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Conserved domains on  [gi|2127877508|ref|YP_010208476|]
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Mg chelatase subunit e (chloroplast) [Pseudo-nitzschia cuspidata]

Protein Classification

ATP-binding protein( domain architecture ID 11414060)

ATP-binding protein with an AAA (ATPases Associated with various cellular Activities) domain, similar to magnesium-chelatase subunit ChlI and RuvB-like helicase 1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
chlI CHL00081
Mg-protoporyphyrin IX chelatase
 1-351 0e+00

Mg-protoporyphyrin IX chelatase


:

Pssm-ID: 177020 [Multi-domain]  Cd Length: 350  Bit Score: 715.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508   1 MVQENSKDFVTPVFPFTAIVGQDEMKLALQLNVIDPKIGGVLIMGDRGTGKSTTIRAIADLLPEIEVVAEDPFNSHPTNL 80
Cdd:CHL00081    1 MVTNNLKKKERPVFPFTAIVGQEEMKLALILNVIDPKIGGVMIMGDRGTGKSTTIRALVDLLPEIEVVKDDPFNSHPSDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508  81 ELMSSEVKSQIQSDSNdIETDFIKIPMIDLPLGATEDRVCGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDH 160
Cdd:CHL00081   81 ELMSDEVREAIQNGET-IETEKIKIPMVDLPLGATEDRVCGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDH 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508 161 LVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPEEGELRPQLLDRFGMQAEIRTVKDPTLRVKVVEERTSFDQTPM 240
Cdd:CHL00081  160 LVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPEEGELRPQLLDRFGMHAEIRTVKDPELRVKIVEQRTSFDKNPQ 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508 241 VWIDKYEQQQQELRDRIVSAQQLLPSVQIDYDLRIKISEVCSRLDVDGLRGDIVTTRAAQAHAAYDNRDKVTVDDIAAII 320
Cdd:CHL00081  240 EFREKYEESQEELRSKIVAAQNLLPKVEIDYDLRVKISQICSELDVDGLRGDIVTNRAAKALAAFEGRTEVTPKDIFKVI 319

                         330       340       350
                  ....*....|....*....|....*....|.
gi 2127877508 321 VLCLRHRLRKDPLESIAEGNKVEKIFKEIFE 351
Cdd:CHL00081  320 TLCLRHRLRKDPLESIDSGDKVQKVFKEVFG 350
 
Name Accession Description Interval E-value
chlI CHL00081
Mg-protoporyphyrin IX chelatase
 1-351 0e+00

Mg-protoporyphyrin IX chelatase


Pssm-ID: 177020 [Multi-domain]  Cd Length: 350  Bit Score: 715.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508   1 MVQENSKDFVTPVFPFTAIVGQDEMKLALQLNVIDPKIGGVLIMGDRGTGKSTTIRAIADLLPEIEVVAEDPFNSHPTNL 80
Cdd:CHL00081    1 MVTNNLKKKERPVFPFTAIVGQEEMKLALILNVIDPKIGGVMIMGDRGTGKSTTIRALVDLLPEIEVVKDDPFNSHPSDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508  81 ELMSSEVKSQIQSDSNdIETDFIKIPMIDLPLGATEDRVCGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDH 160
Cdd:CHL00081   81 ELMSDEVREAIQNGET-IETEKIKIPMVDLPLGATEDRVCGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDH 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508 161 LVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPEEGELRPQLLDRFGMQAEIRTVKDPTLRVKVVEERTSFDQTPM 240
Cdd:CHL00081  160 LVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPEEGELRPQLLDRFGMHAEIRTVKDPELRVKIVEQRTSFDKNPQ 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508 241 VWIDKYEQQQQELRDRIVSAQQLLPSVQIDYDLRIKISEVCSRLDVDGLRGDIVTTRAAQAHAAYDNRDKVTVDDIAAII 320
Cdd:CHL00081  240 EFREKYEESQEELRSKIVAAQNLLPKVEIDYDLRVKISQICSELDVDGLRGDIVTNRAAKALAAFEGRTEVTPKDIFKVI 319

                         330       340       350
                  ....*....|....*....|....*....|.
gi 2127877508 321 VLCLRHRLRKDPLESIAEGNKVEKIFKEIFE 351
Cdd:CHL00081  320 TLCLRHRLRKDPLESIDSGDKVQKVFKEVFG 350
ChlI COG1239
Mg-chelatase subunit ChlI [Coenzyme transport and metabolism];
11-336 0e+00

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


Pssm-ID: 440852 [Multi-domain]  Cd Length: 344  Bit Score: 552.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508  11 TPVFPFTAIVGQDEMKLALQLNVIDPKIGGVLIMGDRGTGKSTTIRAIADLLPEIEVVAEDPFNSHPTNLELMSSEVKSQ 90
Cdd:COG1239     3 RTVFPFTAIVGQEEMKLALLLNAVDPGIGGVLIRGEKGTAKSTAVRALAALLPPIEVVKGCPYNCDPDDPDELCPDCRER 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508  91 IQsDSNDIETDFIKIPMIDLPLGATEDRVCGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSAA 170
Cdd:COG1239    83 LA-AGEELPTETRPVPVVELPLGATEDRVVGSLDLEKALKEGEKAFEPGLLARAHRGILYVDEVNLLDDHLVDVLLDAAA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508 171 SGWNTVEREGISIRHPARFVLVGSGNPEEGELRPQLLDRFGMQAEIRTVKDPTLRVKVVEERTSFDQTPMVWIDKYEQQQ 250
Cdd:COG1239   162 MGRNTVEREGVSVSHPARFVLVGTMNPEEGELRPQLLDRFGLSVEVEGPRDPEERVEIVRRRLAFEADPEAFAAEYAEEQ 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508 251 QELRDRIVSAQQLLPSVQIDYDLRIKISEVCSRLDVDGLRGDIVTTRAAQAHAAYDNRDKVTVDDIAAIIVLCLRHRLRK 330
Cdd:COG1239   242 AELRERIAAARELLPEVTIPDELLRYIAELCIALGVDGHRADIVIARAARALAALEGRTEVTAEDIRRAAELALPHRLRR 321


                  ....*.
gi 2127877508 331 DPLESI 336
Cdd:COG1239   322 DPFEEP 327
BchI-ChlI TIGR02030
magnesium chelatase ATPase subunit I; This model represents one of two ATPase subunits of the ...
 14-350 0e+00

magnesium chelatase ATPase subunit I; This model represents one of two ATPase subunits of the trimeric magnesium chelatase responsible for insertion of magnesium ion into protoporphyrin IX. This is an essential step in the biosynthesis of both chlorophyll and bacteriochlorophyll. This subunit is found in green plants, photosynthetic algae, cyanobacteria and other photosynthetic bacteria. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 131085 [Multi-domain]  Cd Length: 337  Bit Score: 511.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508  14 FPFTAIVGQDEMKLALQLNVIDPKIGGVLIMGDRGTGKSTTIRAIADLLPEIEVVAEDPFNSHPTNLELMSSEVKSQIQS 93
Cdd:TIGR02030   1 FPFTAIVGQDEMKLALLLNVIDPKIGGVMVMGDRGTGKSTAVRALAALLPEIKAVAGCPFNSSPSDPEMMCEEVRIRVDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508  94 dSNDIETDFIKIPMIDLPLGATEDRVCGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGW 173
Cdd:TIGR02030  81 -QEPLSIIKKPVPVVDLPLGATEDRVCGTLDIERALTEGVKAFEPGLLARANRGILYIDEVNLLEDHLVDVLLDVAASGW 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508 174 NTVEREGISIRHPARFVLVGSGNPEEGELRPQLLDRFGMQAEIRTVKDPTLRVKVVEERTSFDQTPMVWIDKYEQQQQEL 253
Cdd:TIGR02030 160 NVVEREGISIRHPARFVLVGSGNPEEGELRPQLLDRFGLHAEIRTVRDVELRVEIVERRTEYDADPHAFCEKWQTEQEAL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508 254 RDRIVSAQQLLPSVQIDYDLRIKISEVCSRLDVDGLRGDIVTTRAAQAHAAYDNRDKVTVDDIAAIIVLCLRHRLRKDPL 333
Cdd:TIGR02030 240 QAKIVNAQNLLPQVTIPYDVLVKVAELCAELDVDGLRGELTLNRAAKALAAFEGRTEVTVDDIRRVAVLALRHRLRKDPL 319

                         330
                  ....*....|....*..
gi 2127877508 334 ESIAEGNKVEKIFKEIF 350
Cdd:TIGR02030 320 ESIDSGSRVERVVKEVL 336
AAA_lid_2 pfam17863
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 277-349 2.47e-18

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: 78.41  E-value: 2.47e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2127877508 277 ISEVCSRLDVDGLRGDIVTTRAAQAHAAYDNRDKVTVDDIAAIIVLCLRHRLRKDPLesiAEGNKVEKIFKEI 349
Cdd:pfam17863   4 RAHLAIALGVSPRRADLALLRAARALAALEGRDYVTPEDVKEAAPLVLAHRLRREPE---AEGETAEEILEEI 73
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 20-211 3.77e-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: 3.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508  20 VGQDEMKLALQLNVIDPKIGGVLIMGDRGTGKSTTIRAIADLLPEIEVvaedpfnshptnlelmssevksqiqsdsndie 99
Cdd:cd00009     1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGA-------------------------------- 48

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508 100 tDFIKIPMIDLPLGAtedrvcgtiDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLdsaasgwNTVERE 179
Cdd:cd00009    49 -PFLYLNASDLLEGL---------VVAELFGHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALL-------RVLETL 111

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2127877508 180 GISIRHPARFVLVGSGN-PEEGELRPQLLDRFG 211
Cdd:cd00009   112 NDLRIDRENVRVIGATNrPLLGDLDRALYDRLD 144
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 39-219 1.26e-04

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: 41.59  E-value: 1.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508   39 GGVLIMGDRGTGKSTTIRAIADLLpeievvaedpfnshptnlelmssevksqiqsdsNDIETDFIKIPMIDLPLGATEDR 118
Cdd:smart00382   3 EVILIVGPPGSGKTTLARALAREL---------------------------------GPPGGGVIYIDGEDILEEVLDQL 49

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508  119 VCGTIDIEKALTEGVKAFEpGLLAKANR---GILYVDEVNLLDDHLVDILLDSAAsgwntVEREGISIRHPARFVLVGSG 195
Cdd:smart00382  50 LLIIVGGKKASGSGELRLR-LALALARKlkpDVLILDEITSLLDAEQEALLLLLE-----ELRLLLLLKSEKNLTVILTT 123

                          170       180
                   ....*....|....*....|....
gi 2127877508  196 NPEEGELRPQLLDRFGMQAEIRTV 219
Cdd:smart00382 124 NDEKDLGPALLRRRFDRRIVLLLI 147
 
Name Accession Description Interval E-value
chlI CHL00081
Mg-protoporyphyrin IX chelatase
 1-351 0e+00

Mg-protoporyphyrin IX chelatase


Pssm-ID: 177020 [Multi-domain]  Cd Length: 350  Bit Score: 715.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508   1 MVQENSKDFVTPVFPFTAIVGQDEMKLALQLNVIDPKIGGVLIMGDRGTGKSTTIRAIADLLPEIEVVAEDPFNSHPTNL 80
Cdd:CHL00081    1 MVTNNLKKKERPVFPFTAIVGQEEMKLALILNVIDPKIGGVMIMGDRGTGKSTTIRALVDLLPEIEVVKDDPFNSHPSDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508  81 ELMSSEVKSQIQSDSNdIETDFIKIPMIDLPLGATEDRVCGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDH 160
Cdd:CHL00081   81 ELMSDEVREAIQNGET-IETEKIKIPMVDLPLGATEDRVCGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDH 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508 161 LVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPEEGELRPQLLDRFGMQAEIRTVKDPTLRVKVVEERTSFDQTPM 240
Cdd:CHL00081  160 LVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPEEGELRPQLLDRFGMHAEIRTVKDPELRVKIVEQRTSFDKNPQ 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508 241 VWIDKYEQQQQELRDRIVSAQQLLPSVQIDYDLRIKISEVCSRLDVDGLRGDIVTTRAAQAHAAYDNRDKVTVDDIAAII 320
Cdd:CHL00081  240 EFREKYEESQEELRSKIVAAQNLLPKVEIDYDLRVKISQICSELDVDGLRGDIVTNRAAKALAAFEGRTEVTPKDIFKVI 319

                         330       340       350
                  ....*....|....*....|....*....|.
gi 2127877508 321 VLCLRHRLRKDPLESIAEGNKVEKIFKEIFE 351
Cdd:CHL00081  320 TLCLRHRLRKDPLESIDSGDKVQKVFKEVFG 350
ChlI COG1239
Mg-chelatase subunit ChlI [Coenzyme transport and metabolism];
11-336 0e+00

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


Pssm-ID: 440852 [Multi-domain]  Cd Length: 344  Bit Score: 552.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508  11 TPVFPFTAIVGQDEMKLALQLNVIDPKIGGVLIMGDRGTGKSTTIRAIADLLPEIEVVAEDPFNSHPTNLELMSSEVKSQ 90
Cdd:COG1239     3 RTVFPFTAIVGQEEMKLALLLNAVDPGIGGVLIRGEKGTAKSTAVRALAALLPPIEVVKGCPYNCDPDDPDELCPDCRER 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508  91 IQsDSNDIETDFIKIPMIDLPLGATEDRVCGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSAA 170
Cdd:COG1239    83 LA-AGEELPTETRPVPVVELPLGATEDRVVGSLDLEKALKEGEKAFEPGLLARAHRGILYVDEVNLLDDHLVDVLLDAAA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508 171 SGWNTVEREGISIRHPARFVLVGSGNPEEGELRPQLLDRFGMQAEIRTVKDPTLRVKVVEERTSFDQTPMVWIDKYEQQQ 250
Cdd:COG1239   162 MGRNTVEREGVSVSHPARFVLVGTMNPEEGELRPQLLDRFGLSVEVEGPRDPEERVEIVRRRLAFEADPEAFAAEYAEEQ 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508 251 QELRDRIVSAQQLLPSVQIDYDLRIKISEVCSRLDVDGLRGDIVTTRAAQAHAAYDNRDKVTVDDIAAIIVLCLRHRLRK 330
Cdd:COG1239   242 AELRERIAAARELLPEVTIPDELLRYIAELCIALGVDGHRADIVIARAARALAALEGRTEVTAEDIRRAAELALPHRLRR 321


                  ....*.
gi 2127877508 331 DPLESI 336
Cdd:COG1239   322 DPFEEP 327
BchI-ChlI TIGR02030
magnesium chelatase ATPase subunit I; This model represents one of two ATPase subunits of the ...
 14-350 0e+00

magnesium chelatase ATPase subunit I; This model represents one of two ATPase subunits of the trimeric magnesium chelatase responsible for insertion of magnesium ion into protoporphyrin IX. This is an essential step in the biosynthesis of both chlorophyll and bacteriochlorophyll. This subunit is found in green plants, photosynthetic algae, cyanobacteria and other photosynthetic bacteria. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 131085 [Multi-domain]  Cd Length: 337  Bit Score: 511.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508  14 FPFTAIVGQDEMKLALQLNVIDPKIGGVLIMGDRGTGKSTTIRAIADLLPEIEVVAEDPFNSHPTNLELMSSEVKSQIQS 93
Cdd:TIGR02030   1 FPFTAIVGQDEMKLALLLNVIDPKIGGVMVMGDRGTGKSTAVRALAALLPEIKAVAGCPFNSSPSDPEMMCEEVRIRVDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508  94 dSNDIETDFIKIPMIDLPLGATEDRVCGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGW 173
Cdd:TIGR02030  81 -QEPLSIIKKPVPVVDLPLGATEDRVCGTLDIERALTEGVKAFEPGLLARANRGILYIDEVNLLEDHLVDVLLDVAASGW 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508 174 NTVEREGISIRHPARFVLVGSGNPEEGELRPQLLDRFGMQAEIRTVKDPTLRVKVVEERTSFDQTPMVWIDKYEQQQQEL 253
Cdd:TIGR02030 160 NVVEREGISIRHPARFVLVGSGNPEEGELRPQLLDRFGLHAEIRTVRDVELRVEIVERRTEYDADPHAFCEKWQTEQEAL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508 254 RDRIVSAQQLLPSVQIDYDLRIKISEVCSRLDVDGLRGDIVTTRAAQAHAAYDNRDKVTVDDIAAIIVLCLRHRLRKDPL 333
Cdd:TIGR02030 240 QAKIVNAQNLLPQVTIPYDVLVKVAELCAELDVDGLRGELTLNRAAKALAAFEGRTEVTVDDIRRVAVLALRHRLRKDPL 319

                         330
                  ....*....|....*..
gi 2127877508 334 ESIAEGNKVEKIFKEIF 350
Cdd:TIGR02030 320 ESIDSGSRVERVVKEVL 336
Cob-chelat-sub TIGR02442
cobaltochelatase subunit; Cobaltochelatase is responsible for the insertion of cobalt into the ...
 14-335 1.58e-148

cobaltochelatase subunit; Cobaltochelatase is responsible for the insertion of cobalt into the corrin ring of coenzyme B12 during its biosynthesis. Two versions have been well described. CbiK/CbiX is a monomeric, anaerobic version which acts early in the biosynthesis (pfam06180). CobNST is a trimeric, ATP-dependent, aerobic version which acts late in the biosynthesis (TIGR02257/TIGR01650/TIGR01651). A number of genomes (actinobacteria, cyanobacteria, betaproteobacteria and pseudomonads) which apparently biosynthesize B12, encode a cobN gene but are demonstrably lacking cobS and cobT. These genomes do, however contain a homolog (modelled here) of the magnesium chelatase subunits BchI/BchD family. Aside from the cyanobacteria (which have a separate magnesium chelatase trimer), these species do not make chlorins, so do not have any use for a magnesium chelatase. Furthermore, in nearly all cases the members of this family are proximal to either CobN itself or other genes involved in cobalt transport or B12 biosynthesis.


Pssm-ID: 274135 [Multi-domain]  Cd Length: 633  Bit Score: 432.96  E-value: 1.58e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508  14 FPFTAIVGQDEMKLALQLNVIDPKIGGVLIMGDRGTGKSTTIRAIADLLPEIEVVAEDPFNSHPTNLELMSSEVKSQIQS 93
Cdd:TIGR02442   1 FPFTAIVGQEDLKLALLLNAVDPRIGGVLIRGEKGTAKSTAARGLAALLPPIDVVAGCPFSCDPDDPEEWCEECRRKYRP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508  94 DSNdietdfIKIPMIDLPLGATEDRVCGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGW 173
Cdd:TIGR02442  81 SEQ------RPVPFVNLPLGATEDRVVGSLDIERALREGEKAFQPGLLAEAHRGILYIDEVNLLDDHLVDVLLDAAAMGV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508 174 NTVEREGISIRHPARFVLVGSGNPEEGELRPQLLDRFGMQAEIRTVKDPTLRVKVVEERTSFDQTPMVWIDKYEQQQQEL 253
Cdd:TIGR02442 155 NRVEREGLSVSHPARFVLIGTMNPEEGDLRPQLLDRFGLCVDVAAPRDPEERVEIIRRRLAFDADPEAFAARWAAEQEEL 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508 254 RDRIVSAQQLLPSVQIDYDLRIKISEVCSRLDVDGLRGDIVTTRAAQAHAAYDNRDKVTVDDIAAIIVLCLRHRLRKDPL 333
Cdd:TIGR02442 235 RNRIARARSLLPSVRISDSLIRFISELCIEFGVDGHRADIVMARAARALAALDGRRRVTAEDVREAAELVLPHRRRRKPF 314


                  ..
gi 2127877508 334 ES 335
Cdd:TIGR02442 315 EQ 316
AAA_lid_2 pfam17863
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 277-349 2.47e-18

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: 78.41  E-value: 2.47e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2127877508 277 ISEVCSRLDVDGLRGDIVTTRAAQAHAAYDNRDKVTVDDIAAIIVLCLRHRLRKDPLesiAEGNKVEKIFKEI 349
Cdd:pfam17863   4 RAHLAIALGVSPRRADLALLRAARALAALEGRDYVTPEDVKEAAPLVLAHRLRREPE---AEGETAEEILEEI 73
bchD PRK13406
magnesium chelatase subunit D; Provisional
 106-327 1.35e-17

magnesium chelatase subunit D; Provisional


Pssm-ID: 237378 [Multi-domain]  Cd Length: 584  Bit Score: 83.92  E-value: 1.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508 106 PMIDLPLGATEDRVCGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRH 185
Cdd:PRK13406   54 PLRRLPPGIADDRLLGGLDLAATLRAGRPVAQRGLLAEADGGVLVLAMAERLEPGTAARLAAALDTGEVRLERDGLALRL 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508 186 PARFVLVG--SGNPEEGELRPQLLDRFGMQAEIRTVkdptlrvkvveertSFDQTPMVWIDKyeqqqqelrDRIVSAQQL 263
Cdd:PRK13406  134 PARFGLVAldEGAEEDERAPAALADRLAFHLDLDGL--------------ALRDAREIPIDA---------DDIAAARAR 190

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2127877508 264 LPSVQIDYDLRIKISEVCSRLDVDGLRGDIVTTRAAQAHAAYDNRDKVTVDDIAAIIVLCLRHR 327
Cdd:PRK13406  191 LPAVGPPPEAIAALCAAAAALGIASLRAPLLALRAARAAAALAGRTAVEEEDLALAARLVLAPR 254
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 17-343 4.18e-10

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: 59.80  E-value: 4.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508  17 TAIVGQDEMK----LALQLNvidpkiGGVLIMGDRGTGKSTTIRAIADLLpeievvaedpfnshptnlelmssevksqiq 92
Cdd:COG0714    12 KVYVGQEELIelvlIALLAG------GHLLLEGVPGVGKTTLAKALARAL------------------------------ 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508  93 sdsndiETDFIKIPmidlplgATED----RVCGTIDIEKAltEGVKAFEPG-LLAkanrGILYVDEVN---------LL- 157
Cdd:COG0714    56 ------GLPFIRIQ-------FTPDllpsDILGTYIYDQQ--TGEFEFRPGpLFA----NVLLADEINrappktqsaLLe 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508 158 --DDHLVDIlldsaasgwntverEGISIRHPARFVLVGSGNPEEGE----LRPQLLDRFGMQAEIRTVKDPTLRvKVVEE 231
Cdd:COG0714   117 amEERQVTI--------------PGGTYKLPEPFLVIATQNPIEQEgtypLPEAQLDRFLLKLYIGYPDAEEER-EILRR 181

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508 232 RTSFDQtpmvwidkyEQQQQEL-RDRIVSAQQLLPSVQIDYDLRIKISEVCSRL----DVD---GLRGDIVTTRAAQAHA 303
Cdd:COG0714   182 HTGRHL---------AEVEPVLsPEELLALQELVRQVHVSEAVLDYIVDLVRATrehpDLRkgpSPRASIALLRAARALA 252

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 2127877508 304 AYDNRDKVTVDDIAAIIVLCLRHRLRKDPlESIAEGNKVE 343
Cdd:COG0714   253 LLDGRDYVTPDDVKAVAGPVLKHRLILSP-EADAEGVTAD 291
PRK09862 PRK09862
ATP-dependent protease;
8-216 3.89e-09

ATP-dependent protease;


Pssm-ID: 182120 [Multi-domain]  Cd Length: 506  Bit Score: 57.68  E-value: 3.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508   8 DFVTPVFP--FTAIVGQDEMKLALQLNVIdpkiGG--VLIMGDRGTGKSTTIRAIADLLPeievvaedPFNSHPTnleLM 83
Cdd:PRK09862  180 DAVSRALQhdLSDVIGQEQGKRGLEITAA----GGhnLLLIGPPGTGKTMLASRINGLLP--------DLSNEEA---LE 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508  84 SSEVKSQIQSDSndIETDFIKIPMIDLPLGATedrVCgtidiekALTEGVKAFEPGLLAKANRGILYVDEVNLLDDHLVD 163
Cdd:PRK09862  245 SAAILSLVNAES--VQKQWRQRPFRSPHHSAS---LT-------AMVGGGAIPGPGEISLAHNGVLFLDELPEFERRTLD 312

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2127877508 164 ILLDSAASGWNTVEREGISIRHPARFVLVGSGNPEE--------------------GELRPQLLDRFGMQAEI 216
Cdd:PRK09862  313 ALREPIESGQIHLSRTRAKITYPARFQLVAAMNPSPtghyqgnhnrctpeqtlrylNRLSGPFLDRFDLSLEI 385
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 20-211 3.77e-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: 3.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508  20 VGQDEMKLALQLNVIDPKIGGVLIMGDRGTGKSTTIRAIADLLPEIEVvaedpfnshptnlelmssevksqiqsdsndie 99
Cdd:cd00009     1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGA-------------------------------- 48

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508 100 tDFIKIPMIDLPLGAtedrvcgtiDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLdsaasgwNTVERE 179
Cdd:cd00009    49 -PFLYLNASDLLEGL---------VVAELFGHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALL-------RVLETL 111

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2127877508 180 GISIRHPARFVLVGSGN-PEEGELRPQLLDRFG 211
Cdd:cd00009   112 NDLRIDRENVRVIGATNrPLLGDLDRALYDRLD 144
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
 19-224 1.40e-05

Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that catalyzes the insertion of Mg2+ into protoporphyrin IX. This is the first unique step in the synthesis of (bacterio)chlorophyll. Due to this, it is thought that Mg-chelatase has an important role in channelling inter- mediates into the (bacterio)chlorophyll branch in response to conditions suitable for photosynthetic growth. ChlI and BchD have molecular weight between 38-42 kDa.


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 45.60  E-value: 1.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508  19 IVGQDEMKLALQLNVIdpkiGG--VLIMGDRGTGKSTTIRAIADLLPEievvaedpfnshPTNLELMssEVkSQIQSDSN 96
Cdd:pfam01078   5 VKGQEQAKRALEIAAA----GGhnLLMIGPPGSGKTMLAKRLPGILPP------------LTEAEAL--EV-TAIHSVAG 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508  97 -DIETDFIKIPmidlPLGA---TEDRVcgtidiekALTEGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSAASG 172
Cdd:pfam01078  66 lGGDGGLIRRR----PFRAphhSASAA--------ALVGGGSIPRPGEISLAHNGVLFLDELPEFKRRVLESLRQPLEDG 133

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2127877508 173 WNTVEREGISIRHPARFVLVGSGNP----------EEGELRPQ------------LLDRFGMQAEIRTVKDPTL 224
Cdd:pfam01078 134 EITISRARAKVTFPARFQLVAAMNPcpcgylgdpnKRCRCSPRqirrylsrlsgpLLDRIDLQVEVPRLPGEEL 207
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 39-219 1.26e-04

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: 41.59  E-value: 1.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508   39 GGVLIMGDRGTGKSTTIRAIADLLpeievvaedpfnshptnlelmssevksqiqsdsNDIETDFIKIPMIDLPLGATEDR 118
Cdd:smart00382   3 EVILIVGPPGSGKTTLARALAREL---------------------------------GPPGGGVIYIDGEDILEEVLDQL 49

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508  119 VCGTIDIEKALTEGVKAFEpGLLAKANR---GILYVDEVNLLDDHLVDILLDSAAsgwntVEREGISIRHPARFVLVGSG 195
Cdd:smart00382  50 LLIIVGGKKASGSGELRLR-LALALARKlkpDVLILDEITSLLDAEQEALLLLLE-----ELRLLLLLKSEKNLTVILTT 123

                          170       180
                   ....*....|....*....|....
gi 2127877508  196 NPEEGELRPQLLDRFGMQAEIRTV 219
Cdd:smart00382 124 NDEKDLGPALLRRRFDRRIVLLLI 147
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
 41-63 1.45e-03

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).


Pssm-ID: 213190 [Multi-domain]  Cd Length: 166  Bit Score: 39.06  E-value: 1.45e-03
                          10        20
                  ....*....|....*....|...
gi 2127877508  41 VLIMGDRGTGKSTTIRAIADLLP 63
Cdd:cd03223    30 LLITGPSGTGKSSLFRALAGLWP 52
MCM cd17706
MCM helicase family; MCM helicases are a family of helicases that play an important role in ...
 137-320 2.98e-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: 2.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508 137 EPGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPEEG------------ELRP 204
Cdd:cd17706    97 EAGALVLADGGVCCIDEFDKMKELDRTALHEAMEQQTISIAKAGIVTTLNARCSILAAANPKGGrynpklspieniNLPS 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877508 205 QLLDRFGMQAEIRTVKDP----TLRVKVVEERTSFDQTPMVW--IDKYEQQQQELRDRIVSAQQLLPsvQIDYDLRIKIS 278
Cdd:cd17706   177 PLLSRFDLIFVIRDDPDEerdeELAEHIIDLHRGSDPEEQVKpeEDGIPIDIELLRKYILYARQIHP--KISEEAREKLV 254

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2127877508 279 E--VCSRLDVDGLRGDIVTTRA-------AQAHAAYDNRDKVTVDDIAAII 320
Cdd:cd17706   255 RwyVELRKESERRSTIPITARQlesvirlAEAHAKMRLSEVVTEEDVEEAI 305
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
 40-63 4.10e-03

ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 39.02  E-value: 4.10e-03
                          10        20
                  ....*....|....*....|....
gi 2127877508  40 GVLIMGDRGTGKSTTIRAIADLLP 63
Cdd:COG4178   391 RLLITGPSGSGKSTLLRAIAGLWP 414
 
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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