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Conserved domains on  [gi|1920112197|ref|WP_193522447|]
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MULTISPECIES: MoxR family ATPase [Pseudoalteromonas]

Protein Classification

AAA family ATPase( domain architecture ID 11431245)

AAA family ATPase with an AAA (ATPases Associated with various cellular Activities) domain functions as a modulator of stress response pathways and may have a chaperone-like role for the maturation of specific protein complexes or for the insertion of cofactors into proteins; similar to MoxR that is involved in the formation of active methanol dehydrogenase

CATH:  3.40.50.300
Gene Ontology:  GO:0005524|GO:0016887
PubMed:  16072036|11916378|15037234|17897320|18466635
SCOP:  2000039

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 1-289 4.66e-136

MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


:

Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 386.45  E-value: 4.66e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920112197   1 MNEEikKLTDALSTVILEKPEQIKLAICSLLCRGHLLIEDLPGMGKTTLSHSLADVLGLTYRRVQFTSDLLPADITGTSI 80
Cdd:COG0714     1 MTEA--RLRAEIGKVYVGQEELIELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920112197  81 FNREHQSFEFHPGPIFSQVLLADEINRASPKTQSALLESMEEHQVTIDGVSHELPSPFFVIATQNPQHQSGTHPLPESQL 160
Cdd:COG0714    79 YDQQTGEFEFRPGPLFANVLLADEINRAPPKTQSALLEAMEERQVTIPGGTYKLPEPFLVIATQNPIEQEGTYPLPEAQL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920112197 161 DRFFMRISLGYPSEMAEAQLIKLAGkARKLTQAPQVIDGKTLLAYQQVVPNIVLSDAIIDYILRLVNYTRSSGQFSDPLS 240
Cdd:COG0714   159 DRFLLKLYIGYPDAEEEREILRRHT-GRHLAEVEPVLSPEELLALQELVRQVHVSEAVLDYIVDLVRATREHPDLRKGPS 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1920112197 241 PRASIALAAASRAYAFISGRDFVIPDDVQAVFTSVCAHRLGVTTTNEAE 289
Cdd:COG0714   238 PRASIALLRAARALALLDGRDYVTPDDVKAVAGPVLKHRLILSPEADAE 286
 
Name Accession Description Interval E-value
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 1-289 4.66e-136

MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 386.45  E-value: 4.66e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920112197   1 MNEEikKLTDALSTVILEKPEQIKLAICSLLCRGHLLIEDLPGMGKTTLSHSLADVLGLTYRRVQFTSDLLPADITGTSI 80
Cdd:COG0714     1 MTEA--RLRAEIGKVYVGQEELIELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920112197  81 FNREHQSFEFHPGPIFSQVLLADEINRASPKTQSALLESMEEHQVTIDGVSHELPSPFFVIATQNPQHQSGTHPLPESQL 160
Cdd:COG0714    79 YDQQTGEFEFRPGPLFANVLLADEINRAPPKTQSALLEAMEERQVTIPGGTYKLPEPFLVIATQNPIEQEGTYPLPEAQL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920112197 161 DRFFMRISLGYPSEMAEAQLIKLAGkARKLTQAPQVIDGKTLLAYQQVVPNIVLSDAIIDYILRLVNYTRSSGQFSDPLS 240
Cdd:COG0714   159 DRFLLKLYIGYPDAEEEREILRRHT-GRHLAEVEPVLSPEELLALQELVRQVHVSEAVLDYIVDLVRATREHPDLRKGPS 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1920112197 241 PRASIALAAASRAYAFISGRDFVIPDDVQAVFTSVCAHRLGVTTTNEAE 289
Cdd:COG0714   238 PRASIALLRAARALALLDGRDYVTPDDVKAVAGPVLKHRLILSPEADAE 286
AAA_3 pfam07726
ATPase family associated with various cellular activities (AAA); This Pfam entry includes some ...
 35-165 5.81e-87

ATPase family associated with various cellular activities (AAA); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 429622 [Multi-domain]  Cd Length: 131  Bit Score: 255.95  E-value: 5.81e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920112197  35 HLLIEDLPGMGKTTLSHSLADVLGLTYRRVQFTSDLLPADITGTSIFNREHQSFEFHPGPIFSQVLLADEINRASPKTQS 114
Cdd:pfam07726   1 HVLLEGVPGLAKTLLVRTLARSLGLDFRRIQFTPDLLPSDITGTEVFDQKTREFEFRPGPVFANVLLADEINRAPPKTQS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1920112197 115 ALLESMEEHQVTIDGVSHELPSPFFVIATQNPQHQSGTHPLPESQLDRFFM 165
Cdd:pfam07726  81 ALLEAMQERQVTIDGETHPLPEPFFVLATQNPIEQEGTYPLPEAQLDRFLM 131
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 21-171 3.25e-07

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 49.07  E-value: 3.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920112197  21 EQIKLAICSLLCR---GHLLIEDLPGMGKTTLSHSLADVLGLTYRRV------QFTSDLLPADITGTSIFNREHQSFEFH 91
Cdd:cd00009     4 EEAIEALREALELpppKNLLLYGPPGTGKTTLARAIANELFRPGAPFlylnasDLLEGLVVAELFGHFLVRLLFELAEKA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920112197  92 PGPIfsqvLLADEINRASPKTQSALLESMEEHQVTIDGVSHElpspFFVIATQNPQHQsgthPLPESQLDRFFMRISLGY 171
Cdd:cd00009    84 KPGV----LFIDEIDSLSRGAQNALLRVLETLNDLRIDRENV----RVIGATNRPLLG----DLDRALYDRLDIRIVIPL 151
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
21-127 3.49e-04

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 41.65  E-value: 3.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920112197  21 EQIKLAICSLLCRG----HLLIEDLPGMGKTTLSHSLADVLGLTYRrvqFTS-DLL--PADITG--TSIfnrehqsfefH 91
Cdd:PRK00080   35 ENLKIFIEAAKKRGealdHVLLYGPPGLGKTTLANIIANEMGVNIR---ITSgPALekPGDLAAilTNL----------E 101

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1920112197  92 PGpifsQVLLADEINRASPKTQSALLESMEEHQVTI 127
Cdd:PRK00080  102 EG----DVLFIDEIHRLSPVVEEILYPAMEDFRLDI 133
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 33-167 1.64e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 38.12  E-value: 1.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920112197   33 RGHLLIEDLPGMGKTTLSHSLADVLGLTYRRVQFTSdllPADITGTSIFNREHQSFEFHPGPIFS--------------- 97
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYID---GEDILEEVLDQLLLIIVGGKKASGSGelrlrlalalarklk 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1920112197   98 -QVLLADEINRASPKTQSALLESMEEHQVTIdgvSHELPSPFFVIATQNPQHQSGTHPLpesqLDRFFMRI 167
Cdd:smart00382  79 pDVLILDEITSLLDAEQEALLLLLEELRLLL---LLKSEKNLTVILTTNDEKDLGPALL----RRRFDRRI 142
 
Name Accession Description Interval E-value
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 1-289 4.66e-136

MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 386.45  E-value: 4.66e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920112197   1 MNEEikKLTDALSTVILEKPEQIKLAICSLLCRGHLLIEDLPGMGKTTLSHSLADVLGLTYRRVQFTSDLLPADITGTSI 80
Cdd:COG0714     1 MTEA--RLRAEIGKVYVGQEELIELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920112197  81 FNREHQSFEFHPGPIFSQVLLADEINRASPKTQSALLESMEEHQVTIDGVSHELPSPFFVIATQNPQHQSGTHPLPESQL 160
Cdd:COG0714    79 YDQQTGEFEFRPGPLFANVLLADEINRAPPKTQSALLEAMEERQVTIPGGTYKLPEPFLVIATQNPIEQEGTYPLPEAQL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920112197 161 DRFFMRISLGYPSEMAEAQLIKLAGkARKLTQAPQVIDGKTLLAYQQVVPNIVLSDAIIDYILRLVNYTRSSGQFSDPLS 240
Cdd:COG0714   159 DRFLLKLYIGYPDAEEEREILRRHT-GRHLAEVEPVLSPEELLALQELVRQVHVSEAVLDYIVDLVRATREHPDLRKGPS 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1920112197 241 PRASIALAAASRAYAFISGRDFVIPDDVQAVFTSVCAHRLGVTTTNEAE 289
Cdd:COG0714   238 PRASIALLRAARALALLDGRDYVTPDDVKAVAGPVLKHRLILSPEADAE 286
AAA_3 pfam07726
ATPase family associated with various cellular activities (AAA); This Pfam entry includes some ...
 35-165 5.81e-87

ATPase family associated with various cellular activities (AAA); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 429622 [Multi-domain]  Cd Length: 131  Bit Score: 255.95  E-value: 5.81e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920112197  35 HLLIEDLPGMGKTTLSHSLADVLGLTYRRVQFTSDLLPADITGTSIFNREHQSFEFHPGPIFSQVLLADEINRASPKTQS 114
Cdd:pfam07726   1 HVLLEGVPGLAKTLLVRTLARSLGLDFRRIQFTPDLLPSDITGTEVFDQKTREFEFRPGPVFANVLLADEINRAPPKTQS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1920112197 115 ALLESMEEHQVTIDGVSHELPSPFFVIATQNPQHQSGTHPLPESQLDRFFM 165
Cdd:pfam07726  81 ALLEAMQERQVTIDGETHPLPEPFFVLATQNPIEQEGTYPLPEAQLDRFLM 131
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 35-163 1.64e-13

AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 66.16  E-value: 1.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920112197  35 HLLIEDLPGMGKTTLSHSLADVL-GLTYRRVQFTSDLLPADITGtsIFNREHQSFEFHPGPIF-----SQVLLADEINRA 108
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALsNRPVFYVQLTRDTTEEDLFG--RRNIDPGGASWVDGPLVraareGEIAVLDEINRA 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1920112197 109 SPKTQSALLESMEE---HQVTIDGVSHELPSPFFVIATQNPQHQSGtHPLPESQLDRF 163
Cdd:pfam07728  79 NPDVLNSLLSLLDErrlLLPDGGELVKAAPDGFRLIATMNPLDRGL-NELSPALRSRF 135
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 21-171 3.25e-07

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 49.07  E-value: 3.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920112197  21 EQIKLAICSLLCR---GHLLIEDLPGMGKTTLSHSLADVLGLTYRRV------QFTSDLLPADITGTSIFNREHQSFEFH 91
Cdd:cd00009     4 EEAIEALREALELpppKNLLLYGPPGTGKTTLARAIANELFRPGAPFlylnasDLLEGLVVAELFGHFLVRLLFELAEKA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920112197  92 PGPIfsqvLLADEINRASPKTQSALLESMEEHQVTIDGVSHElpspFFVIATQNPQHQsgthPLPESQLDRFFMRISLGY 171
Cdd:cd00009    84 KPGV----LFIDEIDSLSRGAQNALLRVLETLNDLRIDRENV----RVIGATNRPLLG----DLDRALYDRLDIRIVIPL 151
AAA_lid_2 pfam17863
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 256-280 9.32e-07

AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains.


Pssm-ID: 465538 [Multi-domain]  Cd Length: 73  Bit Score: 45.67  E-value: 9.32e-07
                          10        20
                  ....*....|....*....|....*
gi 1920112197 256 FISGRDFVIPDDVQAVFTSVCAHRL 280
Cdd:pfam17863  31 ALEGRDYVTPEDVKEAAPLVLAHRL 55
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
 21-127 3.62e-05

Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the RuvABC revolvasome which catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. Branch migration is catalyzed by the RuvB protein that is targeted to the Holliday junction by the structure specific RuvA protein. This family contains the N-terminal region of the protein.


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 43.26  E-value: 3.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920112197  21 EQIKLAICSLLCRG----HLLIEDLPGMGKTTLSHSLADVLGLTYRrvqFTSDLL---PADITG--TSIFNREhqsfefh 91
Cdd:pfam05496  17 ENLKIFIEAAKQRGealdHVLLYGPPGLGKTTLANIIANEMGVNIR---ITSGPAierPGDLAAilTNLEPGD------- 86

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1920112197  92 pgpifsqVLLADEINRASPKTQSALLESMEEHQVTI 127
Cdd:pfam05496  87 -------VLFIDEIHRLNRAVEEILYPAMEDFRLDI 115
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 42-171 8.23e-05

ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 41.42  E-value: 8.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920112197  42 PGMGKTTLSHSLADVLGLTYRRVQftsdllPADITGTSIFNRE---HQSFE--FHPGPIfsqVLLADEINRASPK----- 111
Cdd:pfam00004   7 PGTGKTTLAKAVAKELGAPFIEIS------GSELVSKYVGESEkrlRELFEaaKKLAPC---VIFIDEIDALAGSrgsgg 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920112197 112 ------TQSALLESMEEHQVTIDGVshelpspFFVIATQNPQHqsgthpLPESQLDRFFMRISLGY 171
Cdd:pfam00004  78 dsesrrVVNQLLTELDGFTSSNSKV-------IVIAATNRPDK------LDPALLGRFDRIIEFPL 130
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
21-127 3.49e-04

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 41.65  E-value: 3.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920112197  21 EQIKLAICSLLCRG----HLLIEDLPGMGKTTLSHSLADVLGLTYRrvqFTS-DLL--PADITG--TSIfnrehqsfefH 91
Cdd:PRK00080   35 ENLKIFIEAAKKRGealdHVLLYGPPGLGKTTLANIIANEMGVNIR---ITSgPALekPGDLAAilTNL----------E 101

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1920112197  92 PGpifsQVLLADEINRASPKTQSALLESMEEHQVTI 127
Cdd:PRK00080  102 EG----DVLFIDEIHRLSPVVEEILYPAMEDFRLDI 133
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 42-141 6.40e-04

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 40.84  E-value: 6.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920112197  42 PGMGKTTLSHSLADVLGLTYRRVQFTSDLLpADITgtSIFNREHQSFEFHPGPIfsqvLLADEINRASPKTQSALLESME 121
Cdd:PRK13342   45 PGTGKTTLARIIAGATDAPFEALSAVTSGV-KDLR--EVIEEARQRRSAGRRTI----LFIDEIHRFNKAQQDALLPHVE 117

                          90       100
                  ....*....|....*....|
gi 1920112197 122 EHQVTIDGVSHElpSPFFVI 141
Cdd:PRK13342  118 DGTITLIGATTE--NPSFEV 135
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 33-167 1.64e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 38.12  E-value: 1.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920112197   33 RGHLLIEDLPGMGKTTLSHSLADVLGLTYRRVQFTSdllPADITGTSIFNREHQSFEFHPGPIFS--------------- 97
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYID---GEDILEEVLDQLLLIIVGGKKASGSGelrlrlalalarklk 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1920112197   98 -QVLLADEINRASPKTQSALLESMEEHQVTIdgvSHELPSPFFVIATQNPQHQSGTHPLpesqLDRFFMRI 167
Cdd:smart00382  79 pDVLILDEITSLLDAEQEALLLLLEELRLLL---LLKSEKNLTVILTTNDEKDLGPALL----RRRFDRRI 142
MCM cd17706
MCM helicase family; MCM helicases are a family of helicases that play an important role in ...
 99-163 2.99e-03

MCM helicase family; MCM helicases are a family of helicases that play an important role in replication and homologous recombination repair. The heterohexameric ring-shaped Mcm2-7 complex is part of the replicative helicase that unwinds parental double-stranded DNA at a replication fork to provide single-stranded DNA templates for the replicative polymerases. Mcm8 and Mcm9, form a complex required for homologous recombination (HR) repair induced by DNA interstrand crosslinks (ICLs).


Pssm-ID: 350658 [Multi-domain]  Cd Length: 311  Bit Score: 38.86  E-value: 2.99e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920112197  99 VLLADEINRASPKTQSALLESMEEHQVTID--GVSHELPSPFFVIATQNP---QHQSGTHP-----LPESQLDRF 163
Cdd:cd17706   108 VCCIDEFDKMKELDRTALHEAMEQQTISIAkaGIVTTLNARCSILAAANPkggRYNPKLSPieninLPSPLLSRF 182
ChlI COG1239
Mg-chelatase subunit ChlI [Coenzyme transport and metabolism];
90-280 5.35e-03

Mg-chelatase subunit ChlI [Coenzyme transport and metabolism];


Pssm-ID: 440852 [Multi-domain]  Cd Length: 344  Bit Score: 37.81  E-value: 5.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920112197  90 FHPGpifsqvLLA---------DEINRASPKTQSALLESMEEHQVTI--DGVSHELPSPFFVIATQNPQHQsgthPLPES 158
Cdd:COG1239   127 FEPG------LLArahrgilyvDEVNLLDDHLVDVLLDAAAMGRNTVerEGVSVSHPARFVLVGTMNPEEG----ELRPQ 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920112197 159 QLDRFFMRISLGYPSEMAE-AQLIKLA--------GKARKLTQAPQVIDGKTLLAyQQVVPNIVLSDAIIDYILRLVNYT 229
Cdd:COG1239   197 LLDRFGLSVEVEGPRDPEErVEIVRRRlafeadpeAFAAEYAEEQAELRERIAAA-RELLPEVTIPDELLRYIAELCIAL 275

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1920112197 230 RSSGQfsdplspRASIALAAASRAYAFISGRDFVIPDDVQAVFTSVCAHRL 280
Cdd:COG1239   276 GVDGH-------RADIVIARAARALAALEGRTEVTAEDIRRAAELALPHRL 319
 
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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