSIEPADRFKTKFIAGKIIPAIATSTATVSGLVCLELIKVTDGgyKFEVYKNCFLN 885
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 13-161 2.41e-39

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: 144.89  E-value: 2.41e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649   13 EAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAY 92
Cdd:COG0476  23 EKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGRPKVEAAAERLRALNPDVEVEAI 102

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649   93 HDSImNPDyNV-EFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTECYEC 161
Cdd:COG0476 103 PERL-TEE-NAlELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQVTVFIPGDTPCYRC 170
UBA2_C pfam16195
SUMO-activating enzyme subunit 2 C-terminus;
549-635 3.49e-33

SUMO-activating enzyme subunit 2 C-terminus;


Pssm-ID: 465058  Cd Length: 93  Bit Score: 122.33  E-value: 3.49e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649    549 DAPEKVGPKQA-EDAAKSITNGSDDGAQPSTST--AQEQDDVLIVDSDEEDSSNNADVSEEERSRKRKLD-EKENLSAKR 624
Cdd:pfam16195   1 DAPEKAPPKQAnPEEVNSIANGNKDSAQPSTSTkaAPEQDDVLIVDSDEEGPSSSADVATEGSGRKRKLDaDTEEASTKR 80

                          90
                  ....*....|.
gi 4885649    625 SRIEQKEELDD 635
Cdd:pfam16195  81 SRTEQSAADDD 91
UAE_UbL pfam14732
Ubiquitin/SUMO-activating enzyme ubiquitin-like domain; This is the C-terminal domain of ...
 452-538 2.59e-31

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: 116.91  E-value: 2.59e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649    452 VRLNVHKVTVLTLQDKIVKEKFAMVAPDVQIEDGKGTILISSEEGETEA-NNHKKLSEFGIRNGSRLQADDFLQDYTLLI 530
Cdd:pfam14732   1 LKVDTEKATLGDLVEDVLKKKLGMVAPDVSLSGGGTILYLSSEEDETEDdNLPKKLSELGIKNGSILTVDDFLQDFEVNL 80


                  ....*...
gi 4885649    531 NILHSEDL 538
Cdd:pfam14732  81 VILHREEL 88
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 13-161 8.93e-25

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 103.39  E-value: 8.93e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649    13 EAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAy 92
Cdd:PRK05690  28 EKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIGQPKVESARAALARINPHIAIET- 106

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4885649    93 HDSIMNPDYNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIeSGTAGYL-GQVTTIKKGVTE-CYEC 161
Cdd:PRK05690 107 INARLDDDELAALIAGHDLVLDCTDNVATRNQLNRACFAAKKPLV-SGAAIRMeGQVTVFTYQDDEpCYRC 176
UBA_E1_SCCH pfam10585
Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ...
 179-362 4.09e-05

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: 45.68  E-value: 4.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649    179 PSEPIHCIVWAKYLFNQLFGE--EDADQEVSPdradPEAAWEPTEAEararASNEDGDI----------KRISTKE---- 242
Cdd:pfam10585   1 PNAIEHTIQWARDEFEGLFVQppEEVNKYLQP----PQNFIESLLKQ----GGGQKLETlesvrkslvtERPKTFEdcva 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649    243 WAkstgydpVKLFTKLFKDDIRYLLT---MDKL-------WR--KRkPPVPLDW------------------AEVQSQGE 292
Cdd:pfam10585  73 WA-------RLKFEKLFNNDIKQLLYnfpPDHKtssgapfWSgpKR-PPTPLEFdpnnplhldfvvaaanlrAQVYGIPG 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649    293 ETNASDQQN----------EPQLGLK----DQQVLDVKSYARLFSKSIETLRVHLAEKGDGAE---------LIWDKDDP 349
Cdd:pfam10585 145 SRDREAIAKvlskvkvpefKPKSGVKiqvnDEEAADPNAESEDDEDELDELLEELPKLAVSPSslagfrlnpIEFEKDDD 224

                         250
                  ....*....|....*
gi 4885649    350 SA--MDFVTSAANLR 362
Cdd:pfam10585 225 TNfhIDFITAASNLR 239
 
Name Accession Description Interval E-value
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 19-444 0e+00

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


Pssm-ID: 238766 [Multi-domain]  Cd Length: 312  Bit Score: 615.93  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649   19 RVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAYHDSIMN 98
Cdd:cd01489   1 KVLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649   99 PDYNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTECYECHPKPTQRTFPGCTIRNT 178
Cdd:cd01489  81 PDFNVEFFKQFDLVFNALDNLAARRHVNKMCLAADVPLIESGTTGFLGQVQVIKKGKTECYECQPKETPKTFPVCTIRST 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649  179 PSEPIHCIVWAKYLFNqlfgeedadqevspdradpeaawepteaeararasnedgdikristkewakstgydpvkLFTKL 258
Cdd:cd01489 161 PSQPIHCIVWAKSLFF-----------------------------------------------------------LFNKV 181

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649  259 FKDDIRYLLTMDKLWRKRKPPVPLDWaevqsqgeetnasdqqnepqlglkdqqvldvksyarlfsksietlrvhlaekgd 338
Cdd:cd01489 182 FKDDIERLLSMEELWKTRKPPVPLSW------------------------------------------------------ 207

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649  339 gAELIWDKDDPSAMDFVTSAANLRMHIFSMNMKSRFDIKSMAGNIIPAIATTNAVIAGLIVLEGLKILSGKIDQCRTIFL 418
Cdd:cd01489 208 -KELTFDKDDQDALDFVAAAANLRSHVFGIPMKSRFDIKQMAGNIIPAIATTNAIIAGLIVLEALKVLSGDKEQCRTVFL 286

                       410       420
                ....*....|....*....|....*.
gi 4885649  419 NKQPNPRKKLLVPCALDPPNPNCYVC 444
Cdd:cd01489 287 NLQPNRRKRLLVPCKLDPPNPNCYVC 312
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 19-401 1.56e-78

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: 249.03  E-value: 1.56e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649   19 RVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAYHDSIMN 98
Cdd:cd01484   1 KVLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQNKVGP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649   99 P-DYNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTECYECHPKPTQRTFPGCTIRN 177
Cdd:cd01484  81 EqDFNDTFFEQFHIIVNALDNIIARRYVNGMLIFLIVPLIESGTEGFKGNAQVILPGMTECIECTLYPPQKNFPMCTIAS 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649  178 TPSEPIHCIVWAKYLFnqlfgeedadqevspdradpeaawepteaeararasnedgdikristkewakstgydpvklftk 257
Cdd:cd01484 161 MPRLPEHCIEWARMLQ---------------------------------------------------------------- 176

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649  258 lfkddirylltmdklwrkrkppvpldwaevqsqgeetnasdqqnepqlglkdqqvldvksyarlfsksietlrvhlaekg 337
Cdd:cd01484     --------------------------------------------------------------------------------

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4885649  338 dgaeliwdKDDPSAMDFVTSAANLRMHIFSMNMKSRFDIKSMAGNIIPAIATTNAVIAGLIVLE 401
Cdd:cd01484 177 --------WDDPEHIQFIFQASNERASQYNIRGVTYFLTKGVAGRIIPAVATTNAVVAGVCALE 232
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 19-419 6.83e-71

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: 236.03  E-value: 6.83e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649   19 RVLVVGAGGIGCELLKNLVLTGFS-----HIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAYH 93
Cdd:cd01490   1 KVFLVGAGAIGCELLKNFALMGVGtgesgEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITALQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649   94 DSiMNPD----YNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTECYECHPKPTQRT 169
Cdd:cd01490  81 NR-VGPEtehiFNDEFWEKLDGVANALDNVDARMYVDRRCVYYRKPLLESGTLGTKGNTQVVIPHLTESYSSSRDPPEKS 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649  170 FPGCTIRNTPSEPIHCIVWAKYLFNQLFgeedadqevspdRADPEAA----WEPTEAEARArasnedgdikristkewak 245
Cdd:cd01490 160 IPLCTLKNFPNAIEHTIQWARDEFEGLF------------KQPPENVnqylFEDCVRWARL------------------- 208

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649  246 stgydpvkLFTKLFKDDIRYLLT---MDKL-------WR--KRkPPVPLdwaevqsqgeetnasdqqnepQLGLKDQQVL 313
Cdd:cd01490 209 --------LFEKYFNNNIKQLLHnfpPDAVtsdgapfWSgpKR-CPTPL---------------------EFDVNNPLHL 258

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649  314 D-VKSYARLFSKS--IEtlrvhlaekgdgaelIWDKDDPSA--MDFVTSAANLRMHIFSMNMKSRFDIKSMAGNIIPAIA 388
Cdd:cd01490 259 DfVLAAANLYAEVygIP---------------GFEKDDDTNfhMDFITAASNLRARNYSIPPADRHKTKRIAGKIIPAIA 323

                       410       420       430
                ....*....|....*....|....*....|...
gi 4885649  389 TTNAVIAGLIVLEGLKILSGK--IDQCRTIFLN 419
Cdd:cd01490 324 TTTAAVTGLVCLELYKVVDGKrpLEAYKNAFLN 356
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 3-178 1.09e-66

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: 218.28  E-value: 1.09e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649      3 LSRGLPRELAEAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQ 82
Cdd:pfam00899   6 ALPLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAAERLRE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649     83 FYPKANIVAYHDSIMNPDyNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTECYECH 162
Cdd:pfam00899  86 INPDVEVEAYTERLTPEN-AEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVVIPGKTPCYRCL 164

                         170
                  ....*....|....*...
gi 4885649    163 P--KPTQRTFPGCTIRNT 178
Cdd:pfam00899 165 FpeDPPPKLVPSCTVAGV 182
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 19-408 4.48e-62

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: 207.98  E-value: 4.48e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649   19 RVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAYHDSIMn 98
Cdd:cd01488   1 KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQ- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649   99 pDYNVEFFRQFILVMNALDNRAARNHVN----RMCLAAD----VPLIESGTAGYLGQVTTIKKGVTECYECHPK--PTQR 168
Cdd:cd01488  80 -DKDEEFYRQFNIIICGLDSIEARRWINgtlvSLLLYEDpesiIPLIDGGTEGFKGHARVILPGITACIECSLDlfPPQV 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649  169 TFPGCTIRNTPSEPIHCIVWAKYLfnqlfgeedadqevspdradpeaawepteaeararasnedgdikristkewakstg 248
Cdd:cd01488 159 TFPLCTIANTPRLPEHCIEYASLI-------------------------------------------------------- 182

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649  249 ydpvklftklfkddirylltmdkLWRKRKPPVPLdwaevqsqgeetnasdqqnepqlglkdqqvldvksyarlfsksiet 328
Cdd:cd01488 183 -----------------------QWPKEFPFVPL---------------------------------------------- 193

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649  329 lrvhlaekgdgaeliwDKDDPSAMDFVTSAANLRMHIFSMNMKSRFDIKSMAGNIIPAIATTNAVIAGLIVLEGLKILSG 408
Cdd:cd01488 194 ----------------DGDDPEHIEWLYQKALERAAQFNISGVTYSLTQGVVKRIIPAVASTNAIIAAACCLEALKIATD 257
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 10-419 1.72e-56

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: 206.66  E-value: 1.72e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649      10 ELAEAVAGGRVLVVGAGGIGCELLKNLVLTGFS-----HIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFY 84
Cdd:TIGR01408  412 TFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVGtgkkgMITVTDPDLIEKSNLNRQFLFRPHHIGKPKSYTAADATLKIN 491

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649      85 PKANIVAYHDSImNPD----YNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTECYE 160
Cdd:TIGR01408  492 PQIKIDAHQNRV-GPEtetiFNDEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGTLGTKGNTQVVVPHLTESYG 570

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649     161 CHPKPTQRTFPGCTIRNTPSEPIHCIVWAKYLFNQLFGEEDAdqEVSPDRADPEAAWEPTEAEARARASNEDGDIKRIST 240
Cdd:TIGR01408  571 SSRDPPEKEIPFCTLKSFPAAIEHTIQWARDKFEGLFSHKPS--LVNKYLSSPSSAEEVLQKIQSGHSREGLEQIIKLLS 648

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649     241 KE----WAKSTGYDPVKlFTKLFKDDIRYLL----------TMDKLWRK-RKPPVPLDW------------------AEV 287
Cdd:TIGR01408  649 KEkprnFSQCVEWARLK-FEKYFNNKALQLLhcfpldirtsTGSPFWSSpKRPPSPLKFdlneplhlsfiqaaaklyATV 727

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649     288 QS--QGEETNASD-----------QQNEPQLGLKDQ--------QVLDVKSYARLFS--KSIETLRvHLAEKGDGAELIW 344
Cdd:TIGR01408  728 YGipFAEEDLSADallnilsevkiPEFKPRSNKKIQtdetarkpDTAPIDDRNAIFQleKAILSNE-ATKSDFRMAPLSF 806

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4885649     345 DKDDPSA--MDFVTSAANLRMHIFSMNMKSRFDIKSMAGNIIPAIATTNAVIAGLIVLEGLKILSG--KIDQCRTIFLN 419
Cdd:TIGR01408  807 EKDDDHNghIDFITAASNLRAKNYSIEPADRFKTKFIAGKIIPAIATSTATVSGLVCLELIKVTDGgyKFEVYKNCFLN 885
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 13-161 2.41e-39

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: 144.89  E-value: 2.41e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649   13 EAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAY 92
Cdd:COG0476  23 EKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGRPKVEAAAERLRALNPDVEVEAI 102

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649   93 HDSImNPDyNV-EFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTECYEC 161
Cdd:COG0476 103 PERL-TEE-NAlELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQVTVFIPGDTPCYRC 170
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 19-173 4.88e-38

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: 140.69  E-value: 4.88e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649   19 RVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAYHDSImN 98
Cdd:cd00757  23 RVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAAAERLRAINPDVEIEAYNERL-D 101

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4885649   99 PDYNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTECYEC-HPKPTQRTFPGC 173
Cdd:cd00757 102 AENAEELIAGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLGFEGQVTVFIPGEGPCYRClFPEPPPPGVPSC 177
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 19-151 2.70e-36

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


Pssm-ID: 238760 [Multi-domain]  Cd Length: 143  Bit Score: 132.78  E-value: 2.70e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649   19 RVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAYHDSIMN 98
Cdd:cd01483   1 RVLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEGISE 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 4885649   99 PDYNvEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTI 151
Cdd:cd01483  81 DNLD-DFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQVI 132
UBA2_C pfam16195
SUMO-activating enzyme subunit 2 C-terminus;
549-635 3.49e-33

SUMO-activating enzyme subunit 2 C-terminus;


Pssm-ID: 465058  Cd Length: 93  Bit Score: 122.33  E-value: 3.49e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649    549 DAPEKVGPKQA-EDAAKSITNGSDDGAQPSTST--AQEQDDVLIVDSDEEDSSNNADVSEEERSRKRKLD-EKENLSAKR 624
Cdd:pfam16195   1 DAPEKAPPKQAnPEEVNSIANGNKDSAQPSTSTkaAPEQDDVLIVDSDEEGPSSSADVATEGSGRKRKLDaDTEEASTKR 80

                          90
                  ....*....|.
gi 4885649    625 SRIEQKEELDD 635
Cdd:pfam16195  81 SRTEQSAADDD 91
UAE_UbL pfam14732
Ubiquitin/SUMO-activating enzyme ubiquitin-like domain; This is the C-terminal domain of ...
 452-538 2.59e-31

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: 116.91  E-value: 2.59e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649    452 VRLNVHKVTVLTLQDKIVKEKFAMVAPDVQIEDGKGTILISSEEGETEA-NNHKKLSEFGIRNGSRLQADDFLQDYTLLI 530
Cdd:pfam14732   1 LKVDTEKATLGDLVEDVLKKKLGMVAPDVSLSGGGTILYLSSEEDETEDdNLPKKLSELGIKNGSILTVDDFLQDFEVNL 80


                  ....*...
gi 4885649    531 NILHSEDL 538
Cdd:pfam14732  81 VILHREEL 88
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 13-161 8.93e-25

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 103.39  E-value: 8.93e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649    13 EAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAy 92
Cdd:PRK05690  28 EKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIGQPKVESARAALARINPHIAIET- 106

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4885649    93 HDSIMNPDYNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIeSGTAGYL-GQVTTIKKGVTE-CYEC 161
Cdd:PRK05690 107 INARLDDDELAALIAGHDLVLDCTDNVATRNQLNRACFAAKKPLV-SGAAIRMeGQVTVFTYQDDEpCYRC 176
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 10-173 5.63e-21

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 95.33  E-value: 5.63e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649    10 ELAEAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANI 89
Cdd:PRK05600  34 EQQERLHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDVGRPKVEVAAERLKEIQPDIRV 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649    90 VAYHDSImNPDYNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTEC----YECHP-K 164
Cdd:PRK05600 114 NALRERL-TAENAVELLNGVDLVLDGSDSFATKFLVADAAEITGTPLVWGTVLRFHGELAVFNSGPDHRgvglRDLFPeQ 192


                 ....*....
gi 4885649   165 PTQRTFPGC 173
Cdd:PRK05600 193 PSGDSIPDC 201
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 19-165 1.06e-20

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 94.77  E-value: 1.06e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649    19 RVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVaYHDSIMN 98
Cdd:PRK07878  44 RVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRQVIHGQSDVGRSKAQSARDSIVEINPLVNVR-LHEFRLD 122

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4885649    99 PDYNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTI----KKGVTECYEC-HPKP 165
Cdd:PRK07878 123 PSNAVELFSQYDLILDGTDNFATRYLVNDAAVLAGKPYVWGSIYRFEGQASVFwedaPDGLGLNYRDlYPEP 194
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
9-174 6.27e-20

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 92.00  E-value: 6.27e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649     9 RELAEAvaggRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKAN 88
Cdd:PRK08762 131 RRLLEA----RVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVGQPKVDSAAQRLAALNPDVQ 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649    89 IVAyHDSIMNPDyNVE-FFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTE----CYEC-H 162
Cdd:PRK08762 207 VEA-VQERVTSD-NVEaLLQDVDVVVDGADNFPTRYLLNDACVKLGKPLVYGAVFRFEGQVSVFDAGRQRgqapCYRClF 284

                        170
                 ....*....|...
gi 4885649   163 PKPTQRTF-PGCT 174
Cdd:PRK08762 285 PEPPPPELaPSCA 297
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 10-143 6.64e-19

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: 86.12  E-value: 6.64e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649   10 ELAEAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANI 89
Cdd:cd00755   4 EGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPECEV 83

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 4885649   90 VAYHDSImNPDyNVE--FFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAG 143
Cdd:cd00755  84 DAVEEFL-TPD-NSEdlLGGDPDFVVDAIDSIRAKVALIAYCRKRKIPVISSMGAG 137
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 19-143 8.42e-19

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: 86.29  E-value: 8.42e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649   19 RVLVVGAGGIG---CEllkNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAYHDS 95
Cdd:COG1179  26 HVAVVGLGGVGswaAE---ALARSGVGRLTLVDLDDVCESNINRQLHALDSTVGRPKVEVMAERIRDINPDCEVTAIDEF 102

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 4885649   96 ImNPDyNVE--FFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAG 143
Cdd:COG1179 103 V-TPE-NADelLSEDYDYVIDAIDSVSAKAALIAWCRRRGIPIISSMGAG 150
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 19-148 1.78e-18

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: 83.88  E-value: 1.78e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649   19 RVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAyhDSIMN 98
Cdd:cd01492  23 RILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEASLERLRALNPRVKVSV--DTDDI 100

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 4885649   99 PDYNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQV 148
Cdd:cd01492 101 SEKPEEFFSQFDVVVATELSRAELVKINELCRKLGVKFYATGVHGLFGFV 150
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
2-144 3.00e-17

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 80.67  E-value: 3.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649     2 ALSRGLPRELAEAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFqKKHVGRSKAQVAKESVL 81
Cdd:PRK08644  13 MLASRHTPKLLEKLKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVVEPSNLNRQQYF-ISQIGMPKVEALKENLL 91

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4885649    82 QFYPKANIVAyHDSIMNPDyNV-EFFRQFILVMNALDN--------RAARNHVNRMCLAAdvplieSGTAGY 144
Cdd:PRK08644  92 EINPFVEIEA-HNEKIDED-NIeELFKDCDIVVEAFDNaetkamlvETVLEHPGKKLVAA------SGMAGY 155
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 13-151 2.22e-15

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: 75.15  E-value: 2.22e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649   13 EAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHV--GRSKAQVAKESVLQFYPKANIV 90
Cdd:cd01485  15 NKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFLDAEVSnsGMNRAAASYEFLQELNPNVKLS 94

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4885649   91 AYHDSIMNPDYNV-EFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTI 151
Cdd:cd01485  95 IVEEDSLSNDSNIeEYLQKFTLVIATEENYERTAKVNDVCRKHHIPFISCATYGLIGYAFFD 156
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 13-174 1.17e-14

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 75.68  E-value: 1.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649    13 EAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAY 92
Cdd:PRK05597  24 QSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVGQPKAESAREAMLALNPDVKVTVS 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649    93 HDSiMNPDYNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTECYE-CHPK-PTQRTF 170
Cdd:PRK05597 104 VRR-LTWSNALDELRDADVILDGSDNFDTRHLASWAAARLGIPHVWASILGFDAQLSVFHAGHGPIYEdLFPTpPPPGSV 182


                 ....
gi 4885649   171 PGCT 174
Cdd:PRK05597 183 PSCS 186
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 16-148 1.45e-14

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 74.07  E-value: 1.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649    16 AGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAYHDS 95
Cdd:PRK15116  29 ADAHICVVGIGGVGSWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMAERIRQINPECRVTVVDDF 108

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 4885649    96 ImNPDYNVEFFRQ-FILVMNALDNRAARNHVNRMCLAADVPLIESGTAGylGQV 148
Cdd:PRK15116 109 I-TPDNVAEYMSAgFSYVIDAIDSVRPKAALIAYCRRNKIPLVTTGGAG--GQI 159
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 19-144 5.44e-14

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: 70.49  E-value: 5.44e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649   19 RVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQkKHVGRSKAQVAKESVLQFYPKANIVAyHDSIMN 98
Cdd:cd01487   1 KVGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQYFL-SQIGEPKVEALKENLREINPFVKIEA-INIKID 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 4885649   99 PDYNVEFFRQFILVMNALDN--------RAARNHVNRMCLAAdvplieSGTAGY 144
Cdd:cd01487  79 ENNLEGLFGDCDIVVEAFDNaetkamlaESLLGNKNKPVVCA------SGMAGF 126
PRK08328 PRK08328
hypothetical protein; Provisional
 10-171 1.13e-11

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 64.82  E-value: 1.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649    10 ELAEAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGR-SKAQVAKESVLQFYPKAN 88
Cdd:PRK08328  20 EGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEDLGKnPKPLSAKWKLERFNSDIK 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649    89 IVAYHDSIMNPDYNvEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTECY-ECHPKPTQ 167
Cdd:PRK08328 100 IETFVGRLSEENID-EVLKGVDVIVDCLDNFETRYLLDDYAHKKGIPLVHGAVEGTYGQVTTIVPGKTKRLrEIFPKVKK 178


                 ....*.
gi 4885649   168 RT--FP 171
Cdd:PRK08328 179 KKgkFP 184
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
18-165 1.25e-11

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 66.68  E-value: 1.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649    18 GRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAYhDSIM 97
Cdd:PRK07411  39 ASVLCIGTGGLGSPLLLYLAAAGIGRIGIVDFDVVDSSNLQRQVIHGTSWVGKPKIESAKNRILEINPYCQVDLY-ETRL 117

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4885649    98 NPDYNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTECYEC-HPKP 165
Cdd:PRK07411 118 SSENALDILAPYDVVVDGTDNFPTRYLVNDACVLLNKPNVYGSIFRFEGQATVFNYEGGPNYRDlYPEP 186
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 16-148 1.84e-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: 1.84e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649   16 AGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAYHDS 95
Cdd:cd01491  18 QKSNVLISGLGGLGVEIAKNLILAGVKSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAEASQARLAELNPYVPVTVSTGP 97

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 4885649   96 ImnpdyNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQV 148
Cdd:cd01491  98 L-----TTDELLKFQVVVLTDASLEDQLKINEFCHSPGIKFISADTRGLFGSI 145
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 13-167 4.63e-11

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: 65.40  E-value: 4.63e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649   13 EAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKaniVAY 92
Cdd:cd01493  16 AALESAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAEATCELLQELNPD---VNG 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649   93 HDSIMNP----DYNVEFFRQFILVMNaldnrAARNHVNRMCLA-----ADVPLIESGTAGYLGQVTTIKK--GVTecyEC 161
Cdd:cd01493  93 SAVEESPeallDNDPSFFSQFTVVIA-----TNLPESTLLRLAdvlwsANIPLLYVRSYGLYGYIRIQLKehTIV---ES 164


                ....*.
gi 4885649  162 HPKPTQ 167
Cdd:cd01493 165 HPDNAL 170
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 13-161 6.94e-11

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 63.98  E-value: 6.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649    13 EAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLF------QKKhvgrSKAQVAKESVLQFYPK 86
Cdd:PRK12475  20 RKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYteedakQKK----PKAIAAKEHLRKINSE 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4885649    87 ANIVAYhdsIMnpDYNVEFFRQFI----LVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTECYEC 161
Cdd:PRK12475  96 VEIVPV---VT--DVTVEELEELVkevdLIIDATDNFDTRLLINDLSQKYNIPWIYGGCVGSYGVTYTIIPGKTPCLRC 169
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 13-161 4.72e-09

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 58.47  E-value: 4.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649    13 EAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQ----KKHVgrSKAqVAKESVLQfypKAN 88
Cdd:PRK07688  20 QKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTesdvKNNL--PKA-VAAKKRLE---EIN 93

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4885649    89 -IVAYHDSIMnpDYNVEFFRQFI----LVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTECYEC 161
Cdd:PRK07688  94 sDVRVEAIVQ--DVTAEELEELVtgvdLIIDATDNFETRFIVNDAAQKYGIPWIYGACVGSYGLSYTIIPGKTPCLRC 169
PRK14851 PRK14851
hypothetical protein; Provisional
 2-144 2.91e-08

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 56.79  E-value: 2.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649     2 ALSR--GL--PRElAEAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAK 77
Cdd:PRK14851  25 AFSRniGLftPGE-QERLAEAKVAIPGMGGVGGVHLITMVRTGIGRFHIADFDQFEPVNVNRQFGARVPSFGRPKLAVMK 103

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4885649    78 ESVLQFYPKANIVAYHDSImNPDYNVEFFRQFILVMNALDNRA--ARNHVNRMCLAADVPLIESGTAGY 144
Cdd:PRK14851 104 EQALSINPFLEITPFPAGI-NADNMDAFLDGVDVVLDGLDFFQfeIRRTLFNMAREKGIPVITAGPLGY 171
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
 19-103 6.80e-08

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: 54.69  E-value: 6.80e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649   19 RVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHV--GRSKAQVAKESVLQFYPKANIVAYHDSI 96
Cdd:cd01486   1 KCLLLGAGTLGCNVARNLLGWGVRHITFVDSGKVSYSNPVRQSLFTFEDCkgGKPKAEAAAERLKEIFPSIDATGIVLSI 80


                ....*..
gi 4885649   97 MNPDYNV 103
Cdd:cd01486  81 PMPGHPI 87
PRK14852 PRK14852
hypothetical protein; Provisional
 19-144 3.30e-07

hypothetical protein; Provisional


Pssm-ID: 184854 [Multi-domain]  Cd Length: 989  Bit Score: 53.55  E-value: 3.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649    19 RVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAYHDSIMN 98
Cdd:PRK14852 334 RVAIAGLGGVGGIHLMTLARTGIGNFNLADFDAYSPVNLNRQYGASIASFGRGKLDVMTERALSVNPFLDIRSFPEGVAA 413

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 4885649    99 PDYNVeFFRQFILVMNALDNRA--ARNHVNRMCLAADVPLIESGTAGY 144
Cdd:PRK14852 414 ETIDA-FLKDVDLLVDGIDFFAldIRRRLFNRALELGIPVITAGPLGY 460
PRK08223 PRK08223
hypothetical protein; Validated
 17-151 2.41e-06

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 49.68  E-value: 2.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649    17 GGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAYHDSI 96
Cdd:PRK08223  27 NSRVAIAGLGGVGGIHLLTLARLGIGKFTIADFDVFELRNFNRQAGAMMSTLGRPKAEVLAEMVRDINPELEIRAFPEGI 106

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 4885649    97 mnPDYNVEFFRQFI-LVMNALDNRA--ARNHVNRMCLAADVPLIesgTAGYLGQVTTI 151
Cdd:PRK08223 107 --GKENADAFLDGVdVYVDGLDFFEfdARRLVFAACQQRGIPAL---TAAPLGMGTAL 159
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 7-113 4.44e-06

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


Pssm-ID: 273603 [Multi-domain]  Cd Length: 1006  Bit Score: 49.89  E-value: 4.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649       7 LPRELAEAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPk 86
Cdd:TIGR01408   14 LGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRAEAVVKKLAELNP- 92

                           90       100
                   ....*....|....*....|....*..
gi 4885649      87 anivAYHDSIMNPDYNVEFFRQFILVM 113
Cdd:TIGR01408   93 ----YVHVSSSSVPFNEEFLDKFQCVV 115
E1_like_apg7 TIGR01381
E1-like protein-activating enzyme Gsa7p/Apg7p; This model represents a family of eukaryotic ...
 5-132 1.64e-05

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


Pssm-ID: 273590 [Multi-domain]  Cd Length: 664  Bit Score: 48.01  E-value: 1.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649      5 RGLPRELAEAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHV---GRSKAQVAKESVL 81
Cdd:TIGR01381 326 RLHPDLQLERYSQLKVLLLGAGTLGCNVARCLIGWGVRHITFVDNGKVSYSNPVRQSLSNFEDCllgGRGKAETAQKALK 405

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4885649     82 QFYPKANIVAYHDSIMNP--------------DYN--VEFFRQFILVMNALDNRAAR-------NHVNRMCLAA 132
Cdd:TIGR01381 406 RIFPSIQATGHRLTVPMPghpidekdvpelekDIArlEQLIKDHDVVFLLLDSREARwlptvlcSRHKKIAISA 479
UBA_E1_SCCH pfam10585
Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ...
 179-362 4.09e-05

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: 45.68  E-value: 4.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649    179 PSEPIHCIVWAKYLFNQLFGE--EDADQEVSPdradPEAAWEPTEAEararASNEDGDI----------KRISTKE---- 242
Cdd:pfam10585   1 PNAIEHTIQWARDEFEGLFVQppEEVNKYLQP----PQNFIESLLKQ----GGGQKLETlesvrkslvtERPKTFEdcva 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649    243 WAkstgydpVKLFTKLFKDDIRYLLT---MDKL-------WR--KRkPPVPLDW------------------AEVQSQGE 292
Cdd:pfam10585  73 WA-------RLKFEKLFNNDIKQLLYnfpPDHKtssgapfWSgpKR-PPTPLEFdpnnplhldfvvaaanlrAQVYGIPG 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885649    293 ETNASDQQN----------EPQLGLK----DQQVLDVKSYARLFSKSIETLRVHLAEKGDGAE---------LIWDKDDP 349
Cdd:pfam10585 145 SRDREAIAKvlskvkvpefKPKSGVKiqvnDEEAADPNAESEDDEDELDELLEELPKLAVSPSslagfrlnpIEFEKDDD 224

                         250
                  ....*....|....*
gi 4885649    350 SA--MDFVTSAANLR 362
Cdd:pfam10585 225 TNfhIDFITAASNLR 239
 
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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