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Conserved domains on  [gi|557357751|ref|NP_001273429|]
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NEDD8-activating enzyme E1 regulatory subunit isoform d [Homo sapiens]

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 ...
 11-535 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: 735.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751  11 QKYDRQLRLWGDHGQEALESAHVCLINATATGTEILKNLVLPGnvgIGSFTIIDGNQVSGEDAGNNFFLQRSSIGKNRAE 90
Cdd:cd01493    1 QKYDRQLRLWGEHGQAALESAHVCLLNATATGTEILKNLVLPG---IGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751  91 AAMEFLQELNSDVSGSFVEESPENLLDNDPSFFCRFTVVVATQLPESTSLRLADVLWNSQIPLLICRTYGLVGYMRIIIK 170
Cdd:cd01493   78 ATCELLQELNPDVNGSAVEESPEALLDNDPSFFSQFTVVIATNLPESTLLRLADVLWSANIPLLYVRSYGLYGYIRIQLK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751 171 EHPVIESHPDNALEDLRLDKPFPELREHFQSYDLDHMEKKDHSHTPWIVIIAKYLAQWYSETNGRIPKTYKEKEDFRDLI 250
Cdd:cd01493  158 EHTIVESHPDNALEDLRLDNPFPELREHADSIDLDDMDPAEHSHTPYIVILIKYLEKWRSAHNGQLPSTYKEKKEFRDLV 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751 251 RQGILKNengapEDEENFEEAIKNVNTALNTTQIPSSIEDIFNDDRCINITKQTPSFWILARALKEFVAKEgQGNLPVRG 330
Cdd:cd01493  238 RSLMRSN-----EDEENFEEAIKAVNKALNRTKIPSSVEEIFNDDRCENLTSQSSSFWIMARALKEFVAEE-NGLLPLPG 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751 331 TIPDMIADSGKYIKLQNVYREKAKKDAAAVGNHVAKLLQSIGQAPESISEKELKLLCSNSAFLRVVRCRSLAeeygldti 410
Cdd:cd01493  312 TLPDMTADTEKYIKLQNIYREKAEKDAAEVEKYVREILKSLGRSPDSISDKEIKLFCKNAAFLRVIRGRSLE-------- 383

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751 411 nkdeiissmdnpdneivlylmlravdrfhkqqgrypgvsnyqveedigklkscltgflqeyglsvmvkddyvhefcryga 490
Cdd:cd01493      --------------------------------------------------------------------------------

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*
gi 557357751 491 aepHTIAAFLGGAAAQEVIKIITKQFVIFNNTYIYSGMSQTSATF 535
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 ...
 11-535 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: 735.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751  11 QKYDRQLRLWGDHGQEALESAHVCLINATATGTEILKNLVLPGnvgIGSFTIIDGNQVSGEDAGNNFFLQRSSIGKNRAE 90
Cdd:cd01493    1 QKYDRQLRLWGEHGQAALESAHVCLLNATATGTEILKNLVLPG---IGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751  91 AAMEFLQELNSDVSGSFVEESPENLLDNDPSFFCRFTVVVATQLPESTSLRLADVLWNSQIPLLICRTYGLVGYMRIIIK 170
Cdd:cd01493   78 ATCELLQELNPDVNGSAVEESPEALLDNDPSFFSQFTVVIATNLPESTLLRLADVLWSANIPLLYVRSYGLYGYIRIQLK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751 171 EHPVIESHPDNALEDLRLDKPFPELREHFQSYDLDHMEKKDHSHTPWIVIIAKYLAQWYSETNGRIPKTYKEKEDFRDLI 250
Cdd:cd01493  158 EHTIVESHPDNALEDLRLDNPFPELREHADSIDLDDMDPAEHSHTPYIVILIKYLEKWRSAHNGQLPSTYKEKKEFRDLV 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751 251 RQGILKNengapEDEENFEEAIKNVNTALNTTQIPSSIEDIFNDDRCINITKQTPSFWILARALKEFVAKEgQGNLPVRG 330
Cdd:cd01493  238 RSLMRSN-----EDEENFEEAIKAVNKALNRTKIPSSVEEIFNDDRCENLTSQSSSFWIMARALKEFVAEE-NGLLPLPG 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751 331 TIPDMIADSGKYIKLQNVYREKAKKDAAAVGNHVAKLLQSIGQAPESISEKELKLLCSNSAFLRVVRCRSLAeeygldti 410
Cdd:cd01493  312 TLPDMTADTEKYIKLQNIYREKAEKDAAEVEKYVREILKSLGRSPDSISDKEIKLFCKNAAFLRVIRGRSLE-------- 383

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751 411 nkdeiissmdnpdneivlylmlravdrfhkqqgrypgvsnyqveedigklkscltgflqeyglsvmvkddyvhefcryga 490
Cdd:cd01493      --------------------------------------------------------------------------------

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*
gi 557357751 491 aepHTIAAFLGGAAAQEVIKIITKQFVIFNNTYIYSGMSQTSATF 535
Cdd:cd01493  384 ---HNISAFMGGIAAQEVIKLITKQYVPIDNTFIFDGIRSKSATF 425
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 13-172 1.25e-18

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: 85.00  E-value: 1.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751   13 YDRQLRL--WGDHGQEALESAHVCLINATATGTEILKNLVLpgnVGIGSFTIIDGNQVSGEDAGNNFFLQRSSIGKNRAE 90
Cdd:pfam00899   1 YSRQLALplIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLAR---AGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751   91 AAMEFLQELNSDVSGSFVEE--SPENLLDndpsFFCRFTVVVATQLPESTSLRLADVLWNSQIPLLICRTYGLVGYMRII 168
Cdd:pfam00899  78 VAAERLREINPDVEVEAYTErlTPENAEE----LIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVV 153


                  ....
gi 557357751  169 IKEH 172
Cdd:pfam00899 154 IPGK 157
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 10-516 5.14e-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: 81.47  E-value: 5.14e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751    10 EQKYDRQLRLWGDHGQEALESAHVCLINATATGTEILKNLVLpgnVGIGSFTIIDGNQVSGEDAGNNFFLQRSSIGKNRA 89
Cdd:TIGR01408    4 EALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVL---AGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751    90 EAAMEFLQELNSDVSGSFVEES-PENLLDNdpsffcrFTVVVATQLPESTSLRLADVLWNSQIPL--LICRTYGLVGYMr 166
Cdd:TIGR01408   81 EAVVKKLAELNPYVHVSSSSVPfNEEFLDK-------FQCVVLTEMSLPLQKEINDFCHSQCPPIafISADVRGLFGSL- 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751   167 iiikehpvieshpdnaledlrldkpFPELREHFQSYDLDHMEkkdhshtPWIVIIAkylaqwySETNgripktykEKEDF 246
Cdd:TIGR01408  153 -------------------------FCDFGDEFEVLDTDGEE-------PKTGFIA-------SITQ--------ANPGI 185

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751   247 RDLIRQGILKNENGapeDEENFEEAikNVNTALnttqipssiedifNDDRCINITKQTP-SFWIlaralkefvakegqgn 325
Cdd:TIGR01408  186 VTCLENHRHKLETG---DFVTFREV--NGMTGL-------------NDGSPRKITVISPySFSI---------------- 231

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751   326 lpvrgtipDMIADSGKYIKlqnvyrekakkdaAAVGNHVakllqsigQAPESISEKELKllcsnsaflrvvrcRSLAeey 405
Cdd:TIGR01408  232 --------GDTTELGPYLH-------------GGIATQV--------KTPKTVFFKSLR--------------EQLK--- 265

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751   406 gldtiNKDEIISSMDNPDNEIVLYLMLRAVDRFHKQQGRYPGVSNYQVEEDIGKLKSCLTGFLQEYglSVMVKDDYVHEF 485
Cdd:TIGR01408  266 -----DPKCLIVDFSKPERPPEIHTAFQALDQFQEKYSRKPNVGCQQDAEELLKLATSISETLEEK--VPDVDAKLVHWL 338

                          490       500       510
                   ....*....|....*....|....*....|.
gi 557357751   486 CRYGAAEPHTIAAFLGGAAAQEVIKIITKQF 516
Cdd:TIGR01408  339 SWTAQGFLSPMAAAVGGVVSQEVLKAVTGKF 369
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 13-163 9.22e-15

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: 74.01  E-value: 9.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751  13 YDRQLRL--WGDHGQEALESAHVCLINATATGTEILKNLVLpgnVGIGSFTIIDGNQVsgeDAGNnffLQR------SSI 84
Cdd:COG0476    8 YSRQILLpeIGEEGQEKLKAARVLVVGAGGLGSPVALYLAA---AGVGTLTLVDDDVV---ELSN---LQRqilyteADV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751  85 GKNRAEAAMEFLQELNSDVSgsfVEE-----SPENLLDndpsFFCRFTVVV-ATQlPESTSLRLADVLWNSQIPLL---I 155
Cdd:COG0476   79 GRPKVEAAAERLRALNPDVE---VEAiperlTEENALE----LLAGADLVLdCTD-NFATRYLLNDACVKLGIPLVsgaV 150


                 ....*...
gi 557357751 156 CRTYGLVG 163
Cdd:COG0476  151 IGFEGQVT 158
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 5-117 4.14e-08

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 55.26  E-value: 4.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751   5 GKLLKEQKYDRQLRL--WGDHGQEALESAHVCLINATATGTEILknLVLPGnVGIGSFTIIDGNQVSGEDAGNNFFLQRS 82
Cdd:PRK05597   1 VKNLDIARYRRQIMLgeIGQQGQQSLFDAKVAVIGAGGLGSPAL--LYLAG-AGVGHITIIDDDTVDLSNLHRQVIHSTA 77

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 557357751  83 SIGKNRAEAAMEFLQELNSD--VSGSFVEESPENLLD 117
Cdd:PRK05597  78 GVGQPKAESAREAMLALNPDvkVTVSVRRLTWSNALD 114
 
Name Accession Description Interval E-value
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 11-535 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: 735.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751  11 QKYDRQLRLWGDHGQEALESAHVCLINATATGTEILKNLVLPGnvgIGSFTIIDGNQVSGEDAGNNFFLQRSSIGKNRAE 90
Cdd:cd01493    1 QKYDRQLRLWGEHGQAALESAHVCLLNATATGTEILKNLVLPG---IGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751  91 AAMEFLQELNSDVSGSFVEESPENLLDNDPSFFCRFTVVVATQLPESTSLRLADVLWNSQIPLLICRTYGLVGYMRIIIK 170
Cdd:cd01493   78 ATCELLQELNPDVNGSAVEESPEALLDNDPSFFSQFTVVIATNLPESTLLRLADVLWSANIPLLYVRSYGLYGYIRIQLK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751 171 EHPVIESHPDNALEDLRLDKPFPELREHFQSYDLDHMEKKDHSHTPWIVIIAKYLAQWYSETNGRIPKTYKEKEDFRDLI 250
Cdd:cd01493  158 EHTIVESHPDNALEDLRLDNPFPELREHADSIDLDDMDPAEHSHTPYIVILIKYLEKWRSAHNGQLPSTYKEKKEFRDLV 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751 251 RQGILKNengapEDEENFEEAIKNVNTALNTTQIPSSIEDIFNDDRCINITKQTPSFWILARALKEFVAKEgQGNLPVRG 330
Cdd:cd01493  238 RSLMRSN-----EDEENFEEAIKAVNKALNRTKIPSSVEEIFNDDRCENLTSQSSSFWIMARALKEFVAEE-NGLLPLPG 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751 331 TIPDMIADSGKYIKLQNVYREKAKKDAAAVGNHVAKLLQSIGQAPESISEKELKLLCSNSAFLRVVRCRSLAeeygldti 410
Cdd:cd01493  312 TLPDMTADTEKYIKLQNIYREKAEKDAAEVEKYVREILKSLGRSPDSISDKEIKLFCKNAAFLRVIRGRSLE-------- 383

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751 411 nkdeiissmdnpdneivlylmlravdrfhkqqgrypgvsnyqveedigklkscltgflqeyglsvmvkddyvhefcryga 490
Cdd:cd01493      --------------------------------------------------------------------------------

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*
gi 557357751 491 aepHTIAAFLGGAAAQEVIKIITKQFVIFNNTYIYSGMSQTSATF 535
Cdd:cd01493  384 ---HNISAFMGGIAAQEVIKLITKQYVPIDNTFIFDGIRSKSATF 425
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 12-169 1.54e-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: 237.32  E-value: 1.54e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751  12 KYDRQLRLWGDHGQEALESAHVCLINATATGTEILKNLVLPGnvgIGSFTIIDGNQVSGEDAGNNFFLQR--SSIGKNRA 89
Cdd:cd01485    1 LYDRQIRLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAG---IDSITIVDHRLVSTEDLGSNFFLDAevSNSGMNRA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751  90 EAAMEFLQELNSDVSGSFVEESPENLLDNDPSFFCRFTVVVATQLPESTSLRLADVLWNSQIPLLICRTYGLVGYMRIII 169
Cdd:cd01485   78 AASYEFLQELNPNVKLSIVEEDSLSNDSNIEEYLQKFTLVIATEENYERTAKVNDVCRKHHIPFISCATYGLIGYAFFDF 157
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 13-165 1.66e-36

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: 134.34  E-value: 1.66e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751  13 YDRQLRLWGDHGQEALESAHVCLINATATGTEILKNLVLPgnvGIGSFTIIDGNQVSGEDAGNNFFLQRSSIGKNRAEAA 92
Cdd:cd01492    4 YDRQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLS---GIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEAS 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 557357751  93 MEFLQELNSDVSgsfVEESPENLLDNDPSFFCRFTVVVATQLPESTSLRLADVLWNSQIPLLICRTYGLVGYM 165
Cdd:cd01492   81 LERLRALNPRVK---VSVDTDDISEKPEEFFSQFDVVVATELSRAELVKINELCRKLGVKFYATGVHGLFGFV 150
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 32-169 5.64e-31

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: 117.37  E-value: 5.64e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751  32 HVCLINATATGTEILKNLVLpgnVGIGSFTIIDGNQVSGEDAGNNFFLQRSSIGKNRAEAAMEFLQELNSDVSGSFVEES 111
Cdd:cd01483    1 RVLLVGLGGLGSEIALNLAR---SGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEG 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 557357751 112 PENllDNDPSFFCRFTVVVATQLPESTSLRLADVLWNSQIPLLICRTYGLVGYMRIII 169
Cdd:cd01483   78 ISE--DNLDDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQVID 133
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 13-164 4.25e-19

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: 87.71  E-value: 4.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751  13 YDRQLRLWGDHGQEALESAHVCLINATATGTEILKNLVLpgnVGIGSFTIIDGNQVSGEDAGNNFFLQRSSIGKNRAEAA 92
Cdd:cd01491    2 YSRQLYVLGHEAMKKLQKSNVLISGLGGLGVEIAKNLIL---AGVKSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAEAS 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557357751  93 MEFLQELNSDVSgsfVEESPENLLDNdpsFFCRFTVVVATQLPESTSLRLADVLWNSQIPLLICRTYGLVGY 164
Cdd:cd01491   79 QARLAELNPYVP---VTVSTGPLTTD---ELLKFQVVVLTDASLEDQLKINEFCHSPGIKFISADTRGLFGS 144
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 13-172 1.25e-18

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: 85.00  E-value: 1.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751   13 YDRQLRL--WGDHGQEALESAHVCLINATATGTEILKNLVLpgnVGIGSFTIIDGNQVSGEDAGNNFFLQRSSIGKNRAE 90
Cdd:pfam00899   1 YSRQLALplIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLAR---AGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751   91 AAMEFLQELNSDVSGSFVEE--SPENLLDndpsFFCRFTVVVATQLPESTSLRLADVLWNSQIPLLICRTYGLVGYMRII 168
Cdd:pfam00899  78 VAAERLREINPDVEVEAYTErlTPENAEE----LIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVV 153


                  ....
gi 557357751  169 IKEH 172
Cdd:pfam00899 154 IPGK 157
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 10-516 5.14e-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: 81.47  E-value: 5.14e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751    10 EQKYDRQLRLWGDHGQEALESAHVCLINATATGTEILKNLVLpgnVGIGSFTIIDGNQVSGEDAGNNFFLQRSSIGKNRA 89
Cdd:TIGR01408    4 EALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVL---AGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751    90 EAAMEFLQELNSDVSGSFVEES-PENLLDNdpsffcrFTVVVATQLPESTSLRLADVLWNSQIPL--LICRTYGLVGYMr 166
Cdd:TIGR01408   81 EAVVKKLAELNPYVHVSSSSVPfNEEFLDK-------FQCVVLTEMSLPLQKEINDFCHSQCPPIafISADVRGLFGSL- 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751   167 iiikehpvieshpdnaledlrldkpFPELREHFQSYDLDHMEkkdhshtPWIVIIAkylaqwySETNgripktykEKEDF 246
Cdd:TIGR01408  153 -------------------------FCDFGDEFEVLDTDGEE-------PKTGFIA-------SITQ--------ANPGI 185

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751   247 RDLIRQGILKNENGapeDEENFEEAikNVNTALnttqipssiedifNDDRCINITKQTP-SFWIlaralkefvakegqgn 325
Cdd:TIGR01408  186 VTCLENHRHKLETG---DFVTFREV--NGMTGL-------------NDGSPRKITVISPySFSI---------------- 231

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751   326 lpvrgtipDMIADSGKYIKlqnvyrekakkdaAAVGNHVakllqsigQAPESISEKELKllcsnsaflrvvrcRSLAeey 405
Cdd:TIGR01408  232 --------GDTTELGPYLH-------------GGIATQV--------KTPKTVFFKSLR--------------EQLK--- 265

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751   406 gldtiNKDEIISSMDNPDNEIVLYLMLRAVDRFHKQQGRYPGVSNYQVEEDIGKLKSCLTGFLQEYglSVMVKDDYVHEF 485
Cdd:TIGR01408  266 -----DPKCLIVDFSKPERPPEIHTAFQALDQFQEKYSRKPNVGCQQDAEELLKLATSISETLEEK--VPDVDAKLVHWL 338

                          490       500       510
                   ....*....|....*....|....*....|.
gi 557357751   486 CRYGAAEPHTIAAFLGGAAAQEVIKIITKQF 516
Cdd:TIGR01408  339 SWTAQGFLSPMAAAVGGVVSQEVLKAVTGKF 369
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 13-163 9.22e-15

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: 74.01  E-value: 9.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751  13 YDRQLRL--WGDHGQEALESAHVCLINATATGTEILKNLVLpgnVGIGSFTIIDGNQVsgeDAGNnffLQR------SSI 84
Cdd:COG0476    8 YSRQILLpeIGEEGQEKLKAARVLVVGAGGLGSPVALYLAA---AGVGTLTLVDDDVV---ELSN---LQRqilyteADV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751  85 GKNRAEAAMEFLQELNSDVSgsfVEE-----SPENLLDndpsFFCRFTVVV-ATQlPESTSLRLADVLWNSQIPLL---I 155
Cdd:COG0476   79 GRPKVEAAAERLRALNPDVE---VEAiperlTEENALE----LLAGADLVLdCTD-NFATRYLLNDACVKLGIPLVsgaV 150


                 ....*...
gi 557357751 156 CRTYGLVG 163
Cdd:COG0476  151 IGFEGQVT 158
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 495-535 1.17e-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: 1.17e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 557357751 495 TIAAFLGGAAAQEVIKIITKQFVIFNNTYIYSGMSQTSATF 535
Cdd:cd01485  158 PIAAFLGGVVAQEAIKSISGKFTPLNNLYIYDGFESTGPMC 198
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 13-103 7.25e-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: 62.11  E-value: 7.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751  13 YDRQLRL--WGDHGQEALESAHVCLINATATGTEILKNLVlpgNVGIGSFTIIDGNQVsgeDAGNnffLQR------SSI 84
Cdd:cd00757    2 YSRQILLpeIGEEGQEKLKNARVLVVGAGGLGSPAAEYLA---AAGVGKLGLVDDDVV---ELSN---LQRqilhteADV 72

                         90
                 ....*....|....*....
gi 557357751  85 GKNRAEAAMEFLQELNSDV 103
Cdd:cd00757   73 GQPKAEAAAERLRAINPDV 91
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 5-117 4.14e-08

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 55.26  E-value: 4.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751   5 GKLLKEQKYDRQLRL--WGDHGQEALESAHVCLINATATGTEILknLVLPGnVGIGSFTIIDGNQVSGEDAGNNFFLQRS 82
Cdd:PRK05597   1 VKNLDIARYRRQIMLgeIGQQGQQSLFDAKVAVIGAGGLGSPAL--LYLAG-AGVGHITIIDDDTVDLSNLHRQVIHSTA 77

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 557357751  83 SIGKNRAEAAMEFLQELNSD--VSGSFVEESPENLLD 117
Cdd:PRK05597  78 GVGQPKAESAREAMLALNPDvkVTVSVRRLTWSNALD 114
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 32-169 2.11e-07

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: 52.74  E-value: 2.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751  32 HVCLINATATGTEILKNLVLpgnVGIGSFTIIDGNQVSGEDAGNNFFLQRSSIGKNRAEAAMEFLQELnsdVSGSFVEES 111
Cdd:cd01488    1 KILVIGAGGLGCELLKNLAL---SGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDR---VPGVNVTPH 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 557357751 112 PENLLDNDPSFFCRFTVVV-------ATQLPESTSLRLADVL-WNSQIPLLICRTYGLVGYMRIII 169
Cdd:cd01488   75 FGKIQDKDEEFYRQFNIIIcgldsieARRWINGTLVSLLLYEdPESIIPLIDGGTEGFKGHARVIL 140
PTZ00245 PTZ00245
ubiquitin activating enzyme; Provisional
 12-104 2.52e-07

ubiquitin activating enzyme; Provisional


Pssm-ID: 140272  Cd Length: 287  Bit Score: 52.37  E-value: 2.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751  12 KYDRQLRLWGDHGQEALESAHVCLINATATGTEILKNLVLpgnVGIGSFTIIDGNQVSGEDAGNNFFLQRSSiGKNRAEA 91
Cdd:PTZ00245   8 RYDRQIRLWGKSTQQQLMHTSVALHGVAGAAAEAAKNLVL---AGVRAVAVADEGLVTDADVCTNYLMQGEA-GGTRGAR 83

                         90
                 ....*....|...
gi 557357751  92 AMEFLQELNSDVS 104
Cdd:PTZ00245  84 ALGALQRLNPHVS 96
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 12-115 2.73e-07

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 52.69  E-value: 2.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751  12 KYDRQLRLW--GDHGQEALESAHVCLINATATGTEILKNLVlpgNVGIGSFTIIDGNQVsgeDAGNnffLQRSSI----- 84
Cdd:PRK07688   4 RYSRQELFSpiGEEGQQKLREKHVLIIGAGALGTANAEMLV---RAGVGKVTIVDRDYV---EWSN---LQRQQLytesd 74

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 557357751  85 GKNR---AEAAMEFLQELNSDVS-GSFVEE-SPENL 115
Cdd:PRK07688  75 VKNNlpkAVAAKKRLEEINSDVRvEAIVQDvTAEEL 110
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 12-169 4.86e-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: 52.58  E-value: 4.86e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751    12 KYDRQLRLWGDHGQEALESAHVCLINATATGTEILKNLVLPGnVGIGS---FTIIDGNQVSGEDAGNNFFLQRSSIGKNR 88
Cdd:TIGR01408  401 RYDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMG-VGTGKkgmITVTDPDLIEKSNLNRQFLFRPHHIGKPK 479

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751    89 AEAAMEFLQELNSDVSGSFVEE----SPENLLDNDpsFFCRFTVVVaTQLPESTSLRLAD--VLWNsQIPLLICRTYGLV 162
Cdd:TIGR01408  480 SYTAADATLKINPQIKIDAHQNrvgpETETIFNDE--FYEKLDVVI-NALDNVEARRYVDsrCLAF-LKPLLESGTLGTK 555


                   ....*..
gi 557357751   163 GYMRIII 169
Cdd:TIGR01408  556 GNTQVVV 562
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 10-103 1.77e-06

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 50.11  E-value: 1.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751  10 EQKYDRQLRL--WGDHGQEALESAHVCLINATATGTEILKNLVlpgNVGIGSFTIIDGNQVSGEDagnnffLQRSSI--- 84
Cdd:PRK12475   2 QERYSRQILFsgIGEEGQRKIREKHVLIVGAGALGAANAEALV---RAGIGKLTIADRDYVEWSN------LQRQQLyte 72

                         90       100
                 ....*....|....*....|....
gi 557357751  85 -----GKNRAEAAMEFLQELNSDV 103
Cdd:PRK12475  73 edakqKKPKAIAAKEHLRKINSEV 96
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 33-218 5.13e-06

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: 47.96  E-value: 5.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751  33 VCLINATATGTEILKNLVLpgnVGIGSFTIIDGNQVSGEDAGNNFFLQRSSIGKNRAEAAMEFLQEL--NSDVSGSFVEE 110
Cdd:cd01484    2 VLLVGAGGIGCELLKNLAL---MGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRnpNCKVVPYQNKV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751 111 SPENLLDNdpSFFCRFTVVVaTQLPESTSLRLAD-VLWNSQIPLLICRTYGLVGYMRIII---------KEHPVIESHPD 180
Cdd:cd01484   79 GPEQDFND--TFFEQFHIIV-NALDNIIARRYVNgMLIFLIVPLIESGTEGFKGNAQVILpgmteciecTLYPPQKNFPM 155

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 557357751 181 NALedlrldKPFPELREHFQSYDLDHMEKKDHsHTPWI 218
Cdd:cd01484  156 CTI------ASMPRLPEHCIEWARMLQWDDPE-HIQFI 186
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 33-170 3.13e-04

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: 42.75  E-value: 3.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751  33 VCLINATATGTEILKNLVLpgnVGIGSFTIIDGNQVSGEDAGNNFFLQRSSIGKNRAEAAMEFLQELNSDVSgsfVEESP 112
Cdd:cd01489    2 VLVVGAGGIGCELLKNLVL---TGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVK---IVAYH 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 557357751 113 ENLLDND--PSFFCRFTVVVaTQLPESTSLRLADVL-WNSQIPLLICRTYGLVGYMRIIIK 170
Cdd:cd01489   76 ANIKDPDfnVEFFKQFDLVF-NALDNLAARRHVNKMcLAADVPLIESGTTGFLGQVQVIKK 135
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 12-103 1.61e-03

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 40.21  E-value: 1.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751  12 KYDRQ--LRLWGDHGQEALESAHVCLINATATGTEILKNLvlpGNVGIGSFTIIDGNQVSgedAGNnffLQR------SS 83
Cdd:PRK05690  12 RYNRQiiLRGFDFDGQEKLKAARVLVVGLGGLGCAASQYL---AAAGVGTLTLVDFDTVS---LSN---LQRqvlhddAT 82

                         90       100
                 ....*....|....*....|
gi 557357751  84 IGKNRAEAAMEFLQELNSDV 103
Cdd:PRK05690  83 IGQPKVESARAALARINPHI 102
PRK08328 PRK08328
hypothetical protein; Provisional
 11-118 3.04e-03

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 39.39  E-value: 3.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751  11 QKYDRQLRLWGDHGQEALESAHVCLINATATGTEILKNLVLpgnVGIGSFTIIDGNQVSGEDAGNNFFLQRSSIGKN-RA 89
Cdd:PRK08328   8 ERYDRQIMIFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAA---AGVGRILLIDEQTPELSNLNRQILHWEEDLGKNpKP 84

                         90       100       110
                 ....*....|....*....|....*....|....
gi 557357751  90 EAAMEFLQELNSDV-----SGSFVEESPENLLDN 118
Cdd:PRK08328  85 LSAKWKLERFNSDIkietfVGRLSEENIDEVLKG 118
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 11-122 4.05e-03

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 39.40  E-value: 4.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751  11 QKYDRQLRLWGDHGQEALESAHVCLINATATGTEILKNLVlpgNVGIGSFTIIDGNQVSGEDAGNNFFLQRSSIGKNRAE 90
Cdd:PRK15116  11 QRFGGTARLYGEKALQLFADAHICVVGIGGVGSWAAEALA---RTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAE 87

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 557357751  91 AAMEFLQELNSDVSGSFVEE--SPEN---LLDNDPSF 122
Cdd:PRK15116  88 VMAERIRQINPECRVTVVDDfiTPDNvaeYMSAGFSY 124
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 11-117 8.44e-03

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 38.54  E-value: 8.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557357751  11 QKYDRQLRL--WGDHGQEALESAHVCLINATATGTEILKNLvlpGNVGIGSFTIIDGNQVsgeDAGNnffLQR------S 82
Cdd:PRK07878  21 ARYSRHLIIpdVGVDGQKRLKNARVLVIGAGGLGSPTLLYL---AAAGVGTLGIVEFDVV---DESN---LQRqvihgqS 91

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 557357751  83 SIGKNRAEAAMEFLQELNSDVSGSFVEE--SPENLLD 117
Cdd:PRK07878  92 DVGRSKAQSARDSIVEINPLVNVRLHEFrlDPSNAVE 128
 
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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