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Conserved domains on  [gi|21450341|ref|NP_659180|]
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NEDD8-activating enzyme E1 regulatory subunit isoform 1 [Mus musculus]

Protein Classification

NEDD8-activating enzyme E1 regulatory subunit( domain architecture ID 10107339)

NEDD8-activating enzyme E1 regulatory subunit is a component of the dimeric UBA3-NAE1 E1 enzyme that activates NEDD8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP

Gene Ontology:  GO:0016567|GO:0045116|GO:0006974|GO:0031625|GO:0004839|GO:0046982|GO:0019781|GO:0006511
SCOP:  4000139|4007684

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 11-532 0e+00

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: 736.81  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341  11 QKYDRQLRLWGDHGQEALESAHVCLINATATGTEILKNLVLPGIGSFTIIDGNLVSGEDAGNNFFLQKSSIGKNRAQAAM 90
Cdd:cd01493   1 QKYDRQLRLWGEHGQAALESAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAEATC 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341  91 EFLQELNSDVSGSFVEESPENLLDNDPSFFCRFTIVVATQLLESTLLRLADVLWNSQIPLLICRTYGLVGYMRIIIKEHP 170
Cdd:cd01493  81 ELLQELNPDVNGSAVEESPEALLDNDPSFFSQFTVVIATNLPESTLLRLADVLWSANIPLLYVRSYGLYGYIRIQLKEHT 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341 171 VIESHPDNALEDLRLDKPFPELREHLQSYDLDHMEKKDHSHTPWIVIIAKYLAQWYNETNGRIPKSYKEKEDFRDLIRQG 250
Cdd:cd01493 161 IVESHPDNALEDLRLDNPFPELREHADSIDLDDMDPAEHSHTPYIVILIKYLEKWRSAHNGQLPSTYKEKKEFRDLVRSL 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341 251 ILKNengapEDEENFEEAIKNVNTALNTTQIPSSIEDIFNDDRCINITKQTPTFWILARALKEFVAKEgQGNLPVRGTIP 330
Cdd:cd01493 241 MRSN-----EDEENFEEAIKAVNKALNRTKIPSSVEEIFNDDRCENLTSQSSSFWIMARALKEFVAEE-NGLLPLPGTLP 314

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341 331 DMIADSNKYIKLQNVYREKAKKDAAAVGNHVAKLLQSVGQAPESISEKELKLLCSNSAFLRVVRCRSLAeeygldtvnkd 410
Cdd:cd01493 315 DMTADTEKYIKLQNIYREKAEKDAAEVEKYVREILKSLGRSPDSISDKEIKLFCKNAAFLRVIRGRSLE----------- 383

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341 411 eiissmdnpdneivlylmlravdrfhkqhgrypgvsnyqveedigklkscltgflqeyglsvmvkddyvhefcrygaaep 490
Cdd:cd01493     --------------------------------------------------------------------------------

                       490       500       510       520
                ....*....|....*....|....*....|....*....|..
gi 21450341 491 HTIAAFLGGAAAQEVIKIITKQFVIFNNTYIYSGMSQTSATF 532
Cdd:cd01493 384 HNISAFMGGIAAQEVIKLITKQYVPIDNTFIFDGIRSKSATF 425
 
Name Accession Description Interval E-value
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 11-532 0e+00

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: 736.81  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341  11 QKYDRQLRLWGDHGQEALESAHVCLINATATGTEILKNLVLPGIGSFTIIDGNLVSGEDAGNNFFLQKSSIGKNRAQAAM 90
Cdd:cd01493   1 QKYDRQLRLWGEHGQAALESAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAEATC 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341  91 EFLQELNSDVSGSFVEESPENLLDNDPSFFCRFTIVVATQLLESTLLRLADVLWNSQIPLLICRTYGLVGYMRIIIKEHP 170
Cdd:cd01493  81 ELLQELNPDVNGSAVEESPEALLDNDPSFFSQFTVVIATNLPESTLLRLADVLWSANIPLLYVRSYGLYGYIRIQLKEHT 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341 171 VIESHPDNALEDLRLDKPFPELREHLQSYDLDHMEKKDHSHTPWIVIIAKYLAQWYNETNGRIPKSYKEKEDFRDLIRQG 250
Cdd:cd01493 161 IVESHPDNALEDLRLDNPFPELREHADSIDLDDMDPAEHSHTPYIVILIKYLEKWRSAHNGQLPSTYKEKKEFRDLVRSL 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341 251 ILKNengapEDEENFEEAIKNVNTALNTTQIPSSIEDIFNDDRCINITKQTPTFWILARALKEFVAKEgQGNLPVRGTIP 330
Cdd:cd01493 241 MRSN-----EDEENFEEAIKAVNKALNRTKIPSSVEEIFNDDRCENLTSQSSSFWIMARALKEFVAEE-NGLLPLPGTLP 314

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341 331 DMIADSNKYIKLQNVYREKAKKDAAAVGNHVAKLLQSVGQAPESISEKELKLLCSNSAFLRVVRCRSLAeeygldtvnkd 410
Cdd:cd01493 315 DMTADTEKYIKLQNIYREKAEKDAAEVEKYVREILKSLGRSPDSISDKEIKLFCKNAAFLRVIRGRSLE----------- 383

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341 411 eiissmdnpdneivlylmlravdrfhkqhgrypgvsnyqveedigklkscltgflqeyglsvmvkddyvhefcrygaaep 490
Cdd:cd01493     --------------------------------------------------------------------------------

                       490       500       510       520
                ....*....|....*....|....*....|....*....|..
gi 21450341 491 HTIAAFLGGAAAQEVIKIITKQFVIFNNTYIYSGMSQTSATF 532
Cdd:cd01493 384 HNISAFMGGIAAQEVIKLITKQYVPIDNTFIFDGIRSKSATF 425
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 13-169 3.32e-19

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: 86.93  E-value: 3.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341    13 YDRQLRL--WGDHGQEALESAHVCLINATATGTEILKNLVLPGIGSFTIIDGNLVSGEDAGNNFFLQKSSIGKNRAQAAM 90
Cdd:pfam00899   1 YSRQLALplIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341    91 EFLQELNSDVSGSFVEE--SPENLLDndpsFFCRFTIVV-ATQLLESTLLrLADVLWNSQIPLLICRTYGLVGYMRIIIK 167
Cdd:pfam00899  81 ERLREINPDVEVEAYTErlTPENAEE----LIKSFDIVVdATDNFAARYL-VNDACVKLGKPLIEAGVLGFKGQVTVVIP 155


                  ..
gi 21450341   168 EH 169
Cdd:pfam00899 156 GK 157
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 10-150 4.44e-16

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: 81.86  E-value: 4.44e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341     10 EQKYDRQLRLWGDHGQEALESAHVCLINATATGTEILKNLVLPGIGSFTIIDGNLVSGEDAGNNFFLQKSSIGKNRAQAA 89
Cdd:TIGR01408    4 EALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRAEAV 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21450341     90 MEFLQELNSDVSGSFVEES-PENLLDNdpsffcrFTIVVATQLLESTLLRLADVLWNSQIPL 150
Cdd:TIGR01408   84 VKKLAELNPYVHVSSSSVPfNEEFLDK-------FQCVVLTEMSLPLQKEINDFCHSQCPPI 138
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 13-160 1.72e-13

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: 70.16  E-value: 1.72e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341  13 YDRQLRL--WGDHGQEALESAHVCLINATATGTEILKNLVLPGIGSFTIIDGNLVsgeDAGNnffLQK------SSIGKN 84
Cdd:COG0476   8 YSRQILLpeIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVV---ELSN---LQRqilyteADVGRP 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341  85 RAQAAMEFLQELNSDVSgsfVEE-----SPENLLDndpsFFCRFTIVV------ATQLLestllrLADVLWNSQIPLL-- 151
Cdd:COG0476  82 KVEAAAERLRALNPDVE---VEAiperlTEENALE----LLAGADLVLdctdnfATRYL------LNDACVKLGIPLVsg 148

                       170
                ....*....|
gi 21450341 152 -ICRTYGLVG 160
Cdd:COG0476 149 aVIGFEGQVT 158
PTZ00245 PTZ00245
ubiquitin activating enzyme; Provisional
 12-101 1.62e-09

ubiquitin activating enzyme; Provisional


Pssm-ID: 140272  Cd Length: 287  Bit Score: 58.92  E-value: 1.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341   12 KYDRQLRLWGDHGQEALESAHVCLINATATGTEILKNLVLPGIGSFTIIDGNLVSGEDAGNNFFLQKSSiGKNRAQAAME 91
Cdd:PTZ00245   8 RYDRQIRLWGKSTQQQLMHTSVALHGVAGAAAEAAKNLVLAGVRAVAVADEGLVTDADVCTNYLMQGEA-GGTRGARALG 86

                         90
                 ....*....|
gi 21450341   92 FLQELNSDVS 101
Cdd:PTZ00245  87 ALQRLNPHVS 96
 
Name Accession Description Interval E-value
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 11-532 0e+00

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: 736.81  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341  11 QKYDRQLRLWGDHGQEALESAHVCLINATATGTEILKNLVLPGIGSFTIIDGNLVSGEDAGNNFFLQKSSIGKNRAQAAM 90
Cdd:cd01493   1 QKYDRQLRLWGEHGQAALESAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAEATC 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341  91 EFLQELNSDVSGSFVEESPENLLDNDPSFFCRFTIVVATQLLESTLLRLADVLWNSQIPLLICRTYGLVGYMRIIIKEHP 170
Cdd:cd01493  81 ELLQELNPDVNGSAVEESPEALLDNDPSFFSQFTVVIATNLPESTLLRLADVLWSANIPLLYVRSYGLYGYIRIQLKEHT 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341 171 VIESHPDNALEDLRLDKPFPELREHLQSYDLDHMEKKDHSHTPWIVIIAKYLAQWYNETNGRIPKSYKEKEDFRDLIRQG 250
Cdd:cd01493 161 IVESHPDNALEDLRLDNPFPELREHADSIDLDDMDPAEHSHTPYIVILIKYLEKWRSAHNGQLPSTYKEKKEFRDLVRSL 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341 251 ILKNengapEDEENFEEAIKNVNTALNTTQIPSSIEDIFNDDRCINITKQTPTFWILARALKEFVAKEgQGNLPVRGTIP 330
Cdd:cd01493 241 MRSN-----EDEENFEEAIKAVNKALNRTKIPSSVEEIFNDDRCENLTSQSSSFWIMARALKEFVAEE-NGLLPLPGTLP 314

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341 331 DMIADSNKYIKLQNVYREKAKKDAAAVGNHVAKLLQSVGQAPESISEKELKLLCSNSAFLRVVRCRSLAeeygldtvnkd 410
Cdd:cd01493 315 DMTADTEKYIKLQNIYREKAEKDAAEVEKYVREILKSLGRSPDSISDKEIKLFCKNAAFLRVIRGRSLE----------- 383

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341 411 eiissmdnpdneivlylmlravdrfhkqhgrypgvsnyqveedigklkscltgflqeyglsvmvkddyvhefcrygaaep 490
Cdd:cd01493     --------------------------------------------------------------------------------

                       490       500       510       520
                ....*....|....*....|....*....|....*....|..
gi 21450341 491 HTIAAFLGGAAAQEVIKIITKQFVIFNNTYIYSGMSQTSATF 532
Cdd:cd01493 384 HNISAFMGGIAAQEVIKLITKQYVPIDNTFIFDGIRSKSATF 425
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 12-166 2.10e-75

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: 236.93  E-value: 2.10e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341  12 KYDRQLRLWGDHGQEALESAHVCLINATATGTEILKNLVLPGIGSFTIIDGNLVSGEDAGNNFFLQK--SSIGKNRAQAA 89
Cdd:cd01485   1 LYDRQIRLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFLDAevSNSGMNRAAAS 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21450341  90 MEFLQELNSDVSGSFVEESPENLLDNDPSFFCRFTIVVATQLLESTLLRLADVLWNSQIPLLICRTYGLVGYMRIII 166
Cdd:cd01485  81 YEFLQELNPNVKLSIVEEDSLSNDSNIEEYLQKFTLVIATEENYERTAKVNDVCRKHHIPFISCATYGLIGYAFFDF 157
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 13-162 3.84e-38

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: 138.58  E-value: 3.84e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341  13 YDRQLRLWGDHGQEALESAHVCLINATATGTEILKNLVLPGIGSFTIIDGNLVSGEDAGNNFFLQKSSIGKNRAQAAMEF 92
Cdd:cd01492   4 YDRQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEASLER 83

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341  93 LQELNSDVSgsfVEESPENLLDNDPSFFCRFTIVVATQLLESTLLRLADVLWNSQIPLLICRTYGLVGYM 162
Cdd:cd01492  84 LRALNPRVK---VSVDTDDISEKPEEFFSQFDVVVATELSRAELVKINELCRKLGVKFYATGVHGLFGFV 150
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 32-166 3.85e-30

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: 115.06  E-value: 3.85e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341  32 HVCLINATATGTEILKNLVLPGIGSFTIIDGNLVSGEDAGNNFFLQKSSIGKNRAQAAMEFLQELNSDVSGSFVEESPEN 111
Cdd:cd01483   1 RVLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEGISE 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21450341 112 llDNDPSFFCRFTIVVATQLLESTLLRLADVLWNSQIPLLICRTYGLVGYMRIII 166
Cdd:cd01483  81 --DNLDDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQVID 133
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 13-161 3.33e-20

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: 90.79  E-value: 3.33e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341  13 YDRQLRLWGDHGQEALESAHVCLINATATGTEILKNLVLPGIGSFTIIDGNLVSGEDAGNNFFLQKSSIGKNRAQAAMEF 92
Cdd:cd01491   2 YSRQLYVLGHEAMKKLQKSNVLISGLGGLGVEIAKNLILAGVKSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAEASQAR 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21450341  93 LQELNSDVSgsfVEESPENLLDNdpsFFCRFTIVVATQLLESTLLRLADVLWNSQIPLLICRTYGLVGY 161
Cdd:cd01491  82 LAELNPYVP---VTVSTGPLTTD---ELLKFQVVVLTDASLEDQLKINEFCHSPGIKFISADTRGLFGS 144
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 13-169 3.32e-19

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: 86.93  E-value: 3.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341    13 YDRQLRL--WGDHGQEALESAHVCLINATATGTEILKNLVLPGIGSFTIIDGNLVSGEDAGNNFFLQKSSIGKNRAQAAM 90
Cdd:pfam00899   1 YSRQLALplIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341    91 EFLQELNSDVSGSFVEE--SPENLLDndpsFFCRFTIVV-ATQLLESTLLrLADVLWNSQIPLLICRTYGLVGYMRIIIK 167
Cdd:pfam00899  81 ERLREINPDVEVEAYTErlTPENAEE----LIKSFDIVVdATDNFAARYL-VNDACVKLGKPLIEAGVLGFKGQVTVVIP 155


                  ..
gi 21450341   168 EH 169
Cdd:pfam00899 156 GK 157
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 10-150 4.44e-16

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: 81.86  E-value: 4.44e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341     10 EQKYDRQLRLWGDHGQEALESAHVCLINATATGTEILKNLVLPGIGSFTIIDGNLVSGEDAGNNFFLQKSSIGKNRAQAA 89
Cdd:TIGR01408    4 EALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRAEAV 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21450341     90 MEFLQELNSDVSGSFVEES-PENLLDNdpsffcrFTIVVATQLLESTLLRLADVLWNSQIPL 150
Cdd:TIGR01408   84 VKKLAELNPYVHVSSSSVPfNEEFLDK-------FQCVVLTEMSLPLQKEINDFCHSQCPPI 138
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 13-160 1.72e-13

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: 70.16  E-value: 1.72e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341  13 YDRQLRL--WGDHGQEALESAHVCLINATATGTEILKNLVLPGIGSFTIIDGNLVsgeDAGNnffLQK------SSIGKN 84
Cdd:COG0476   8 YSRQILLpeIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVV---ELSN---LQRqilyteADVGRP 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341  85 RAQAAMEFLQELNSDVSgsfVEE-----SPENLLDndpsFFCRFTIVV------ATQLLestllrLADVLWNSQIPLL-- 151
Cdd:COG0476  82 KVEAAAERLRALNPDVE---VEAiperlTEENALE----LLAGADLVLdctdnfATRYL------LNDACVKLGIPLVsg 148

                       170
                ....*....|
gi 21450341 152 -ICRTYGLVG 160
Cdd:COG0476 149 aVIGFEGQVT 158
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 492-532 1.18e-12

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: 66.68  E-value: 1.18e-12
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 21450341 492 TIAAFLGGAAAQEVIKIITKQFVIFNNTYIYSGMSQTSATF 532
Cdd:cd01485 158 PIAAFLGGVVAQEAIKSISGKFTPLNNLYIYDGFESTGPMC 198
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 13-159 5.09e-11

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: 62.49  E-value: 5.09e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341  13 YDRQLRL--WGDHGQEALESAHVCLINATATGTEILKNLVLPGIGSFTIIDGNLVsgeDAGNnffLQK------SSIGKN 84
Cdd:cd00757   2 YSRQILLpeIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVV---ELSN---LQRqilhteADVGQP 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341  85 RAQAAMEFLQELNSDVSgsfVEESPENL-LDNDPSFFCRFTIVV-ATQLLESTLLrLADVLWNSQIPLL---ICRTYGLV 159
Cdd:cd00757  76 KAEAAAERLRAINPDVE---IEAYNERLdAENAEELIAGYDLVLdCTDNFATRYL-INDACVKLGKPLVsgaVLGFEGQV 151
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 32-166 2.70e-10

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: 61.60  E-value: 2.70e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341  32 HVCLINATATGTEILKNLVLPGIGSFTIIDGNLVSGEDAGNNFFLQKSSIGKNRAQAAMEFLQELnsdVSGSFVEESPEN 111
Cdd:cd01488   1 KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDR---VPGVNVTPHFGK 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21450341 112 LLDNDPSFFCRFTIVV-------ATQLLESTLLRLADVL-WNSQIPLLICRTYGLVGYMRIII 166
Cdd:cd01488  78 IQDKDEEFYRQFNIIIcgldsieARRWINGTLVSLLLYEdPESIIPLIDGGTEGFKGHARVIL 140
PTZ00245 PTZ00245
ubiquitin activating enzyme; Provisional
 12-101 1.62e-09

ubiquitin activating enzyme; Provisional


Pssm-ID: 140272  Cd Length: 287  Bit Score: 58.92  E-value: 1.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341   12 KYDRQLRLWGDHGQEALESAHVCLINATATGTEILKNLVLPGIGSFTIIDGNLVSGEDAGNNFFLQKSSiGKNRAQAAME 91
Cdd:PTZ00245   8 RYDRQIRLWGKSTQQQLMHTSVALHGVAGAAAEAAKNLVLAGVRAVAVADEGLVTDADVCTNYLMQGEA-GGTRGARALG 86

                         90
                 ....*....|
gi 21450341   92 FLQELNSDVS 101
Cdd:PTZ00245  87 ALQRLNPHVS 96
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 5-114 6.50e-09

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 57.57  E-value: 6.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341    5 GKILKEQKYDRQLRL--WGDHGQEALESAHVCLINATATGTEILKNLVLPGIGSFTIIDGNLVSGEDAGNNFFLQKSSIG 82
Cdd:PRK05597   1 VKNLDIARYRRQIMLgeIGQQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVG 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 21450341   83 KNRAQAAMEFLQELNSD--VSGSFVEESPENLLD 114
Cdd:PRK05597  81 QPKAESAREAMLALNPDvkVTVSVRRLTWSNALD 114
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 33-227 1.71e-08

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: 55.28  E-value: 1.71e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341  33 VCLINATATGTEILKNLVLPGIGSFTIIDGNLVSGEDAGNNFFLQKSSIGKNRAQAAMEFLQEL--NSDVSGSFVEESPE 110
Cdd:cd01484   2 VLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRnpNCKVVPYQNKVGPE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341 111 NLLDNdpSFFCRFTIVVATqlLESTLLR--LADVLWNSQIPLLICRTYGLVGYMRIII---------KEHPVIESHPDNA 179
Cdd:cd01484  82 QDFND--TFFEQFHIIVNA--LDNIIARryVNGMLIFLIVPLIESGTEGFKGNAQVILpgmteciecTLYPPQKNFPMCT 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 21450341 180 LedlrldKPFPELREHLQSYDLDHMEKKDHsHTPWIVIIAKYLAQWYN 227
Cdd:cd01484 158 I------ASMPRLPEHCIEWARMLQWDDPE-HIQFIFQASNERASQYN 198
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 8-179 2.77e-08

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 56.04  E-value: 2.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341    8 LKEQKYDRQLRL--WGDHGQEALESAHVCLINATATGTEILKNLVLPGIGSFTIIDGNLVSGEDAGNNFFLQKSSIGKNR 85
Cdd:PRK05600  17 SELRRTARQLALpgFGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDVGRPK 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341   86 AQAAMEFLQELNSDVSGSFVEE--SPEN----------LLDNDPSFFCRFTI-----VVATQLLESTLLRLAD--VLWNS 146
Cdd:PRK05600  97 VEVAAERLKEIQPDIRVNALRErlTAENavellngvdlVLDGSDSFATKFLVadaaeITGTPLVWGTVLRFHGelAVFNS 176

                        170       180       190
                 ....*....|....*....|....*....|...
gi 21450341  147 QIPLlicRTYGLvgymRIIIKEHPVIESHPDNA 179
Cdd:PRK05600 177 GPDH---RGVGL----RDLFPEQPSGDSIPDCA 202
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 12-112 5.60e-08

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 54.61  E-value: 5.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341   12 KYDRQLRLW--GDHGQEALESAHVCLINATATGTEILKNLVLPGIGSFTIIDGNLV-----------SGEDAGNNffLQK 78
Cdd:PRK07688   4 RYSRQELFSpiGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVewsnlqrqqlyTESDVKNN--LPK 81

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 21450341   79 ssigknrAQAAMEFLQELNSDVS-GSFVEE-SPENL 112
Cdd:PRK07688  82 -------AVAAKKRLEEINSDVRvEAIVQDvTAEEL 110
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 10-100 1.11e-07

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 53.97  E-value: 1.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341   10 EQKYDRQLRL--WGDHGQEALESAHVCLINATATGTEILKNLVLPGIGSFTIIDGNLV-----------SGEDAGNNffl 76
Cdd:PRK12475   2 QERYSRQILFsgIGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVewsnlqrqqlyTEEDAKQK--- 78

                         90       100
                 ....*....|....*....|....
gi 21450341   77 qkssigKNRAQAAMEFLQELNSDV 100
Cdd:PRK12475  79 ------KPKAIAAKEHLRKINSEV 96
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 12-166 3.11e-07

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: 53.35  E-value: 3.11e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341     12 KYDRQLRLWGDHGQEALESAHVCLINATATGTEILKNLVLPGI-----GSFTIIDGNLVSGEDAGNNFFLQKSSIGKNR- 85
Cdd:TIGR01408  401 RYDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVgtgkkGMITVTDPDLIEKSNLNRQFLFRPHHIGKPKs 480

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341     86 ---AQAAMEFLQELNSDVSGSFVEESPENLLDNDpsFFCRFTIVV-ATQLLESTLLRLADVLWNsQIPLLICRTYGLVGY 161
Cdd:TIGR01408  481 ytaADATLKINPQIKIDAHQNRVGPETETIFNDE--FYEKLDVVInALDNVEARRYVDSRCLAF-LKPLLESGTLGTKGN 557


                   ....*
gi 21450341    162 MRIII 166
Cdd:TIGR01408  558 TQVVV 562
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 33-167 5.90e-07

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: 51.23  E-value: 5.90e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341  33 VCLINATATGTEILKNLVLPGIGSFTIIDGNLVSGEDAGNNFFLQKSSIGKNRAQAAMEFLQELNSDVSgsfVEESPENL 112
Cdd:cd01489   2 VLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVK---IVAYHANI 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21450341 113 LDND--PSFFCRFTIVVatqlleSTLLRLADVLW------NSQIPLLICRTYGLVGYMRIIIK 167
Cdd:cd01489  79 KDPDfnVEFFKQFDLVF------NALDNLAARRHvnkmclAADVPLIESGTTGFLGQVQVIKK 135
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
10-114 5.97e-05

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 45.39  E-value: 5.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341   10 EQKYDRQLRL--WGDHGQEALESAHVCLINATATGTEILKNLVLPGIGSFTIIDGNLVsgeDAGNnffLQK------SSI 81
Cdd:PRK08762 113 DERYSRHLRLpeVGEEGQRRLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVV---DRSN---LQRqilhteDRV 186

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 21450341   82 GKNRAQAAMEFLQELNSDVSGSFVEE--SPENLLD 114
Cdd:PRK08762 187 GQPKVDSAAQRLAALNPDVQVEAVQErvTSDNVEA 221
PRK08328 PRK08328
hypothetical protein; Provisional
 11-115 9.04e-05

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 44.02  E-value: 9.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341   11 QKYDRQLRLWGDHGQEALESAHVCLINATATGTEILKNLVLPGIGSFTIIDGNLVSGEDAGNNFFLQKSSIGKN-RAQAA 89
Cdd:PRK08328   8 ERYDRQIMIFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEDLGKNpKPLSA 87

                         90       100       110
                 ....*....|....*....|....*....|.
gi 21450341   90 MEFLQELNSDV-----SGSFVEESPENLLDN 115
Cdd:PRK08328  88 KWKLERFNSDIkietfVGRLSEENIDEVLKG 118
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 11-114 9.31e-04

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 41.62  E-value: 9.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341   11 QKYDRQLRL--WGDHGQEALESAHVCLINATATGTEILKNLVLPGIGSFTIIDGNLVsgeDAGNnffLQK------SSIG 82
Cdd:PRK07878  21 ARYSRHLIIpdVGVDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVV---DESN---LQRqvihgqSDVG 94

                         90       100       110
                 ....*....|....*....|....*....|....
gi 21450341   83 KNRAQAAMEFLQELNSDVSGSFVEE--SPENLLD 114
Cdd:PRK07878  95 RSKAQSARDSIVEINPLVNVRLHEFrlDPSNAVE 128
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 11-119 3.27e-03

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 39.40  E-value: 3.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341   11 QKYDRQLRLWGDHGQEALESAHVCLINATATGTEILKNLVLPGIGSFTIIDGNLVSGEDAGNNFFLQKSSIGKNRAQAAM 90
Cdd:PRK15116  11 QRFGGTARLYGEKALQLFADAHICVVGIGGVGSWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMA 90

                         90       100       110
                 ....*....|....*....|....*....|....
gi 21450341   91 EFLQELNSDVSGSFVEE--SPEN---LLDNDPSF 119
Cdd:PRK15116  91 ERIRQINPECRVTVVDDfiTPDNvaeYMSAGFSY 124
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 12-100 5.55e-03

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 38.67  E-value: 5.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450341   12 KYDRQ--LRLWGDHGQEALESAHVCLINATATGTEILKNLVLPGIGSFTIIDGNLVSgedAGNnffLQK------SSIGK 83
Cdd:PRK05690  12 RYNRQiiLRGFDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVS---LSN---LQRqvlhddATIGQ 85

                         90
                 ....*....|....*..
gi 21450341   84 NRAQAAMEFLQELNSDV 100
Cdd:PRK05690  86 PKVESARAALARINPHI 102
 
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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