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Conserved domains on  [gi|1207117378|ref|XP_021337052|]
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SUMO-activating enzyme subunit 1 isoform X1 [Danio rerio]

Protein Classification

ubiquitin-activating E1 family protein( domain architecture ID 10107334)

ubiquitin-activating E1 family protein, such as SUMO1 activating enzyme subunit 1 (SAE1) which is a component of a heterodimer E1 enzyme (SAE1/SAE2) involved in small ubiquitin-like modifier (SUMO)ylation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 17-170 3.00e-77

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: 234.11  E-value: 3.00e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207117378  17 AAQYDRQIRLWGLDAQKRLRGSRVLLVGLRGLGAEVAKNLILAGVKGLTLLDHEQVTEESRRAQFLIPVDADGQNHAQAS 96
Cdd:cd01492     1 IALYDRQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEAS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207117378  97 LERAQFLNPMVEVKADTEPVESKPDDFFFQFDAVCLTRCSRDLMVRVDQLCASRNIKVFCGDVYGYNGYMFSDL 170
Cdd:cd01492    81 LERLRALNPRVKVSVDTDDISEKPEEFFSQFDVVVATELSRAELVKINELCRKLGVKFYATGVHGLFGFVFADL 154
 
Name Accession Description Interval E-value
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 17-170 3.00e-77

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: 234.11  E-value: 3.00e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207117378  17 AAQYDRQIRLWGLDAQKRLRGSRVLLVGLRGLGAEVAKNLILAGVKGLTLLDHEQVTEESRRAQFLIPVDADGQNHAQAS 96
Cdd:cd01492     1 IALYDRQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEAS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207117378  97 LERAQFLNPMVEVKADTEPVESKPDDFFFQFDAVCLTRCSRDLMVRVDQLCASRNIKVFCGDVYGYNGYMFSDL 170
Cdd:cd01492    81 LERLRALNPRVKVSVDTDDISEKPEEFFSQFDVVVATELSRAELVKINELCRKLGVKFYATGVHGLFGFVFADL 154
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 20-167 3.26e-40

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: 140.47  E-value: 3.26e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207117378  20 YDRQIRL--WGLDAQKRLRGSRVLLVGLRGLGAEVAKNLILAGVKGLTLLDHEQVTEESRRAQFLIPVDADGQNHAQASL 97
Cdd:pfam00899   1 YSRQLALplIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207117378  98 ERAQFLNPMVEVKADTEPVESK-PDDFFFQFDAVCLTRCSRDLMVRVDQLCASRNIKVFCGDVYGYNGYMF 167
Cdd:pfam00899  81 ERLREINPDVEVEAYTERLTPEnAEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVT 151
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 14-194 1.02e-26

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: 110.36  E-value: 1.02e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207117378   14 EEEAAQYDRQIRLWGLDAQKRLRGSRVLLVGLRGLGAEVAKNLILAGVKGLTLLDHEQVTEESRRAQFLIPVDADGQNHA 93
Cdd:TIGR01408    1 EIDEALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207117378   94 QASLERAQFLNPMVEVKADTEPVESkpdDFFFQFDAVCLTRCSRDLMVRVDQLCASRN--IKVFCGDVYGYNGYMFSDLG 171
Cdd:TIGR01408   81 EAVVKKLAELNPYVHVSSSSVPFNE---EFLDKFQCVVLTEMSLPLQKEINDFCHSQCppIAFISADVRGLFGSLFCDFG 157

                          170       180
                   ....*....|....*....|....*.
gi 1207117378  172 QEYHYVE---EKPKVVKGSNEANDGP 194
Cdd:TIGR01408  158 DEFEVLDtdgEEPKTGFIASITQANP 183
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 13-167 4.74e-18

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: 81.71  E-value: 4.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207117378  13 SEEEAAQYDRQIRL--WGLDAQKRLRGSRVLLVGLRGLGAEVAKNLILAGVKGLTLLDHEQVtEES---RraQFLIPVDA 87
Cdd:COG0476     1 TDEELERYSRQILLpeIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVV-ELSnlqR--QILYTEAD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207117378  88 DGQNHAQASLERAQFLNPMVEVKADTEPVESKP-DDFFFQFDAVCLtrCSRDLMVR--VDQLCASRNIKVFCGDVYGYNG 164
Cdd:COG0476    78 VGRPKVEAAAERLRALNPDVEVEAIPERLTEENaLELLAGADLVLD--CTDNFATRylLNDACVKLGIPLVSGAVIGFEG 155


                  ...
gi 1207117378 165 YMF 167
Cdd:COG0476   156 QVT 158
PTZ00245 PTZ00245
ubiquitin activating enzyme; Provisional
 14-109 2.60e-13

ubiquitin activating enzyme; Provisional


Pssm-ID: 140272  Cd Length: 287  Bit Score: 68.93  E-value: 2.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207117378  14 EEEAAQYDRQIRLWGLDAQKRLRGSRVLLVGLRGLGAEVAKNLILAGVKGLTLLDHEQVTEESRRAQFLIPVDADGQNHA 93
Cdd:PTZ00245    3 DAEAVRYDRQIRLWGKSTQQQLMHTSVALHGVAGAAAEAAKNLVLAGVRAVAVADEGLVTDADVCTNYLMQGEAGGTRGA 82

                          90
                  ....*....|....*.
gi 1207117378  94 QAsLERAQFLNPMVEV 109
Cdd:PTZ00245   83 RA-LGALQRLNPHVSV 97
 
Name Accession Description Interval E-value
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 17-170 3.00e-77

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: 234.11  E-value: 3.00e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207117378  17 AAQYDRQIRLWGLDAQKRLRGSRVLLVGLRGLGAEVAKNLILAGVKGLTLLDHEQVTEESRRAQFLIPVDADGQNHAQAS 96
Cdd:cd01492     1 IALYDRQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEAS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207117378  97 LERAQFLNPMVEVKADTEPVESKPDDFFFQFDAVCLTRCSRDLMVRVDQLCASRNIKVFCGDVYGYNGYMFSDL 170
Cdd:cd01492    81 LERLRALNPRVKVSVDTDDISEKPEEFFSQFDVVVATELSRAELVKINELCRKLGVKFYATGVHGLFGFVFADL 154
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 20-167 3.26e-40

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: 140.47  E-value: 3.26e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207117378  20 YDRQIRL--WGLDAQKRLRGSRVLLVGLRGLGAEVAKNLILAGVKGLTLLDHEQVTEESRRAQFLIPVDADGQNHAQASL 97
Cdd:pfam00899   1 YSRQLALplIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207117378  98 ERAQFLNPMVEVKADTEPVESK-PDDFFFQFDAVCLTRCSRDLMVRVDQLCASRNIKVFCGDVYGYNGYMF 167
Cdd:pfam00899  81 ERLREINPDVEVEAYTERLTPEnAEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVT 151
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 20-170 3.76e-40

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: 139.09  E-value: 3.76e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207117378  20 YDRQIRLWGLDAQKRLRGSRVLLVGLRGLGAEVAKNLILAGVKGLTLLDHEQVTEESRRAQFLIP--VDADGQNHAQASL 97
Cdd:cd01485     2 YDRQIRLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFLDaeVSNSGMNRAAASY 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207117378  98 ERAQFLNPMVEVKADTEPVESKPD---DFFFQFDAVCLTRCSRDLMVRVDQLCASRNIKVFCGDVYGYNGYMFSDL 170
Cdd:cd01485    82 EFLQELNPNVKLSIVEEDSLSNDSnieEYLQKFTLVIATEENYERTAKVNDVCRKHHIPFISCATYGLIGYAFFDF 157
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 20-174 7.55e-39

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: 138.17  E-value: 7.55e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207117378  20 YDRQIRLWGLDAQKRLRGSRVLLVGLRGLGAEVAKNLILAGVKGLTLLDHEQVTEESRRAQFLIPVDADGQNHAQASLER 99
Cdd:cd01491     2 YSRQLYVLGHEAMKKLQKSNVLISGLGGLGVEIAKNLILAGVKSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAEASQAR 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207117378 100 AQFLNPMVEVKADTEPVESkpdDFFFQFDAVCLTRCSRDLMVRVDQLCASRNIKVFCGDVYGYNGYMFSDLGQEY 174
Cdd:cd01491    82 LAELNPYVPVTVSTGPLTT---DELLKFQVVVLTDASLEDQLKINEFCHSPGIKFISADTRGLFGSIFCDFGDEF 153
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 20-182 8.21e-29

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: 114.32  E-value: 8.21e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207117378  20 YDRQIRLWGLDAQKRLRGSRVLLVGLRGLGAEVAKNLILAGVKGLTLLDHEQVTEESRRAQFLIPVDADGQNHAQASLER 99
Cdd:cd01493     3 YDRQLRLWGEHGQAALESAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAEATCEL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207117378 100 AQFLNPMVEVKADTEPVES---KPDDFFFQFDAVCLTRCSRDLMVRVDQLCASRNIKVFCGDVYGYNGYMFSDLgQEYHY 176
Cdd:cd01493    83 LQELNPDVNGSAVEESPEAlldNDPSFFSQFTVVIATNLPESTLLRLADVLWSANIPLLYVRSYGLYGYIRIQL-KEHTI 161


                  ....*.
gi 1207117378 177 VEEKPK 182
Cdd:cd01493   162 VESHPD 167
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 14-194 1.02e-26

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: 110.36  E-value: 1.02e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207117378   14 EEEAAQYDRQIRLWGLDAQKRLRGSRVLLVGLRGLGAEVAKNLILAGVKGLTLLDHEQVTEESRRAQFLIPVDADGQNHA 93
Cdd:TIGR01408    1 EIDEALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207117378   94 QASLERAQFLNPMVEVKADTEPVESkpdDFFFQFDAVCLTRCSRDLMVRVDQLCASRN--IKVFCGDVYGYNGYMFSDLG 171
Cdd:TIGR01408   81 EAVVKKLAELNPYVHVSSSSVPFNE---EFLDKFQCVVLTEMSLPLQKEINDFCHSQCppIAFISADVRGLFGSLFCDFG 157

                          170       180
                   ....*....|....*....|....*.
gi 1207117378  172 QEYHYVE---EKPKVVKGSNEANDGP 194
Cdd:TIGR01408  158 DEFEVLDtdgEEPKTGFIASITQANP 183
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 20-166 3.28e-19

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: 84.45  E-value: 3.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207117378  20 YDRQIRL--WGLDAQKRLRGSRVLLVGLRGLGAEVAKNLILAGVKGLTLLDHEQVtEES---RraQFLIPVDADGQNHAQ 94
Cdd:cd00757     2 YSRQILLpeIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVV-ELSnlqR--QILHTEADVGQPKAE 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207117378  95 ASLERAQFLNPMVEVKADTEPV-ESKPDDFFFQFDAVCltRCSRDLMVR--VDQLCASRNIKVFCGDVYGYNGYM 166
Cdd:cd00757    79 AAAERLRAINPDVEIEAYNERLdAENAEELIAGYDLVL--DCTDNFATRylINDACVKLGKPLVSGAVLGFEGQV 151
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 13-167 4.74e-18

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: 81.71  E-value: 4.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207117378  13 SEEEAAQYDRQIRL--WGLDAQKRLRGSRVLLVGLRGLGAEVAKNLILAGVKGLTLLDHEQVtEES---RraQFLIPVDA 87
Cdd:COG0476     1 TDEELERYSRQILLpeIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVV-ELSnlqR--QILYTEAD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207117378  88 DGQNHAQASLERAQFLNPMVEVKADTEPVESKP-DDFFFQFDAVCLtrCSRDLMVR--VDQLCASRNIKVFCGDVYGYNG 164
Cdd:COG0476    78 VGRPKVEAAAERLRALNPDVEVEAIPERLTEENaLELLAGADLVLD--CTDNFATRylLNDACVKLGIPLVSGAVIGFEG 155


                  ...
gi 1207117378 165 YMF 167
Cdd:COG0476   156 QVT 158
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 39-166 2.54e-15

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: 71.53  E-value: 2.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207117378  39 RVLLVGLRGLGAEVAKNLILAGVKGLTLLDHEQVTEESRRAQFLIPVDADGQNHAQASLERAQFLNPMVEVKADTEPVES 118
Cdd:cd01483     1 RVLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEGISE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1207117378 119 -KPDDFFFQFDAVCLTRCSRDLMVRVDQLCASRNIKVFCGDVYGYNGYM 166
Cdd:cd01483    81 dNLDDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDI 129
PTZ00245 PTZ00245
ubiquitin activating enzyme; Provisional
 14-109 2.60e-13

ubiquitin activating enzyme; Provisional


Pssm-ID: 140272  Cd Length: 287  Bit Score: 68.93  E-value: 2.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207117378  14 EEEAAQYDRQIRLWGLDAQKRLRGSRVLLVGLRGLGAEVAKNLILAGVKGLTLLDHEQVTEESRRAQFLIPVDADGQNHA 93
Cdd:PTZ00245    3 DAEAVRYDRQIRLWGKSTQQQLMHTSVALHGVAGAAAEAAKNLVLAGVRAVAVADEGLVTDADVCTNYLMQGEAGGTRGA 82

                          90
                  ....*....|....*.
gi 1207117378  94 QAsLERAQFLNPMVEV 109
Cdd:PTZ00245   83 RA-LGALQRLNPHVSV 97
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 9-148 3.92e-13

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 67.56  E-value: 3.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207117378   9 DTIISEEEAAQYDRQIRL--WGLDAQKRLRGSRVLLVGLRGLGAEVAKNLILAGVKGLTLLDHEQVTEESRRAQFLIPVD 86
Cdd:PRK05690    2 MAELSDEEMLRYNRQIILrgFDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDA 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207117378  87 ADGQNHAQASLERAQFLNPMVEVkadtEPVESKPDD-----FFFQFDAVclTRCSRDLMVR--VDQLCA 148
Cdd:PRK05690   82 TIGQPKVESARAALARINPHIAI----ETINARLDDdelaaLIAGHDLV--LDCTDNVATRnqLNRACF 144
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 12-114 3.12e-11

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 63.35  E-value: 3.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207117378  12 ISEEEAAQYDRQIRL--WGLDAQKRLRGSRVLLVGLRGLGAEVAKNLILAGVKGLTLLDHEQVTEESRRAQFLIPVDADG 89
Cdd:PRK05597    1 VKNLDIARYRRQIMLgeIGQQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVG 80

                          90       100
                  ....*....|....*....|....*
gi 1207117378  90 QNHAQASLERAQFLNPMVEVKADTE 114
Cdd:PRK05597   81 QPKAESAREAMLALNPDVKVTVSVR 105
PRK08328 PRK08328
hypothetical protein; Provisional
 11-76 1.25e-10

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 60.19  E-value: 1.25e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207117378  11 IISEEEAAQYDRQIRLWGLDAQKRLRGSRVLLVGLRGLGAEVAKNLILAGVKGLTLLDhEQVTEES 76
Cdd:PRK08328    1 MLSERELERYDRQIMIFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLID-EQTPELS 65
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
10-118 5.90e-10

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 59.64  E-value: 5.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207117378  10 TIISEEEAAQYDRQIRL--WGLDAQKRLRGSRVLLVGLRGLGAEVAKNLILAGVKGLTLLDHEQVTEESRRAQFLIPVDA 87
Cdd:PRK08762  106 RLLTDEQDERYSRHLRLpeVGEEGQRRLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHTEDR 185

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1207117378  88 DGQNHAQASLERAQFLNPMVEVKADTEPVES 118
Cdd:PRK08762  186 VGQPKVDSAAQRLAALNPDVQVEAVQERVTS 216
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 12-128 8.45e-10

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 58.95  E-value: 8.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207117378  12 ISEEEAAQYDRQ--IRLWGLDAQKRLRGSRVLLVGLRGLGAEVAKNLILAGVKGLTLLDHEQVTEESRRAQFLIPVDADG 89
Cdd:PRK07878   15 LTRDEVARYSRHliIPDVGVDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRQVIHGQSDVG 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1207117378  90 QNHAQASLERAQFLNPMVEVKADTEPVE-SKPDDFFFQFD 128
Cdd:PRK07878   95 RSKAQSARDSIVEINPLVNVRLHEFRLDpSNAVELFSQYD 134
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 28-155 9.31e-10

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


Pssm-ID: 238384 [Multi-domain]  Cd Length: 231  Bit Score: 57.61  E-value: 9.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207117378  28 GLDAQKRLRGSRVLLVGLRGLGAEVAKNLILAGVKGLTLLDHEQVTEESRRAQfLIPVDAD-GQNHAQASLERAQFLNPM 106
Cdd:cd00755     2 GEEGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQ-IHALLSTvGKPKVEVMAERIRDINPE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1207117378 107 VEVKADTEPV--ESKPDDFFFQFDAVclTRCSRDLMVRVDQL--CASRNIKVF 155
Cdd:cd00755    81 CEVDAVEEFLtpDNSEDLLGGDPDFV--VDAIDSIRAKVALIayCRKRKIPVI 131
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 22-114 4.63e-09

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 56.81  E-value: 4.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207117378  22 RQIRL--WGLDAQKRLRGSRVLLVGLRGLGAEVAKNLILAGVKGLTLLDHEQVTEESRRAQFLIPVDADGQNHAQASLER 99
Cdd:PRK05600   24 RQLALpgFGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDVGRPKVEVAAER 103

                          90
                  ....*....|....*
gi 1207117378 100 AQFLNPMVEVKADTE 114
Cdd:PRK05600  104 LKEIQPDIRVNALRE 118
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 39-166 1.43e-08

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: 55.08  E-value: 1.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207117378  39 RVLLVGLRGLGAEVAKNLILAGVKGLTLLDHEQVTEESRRAQFLIPVDADGQNHAQASLERAQFLNPMVE-------VKA 111
Cdd:cd01489     1 KVLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKivayhanIKD 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1207117378 112 DTEPVEskpddFFFQFDAVCLTRCSRDLMVRVDQLCASRNIKVFCGDVYGYNGYM 166
Cdd:cd01489    81 PDFNVE-----FFKQFDLVFNALDNLAARRHVNKMCLAADVPLIESGTTGFLGQV 130
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 39-166 1.80e-07

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: 51.04  E-value: 1.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207117378  39 RVLLVGLRGLGAEVAKNLILAGVKGLTLLDHEQVTEESRRAQFLIPVDADGQNHAQASLERAQFLNP---MVEVKADTEP 115
Cdd:cd01484     1 KVLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPnckVVPYQNKVGP 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1207117378 116 VESKPDDFFFQFDAVCltrCSRD-LMVR--VDQLCASRNIKVFCGDVYGYNGYM 166
Cdd:cd01484    81 EQDFNDTFFEQFHIIV---NALDnIIARryVNGMLIFLIVPLIESGTEGFKGNA 131
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 19-111 1.20e-06

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 49.34  E-value: 1.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207117378  19 QYDRQIRLWGL--DAQKRLRGSRVLLVGLRGLGAEVAKNLILAGVKGLTLLDHEQVtEES--RRAQFLIPVDADGQN-HA 93
Cdd:PRK12475    4 RYSRQILFSGIgeEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYV-EWSnlQRQQLYTEEDAKQKKpKA 82

                          90
                  ....*....|....*...
gi 1207117378  94 QASLERAQFLNPMVEVKA 111
Cdd:PRK12475   83 IAAKEHLRKINSEVEIVP 100
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 39-130 1.55e-06

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: 48.89  E-value: 1.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207117378  39 RVLLVGLRGLGAEVAKNLILAGVKGLTLLDHEQVTEESRRAQFLIPVDADGQNHAQASlerAQFLN---PMVEVKADTEP 115
Cdd:cd01488     1 KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVA---AKFVNdrvPGVNVTPHFGK 77

                          90
                  ....*....|....*
gi 1207117378 116 VESKPDDFFFQFDAV 130
Cdd:cd01488    78 IQDKDEEFYRQFNII 92
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 2-242 1.98e-06

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


Pssm-ID: 273603 [Multi-domain]  Cd Length: 1006  Bit Score: 49.12  E-value: 1.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207117378    2 IDTIEKEDTIISEE---EAAQYDRQIRLWGLDAQKRLRGSRVLLVGLRGLGAEVAKNLILAGV----KG-LTLLDHEQVT 73
Cdd:TIGR01408  381 AESLPSLGKPECEEflpRGDRYDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVgtgkKGmITVTDPDLIE 460

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207117378   74 EESRRAQFLIPVDADGQNHAQASLERAQFLNPMVEVKADTEPV----ESKPDDFFFQFDAVCLTrcsrdlmvRVDQLCAS 149
Cdd:TIGR01408  461 KSNLNRQFLFRPHHIGKPKSYTAADATLKINPQIKIDAHQNRVgpetETIFNDEFYEKLDVVIN--------ALDNVEAR 532

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207117378  150 RNIKVFCgdVYGYNGYMFS-DLGQEYHYVEEKPKVVKGSNEANDGPEakkpkidpnettmvkKTISFCSLKE---ALE-- 223
Cdd:TIGR01408  533 RYVDSRC--LAFLKPLLESgTLGTKGNTQVVVPHLTESYGSSRDPPE---------------KEIPFCTLKSfpaAIEht 595

                          250
                   ....*....|....*....
gi 1207117378  224 VDWTTEKAKSSLKRIPADY 242
Cdd:TIGR01408  596 IQWARDKFEGLFSHKPSLV 614
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 20-111 2.53e-06

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 48.45  E-value: 2.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207117378  20 YDRQIRLW--GLDAQKRLRGSRVLLVGLRGLGAEVAKNLILAGVKGLTLLDHEQVtEES--RRAQFLIpvDADGQNH--- 92
Cdd:PRK07688    5 YSRQELFSpiGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYV-EWSnlQRQQLYT--ESDVKNNlpk 81

                          90
                  ....*....|....*....
gi 1207117378  93 AQASLERAQFLNPMVEVKA 111
Cdd:PRK07688   82 AVAAKKRLEEINSDVRVEA 100
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 39-131 4.55e-06

E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. The common reaction mechanism catalyzed by E1-like enzymes begins with a nucleophilic attack of the C-terminal carboxylate of the ubiquitin-like substrate, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of the substrate. The exact function of this family is unknown.


Pssm-ID: 238764 [Multi-domain]  Cd Length: 174  Bit Score: 46.22  E-value: 4.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207117378  39 RVLLVGLRGLGAEVAKNLILAGVKGLTLLDHEQVtEES--RRAQFLIpvDADGQNHAQASLERAQFLNPMVEVKADTEPV 116
Cdd:cd01487     1 KVGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVV-EPSnlNRQQYFL--SQIGEPKVEALKENLREINPFVKIEAINIKI 77

                          90
                  ....*....|....*.
gi 1207117378 117 ESKP-DDFFFQFDAVC 131
Cdd:cd01487    78 DENNlEGLFGDCDIVV 93
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
2-109 1.70e-05

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 45.88  E-value: 1.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207117378   2 IDTIEkedtiISEEEAAQYDRQIRL--WGLDAQKRLRGSRVLLVGLRGLGAEVAKNLILAGVKGLTLLDHEQVTEESRRA 79
Cdd:PRK07411    6 LDEIQ-----LSKDEYERYSRHLILpeVGLEGQKRLKAASVLCIGTGGLGSPLLLYLAAAGIGRIGIVDFDVVDSSNLQR 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1207117378  80 QFLIPVDADGQNHAQASLERAQFLNPMVEV 109
Cdd:PRK07411   81 QVIHGTSWVGKPKIESAKNRILEINPYCQV 110
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 19-74 2.53e-05

tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and biogenesis]; tRNA A37 threonylcarbamoyladenosine dehydratase is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440792  Cd Length: 247  Bit Score: 44.69  E-value: 2.53e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207117378  19 QYDRQIRLWGLDAQKRLRGSRVLLVGLRGLGAEVAKNLILAGVKGLTLLDHEQVTE 74
Cdd:COG1179     6 RFSRTERLYGEEGLERLANAHVAVVGLGGVGSWAAEALARSGVGRLTLVDLDDVCE 61
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
28-131 3.06e-05

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 44.08  E-value: 3.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207117378  28 GLDAQKRLRGSRVLLVGLRGLGAEVAKNLILAGVKGLTLLDHEQVtEES--RRAQFLI------PVDADGQNhaqasLER 99
Cdd:PRK08644   19 TPKLLEKLKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVV-EPSnlNRQQYFIsqigmpKVEALKEN-----LLE 92

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1207117378 100 aqfLNPMVEVKADTEPVESKP-DDFFFQFDAVC 131
Cdd:PRK08644   93 ---INPFVEIEAHNEKIDEDNiEELFKDCDIVV 122
PRK14852 PRK14852
hypothetical protein; Provisional
 20-126 3.19e-04

hypothetical protein; Provisional


Pssm-ID: 184854 [Multi-domain]  Cd Length: 989  Bit Score: 42.38  E-value: 3.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207117378  20 YDRQIRLWGLDAQKRLRGSRVLLVGLRGLGAEVAKNLILAGVKGLTLLDHEQVTEESRRAQFLIPVDADGQNHAQASLER 99
Cdd:PRK14852  315 FSRNLGLVDYAGQRRLLRSRVAIAGLGGVGGIHLMTLARTGIGNFNLADFDAYSPVNLNRQYGASIASFGRGKLDVMTER 394

                          90       100
                  ....*....|....*....|....*..
gi 1207117378 100 AQFLNPMVEVKADTEPVESKPDDFFFQ 126
Cdd:PRK14852  395 ALSVNPFLDIRSFPEGVAAETIDAFLK 421
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
 39-111 5.32e-04

Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and Apg8, and assigns them to specific E2 enzymes, Apg10 and Apg3, respectively. This leads to the covalent conjugation of Apg8 with phosphatidylethanolamine, an important step in autophagy. Autophagy is a dynamic membrane phenomenon for bulk protein degradation in the lysosome/vacuole.


Pssm-ID: 238763 [Multi-domain]  Cd Length: 307  Bit Score: 41.20  E-value: 5.32e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207117378  39 RVLLVGLRGLGAEVAKNLILAGVKGLTLLDHEQVTEES--RRAQFLIPVDADGQNHAQASLERAQFLNPMVEVKA 111
Cdd:cd01486     1 KCLLLGAGTLGCNVARNLLGWGVRHITFVDSGKVSYSNpvRQSLFTFEDCKGGKPKAEAAAERLKEIFPSIDATG 75
PRK08223 PRK08223
hypothetical protein; Validated
 22-155 8.24e-04

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 40.44  E-value: 8.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207117378  22 RQIRLWGLDAQKRLRGSRVLLVGLRGLGAEVAKNLILAGVKGLTLLDHEQVTEESRRAQFLIPVDADGQNHAQASLERAQ 101
Cdd:PRK08223   12 RNLGWITPTEQQRLRNSRVAIAGLGGVGGIHLLTLARLGIGKFTIADFDVFELRNFNRQAGAMMSTLGRPKAEVLAEMVR 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207117378 102 FLNPMVEVKADTEPV-ESKPDDF------------FFQFDAvcltrcsRDLMVRVdqlCASRNIKVF 155
Cdd:PRK08223   92 DINPELEIRAFPEGIgKENADAFldgvdvyvdgldFFEFDA-------RRLVFAA---CQQRGIPAL 148
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 25-109 2.50e-03

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 39.02  E-value: 2.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207117378  25 RLWGLDAQKRLRGSRVLLVGLRGLGAEVAKNLILAGVKGLTLLDHEQV--TEESRRAQFLipVDADGQNHAQASLERAQF 102
Cdd:PRK15116   18 RLYGEKALQLFADAHICVVGIGGVGSWAAEALARTGIGAITLIDMDDVcvTNTNRQIHAL--RDNVGLAKAEVMAERIRQ 95


                  ....*..
gi 1207117378 103 LNPMVEV 109
Cdd:PRK15116   96 INPECRV 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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