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Conserved domains on  [gi|19114163|ref|NP_593251|]
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SUMO activating enzyme E1-type Rad31 [Schizosaccharomyces pombe]

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 ...
 11-305 3.93e-87

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: 259.14  E-value: 3.93e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114163  11 IALYDRQIRLWGFNAQQALKQSRVLLITASPLANEIAKNLVLSGIGKLCVLDSMTVYEKDVEEQFFIEASDIGQLRANVF 90
Cdd:cd01492   1 IALYDRQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEAS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114163  91 KKKLHELNPLVEIDTDTSLISEIDEGKISKFSMVIATQLDYEEFCRINELTRICNASFYATSCFGLYGFAFCDLInhnfa 170
Cdd:cd01492  81 LERLRALNPRVKVSVDTDDISEKPEEFFSQFDVVVATELSRAELVKINELCRKLGVKFYATGVHGLFGFVFADLL----- 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114163 171 idrvvdntkveedmfivqKPMkeafQSILGETLkprlakkiptlypamlsllkskksdpdsirqvcieqklnektvlnge 250
Cdd:cd01492 156 ------------------APV----AAVVGGIL----------------------------------------------- 166

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19114163 251 flskfssnisfqwtpvmsvvggvvSQDALNSISKKQFPIDNFWIFDAESGLAPIY 305
Cdd:cd01492 167 ------------------------AQDVINALSKRESPLNNFFVFDGETSEAPIY 197
 
Name Accession Description Interval E-value
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 11-305 3.93e-87

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: 259.14  E-value: 3.93e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114163  11 IALYDRQIRLWGFNAQQALKQSRVLLITASPLANEIAKNLVLSGIGKLCVLDSMTVYEKDVEEQFFIEASDIGQLRANVF 90
Cdd:cd01492   1 IALYDRQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEAS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114163  91 KKKLHELNPLVEIDTDTSLISEIDEGKISKFSMVIATQLDYEEFCRINELTRICNASFYATSCFGLYGFAFCDLInhnfa 170
Cdd:cd01492  81 LERLRALNPRVKVSVDTDDISEKPEEFFSQFDVVVATELSRAELVKINELCRKLGVKFYATGVHGLFGFVFADLL----- 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114163 171 idrvvdntkveedmfivqKPMkeafQSILGETLkprlakkiptlypamlsllkskksdpdsirqvcieqklnektvlnge 250
Cdd:cd01492 156 ------------------APV----AAVVGGIL----------------------------------------------- 166

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19114163 251 flskfssnisfqwtpvmsvvggvvSQDALNSISKKQFPIDNFWIFDAESGLAPIY 305
Cdd:cd01492 167 ------------------------AQDVINALSKRESPLNNFFVFDGETSEAPIY 197
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 12-171 2.62e-20

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: 91.49  E-value: 2.62e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114163     12 ALYDRQIRLWGFNAQQALKQSRVLLITASPLANEIAKNLVLSGIGKLCVLDSMTVYEKDVEEQFFIEASDIGQLRANVFK 91
Cdd:TIGR01408    5 ALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRAEAVV 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114163     92 KKLHELNPLVEIDTDTSLISEIDegkISKFSMVIAT------QLDYEEFCRINELTricnASFYATSCFGLYGFAFCDLi 165
Cdd:TIGR01408   85 KKLAELNPYVHVSSSSVPFNEEF---LDKFQCVVLTemslplQKEINDFCHSQCPP----IAFISADVRGLFGSLFCDF- 156


                   ....*.
gi 19114163    166 NHNFAI 171
Cdd:TIGR01408  157 GDEFEV 162
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 14-111 4.40e-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: 81.53  E-value: 4.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114163    14 YDRQIRL--WGFNAQQALKQSRVLLITASPLANEIAKNLVLSGIGKLCVLDSMTVYEKDVEEQFFIEASDIGQLRANVFK 91
Cdd:pfam00899   1 YSRQLALplIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100
                  ....*....|....*....|
gi 19114163    92 KKLHELNPLVEIDTDTSLIS 111
Cdd:pfam00899  81 ERLREINPDVEVEAYTERLT 100
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 7-105 1.21e-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: 74.78  E-value: 1.21e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114163   7 NAEEIALYDRQIRL--WGFNAQQALKQSRVLLITASPLANEIAKNLVLSGIGKLCVLDsmtvyeKD-VEE-----QFFIE 78
Cdd:COG0476   1 TDEELERYSRQILLpeIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVD------DDvVELsnlqrQILYT 74

                        90       100
                ....*....|....*....|....*..
gi 19114163  79 ASDIGQLRANVFKKKLHELNPLVEIDT 105
Cdd:COG0476  75 EADVGRPKVEAAAERLRALNPDVEVEA 101
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 9-125 3.61e-12

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 64.87  E-value: 3.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114163    9 EEIALYDRQIRL--WGFNAQQALKQSRVLLITASPLANEIAKNLVLSGIGKLCVLDSMTVYEKDVEEQFFIEASDIGQLR 86
Cdd:PRK05690   8 EEMLRYNRQIILrgFDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIGQPK 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 19114163   87 ANVFKKKLHELNPLVEIDTDTSLIS--EIDEgKISKFSMVI 125
Cdd:PRK05690  88 VESARAALARINPHIAIETINARLDddELAA-LIAGHDLVL 127
 
Name Accession Description Interval E-value
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 11-305 3.93e-87

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: 259.14  E-value: 3.93e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114163  11 IALYDRQIRLWGFNAQQALKQSRVLLITASPLANEIAKNLVLSGIGKLCVLDSMTVYEKDVEEQFFIEASDIGQLRANVF 90
Cdd:cd01492   1 IALYDRQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEAS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114163  91 KKKLHELNPLVEIDTDTSLISEIDEGKISKFSMVIATQLDYEEFCRINELTRICNASFYATSCFGLYGFAFCDLInhnfa 170
Cdd:cd01492  81 LERLRALNPRVKVSVDTDDISEKPEEFFSQFDVVVATELSRAELVKINELCRKLGVKFYATGVHGLFGFVFADLL----- 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114163 171 idrvvdntkveedmfivqKPMkeafQSILGETLkprlakkiptlypamlsllkskksdpdsirqvcieqklnektvlnge 250
Cdd:cd01492 156 ------------------APV----AAVVGGIL----------------------------------------------- 166

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19114163 251 flskfssnisfqwtpvmsvvggvvSQDALNSISKKQFPIDNFWIFDAESGLAPIY 305
Cdd:cd01492 167 ------------------------AQDVINALSKRESPLNNFFVFDGETSEAPIY 197
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 13-164 5.33e-37

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: 131.00  E-value: 5.33e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114163  13 LYDRQIRLWGFNAQQALKQSRVLLITASPLANEIAKNLVLSGIGKLCVLDSMTVYEKDVEEQFFI--EASDIGQLRANVF 90
Cdd:cd01485   1 LYDRQIRLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFLdaEVSNSGMNRAAAS 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19114163  91 KKKLHELNPLVEIDTDTSLISEID---EGKISKFSMVIATQLDYEEFCRINELTRICNASFYATSCFGLYGFAFCDL 164
Cdd:cd01485  81 YEFLQELNPNVKLSIVEEDSLSNDsniEEYLQKFTLVIATEENYERTAKVNDVCRKHHIPFISCATYGLIGYAFFDF 157
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 14-159 4.52e-32

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: 123.18  E-value: 4.52e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114163  14 YDRQIRLWGFNAQQALKQSRVLLITASPLANEIAKNLVLSGIGKLCVLDSMTVYEKDVEEQFFIEASDIGQLRANVFKKK 93
Cdd:cd01493   3 YDRQLRLWGEHGQAALESAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAEATCEL 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19114163  94 LHELNPLVEID-TDTSLISEIDE--GKISKFSMVIATQLDYEEFCRINELTRICNASFYATSCFGLYGF 159
Cdd:cd01493  83 LQELNPDVNGSaVEESPEALLDNdpSFFSQFTVVIATNLPESTLLRLADVLWSANIPLLYVRSYGLYGY 151
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 13-164 2.62e-28

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: 110.43  E-value: 2.62e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114163  13 LYDRQIRLWGFNAQQALKQSRVLLITASPLANEIAKNLVLSGIGKLCVLDSMTVYEKDVEEQFFIEASDIGQLRANVFKK 92
Cdd:cd01491   1 LYSRQLYVLGHEAMKKLQKSNVLISGLGGLGVEIAKNLILAGVKSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAEASQA 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19114163  93 KLHELNPLVEIDTDTsliSEIDEGKISKFSMVIATQLDYEEFCRINELTRICNASFYATSCFGLYGFAFCDL 164
Cdd:cd01491  81 RLAELNPYVPVTVST---GPLTTDELLKFQVVVLTDASLEDQLKINEFCHSPGIKFISADTRGLFGSIFCDF 149
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 12-171 2.62e-20

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: 91.49  E-value: 2.62e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114163     12 ALYDRQIRLWGFNAQQALKQSRVLLITASPLANEIAKNLVLSGIGKLCVLDSMTVYEKDVEEQFFIEASDIGQLRANVFK 91
Cdd:TIGR01408    5 ALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRAEAVV 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114163     92 KKLHELNPLVEIDTDTSLISEIDegkISKFSMVIAT------QLDYEEFCRINELTricnASFYATSCFGLYGFAFCDLi 165
Cdd:TIGR01408   85 KKLAELNPYVHVSSSSVPFNEEF---LDKFQCVVLTemslplQKEINDFCHSQCPP----IAFISADVRGLFGSLFCDF- 156


                   ....*.
gi 19114163    166 NHNFAI 171
Cdd:TIGR01408  157 GDEFEV 162
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 14-111 4.40e-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: 81.53  E-value: 4.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114163    14 YDRQIRL--WGFNAQQALKQSRVLLITASPLANEIAKNLVLSGIGKLCVLDSMTVYEKDVEEQFFIEASDIGQLRANVFK 91
Cdd:pfam00899   1 YSRQLALplIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100
                  ....*....|....*....|
gi 19114163    92 KKLHELNPLVEIDTDTSLIS 111
Cdd:pfam00899  81 ERLREINPDVEVEAYTERLT 100
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 7-105 1.21e-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: 74.78  E-value: 1.21e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114163   7 NAEEIALYDRQIRL--WGFNAQQALKQSRVLLITASPLANEIAKNLVLSGIGKLCVLDsmtvyeKD-VEE-----QFFIE 78
Cdd:COG0476   1 TDEELERYSRQILLpeIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVD------DDvVELsnlqrQILYT 74

                        90       100
                ....*....|....*....|....*..
gi 19114163  79 ASDIGQLRANVFKKKLHELNPLVEIDT 105
Cdd:COG0476  75 EADVGRPKVEAAAERLRALNPDVEVEA 101
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 33-158 4.75e-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: 70.76  E-value: 4.75e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114163  33 RVLLITASPLANEIAKNLVLSGIGKLCVLDSMTVYEKDVEEQFFIEASDIGQLRANVFKKKLHELNPLVEIDTDTSLISE 112
Cdd:cd01483   1 RVLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEGISE 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 19114163 113 -IDEGKISKFSMVIATQLDYEEFCRINELTRICNASFYATSCFGLYG 158
Cdd:cd01483  81 dNLDDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGG 127
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 14-105 1.42e-12

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: 65.96  E-value: 1.42e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114163  14 YDRQIRL--WGFNAQQALKQSRVLLITASPLANEIAKNLVLSGIGKLCVLDSMTVYEKDVEEQFFIEASDIGQLRANVFK 91
Cdd:cd00757   2 YSRQILLpeIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAAA 81

                        90
                ....*....|....
gi 19114163  92 KKLHELNPLVEIDT 105
Cdd:cd00757  82 ERLRAINPDVEIEA 95
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 9-125 3.61e-12

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 64.87  E-value: 3.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114163    9 EEIALYDRQIRL--WGFNAQQALKQSRVLLITASPLANEIAKNLVLSGIGKLCVLDSMTVYEKDVEEQFFIEASDIGQLR 86
Cdd:PRK05690   8 EEMLRYNRQIILrgFDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIGQPK 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 19114163   87 ANVFKKKLHELNPLVEIDTDTSLIS--EIDEgKISKFSMVI 125
Cdd:PRK05690  88 VESARAALARINPHIAIETINARLDddELAA-LIAGHDLVL 127
PTZ00245 PTZ00245
ubiquitin activating enzyme; Provisional
 10-103 2.63e-09

ubiquitin activating enzyme; Provisional


Pssm-ID: 140272  Cd Length: 287  Bit Score: 56.99  E-value: 2.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114163   10 EIALYDRQIRLWGFNAQQALKQSRVLLITASPLANEIAKNLVLSGIGKLCVLDSMTVYEKDVEEQFFIEASDIGQLRANV 89
Cdd:PTZ00245   5 EAVRYDRQIRLWGKSTQQQLMHTSVALHGVAGAAAEAAKNLVLAGVRAVAVADEGLVTDADVCTNYLMQGEAGGTRGARA 84

                         90
                 ....*....|....
gi 19114163   90 FkKKLHELNPLVEI 103
Cdd:PTZ00245  85 L-GALQRLNPHVSV 97
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 16-104 1.30e-08

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 55.27  E-value: 1.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114163   16 RQIRL--WGFNAQQALKQSRVLLITASPLANEIAKNLVLSGIGKLCVLDSMTVYEKDVEEQFFIEASDIGQLRANVFKKK 93
Cdd:PRK05600  24 RQLALpgFGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDVGRPKVEVAAER 103

                         90
                 ....*....|.
gi 19114163   94 LHELNPLVEID 104
Cdd:PRK05600 104 LKEIQPDIRVN 114
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 8-104 9.65e-08

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 52.57  E-value: 9.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114163    8 AEEIALYDRQIRL--WGFNAQQALKQSRVLLITASPLANEIAKNLVLSGIGKLCVLDSMTVYEKDVEEQFFIEASDIGQL 85
Cdd:PRK05597   3 NLDIARYRRQIMLgeIGQQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVGQP 82

                         90
                 ....*....|....*....
gi 19114163   86 RANVFKKKLHELNPLVEID 104
Cdd:PRK05597  83 KAESAREAMLALNPDVKVT 101
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 9-103 2.08e-07

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 51.63  E-value: 2.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114163    9 EEIALYDRQ--IRLWGFNAQQALKQSRVLLITASPLANEIAKNLVLSGIGKLCVLDSMTVYEKDVEEQFFIEASDIGQLR 86
Cdd:PRK07878  18 DEVARYSRHliIPDVGVDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRQVIHGQSDVGRSK 97

                         90
                 ....*....|....*..
gi 19114163   87 ANVFKKKLHELNPLVEI 103
Cdd:PRK07878  98 AQSARDSIVEINPLVNV 114
PRK08328 PRK08328
hypothetical protein; Provisional
 6-115 2.28e-07

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 50.56  E-value: 2.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114163    6 INAEEIALYDRQIRLWGFNAQQALKQSRVLLITASPLANEIAKNLVLSGIGKLCVLDSMTVYEKDVEEQFFIEASDIGQL 85
Cdd:PRK08328   2 LSERELERYDRQIMIFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEDLGKN 81

                         90       100       110
                 ....*....|....*....|....*....|...
gi 19114163   86 RANVFKK-KLHELNPLVEIDTDTSLISE--IDE 115
Cdd:PRK08328  82 PKPLSAKwKLERFNSDIKIETFVGRLSEenIDE 114
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 33-140 3.69e-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: 50.43  E-value: 3.69e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114163  33 RVLLITASPLANEIAKNLVLSGIGKLCVLDSMTVYEKDVEEQFFIEASDIGQLRANVFKKKLHELNPLVEIDTDTSLISE 112
Cdd:cd01488   1 KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQD 80

                        90       100
                ....*....|....*....|....*....
gi 19114163 113 IDEGKISKFSMVIATqLDYEEFCR-INEL 140
Cdd:cd01488  81 KDEEFYRQFNIIICG-LDSIEARRwINGT 108
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 14-158 1.88e-06

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 48.57  E-value: 1.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114163   14 YDRQIRLW--GFNAQQALKQSRVLLITASPLANEIAKNLVLSGIGKLCVLDSMTVYEKDVEEQFFIEASDIGQL--RANV 89
Cdd:PRK12475   5 YSRQILFSgiGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTEEDAKQKkpKAIA 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114163   90 FKKKLHELNPLVEIDT-DTSLISEIDEGKISKFSMVIATQLDYEEFCRINELTRICNASFYATSCFGLYG 158
Cdd:PRK12475  85 AKEHLRKINSEVEIVPvVTDVTVEELEELVKEVDLIIDATDNFDTRLLINDLSQKYNIPWIYGGCVGSYG 154
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 33-99 2.03e-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: 2.03e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19114163  33 RVLLITASPLANEIAKNLVLSGIGKLCVLDSMTVYEKDVEEQFFIEASDIGQLRANVFKKKLHELNP 99
Cdd:cd01484   1 KVLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNP 67
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 33-103 3.00e-06

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: 48.14  E-value: 3.00e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19114163  33 RVLLITASPLANEIAKNLVLSGIGKLCVLDSMTVYEKDVEEQFFIEASDIGQLRANVFKKKLHELNPLVEI 103
Cdd:cd01489   1 KVLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKI 71
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 14-105 9.02e-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: 47.19  E-value: 9.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114163     14 YDRQIRLWGFNAQQALKQSRVLLITASPLANEIAKNLVLSGI-----GKLCVLDSMTVYEKDVEEQFFIEASDIGQLRAN 88
Cdd:TIGR01408  402 YDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVgtgkkGMITVTDPDLIEKSNLNRQFLFRPHHIGKPKSY 481

                           90
                   ....*....|....*..
gi 19114163     89 VFKKKLHELNPLVEIDT 105
Cdd:TIGR01408  482 TAADATLKINPQIKIDA 498
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
6-112 2.12e-05

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 45.50  E-value: 2.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114163    6 INAEEIALYDRQIRL--WGFNAQQALKQSRVLLITASPLANEIAKNLVLSGIGKLCVLDSMTVYEKDVEEQFFIEASDIG 83
Cdd:PRK07411  11 LSKDEYERYSRHLILpeVGLEGQKRLKAASVLCIGTGGLGSPLLLYLAAAGIGRIGIVDFDVVDSSNLQRQVIHGTSWVG 90

                         90       100       110
                 ....*....|....*....|....*....|
gi 19114163   84 QLRANVFKKKLHELNPLVEIDT-DTSLISE 112
Cdd:PRK07411  91 KPKIESAKNRILEINPYCQVDLyETRLSSE 120
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 33-182 2.34e-05

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: 43.91  E-value: 2.34e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114163  33 RVLLITASPLANEIAKNLVLSGIGKLCVLDSMTVYEKDVEEQFFIeASDIGQLRANVFKKKLHELNPLVEIDTDTSLISE 112
Cdd:cd01487   1 KVGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQYF-LSQIGEPKVEALKENLREINPFVKIEAINIKIDE 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19114163 113 IDEGKISKFSMVIATQLDyEEFCR---INELTRICNASFYATScfGLYGFAFCDLINH-----NFAIDRVVDNTKVEE 182
Cdd:cd01487  80 NNLEGLFGDCDIVVEAFD-NAETKamlAESLLGNKNKPVVCAS--GMAGFGDSNNIKTkkisdNFYICGDLVNEAKEG 154
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
26-112 3.64e-05

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 44.08  E-value: 3.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114163   26 QQALKQSRVLLITASPLANEIAKNLVLSGIGKLCVLDSmtvyekDVEE-------QFFIeaSDIGQLRANVFKKKLHELN 98
Cdd:PRK08644  23 LEKLKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDF------DVVEpsnlnrqQYFI--SQIGMPKVEALKENLLEIN 94

                         90
                 ....*....|....
gi 19114163   99 PLVEIDTDTSLISE 112
Cdd:PRK08644  95 PFVEIEAHNEKIDE 108
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 14-104 6.10e-05

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 44.21  E-value: 6.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114163   14 YDRQIRLW--GFNAQQALKQSRVLLITASPLANEIAKNLVLSGIGKLCVLDsmtvyeKD-VE------EQFFIEASDIGQ 84
Cdd:PRK07688   5 YSRQELFSpiGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVD------RDyVEwsnlqrQQLYTESDVKNN 78

                         90       100
                 ....*....|....*....|.
gi 19114163   85 L-RANVFKKKLHELNPLVEID 104
Cdd:PRK07688  79 LpKAVAAKKRLEEINSDVRVE 99
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
8-125 8.02e-05

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 43.85  E-value: 8.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114163    8 AEEIALYDRQIRL--WGFNAQQALKQSRVLLITASPLANEIAKNLVLSGIGKLCVLDSMTVYEKDVEEQFFIEASDIGQL 85
Cdd:PRK08762 110 DEQDERYSRHLRLpeVGEEGQRRLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVGQP 189

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 19114163   86 RANVFKKKLHELNPLVEIDT-DTSLISEIDEGKISKFSMVI 125
Cdd:PRK08762 190 KVDSAAQRLAALNPDVQVEAvQERVTSDNVEALLQDVDVVV 230
PRK14851 PRK14851
hypothetical protein; Provisional
 11-104 8.58e-04

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 41.00  E-value: 8.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114163   11 IALYDRQIRLWGFNAQQALKQSRVLLITASPLANEIAKNLVLSGIGKLCVLDsMTVYEK-DVEEQFFIEASDIGQLRANV 89
Cdd:PRK14851  23 EAAFSRNIGLFTPGEQERLAEAKVAIPGMGGVGGVHLITMVRTGIGRFHIAD-FDQFEPvNVNRQFGARVPSFGRPKLAV 101

                         90
                 ....*....|....*
gi 19114163   90 FKKKLHELNPLVEID 104
Cdd:PRK14851 102 MKEQALSINPFLEIT 116
 
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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