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Conserved domains on  [gi|518172521|ref|WP_019342729|]
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MoxR family ATPase [Stutzerimonas stutzeri]

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 ...
 9-307 1.42e-142

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: 403.78  E-value: 1.42e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172521   9 ALRHFLSTQILGQERLIERLLIALLADGHMLVEGAPGLAKTRAIKELAGGLEAEFHRIQFTPDLLPADITGTEIYRPETG 88
Cdd:COG0714    5 RLRAEIGKVYVGQEELIELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDQQTG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172521  89 SFVFQQGPIFHNLVLADEINRAPAKVQSALLEAMAERQVSVGRSTYDLSPLFLVMATQNPIEQEGTYPLPEAQLDRFLLH 168
Cdd:COG0714   85 EFEFRPGPLFANVLLADEINRAPPKTQSALLEAMEERQVTIPGGTYKLPEPFLVIATQNPIEQEGTYPLPEAQLDRFLLK 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172521 169 VKLGFPDASVERRILQQARGEAINgETAPEhrVSQQAIFAARKEILGLYMADAVEEYLVQLVMATRTPAkfdaelagWIA 248
Cdd:COG0714  165 LYIGYPDAEEEREILRRHTGRHLA-EVEPV--LSPEELLALQELVRQVHVSEAVLDYIVDLVRATREHP--------DLR 233

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 518172521 249 YGSSPRGSISLDRCARGHAWLAGRDFVSPEDIQAVLFDVLRHRLILSFEAEAAGIDQDR 307
Cdd:COG0714  234 KGPSPRASIALLRAARALALLDGRDYVTPDDVKAVAGPVLKHRLILSPEADAEGVTADD 292
 
Name Accession Description Interval E-value
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 9-307 1.42e-142

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: 403.78  E-value: 1.42e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172521   9 ALRHFLSTQILGQERLIERLLIALLADGHMLVEGAPGLAKTRAIKELAGGLEAEFHRIQFTPDLLPADITGTEIYRPETG 88
Cdd:COG0714    5 RLRAEIGKVYVGQEELIELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDQQTG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172521  89 SFVFQQGPIFHNLVLADEINRAPAKVQSALLEAMAERQVSVGRSTYDLSPLFLVMATQNPIEQEGTYPLPEAQLDRFLLH 168
Cdd:COG0714   85 EFEFRPGPLFANVLLADEINRAPPKTQSALLEAMEERQVTIPGGTYKLPEPFLVIATQNPIEQEGTYPLPEAQLDRFLLK 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172521 169 VKLGFPDASVERRILQQARGEAINgETAPEhrVSQQAIFAARKEILGLYMADAVEEYLVQLVMATRTPAkfdaelagWIA 248
Cdd:COG0714  165 LYIGYPDAEEEREILRRHTGRHLA-EVEPV--LSPEELLALQELVRQVHVSEAVLDYIVDLVRATREHP--------DLR 233

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 518172521 249 YGSSPRGSISLDRCARGHAWLAGRDFVSPEDIQAVLFDVLRHRLILSFEAEAAGIDQDR 307
Cdd:COG0714  234 KGPSPRASIALLRAARALALLDGRDYVTPDDVKAVAGPVLKHRLILSPEADAEGVTADD 292
AAA_3 pfam07726
ATPase family associated with various cellular activities (AAA); This Pfam entry includes some ...
 37-167 4.43e-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: 257.10  E-value: 4.43e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172521   37 HMLVEGAPGLAKTRAIKELAGGLEAEFHRIQFTPDLLPADITGTEIYRPETGSFVFQQGPIFHNLVLADEINRAPAKVQS 116
Cdd:pfam07726   1 HVLLEGVPGLAKTLLVRTLARSLGLDFRRIQFTPDLLPSDITGTEVFDQKTREFEFRPGPVFANVLLADEINRAPPKTQS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 518172521  117 ALLEAMAERQVSVGRSTYDLSPLFLVMATQNPIEQEGTYPLPEAQLDRFLL 167
Cdd:pfam07726  81 ALLEAMQERQVTIDGETHPLPEPFFVLATQNPIEQEGTYPLPEAQLDRFLM 131
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 20-172 5.79e-06

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: 45.60  E-value: 5.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172521  20 GQERLIERLLIALLAD--GHMLVEGAPGLAKTRAIKELAGGLEAEFHRIQFtpdLLPADITGTEIYRPETGSFVFQQGPI 97
Cdd:cd00009    2 GQEEAIEALREALELPppKNLLLYGPPGTGKTTLARAIANELFRPGAPFLY---LNASDLLEGLVVAELFGHFLVRLLFE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172521  98 F-----HNLVLADEINRAPAKVQSALLEAMAErqvsVGRSTYDLSPLFLVMATQNPIEQEgtypLPEAQLDRFLLHVKLG 172
Cdd:cd00009   79 LaekakPGVLFIDEIDSLSRGAQNALLRVLET----LNDLRIDRENVRVIGATNRPLLGD----LDRALYDRLDIRIVIP 150
chlI CHL00081
Mg-protoporyphyrin IX chelatase
 254-292 7.40e-05

Mg-protoporyphyrin IX chelatase


Pssm-ID: 177020 [Multi-domain]  Cd Length: 350  Bit Score: 43.82  E-value: 7.40e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 518172521 254 RGSISLDRCARGHAWLAGRDFVSPEDIQAVLFDVLRHRL 292
Cdd:CHL00081 289 RGDIVTNRAAKALAAFEGRTEVTPKDIFKVITLCLRHRL 327
MCM smart00350
minichromosome maintenance proteins;
85-281 6.76e-03

minichromosome maintenance proteins;


Pssm-ID: 214631 [Multi-domain]  Cd Length: 509  Bit Score: 38.01  E-value: 6.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172521    85 PETGSFVFQQGPifhnLVLAD-------EINRAPAKVQSALLEAMAERQVSVGRS--TYDLSPLFLVMATQNPIEqeGTY 155
Cdd:smart00350 284 PETREFTLEAGA----LVLADngvccidEFDKMDDSDRTAIHEAMEQQTISIAKAgiTTTLNARCSVLAAANPIG--GRY 357

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172521   156 ----------PLPEAQLDRF-LLHVKLGFPDASVERRI----LQQARGEAINGETAPEHRVSQQAI---FAARKEILGLY 217
Cdd:smart00350 358 dpkltpeeniDLPAPILSRFdLLFVVLDEVDEERDRELakhvVDLHRYSHPEEDEAFEPPLSQEKLrkyIAYAREKIKPK 437

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518172521   218 MADAVEEYLVQLVMATRtpaKFDAELAGWIAYGSSPRGSISLDRCARGHAWLAGRDFVSPEDIQ 281
Cdd:smart00350 438 LSEEAADKLVKAYVDLR---KEDSQTESRSSIPITVRQLESIIRLSEAHAKMRLSDVVEEADVE 498
 
Name Accession Description Interval E-value
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 9-307 1.42e-142

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: 403.78  E-value: 1.42e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172521   9 ALRHFLSTQILGQERLIERLLIALLADGHMLVEGAPGLAKTRAIKELAGGLEAEFHRIQFTPDLLPADITGTEIYRPETG 88
Cdd:COG0714    5 RLRAEIGKVYVGQEELIELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDQQTG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172521  89 SFVFQQGPIFHNLVLADEINRAPAKVQSALLEAMAERQVSVGRSTYDLSPLFLVMATQNPIEQEGTYPLPEAQLDRFLLH 168
Cdd:COG0714   85 EFEFRPGPLFANVLLADEINRAPPKTQSALLEAMEERQVTIPGGTYKLPEPFLVIATQNPIEQEGTYPLPEAQLDRFLLK 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172521 169 VKLGFPDASVERRILQQARGEAINgETAPEhrVSQQAIFAARKEILGLYMADAVEEYLVQLVMATRTPAkfdaelagWIA 248
Cdd:COG0714  165 LYIGYPDAEEEREILRRHTGRHLA-EVEPV--LSPEELLALQELVRQVHVSEAVLDYIVDLVRATREHP--------DLR 233

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 518172521 249 YGSSPRGSISLDRCARGHAWLAGRDFVSPEDIQAVLFDVLRHRLILSFEAEAAGIDQDR 307
Cdd:COG0714  234 KGPSPRASIALLRAARALALLDGRDYVTPDDVKAVAGPVLKHRLILSPEADAEGVTADD 292
AAA_3 pfam07726
ATPase family associated with various cellular activities (AAA); This Pfam entry includes some ...
 37-167 4.43e-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: 257.10  E-value: 4.43e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172521   37 HMLVEGAPGLAKTRAIKELAGGLEAEFHRIQFTPDLLPADITGTEIYRPETGSFVFQQGPIFHNLVLADEINRAPAKVQS 116
Cdd:pfam07726   1 HVLLEGVPGLAKTLLVRTLARSLGLDFRRIQFTPDLLPSDITGTEVFDQKTREFEFRPGPVFANVLLADEINRAPPKTQS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 518172521  117 ALLEAMAERQVSVGRSTYDLSPLFLVMATQNPIEQEGTYPLPEAQLDRFLL 167
Cdd:pfam07726  81 ALLEAMQERQVTIDGETHPLPEPFFVLATQNPIEQEGTYPLPEAQLDRFLM 131
AAA_lid_2 pfam17863
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 247-312 2.17e-14

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: 67.24  E-value: 2.17e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518172521  247 IAYGSSP-RGSISLDRCARGHAWLAGRDFVSPEDIQAVLFDVLRHRLIlsFEAEAAGIDQDRVLQRI 312
Cdd:pfam17863   9 IALGVSPrRADLALLRAARALAALEGRDYVTPEDVKEAAPLVLAHRLR--REPEAEGETAEEILEEI 73
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 37-165 6.55e-12

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: 61.92  E-value: 6.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172521   37 HMLVEGAPGLAKTRAIKELAGGLE-AEFHRIQFTPDLLPADITGteIYRPETGSFVFQQGPIF------HNLVLaDEINR 109
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSnRPVFYVQLTRDTTEEDLFG--RRNIDPGGASWVDGPLVraaregEIAVL-DEINR 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 518172521  110 APAKVQSALLEAMAERQVSVGRST---YDLSPLFLVMATQNPIEQEGTyPLPEAQLDRF 165
Cdd:pfam07728  78 ANPDVLNSLLSLLDERRLLLPDGGelvKAAPDGFRLIATMNPLDRGLN-ELSPALRSRF 135
bpMoxR pfam20030
MoxR domain in the MoxR-vWA-beta-propeller ternary systems; Core MoxR component domain of the ...
 9-170 4.45e-11

MoxR domain in the MoxR-vWA-beta-propeller ternary systems; Core MoxR component domain of the MoxR-vWA-beta-propeller ternary systems, a class of NTP-dependent biological conflict systems.


Pssm-ID: 437862 [Multi-domain]  Cd Length: 205  Bit Score: 61.10  E-value: 4.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172521    9 ALRHfLSTQILGQERLIERLLIALLADGHMLVEGAPGLAKTRAIKELAGGLEA---EFHRIQFT-PDLL--PADI----- 77
Cdd:pfam20030   6 VLRP-LKTGFVGKDEIIDLLGLALVARENLFLLGPPGTAKSALVRRLAARLGGryfEYLLTRFTePNELfgPFDIrklre 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172521   78 ----TGTEIYRPEtGSFVFqqgpifhnlvlADEINRAPAKVQSALLEAMAERQVSVGRSTYDLsPLFLVMATQNpieqeg 153
Cdd:pfam20030  85 gelvTNTEGMLPE-ASLVF-----------LDELFNANSAILNSLLMVLNERIFRRGKETRKL-PALMFVGASN------ 145

                         170       180
                  ....*....|....*....|..
gi 518172521  154 tyPLPE-----AQLDRFLLHVK 170
Cdd:pfam20030 146 --HLPEdealaALFDRFLLRVK 165
ChlI COG1239
Mg-chelatase subunit ChlI [Coenzyme transport and metabolism];
105-292 2.46e-09

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


Pssm-ID: 440852 [Multi-domain]  Cd Length: 344  Bit Score: 57.45  E-value: 2.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172521 105 DEINRAPAKVQSALLEAMA------ERQ-VSV---GRstydlsplFLVMATQNPIEQEgtypLPEAQLDRFLLHVKLGFP 174
Cdd:COG1239  143 DEVNLLDDHLVDVLLDAAAmgrntvEREgVSVshpAR--------FVLVGTMNPEEGE----LRPQLLDRFGLSVEVEGP 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172521 175 D------ASVERRILQQARGEAINGETAPEHRVSQQAIFAARKEILGLYMADAVEEYLVQLVMAtrtpakFDAElagwia 248
Cdd:COG1239  211 RdpeervEIVRRRLAFEADPEAFAAEYAEEQAELRERIAAARELLPEVTIPDELLRYIAELCIA------LGVD------ 278

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 518172521 249 ygsSPRGSISLDRCARGHAWLAGRDFVSPEDIQAVLFDVLRHRL 292
Cdd:COG1239  279 ---GHRADIVIARAARALAALEGRTEVTAEDIRRAAELALPHRL 319
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 20-172 5.79e-06

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: 45.60  E-value: 5.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172521  20 GQERLIERLLIALLAD--GHMLVEGAPGLAKTRAIKELAGGLEAEFHRIQFtpdLLPADITGTEIYRPETGSFVFQQGPI 97
Cdd:cd00009    2 GQEEAIEALREALELPppKNLLLYGPPGTGKTTLARAIANELFRPGAPFLY---LNASDLLEGLVVAELFGHFLVRLLFE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172521  98 F-----HNLVLADEINRAPAKVQSALLEAMAErqvsVGRSTYDLSPLFLVMATQNPIEQEgtypLPEAQLDRFLLHVKLG 172
Cdd:cd00009   79 LaekakPGVLFIDEIDSLSRGAQNALLRVLET----LNDLRIDRENVRVIGATNRPLLGD----LDRALYDRLDIRIVIP 150
chlI CHL00081
Mg-protoporyphyrin IX chelatase
 254-292 7.40e-05

Mg-protoporyphyrin IX chelatase


Pssm-ID: 177020 [Multi-domain]  Cd Length: 350  Bit Score: 43.82  E-value: 7.40e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 518172521 254 RGSISLDRCARGHAWLAGRDFVSPEDIQAVLFDVLRHRL 292
Cdd:CHL00081 289 RGDIVTNRAAKALAAFEGRTEVTPKDIFKVITLCLRHRL 327
MCM4 cd17755
DNA replication licensing factor Mcm4; Mcm4 is a helicase that play an important role in ...
 85-281 2.33e-04

DNA replication licensing factor Mcm4; Mcm4 is a helicase that play an important role in replication. It is part of the heterohexameric ring-shaped Mcm2-7 complex, which 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.


Pssm-ID: 350661 [Multi-domain]  Cd Length: 309  Bit Score: 42.42  E-value: 2.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172521  85 PETGSFVFQQGPifhnLVLAD-------EINRAPAKVQSALLEAMAERQVSVGRS--TYDLSPLFLVMATQNPIEQE--- 152
Cdd:cd17755   90 PDTKQLVLESGA----LVLSDggiccidEFDKMSDSTRSVLHEVMEQQTLSIAKAgiITTLNARTSILASANPIGSRynp 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172521 153 -----GTYPLPEAQLDRF-LLHVKLGFPDASVERRILQ-------QARGEAINGETAPEHrVSQQAIFAARKEILGLYMA 219
Cdd:cd17755  166 kltvvENIDLPPTLLSRFdLIYLVLDKVDEKYDRRLAKhlvslylEDTPEHIQDEVLDVE-VLTDYISYAREHIHPKLSE 244

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518172521 220 DAVEEyLVQLVMATRtpaKFDAELAGWIAygSSPRGSISLDRCARGHAWLAGRDFVSPEDIQ 281
Cdd:cd17755  245 EAAQE-LVQAYVDMR---KMGSDARKRIT--ATPRQLESLIRLAEAHAKMRLSNVVEAEDVE 300
MCM cd17706
MCM helicase family; MCM helicases are a family of helicases that play an important role in ...
 34-290 2.89e-04

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: 41.94  E-value: 2.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172521  34 ADGHMLVEGAPGLAKTRAIKELAGgleaEFHRIQFTP--DLLPADITGTEIYRPETGSFVFQQGPifhnLVLA------- 104
Cdd:cd17706   40 GDIHILLVGDPGTAKSQILKYVLK----IAPRGVYTSgkGSSGAGLTAAVVRDSETGEWYLEAGA----LVLAdggvcci 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172521 105 DEINRAPAKVQSALLEAMaERQ---VSVGRSTYDLSPLFLVMATQNPIeqEGTYP----------LPEAQLDRF-LLHVK 170
Cdd:cd17706  112 DEFDKMKELDRTALHEAM-EQQtisIAKAGIVTTLNARCSILAAANPK--GGRYNpklspieninLPSPLLSRFdLIFVI 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172521 171 LGFP----DASVERRILQQARGEAINGETAPEHRVSQQAIFAARKEIlgLY-------MADAVEEYLVQLVMATRTpakf 239
Cdd:cd17706  189 RDDPdeerDEELAEHIIDLHRGSDPEEQVKPEEDGIPIDIELLRKYI--LYarqihpkISEEAREKLVRWYVELRK---- 262

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 518172521 240 daELAGWIAYGSSPRGSISLDRCARGHAWLAGRDFVSPEDIQAVLfDVLRH 290
Cdd:cd17706  263 --ESERRSTIPITARQLESVIRLAEAHAKMRLSEVVTEEDVEEAI-RLVRH 310
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 22-114 3.41e-03

5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 38.98  E-value: 3.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172521  22 ERLIERLLIALLADGHMLVEGAPGLAKTRAIKELA---GGLEAE-FHRIQFTPDL-LPADITGteiYRPET--GSFVFQQ 94
Cdd:COG1401  208 EETLEAFLAALKTKKNVILAGPPGTGKTYLARRLAealGGEDNGrIEFVQFHPSWsYEDFLLG---YRPSLdeGKYEPTP 284

                         90       100       110
                 ....*....|....*....|....*....|...
gi 518172521  95 GPIFHNLVLA------------DEINRA-PAKV 114
Cdd:COG1401  285 GIFLRFCLKAeknpdkpyvliiDEINRAnVEKY 317
MCM6 cd17757
DNA replication licensing factor Mcm6; Mcm6 is a helicase that play an important role in ...
 30-194 5.99e-03

DNA replication licensing factor Mcm6; Mcm6 is a helicase that play an important role in replication. It is part of the heterohexameric ring-shaped Mcm2-7 complex, which 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.


Pssm-ID: 350663 [Multi-domain]  Cd Length: 307  Bit Score: 37.73  E-value: 5.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172521  30 IALLADGHMLVEGAPGLAKTRAIKELAggleaEFH-RIQFTP--DLLPADITGTEIYRPETGSFVFQQGPifhnLVLAD- 105
Cdd:cd17757   36 ISLRGDINVCIVGDPSTAKSQFLKYVE-----EFSpRAVYTSgkASSAAGLTAAVVRDEETGDFVIEAGA----LMLADn 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172521 106 ------EINRAPAKVQSALLEAMAERQVSVGRS--TYDLSPLFLVMATQNPIeqEGTYP----------LPEAQLDRF-L 166
Cdd:cd17757  107 giccidEFDKMDIKDQVAIHEAMEQQTISITKAgiQATLNARTSILAAANPV--GGRYDrskslkqninISAPIMSRFdL 184

                        170       180       190
                 ....*....|....*....|....*....|....
gi 518172521 167 LHVKLGFPDASVERRI------LQQARGEAINGE 194
Cdd:cd17757  185 FFVLLDECNEVTDYAIashivdLHSKREEAIEPP 218
MCM smart00350
minichromosome maintenance proteins;
85-281 6.76e-03

minichromosome maintenance proteins;


Pssm-ID: 214631 [Multi-domain]  Cd Length: 509  Bit Score: 38.01  E-value: 6.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172521    85 PETGSFVFQQGPifhnLVLAD-------EINRAPAKVQSALLEAMAERQVSVGRS--TYDLSPLFLVMATQNPIEqeGTY 155
Cdd:smart00350 284 PETREFTLEAGA----LVLADngvccidEFDKMDDSDRTAIHEAMEQQTISIAKAgiTTTLNARCSVLAAANPIG--GRY 357

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172521   156 ----------PLPEAQLDRF-LLHVKLGFPDASVERRI----LQQARGEAINGETAPEHRVSQQAI---FAARKEILGLY 217
Cdd:smart00350 358 dpkltpeeniDLPAPILSRFdLLFVVLDEVDEERDRELakhvVDLHRYSHPEEDEAFEPPLSQEKLrkyIAYAREKIKPK 437

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518172521   218 MADAVEEYLVQLVMATRtpaKFDAELAGWIAYGSSPRGSISLDRCARGHAWLAGRDFVSPEDIQ 281
Cdd:smart00350 438 LSEEAADKLVKAYVDLR---KEDSQTESRSSIPITVRQLESIIRLSEAHAKMRLSDVVEEADVE 498
 
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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