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Conserved domains on  [gi|190358874|sp|Q7SXG4|]
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RecName: Full=SUMO-activating enzyme subunit 2; AltName: Full=Ubiquitin-like 1-activating enzyme E1B; AltName: Full=Ubiquitin-like modifier-activating enzyme 2

Protein Classification

Uba2_SUMO and UAE_UbL domain-containing protein( domain architecture ID 10845027)

protein containing domains Uba2_SUMO, UBA_e1_thiolCys, and UAE_UbL

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 ...
 20-449 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: 607.07  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  20 RVLVVGAGGIGCELLKNLVLTGFKNIEVIDLDTIDVSNLNRQFLFQKKHVGKSKAQVAKESVLRFCPSANITAYHDSIMN 99
Cdd:cd01489    1 KVLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874 100 PDYNVEFFRNFQLVMNALDNRAARNHVNRMCLAADIPLIESGTAGYLGQVTVIKKGQTECYECQPKPTQKTFPGCTIRNT 179
Cdd:cd01489   81 PDFNVEFFKQFDLVFNALDNLAARRHVNKMCLAADVPLIESGTTGFLGQVQVIKKGKTECYECQPKETPKTFPVCTIRST 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874 180 PSEPIHCIVWAKYLFNqlfgeedadqevspdtadpeaawnpadaaaratasdqdgdikrvstkewarstgydpikLFNKV 259
Cdd:cd01489  161 PSQPIHCIVWAKSLFF-----------------------------------------------------------LFNKV 181

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874 260 salsqtspylFKDDIMYLLTMDKLWKKRKAPLPLEWeeinqlgsqeqvigsglkdqqvlgvqgyaqlfqhsvetlrsqlk 339
Cdd:cd01489  182 ----------FKDDIERLLSMEELWKTRKPPVPLSW-------------------------------------------- 207

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874 340 ekgdgAELVWDKDDPPAMDFVTAASNLRMNVFSMNMKSRFDVKSMAGNIIPAIATTNAVIAGLIVLEALKILNSDFEQCR 419
Cdd:cd01489  208 -----KELTFDKDDQDALDFVAAAANLRSHVFGIPMKSRFDIKQMAGNIIPAIATTNAIIAGLIVLEALKVLSGDKEQCR 282

                        410       420       430
                 ....*....|....*....|....*....|
gi 190358874 420 TIFLNKQPNPRKKLLVPCALDPPNASCYVC 449
Cdd:cd01489  283 TVFLNLQPNRRKRLLVPCKLDPPNPNCYVC 312
UAE_UbL pfam14732
Ubiquitin/SUMO-activating enzyme ubiquitin-like domain; This is the C-terminal domain of ...
 457-543 5.14e-30

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: 113.44  E-value: 5.14e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  457 VKLNVHKTMVQALQDKILKEKFGMVAPDVQIEDGKGTILISSEEGETEA-NNNKFLSDFGIRNGSRLQADDFLQDYTLLV 535
Cdd:pfam14732   1 LKVDTEKATLGDLVEDVLKKKLGMVAPDVSLSGGGTILYLSSEEDETEDdNLPKKLSELGIKNGSILTVDDFLQDFEVNL 80


                  ....*...
gi 190358874  536 NVIHSEEL 543
Cdd:pfam14732  81 VILHREEL 88
UBA2_C super family cl24692
SUMO-activating enzyme subunit 2 C-terminus;
554-637 1.34e-25

SUMO-activating enzyme subunit 2 C-terminus;


The actual alignment was detected with superfamily member pfam16195:

Pssm-ID: 465058  Cd Length: 93  Bit Score: 101.14  E-value: 1.34e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  554 DAPDKAPAPSA-PEEGKNIANGNKDSAQPSTSSKAAVEDDDVLLVDSDEEPSSSTMD--TESSNRKRKhHDAETDDASSK 630
Cdd:pfam16195   1 DAPEKAPPKQAnPEEVNSIANGNKDSAQPSTSTKAAPEQDDVLIVDSDEEGPSSSADvaTEGSGRKRK-LDADTEEASTK 79


                  ....*..
gi 190358874  631 RKRLDQQ 637
Cdd:pfam16195  80 RSRTEQS 86
 
Name Accession Description Interval E-value
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 20-449 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: 607.07  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  20 RVLVVGAGGIGCELLKNLVLTGFKNIEVIDLDTIDVSNLNRQFLFQKKHVGKSKAQVAKESVLRFCPSANITAYHDSIMN 99
Cdd:cd01489    1 KVLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874 100 PDYNVEFFRNFQLVMNALDNRAARNHVNRMCLAADIPLIESGTAGYLGQVTVIKKGQTECYECQPKPTQKTFPGCTIRNT 179
Cdd:cd01489   81 PDFNVEFFKQFDLVFNALDNLAARRHVNKMCLAADVPLIESGTTGFLGQVQVIKKGKTECYECQPKETPKTFPVCTIRST 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874 180 PSEPIHCIVWAKYLFNqlfgeedadqevspdtadpeaawnpadaaaratasdqdgdikrvstkewarstgydpikLFNKV 259
Cdd:cd01489  161 PSQPIHCIVWAKSLFF-----------------------------------------------------------LFNKV 181

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874 260 salsqtspylFKDDIMYLLTMDKLWKKRKAPLPLEWeeinqlgsqeqvigsglkdqqvlgvqgyaqlfqhsvetlrsqlk 339
Cdd:cd01489  182 ----------FKDDIERLLSMEELWKTRKPPVPLSW-------------------------------------------- 207

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874 340 ekgdgAELVWDKDDPPAMDFVTAASNLRMNVFSMNMKSRFDVKSMAGNIIPAIATTNAVIAGLIVLEALKILNSDFEQCR 419
Cdd:cd01489  208 -----KELTFDKDDQDALDFVAAAANLRSHVFGIPMKSRFDIKQMAGNIIPAIATTNAIIAGLIVLEALKVLSGDKEQCR 282

                        410       420       430
                 ....*....|....*....|....*....|
gi 190358874 420 TIFLNKQPNPRKKLLVPCALDPPNASCYVC 449
Cdd:cd01489  283 TVFLNLQPNRRKRLLVPCKLDPPNPNCYVC 312
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 16-179 8.42e-69

ThiF family; This domain is found in ubiquitin activating E1 family and members of the bacterial ThiF/MoeB/HesA family. It is repeated in Ubiquitin-activating enzyme E1.


Pssm-ID: 459987 [Multi-domain]  Cd Length: 238  Bit Score: 224.06  E-value: 8.42e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874   16 LSSCRVLVVGAGGIGCELLKNLVLTGFKNIEVIDLDTIDVSNLNRQFLFQKKHVGKSKAQVAKESVLRFCPSANITAYHD 95
Cdd:pfam00899  18 LRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAAERLREINPDVEVEAYTE 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874   96 SIMNPDyNVEFFRNFQLVMNALDNRAARNHVNRMCLAADIPLIESGTAGYLGQVTVIKKGQTECYEC--QPKPTQKTFPG 173
Cdd:pfam00899  98 RLTPEN-AEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVVIPGKTPCYRClfPEDPPPKLVPS 176


                  ....*.
gi 190358874  174 CTIRNT 179
Cdd:pfam00899 177 CTVAGV 182
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 11-424 1.07e-53

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: 198.57  E-value: 1.07e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874    11 QLADSLSSCRVLVVGAGGIGCELLKNLVLTGFK-----NIEVIDLDTIDVSNLNRQFLFQKKHVGKSKAQVAKESVLRFC 85
Cdd:TIGR01408  412 TFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVGtgkkgMITVTDPDLIEKSNLNRQFLFRPHHIGKPKSYTAADATLKIN 491

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874    86 PSANITAYHDSImNPD----YNVEFFRNFQLVMNALDNRAARNHVNRMCLAADIPLIESGTAGYLGQVTVIKKGQTECYE 161
Cdd:TIGR01408  492 PQIKIDAHQNRV-GPEtetiFNDEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGTLGTKGNTQVVVPHLTESYG 570

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874   162 CQPKPTQKTFPGCTIRNTPSEPIHCIVWAKYLFNQLFGEEDAdqEVSPDTADPEAAWNPADAAARATASDQDGDIKRVST 241
Cdd:TIGR01408  571 SSRDPPEKEIPFCTLKSFPAAIEHTIQWARDKFEGLFSHKPS--LVNKYLSSPSSAEEVLQKIQSGHSREGLEQIIKLLS 648

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874   242 KE----------WARsTGYDpiKLF-NKVSALSqtspYLFKDDIMyLLTMDKLWKK-RKAPLPL---------------- 293
Cdd:TIGR01408  649 KEkprnfsqcveWAR-LKFE--KYFnNKALQLL----HCFPLDIR-TSTGSPFWSSpKRPPSPLkfdlneplhlsfiqaa 720

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874   294 -------------EW--------EEINQLGSQEQVIGSGLKDQ--------QVLGVQGYAQLFQ-----HSVETLRSQLK 339
Cdd:TIGR01408  721 aklyatvygipfaEEdlsadallNILSEVKIPEFKPRSNKKIQtdetarkpDTAPIDDRNAIFQlekaiLSNEATKSDFR 800

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874   340 EKgdGAELVWDKDDPPAMDFVTAASNLRMNVFSMNMKSRFDVKSMAGNIIPAIATTNAVIAGLIVLEALKILNSD--FEQ 417
Cdd:TIGR01408  801 MA--PLSFEKDDDHNGHIDFITAASNLRAKNYSIEPADRFKTKFIAGKIIPAIATSTATVSGLVCLELIKVTDGGykFEV 878


                   ....*..
gi 190358874   418 CRTIFLN 424
Cdd:TIGR01408  879 YKNCFLN 885
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 16-162 1.45e-42

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: 153.75  E-value: 1.45e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  16 LSSCRVLVVGAGGIGCELLKNLVLTGFKNIEVIDLDTIDVSNLNRQFLFQKKHVGKSKAQVAKESVLRFCPSANITAYHD 95
Cdd:COG0476   25 LKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGRPKVEAAAERLRALNPDVEVEAIPE 104

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 190358874  96 SImNPDyNV-EFFRNFQLVMNALDNRAARNHVNRMCLAADIPLIESGTAGYLGQVTVIKKGQTECYEC 162
Cdd:COG0476  105 RL-TEE-NAlELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQVTVFIPGDTPCYRC 170
UAE_UbL pfam14732
Ubiquitin/SUMO-activating enzyme ubiquitin-like domain; This is the C-terminal domain of ...
 457-543 5.14e-30

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: 113.44  E-value: 5.14e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  457 VKLNVHKTMVQALQDKILKEKFGMVAPDVQIEDGKGTILISSEEGETEA-NNNKFLSDFGIRNGSRLQADDFLQDYTLLV 535
Cdd:pfam14732   1 LKVDTEKATLGDLVEDVLKKKLGMVAPDVSLSGGGTILYLSSEEDETEDdNLPKKLSELGIKNGSILTVDDFLQDFEVNL 80


                  ....*...
gi 190358874  536 NVIHSEEL 543
Cdd:pfam14732  81 VILHREEL 88
UBA2_C pfam16195
SUMO-activating enzyme subunit 2 C-terminus;
554-637 1.34e-25

SUMO-activating enzyme subunit 2 C-terminus;


Pssm-ID: 465058  Cd Length: 93  Bit Score: 101.14  E-value: 1.34e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  554 DAPDKAPAPSA-PEEGKNIANGNKDSAQPSTSSKAAVEDDDVLLVDSDEEPSSSTMD--TESSNRKRKhHDAETDDASSK 630
Cdd:pfam16195   1 DAPEKAPPKQAnPEEVNSIANGNKDSAQPSTSTKAAPEQDDVLIVDSDEEGPSSSADvaTEGSGRKRK-LDADTEEASTK 79


                  ....*..
gi 190358874  631 RKRLDQQ 637
Cdd:pfam16195  80 RSRTEQS 86
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 16-162 9.25e-25

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 103.39  E-value: 9.25e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  16 LSSCRVLVVGAGGIGCELLKNLVLTGFKNIEVIDLDTIDVSNLNRQFLFQKKHVGKSKAQVAKESVLRFCPSANITAyHD 95
Cdd:PRK05690  30 LKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIGQPKVESARAALARINPHIAIET-IN 108

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 190358874  96 SIMNPDYNVEFFRNFQLVMNALDNRAARNHVNRMCLAADIPLIeSGTAGYL-GQVTVIKKGQTE-CYEC 162
Cdd:PRK05690 109 ARLDDDELAALIAGHDLVLDCTDNVATRNQLNRACFAAKKPLV-SGAAIRMeGQVTVFTYQDDEpCYRC 176
 
Name Accession Description Interval E-value
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 20-449 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: 607.07  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  20 RVLVVGAGGIGCELLKNLVLTGFKNIEVIDLDTIDVSNLNRQFLFQKKHVGKSKAQVAKESVLRFCPSANITAYHDSIMN 99
Cdd:cd01489    1 KVLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874 100 PDYNVEFFRNFQLVMNALDNRAARNHVNRMCLAADIPLIESGTAGYLGQVTVIKKGQTECYECQPKPTQKTFPGCTIRNT 179
Cdd:cd01489   81 PDFNVEFFKQFDLVFNALDNLAARRHVNKMCLAADVPLIESGTTGFLGQVQVIKKGKTECYECQPKETPKTFPVCTIRST 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874 180 PSEPIHCIVWAKYLFNqlfgeedadqevspdtadpeaawnpadaaaratasdqdgdikrvstkewarstgydpikLFNKV 259
Cdd:cd01489  161 PSQPIHCIVWAKSLFF-----------------------------------------------------------LFNKV 181

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874 260 salsqtspylFKDDIMYLLTMDKLWKKRKAPLPLEWeeinqlgsqeqvigsglkdqqvlgvqgyaqlfqhsvetlrsqlk 339
Cdd:cd01489  182 ----------FKDDIERLLSMEELWKTRKPPVPLSW-------------------------------------------- 207

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874 340 ekgdgAELVWDKDDPPAMDFVTAASNLRMNVFSMNMKSRFDVKSMAGNIIPAIATTNAVIAGLIVLEALKILNSDFEQCR 419
Cdd:cd01489  208 -----KELTFDKDDQDALDFVAAAANLRSHVFGIPMKSRFDIKQMAGNIIPAIATTNAIIAGLIVLEALKVLSGDKEQCR 282

                        410       420       430
                 ....*....|....*....|....*....|
gi 190358874 420 TIFLNKQPNPRKKLLVPCALDPPNASCYVC 449
Cdd:cd01489  283 TVFLNLQPNRRKRLLVPCKLDPPNPNCYVC 312
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 20-408 4.13e-77

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: 245.57  E-value: 4.13e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  20 RVLVVGAGGIGCELLKNLVLTGFKNIEVIDLDTIDVSNLNRQFLFQKKHVGKSKAQVAKESVLRFCPSANITAYHDSIMN 99
Cdd:cd01484    1 KVLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQNKVGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874 100 P-DYNVEFFRNFQLVMNALDNRAARNHVNRMCLAADIPLIESGTAGYLGQVTVIKKGQTECYECQPKPTQKTFPGCTIRN 178
Cdd:cd01484   81 EqDFNDTFFEQFHIIVNALDNIIARRYVNGMLIFLIVPLIESGTEGFKGNAQVILPGMTECIECTLYPPQKNFPMCTIAS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874 179 TPSEPIHCIVWAKYLFnqlfgeedadqevspdtadpeaawnpadaaaratasdqdgdikrvstkewarstgydpiklfnk 258
Cdd:cd01484  161 MPRLPEHCIEWARMLQ---------------------------------------------------------------- 176

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874 259 vsalsqtspylfkddimylltmdklwkkrkaplpleweeinqlgsqeqvigsglkdqqvlgvqgyaqlfqhsvetlrsql 338
Cdd:cd01484      --------------------------------------------------------------------------------

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874 339 kekgdgaelvwdKDDPPAMDFVTAASNLRMNVFSMNMKSRFDVKSMAGNIIPAIATTNAVIAGLIVLEAL 408
Cdd:cd01484  177 ------------WDDPEHIQFIFQASNERASQYNIRGVTYFLTKGVAGRIIPAVATTNAVVAGVCALEVF 234
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 20-424 6.00e-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: 233.72  E-value: 6.00e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  20 RVLVVGAGGIGCELLKNLVLTGFKN-----IEVIDLDTIDVSNLNRQFLFQKKHVGKSKAQVAKESVLRFCPSANITAYH 94
Cdd:cd01490    1 KVFLVGAGAIGCELLKNFALMGVGTgesgeITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITALQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  95 DSiMNPD----YNVEFFRNFQLVMNALDNRAARNHVNRMCLAADIPLIESGTAGYLGQVTVIKKGQTECYECQPKPTQKT 170
Cdd:cd01490   81 NR-VGPEtehiFNDEFWEKLDGVANALDNVDARMYVDRRCVYYRKPLLESGTLGTKGNTQVVIPHLTESYSSSRDPPEKS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874 171 FPGCTIRNTPSEPIHCIVWAKYLFNQLF--GEEDADQEVSPDTAdpeaawnpadaaaratasdqdgdikrvstkEWARSt 248
Cdd:cd01490  160 IPLCTLKNFPNAIEHTIQWARDEFEGLFkqPPENVNQYLFEDCV------------------------------RWARL- 208

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874 249 gydpikLFNKvsalsqtspyLFKDDIMYLLT---MDKL-------WK--KRkAPLPLEWeEINQLGSQEQVIGSGLKDQQ 316
Cdd:cd01490  209 ------LFEK----------YFNNNIKQLLHnfpPDAVtsdgapfWSgpKR-CPTPLEF-DVNNPLHLDFVLAAANLYAE 270

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874 317 VLGVQGYaqlfqhsvetlrsqlkEKGDgaelvwdkDDPPAMDFVTAASNLRMNVFSMNMKSRFDVKSMAGNIIPAIATTN 396
Cdd:cd01490  271 VYGIPGF----------------EKDD--------DTNFHMDFITAASNLRARNYSIPPADRHKTKRIAGKIIPAIATTT 326

                        410       420       430
                 ....*....|....*....|....*....|
gi 190358874 397 AVIAGLIVLEALKIL--NSDFEQCRTIFLN 424
Cdd:cd01490  327 AAVTGLVCLELYKVVdgKRPLEAYKNAFLN 356
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 16-179 8.42e-69

ThiF family; This domain is found in ubiquitin activating E1 family and members of the bacterial ThiF/MoeB/HesA family. It is repeated in Ubiquitin-activating enzyme E1.


Pssm-ID: 459987 [Multi-domain]  Cd Length: 238  Bit Score: 224.06  E-value: 8.42e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874   16 LSSCRVLVVGAGGIGCELLKNLVLTGFKNIEVIDLDTIDVSNLNRQFLFQKKHVGKSKAQVAKESVLRFCPSANITAYHD 95
Cdd:pfam00899  18 LRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAAERLREINPDVEVEAYTE 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874   96 SIMNPDyNVEFFRNFQLVMNALDNRAARNHVNRMCLAADIPLIESGTAGYLGQVTVIKKGQTECYEC--QPKPTQKTFPG 173
Cdd:pfam00899  98 RLTPEN-AEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVVIPGKTPCYRClfPEDPPPKLVPS 176


                  ....*.
gi 190358874  174 CTIRNT 179
Cdd:pfam00899 177 CTVAGV 182
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 20-413 8.35e-65

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: 215.30  E-value: 8.35e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  20 RVLVVGAGGIGCELLKNLVLTGFKNIEVIDLDTIDVSNLNRQFLFQKKHVGKSKAQVAKESVLRFCPSANITAYHDSIMn 99
Cdd:cd01488    1 KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQ- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874 100 pDYNVEFFRNFQLVMNALDNRAARNHVN----RMCLAAD----IPLIESGTAGYLGQVTVIKKGQTECYECQPK--PTQK 169
Cdd:cd01488   80 -DKDEEFYRQFNIIICGLDSIEARRWINgtlvSLLLYEDpesiIPLIDGGTEGFKGHARVILPGITACIECSLDlfPPQV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874 170 TFPGCTIRNTPSEPIHCIVWAKYLfnqlfgeedadqevspdtadpeaawnpadaaaratasdqdgdikrvstkEWARstg 249
Cdd:cd01488  159 TFPLCTIANTPRLPEHCIEYASLI-------------------------------------------------QWPK--- 186

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874 250 ydpiklfnkvsalsqtspylfkddimylltmdklwKKRKAPLpleweeinqlgsqeqvigsglkdqqvlgvqgyaqlfqh 329
Cdd:cd01488  187 -----------------------------------EFPFVPL-------------------------------------- 193

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874 330 svetlrsqlkekgdgaelvwDKDDPPAMDFVTAASNLRMNVFSMNMKSRFDVKSMAGNIIPAIATTNAVIAGLIVLEALK 409
Cdd:cd01488  194 --------------------DGDDPEHIEWLYQKALERAAQFNISGVTYSLTQGVVKRIIPAVASTNAIIAAACCLEALK 253


                 ....
gi 190358874 410 ILNS 413
Cdd:cd01488  254 IATD 257
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 11-424 1.07e-53

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: 198.57  E-value: 1.07e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874    11 QLADSLSSCRVLVVGAGGIGCELLKNLVLTGFK-----NIEVIDLDTIDVSNLNRQFLFQKKHVGKSKAQVAKESVLRFC 85
Cdd:TIGR01408  412 TFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVGtgkkgMITVTDPDLIEKSNLNRQFLFRPHHIGKPKSYTAADATLKIN 491

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874    86 PSANITAYHDSImNPD----YNVEFFRNFQLVMNALDNRAARNHVNRMCLAADIPLIESGTAGYLGQVTVIKKGQTECYE 161
Cdd:TIGR01408  492 PQIKIDAHQNRV-GPEtetiFNDEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGTLGTKGNTQVVVPHLTESYG 570

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874   162 CQPKPTQKTFPGCTIRNTPSEPIHCIVWAKYLFNQLFGEEDAdqEVSPDTADPEAAWNPADAAARATASDQDGDIKRVST 241
Cdd:TIGR01408  571 SSRDPPEKEIPFCTLKSFPAAIEHTIQWARDKFEGLFSHKPS--LVNKYLSSPSSAEEVLQKIQSGHSREGLEQIIKLLS 648

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874   242 KE----------WARsTGYDpiKLF-NKVSALSqtspYLFKDDIMyLLTMDKLWKK-RKAPLPL---------------- 293
Cdd:TIGR01408  649 KEkprnfsqcveWAR-LKFE--KYFnNKALQLL----HCFPLDIR-TSTGSPFWSSpKRPPSPLkfdlneplhlsfiqaa 720

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874   294 -------------EW--------EEINQLGSQEQVIGSGLKDQ--------QVLGVQGYAQLFQ-----HSVETLRSQLK 339
Cdd:TIGR01408  721 aklyatvygipfaEEdlsadallNILSEVKIPEFKPRSNKKIQtdetarkpDTAPIDDRNAIFQlekaiLSNEATKSDFR 800

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874   340 EKgdGAELVWDKDDPPAMDFVTAASNLRMNVFSMNMKSRFDVKSMAGNIIPAIATTNAVIAGLIVLEALKILNSD--FEQ 417
Cdd:TIGR01408  801 MA--PLSFEKDDDHNGHIDFITAASNLRAKNYSIEPADRFKTKFIAGKIIPAIATSTATVSGLVCLELIKVTDGGykFEV 878


                   ....*..
gi 190358874   418 CRTIFLN 424
Cdd:TIGR01408  879 YKNCFLN 885
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 16-162 1.45e-42

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: 153.75  E-value: 1.45e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  16 LSSCRVLVVGAGGIGCELLKNLVLTGFKNIEVIDLDTIDVSNLNRQFLFQKKHVGKSKAQVAKESVLRFCPSANITAYHD 95
Cdd:COG0476   25 LKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGRPKVEAAAERLRALNPDVEVEAIPE 104

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 190358874  96 SImNPDyNV-EFFRNFQLVMNALDNRAARNHVNRMCLAADIPLIESGTAGYLGQVTVIKKGQTECYEC 162
Cdd:COG0476  105 RL-TEE-NAlELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQVTVFIPGDTPCYRC 170
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 20-152 2.78e-39

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: 141.25  E-value: 2.78e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  20 RVLVVGAGGIGCELLKNLVLTGFKNIEVIDLDTIDVSNLNRQFLFQKKHVGKSKAQVAKESVLRFCPSANITAYHDSIMN 99
Cdd:cd01483    1 RVLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEGISE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 190358874 100 PDYNvEFFRNFQLVMNALDNRAARNHVNRMCLAADIPLIESGTAGYLGQVTVI 152
Cdd:cd01483   81 DNLD-DFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQVI 132
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 16-174 3.07e-39

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: 144.16  E-value: 3.07e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  16 LSSCRVLVVGAGGIGCELLKNLVLTGFKNIEVIDLDTIDVSNLNRQFLFQKKHVGKSKAQVAKESVLRFCPSANITAYHD 95
Cdd:cd00757   19 LKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAAAERLRAINPDVEIEAYNE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  96 SImNPDYNVEFFRNFQLVMNALDNRAARNHVNRMCLAADIPLIESGTAGYLGQVTVIKKGQTECYECQ-PKPTQKTFPGC 174
Cdd:cd00757   99 RL-DAENAEELIAGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLGFEGQVTVFIPGEGPCYRCLfPEPPPPGVPSC 177
UAE_UbL pfam14732
Ubiquitin/SUMO-activating enzyme ubiquitin-like domain; This is the C-terminal domain of ...
 457-543 5.14e-30

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: 113.44  E-value: 5.14e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  457 VKLNVHKTMVQALQDKILKEKFGMVAPDVQIEDGKGTILISSEEGETEA-NNNKFLSDFGIRNGSRLQADDFLQDYTLLV 535
Cdd:pfam14732   1 LKVDTEKATLGDLVEDVLKKKLGMVAPDVSLSGGGTILYLSSEEDETEDdNLPKKLSELGIKNGSILTVDDFLQDFEVNL 80


                  ....*...
gi 190358874  536 NVIHSEEL 543
Cdd:pfam14732  81 VILHREEL 88
UBA2_C pfam16195
SUMO-activating enzyme subunit 2 C-terminus;
554-637 1.34e-25

SUMO-activating enzyme subunit 2 C-terminus;


Pssm-ID: 465058  Cd Length: 93  Bit Score: 101.14  E-value: 1.34e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  554 DAPDKAPAPSA-PEEGKNIANGNKDSAQPSTSSKAAVEDDDVLLVDSDEEPSSSTMD--TESSNRKRKhHDAETDDASSK 630
Cdd:pfam16195   1 DAPEKAPPKQAnPEEVNSIANGNKDSAQPSTSTKAAPEQDDVLIVDSDEEGPSSSADvaTEGSGRKRK-LDADTEEASTK 79


                  ....*..
gi 190358874  631 RKRLDQQ 637
Cdd:pfam16195  80 RSRTEQS 86
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 16-162 9.25e-25

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 103.39  E-value: 9.25e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  16 LSSCRVLVVGAGGIGCELLKNLVLTGFKNIEVIDLDTIDVSNLNRQFLFQKKHVGKSKAQVAKESVLRFCPSANITAyHD 95
Cdd:PRK05690  30 LKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIGQPKVESARAALARINPHIAIET-IN 108

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 190358874  96 SIMNPDYNVEFFRNFQLVMNALDNRAARNHVNRMCLAADIPLIeSGTAGYL-GQVTVIKKGQTE-CYEC 162
Cdd:PRK05690 109 ARLDDDELAALIAGHDLVLDCTDNVATRNQLNRACFAAKKPLV-SGAAIRMeGQVTVFTYQDDEpCYRC 176
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 16-174 4.51e-21

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 95.33  E-value: 4.51e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  16 LSSCRVLVVGAGGIGCELLKNLVLTGFKNIEVIDLDTIDVSNLNRQFLFQKKHVGKSKAQVAKESVLRFCPSANITAYHD 95
Cdd:PRK05600  39 LHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDVGRPKVEVAAERLKEIQPDIRVNALRE 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  96 SImNPDYNVEFFRNFQLVMNALDNRAARNHVNRMCLAADIPLIESGTAGYLGQVTVIKKGQTEC----YECQP-KPTQKT 170
Cdd:PRK05600 119 RL-TAENAVELLNGVDLVLDGSDSFATKFLVADAAEITGTPLVWGTVLRFHGELAVFNSGPDHRgvglRDLFPeQPSGDS 197


                 ....
gi 190358874 171 FPGC 174
Cdd:PRK05600 198 IPDC 201
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 16-166 7.52e-21

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 95.16  E-value: 7.52e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  16 LSSCRVLVVGAGGIGCELLKNLVLTGFKNIEVIDLDTIDVSNLNRQFLFQKKHVGKSKAQVAKESVLRFCPSANITaYHD 95
Cdd:PRK07878  40 LKNARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRQVIHGQSDVGRSKAQSARDSIVEINPLVNVR-LHE 118

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 190358874  96 SIMNPDYNVEFFRNFQLVMNALDNRAARNHVNRMCLAADIPLIESGTAGYLGQVTVI----KKGQTECYEC-QPKP 166
Cdd:PRK07878 119 FRLDPSNAVELFSQYDLILDGTDNFATRYLVNDAAVLAGKPYVWGSIYRFEGQASVFwedaPDGLGLNYRDlYPEP 194
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 16-144 6.03e-20

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: 89.20  E-value: 6.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  16 LSSCRVLVVGAGGIGCELLKNLVLTGFKNIEVIDLDTIDVSNLNRQFLFQKKHVGKSKAQVAKESVLRFCPSANITAYHD 95
Cdd:cd00755    9 LRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPECEVDAVEE 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 190358874  96 SImNPDyNVE--FFRNFQLVMNALDNRAARNHVNRMCLAADIPLIESGTAG 144
Cdd:cd00755   89 FL-TPD-NSEdlLGGDPDFVVDAIDSIRAKVALIAYCRKRKIPVISSMGAG 137
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
16-175 2.83e-19

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 90.07  E-value: 2.83e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  16 LSSCRVLVVGAGGIGCELLKNLVLTGFKNIEVIDLDTIDVSNLNRQFLFQKKHVGKSKAQVAKESVLRFCPSANITAyHD 95
Cdd:PRK08762 133 LLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVGQPKVDSAAQRLAALNPDVQVEA-VQ 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  96 SIMNPDyNVE-FFRNFQLVMNALDNRAARNHVNRMCLAADIPLIESGTAGYLGQVTVIK----KGQTECYEC---QPKPT 167
Cdd:PRK08762 212 ERVTSD-NVEaLLQDVDVVVDGADNFPTRYLLNDACVKLGKPLVYGAVFRFEGQVSVFDagrqRGQAPCYRClfpEPPPP 290


                 ....*...
gi 190358874 168 QKTfPGCT 175
Cdd:PRK08762 291 ELA-PSCA 297
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 16-144 6.00e-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: 86.67  E-value: 6.00e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  16 LSSCRVLVVGAGGIG---CEllkNLVLTGFKNIEVIDLDTIDVSNLNRQFLFQKKHVGKSKAQVAKESVLRFCPSANITA 92
Cdd:COG1179   22 LANAHVAVVGLGGVGswaAE---ALARSGVGRLTLVDLDDVCESNINRQLHALDSTVGRPKVEVMAERIRDINPDCEVTA 98

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 190358874  93 YHDSImNPDyNVE--FFRNFQLVMNALDNRAARNHVNRMCLAADIPLIESGTAG 144
Cdd:COG1179   99 IDEFV-TPE-NADelLSEDYDYVIDAIDSVSAKAALIAWCRRRGIPIISSMGAG 150
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 16-149 6.70e-19

Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating enzyme (E1), specific for the SUMO family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. The E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by SUMO family of ubiquitin-like proteins (Ublps) is involved in cell division, nuclear transport, the stress response and signal transduction. Aos1 contains part of the adenylation domain.


Pssm-ID: 238769 [Multi-domain]  Cd Length: 197  Bit Score: 85.03  E-value: 6.70e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  16 LSSCRVLVVGAGGIGCELLKNLVLTGFKNIEVIDLDTIDVSNLNRQFLFQKKHVGKSKAQVAKESVLRFCPSANITAyhD 95
Cdd:cd01492   19 LRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEASLERLRALNPRVKVSV--D 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 190358874  96 SIMNPDYNVEFFRNFQLVMNALDNRAARNHVNRMCLAADIPLIESGTAGYLGQV 149
Cdd:cd01492   97 TDDISEKPEEFFSQFDVVVATELSRAELVKINELCRKLGVKFYATGVHGLFGFV 150
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
14-145 1.36e-18

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 84.91  E-value: 1.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  14 DSLSSCRVLVVGAGGIGCELLKNLVLTGFKNIEVIDLDTIDVSNLNRQFLFqKKHVGKSKAQVAKESVLRFCPSANITAy 93
Cdd:PRK08644  24 EKLKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVVEPSNLNRQQYF-ISQIGMPKVEALKENLLEINPFVEIEA- 101

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 190358874  94 HDSIMNPDyNV-EFFRNFQLVMNALDN--------RAARNHVNRMCLAAdiplieSGTAGY 145
Cdd:PRK08644 102 HNEKIDED-NIeELFKDCDIVVEAFDNaetkamlvETVLEHPGKKLVAA------SGMAGY 155
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 16-149 9.64e-17

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: 79.00  E-value: 9.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  16 LSSCRVLVVGAGGIGCELLKNLVLTGFKNIEVIDLDTIDVSNLNRQFLFQKKHV--GKSKAQVAKESVLRFCPSANITAY 93
Cdd:cd01485   17 LRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFLDAEVSnsGMNRAAASYEFLQELNPNVKLSIV 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 190358874  94 HDSIMNPDYNV-EFFRNFQLVMNALDNRAARNHVNRMCLAADIPLIESGTAGYLGQV 149
Cdd:cd01485   97 EEDSLSNDSNIeEYLQKFTLVIATEENYERTAKVNDVCRKHHIPFISCATYGLIGYA 153
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 3-175 1.10e-15

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 79.15  E-value: 1.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874   3 ELVGPLRKQLADSLSSCRVLVVGAGGIGCELLKNLVLTGFKNIEVIDLDTIDVSNLNRQFLFQKKHVGKSKAQVAKESVL 82
Cdd:PRK05597  13 IMLGEIGQQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVGQPKAESAREAML 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  83 RFCPSANITAYHDSiMNPDYNVEFFRNFQLVMNALDNRAARNHVNRMCLAADIPLIESGTAGYLGQVTVIKKGQTECYE- 161
Cdd:PRK05597  93 ALNPDVKVTVSVRR-LTWSNALDELRDADVILDGSDNFDTRHLASWAAARLGIPHVWASILGFDAQLSVFHAGHGPIYEd 171

                        170
                 ....*....|....*.
gi 190358874 162 --CQPkPTQKTFPGCT 175
Cdd:PRK05597 172 lfPTP-PPPGSVPSCS 186
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 21-149 4.50e-14

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 72.91  E-value: 4.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  21 VLVVGAGGIGCELLKNLVLTGFKNIEVIDLDTIDVSNLNRQFLFQKKHVGKSKAQVAKESVLRFCPSANITAYHDSImNP 100
Cdd:PRK15116  33 ICVVGIGGVGSWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMAERIRQINPECRVTVVDDFI-TP 111

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 190358874 101 DYNVEFF-RNFQLVMNALDNRAARNHVNRMCLAADIPLIESGTAGylGQV 149
Cdd:PRK15116 112 DNVAEYMsAGFSYVIDAIDSVRPKAALIAYCRRNKIPLVTTGGAG--GQI 159
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 20-145 5.93e-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: 70.10  E-value: 5.93e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  20 RVLVVGAGGIGCELLKNLVLTGFKNIEVIDLDTIDVSNLNRQFLFQkKHVGKSKAQVAKESVLRFCPSANITAyHDSIMN 99
Cdd:cd01487    1 KVGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQYFL-SQIGEPKVEALKENLREINPFVKIEA-INIKID 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 190358874 100 PDYNVEFFRNFQLVMNALDN--------RAARNHVNRMCLAAdiplieSGTAGY 145
Cdd:cd01487   79 ENNLEGLFGDCDIVVEAFDNaetkamlaESLLGNKNKPVVCA------SGMAGF 126
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
16-166 9.34e-14

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 73.62  E-value: 9.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  16 LSSCRVLVVGAGGIGCELLKNLVLTGFKNIEVIDLDTIDVSNLNRQFLFQKKHVGKSKAQVAKESVLRFCPSANITAYhD 95
Cdd:PRK07411  36 LKAASVLCIGTGGLGSPLLLYLAAAGIGRIGIVDFDVVDSSNLQRQVIHGTSWVGKPKIESAKNRILEINPYCQVDLY-E 114

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 190358874  96 SIMNPDYNVEFFRNFQLVMNALDNRAARNHVNRMCLAADIPLIESGTAGYLGQVTVIKKGQTECYEC-QPKP 166
Cdd:PRK07411 115 TRLSSENALDILAPYDVVVDGTDNFPTRYLVNDACVLLNKPNVYGSIFRFEGQATVFNYEGGPNYRDlYPEP 186
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 16-149 1.48e-13

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: 71.53  E-value: 1.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  16 LSSCRVLVVGAGGIGCELLKNLVLTGFKNIEVIDLDTIDVSNLNRQFLFQKKHVGKSKAQVAKESVLRFCPSANITAYHD 95
Cdd:cd01491   17 LQKSNVLISGLGGLGVEIAKNLILAGVKSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAEASQARLAELNPYVPVTVSTG 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 190358874  96 SImnpdyNVEFFRNFQLVMNALDNRAARNHVNRMCLAADIPLIESGTAGYLGQV 149
Cdd:cd01491   97 PL-----TTDELLKFQVVVLTDASLEDQLKINEFCHSPGIKFISADTRGLFGSI 145
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 15-154 2.37e-12

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: 69.26  E-value: 2.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  15 SLSSCRVLVVGAGGIGCELLKNLVLTGFKNIEVIDLDTIDVSNLNRQFLFQKKHVGKSKAQVAKESVLRFCPSANITAyh 94
Cdd:cd01493   17 ALESAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAEATCELLQELNPDVNGSA-- 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 190358874  95 dSIMNP----DYNVEFFRNFQLVMNaldnrAARNHVNRMCLA-----ADIPLIESGTAGYLGQVTVIKK 154
Cdd:cd01493   95 -VEESPeallDNDPSFFSQFTVVIA-----TNLPESTLLRLAdvlwsANIPLLYVRSYGLYGYIRIQLK 157
PRK08328 PRK08328
hypothetical protein; Provisional
 14-172 2.97e-12

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 66.74  E-value: 2.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  14 DSLSSCRVLVVGAGGIGCELLKNLVLTGFKNIEVIDLDTIDVSNLNRQFLFQKKHVGK-SKAQVAKESVLRFCPSANITA 92
Cdd:PRK08328  23 EKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEDLGKnPKPLSAKWKLERFNSDIKIET 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  93 YHDSIMNPDYNvEFFRNFQLVMNALDNRAARNHVNRMCLAADIPLIESGTAGYLGQVTVIKKGQTECY-ECQPKPTQKT- 170
Cdd:PRK08328 103 FVGRLSEENID-EVLKGVDVIVDCLDNFETRYLLDDYAHKKGIPLVHGAVEGTYGQVTTIVPGKTKRLrEIFPKVKKKKg 181


                 ...
gi 190358874 171 -FP 172
Cdd:PRK08328 182 kFP 184
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 3-162 2.90e-10

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 62.32  E-value: 2.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874   3 ELVGPLRKQLADSLSSCRVLVVGAGGIGCELLKNLVLTGFKNIEVIDLDTIDVSNLNRQFLFQKKHVGKS--KAQVAKES 80
Cdd:PRK07688   9 ELFSPIGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDVKNNlpKAVAAKKR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  81 VLRFCPSANITAYhdsIMnpDYNVE----FFRNFQLVMNALDNRAARNHVNRMCLAADIPLIESGTAGYLGQVTVIKKGQ 156
Cdd:PRK07688  89 LEEINSDVRVEAI---VQ--DVTAEeleeLVTGVDLIIDATDNFETRFIVNDAAQKYGIPWIYGACVGSYGLSYTIIPGK 163


                 ....*.
gi 190358874 157 TECYEC 162
Cdd:PRK07688 164 TPCLRC 169
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
 20-104 3.69e-10

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: 61.62  E-value: 3.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  20 RVLVVGAGGIGCELLKNLVLTGFKNIEVIDLDTIDVSNLNRQFLFQKKHV--GKSKAQVAKESVLRFCPSANITAYHDSI 97
Cdd:cd01486    1 KCLLLGAGTLGCNVARNLLGWGVRHITFVDSGKVSYSNPVRQSLFTFEDCkgGKPKAEAAAERLKEIFPSIDATGIVLSI 80


                 ....*..
gi 190358874  98 MNPDYNV 104
Cdd:cd01486   81 PMPGHPI 87
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 21-162 4.14e-09

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 58.59  E-value: 4.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  21 VLVVGAGGIGCELLKNLVLTGFKNIEVIDLDTIDVSNLNRQFLFQKKHVG--KSKAQVAKESVLRFCPSANITAY-HDSI 97
Cdd:PRK12475  27 VLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTEEDAKqkKPKAIAAKEHLRKINSEVEIVPVvTDVT 106

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 190358874  98 MNpdyNVE-FFRNFQLVMNALDNRAARNHVNRMCLAADIPLIESGTAGYLGQVTVIKKGQTECYEC 162
Cdd:PRK12475 107 VE---ELEeLVKEVDLIIDATDNFDTRLLINDLSQKYNIPWIYGGCVGSYGVTYTIIPGKTPCLRC 169
PRK14851 PRK14851
hypothetical protein; Provisional
 5-145 1.19e-08

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 58.33  E-value: 1.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874   5 VGPLRKQLADSLSSCRVLVVGAGGIGCELLKNLVLTGFKNIEVIDLDTIDVSNLNRQFLFQKKHVGKSKAQVAKESVLRF 84
Cdd:PRK14851  30 IGLFTPGEQERLAEAKVAIPGMGGVGGVHLITMVRTGIGRFHIADFDQFEPVNVNRQFGARVPSFGRPKLAVMKEQALSI 109

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 190358874  85 CPSANITAYHDSImNPDYNVEFFRNFQLVMNALDNRA--ARNHVNRMCLAADIPLIESGTAGY 145
Cdd:PRK14851 110 NPFLEITPFPAGI-NADNMDAFLDGVDVVLDGLDFFQfeIRRTLFNMAREKGIPVITAGPLGY 171
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 16-114 9.62e-08

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: 55.28  E-value: 9.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874    16 LSSCRVLVVGAGGIGCELLKNLVLTGFKNIEVIDLDTIDVSNLNRQFLFQKKHVGKSKAQVAKESVLRFCPsanitAYHD 95
Cdd:TIGR01408   22 MAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRAEAVVKKLAELNP-----YVHV 96

                           90
                   ....*....|....*....
gi 190358874    96 SIMNPDYNVEFFRNFQLVM 114
Cdd:TIGR01408   97 SSSSVPFNEEFLDKFQCVV 115
PRK08223 PRK08223
hypothetical protein; Validated
 14-147 1.07e-07

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 53.92  E-value: 1.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  14 DSLSSCRVLVVGAGGIGCELLKNLVLTGFKNIEVIDLDTIDVSNLNRQFLFQKKHVGKSKAQVAKESVLRFCPSANITAY 93
Cdd:PRK08223  23 QRLRNSRVAIAGLGGVGGIHLLTLARLGIGKFTIADFDVFELRNFNRQAGAMMSTLGRPKAEVLAEMVRDINPELEIRAF 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 190358874  94 HDSImNPDYNVEFFRNFQLVMNALDNRA--ARNHVNRMCLAADIPLIesgTAGYLG 147
Cdd:PRK08223 103 PEGI-GKENADAFLDGVDVYVDGLDFFEfdARRLVFAACQQRGIPAL---TAAPLG 154
PRK14852 PRK14852
hypothetical protein; Provisional
 20-155 1.27e-07

hypothetical protein; Provisional


Pssm-ID: 184854 [Multi-domain]  Cd Length: 989  Bit Score: 55.09  E-value: 1.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874  20 RVLVVGAGGIGCELLKNLVLTGFKNIEVIDLDTIDVSNLNRQFLFQKKHVGKSKAQVAKESVLRFCPSANITAYHDSIMN 99
Cdd:PRK14852 334 RVAIAGLGGVGGIHLMTLARTGIGNFNLADFDAYSPVNLNRQYGASIASFGRGKLDVMTERALSVNPFLDIRSFPEGVAA 413

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 190358874 100 PDYNVeFFRNFQLVMNALDNRA--ARNHVNRMCLAADIPLIESGTAGYLGQVTVIKKG 155
Cdd:PRK14852 414 ETIDA-FLKDVDLLVDGIDFFAldIRRRLFNRALELGIPVITAGPLGYSCALLVFMPG 470
E1_like_apg7 TIGR01381
E1-like protein-activating enzyme Gsa7p/Apg7p; This model represents a family of eukaryotic ...
 14-135 1.53e-06

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: 51.48  E-value: 1.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358874   14 DSLSSCRVLVVGAGGIGCELLKNLVLTGFKNIEVIDLDTIDVSNLNRQFLFQKKHV---GKSKAQVAKESVLRFCPSANI 90
Cdd:TIGR01381 334 ERYSQLKVLLLGAGTLGCNVARCLIGWGVRHITFVDNGKVSYSNPVRQSLSNFEDCllgGRGKAETAQKALKRIFPSIQA 413

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 190358874   91 TAYHDSIMNP--------------DYN--VEFFRNFQLVMNALDNRAAR-------NHVNRMCLAADI 135
Cdd:TIGR01381 414 TGHRLTVPMPghpidekdvpelekDIArlEQLIKDHDVVFLLLDSREARwlptvlcSRHKKIAISAAL 481
Shikimate_DH pfam01488
Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate ...
 8-48 1.51e-03

Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate dehydrogenases. Shikimate 5-dehydrogenase catalyzes the conversion of shikimate to 5-dehydroshikimate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids. Quinate 5-dehydrogenase catalyzes the conversion of quinate to 5-dehydroquinate. This reaction is part of the quinate pathway where quinic acid is exploited as a source of carbon in prokaryotes and microbial eukaryotes. Both the shikimate and quinate pathways share two common pathway metabolites 3-dehydroquinate and dehydroshikimate.


Pssm-ID: 460229 [Multi-domain]  Cd Length: 136  Bit Score: 39.09  E-value: 1.51e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 190358874    8 LRKQLADSLSSCRVLVVGAGGIGCELLKNLVLTGFKNIEVI 48
Cdd:pfam01488   2 LAKKIFGDLKDKKVLLIGAGEMGELVAKHLLAKGAKEVTIA 42
 
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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