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Conserved domains on  [gi|1557899041|gb|QAA92031|]
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Mg-protoporyphyrin IX chelatase, partial (plastid) [Hemiselmis tepida]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
chlI super family cl31777
Mg-protoporyphyrin IX chelatase
1-279 0e+00

Mg-protoporyphyrin IX chelatase


The actual alignment was detected with superfamily member CHL00081:

Pssm-ID: 177020 [Multi-domain]  Cd Length: 350  Bit Score: 551.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899041   1 IGGVIIMGDRGTGKSTTIRAITDILPEIQIVEDDPFNSDPTDLELMSDEVRRSIENGEDIKVTSTKVPMVDLPLGATEDR 80
Cdd:CHL00081   38 IGGVMIMGDRGTGKSTTIRALVDLLPEIEVVKDDPFNSHPSDPELMSDEVREAIQNGETIETEKIKIPMVDLPLGATEDR 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899041  81 VCGTIDIEKALTEGVKAFEPGLLAKANRGLLYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPE 160
Cdd:CHL00081  118 VCGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPE 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899041 161 EGELRPQLLDRFGMHSEIRTVRDPELRVQIVEQRSDFDKNPEECLTRYQEQQDNFKKTITEAQKLLSQTNIDYALRVKIS 240
Cdd:CHL00081  198 EGELRPQLLDRFGMHAEIRTVKDPELRVKIVEQRTSFDKNPQEFREKYEESQEELRSKIVAAQNLLPKVEIDYDLRVKIS 277
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1557899041 241 QVCGELDVDGLRGDIVTNRAARAYAAYEGRTEVTVEDIQ 279
Cdd:CHL00081  278 QICSELDVDGLRGDIVTNRAAKALAAFEGRTEVTPKDIF 316
 
Name Accession Description Interval E-value
chlI CHL00081
Mg-protoporyphyrin IX chelatase
1-279 0e+00

Mg-protoporyphyrin IX chelatase


Pssm-ID: 177020 [Multi-domain]  Cd Length: 350  Bit Score: 551.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899041   1 IGGVIIMGDRGTGKSTTIRAITDILPEIQIVEDDPFNSDPTDLELMSDEVRRSIENGEDIKVTSTKVPMVDLPLGATEDR 80
Cdd:CHL00081   38 IGGVMIMGDRGTGKSTTIRALVDLLPEIEVVKDDPFNSHPSDPELMSDEVREAIQNGETIETEKIKIPMVDLPLGATEDR 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899041  81 VCGTIDIEKALTEGVKAFEPGLLAKANRGLLYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPE 160
Cdd:CHL00081  118 VCGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPE 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899041 161 EGELRPQLLDRFGMHSEIRTVRDPELRVQIVEQRSDFDKNPEECLTRYQEQQDNFKKTITEAQKLLSQTNIDYALRVKIS 240
Cdd:CHL00081  198 EGELRPQLLDRFGMHAEIRTVKDPELRVKIVEQRTSFDKNPQEFREKYEESQEELRSKIVAAQNLLPKVEIDYDLRVKIS 277
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1557899041 241 QVCGELDVDGLRGDIVTNRAARAYAAYEGRTEVTVEDIQ 279
Cdd:CHL00081  278 QICSELDVDGLRGDIVTNRAAKALAAFEGRTEVTPKDIF 316
ChlI COG1239
Mg-chelatase subunit ChlI [Coenzyme transport and metabolism];
1-279 2.34e-160

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


Pssm-ID: 440852 [Multi-domain]  Cd Length: 344  Bit Score: 449.20  E-value: 2.34e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899041   1 IGGVIIMGDRGTGKSTTIRAITDILPEIQIVEDDPFNSDPTDLELMSDEVRRSIENGEDIKVTSTKVPMVDLPLGATEDR 80
Cdd:COG1239    30 IGGVLIRGEKGTAKSTAVRALAALLPPIEVVKGCPYNCDPDDPDELCPDCRERLAAGEELPTETRPVPVVELPLGATEDR 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899041  81 VCGTIDIEKALTEGVKAFEPGLLAKANRGLLYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPE 160
Cdd:COG1239   110 VVGSLDLEKALKEGEKAFEPGLLARAHRGILYVDEVNLLDDHLVDVLLDAAAMGRNTVEREGVSVSHPARFVLVGTMNPE 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899041 161 EGELRPQLLDRFGMHSEIRTVRDPELRVQIVEQRSDFDKNPEECLTRYQEQQDNFKKTITEAQKLLSQTNIDYALRVKIS 240
Cdd:COG1239   190 EGELRPQLLDRFGLSVEVEGPRDPEERVEIVRRRLAFEADPEAFAAEYAEEQAELRERIAAARELLPEVTIPDELLRYIA 269
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1557899041 241 QVCGELDVDGLRGDIVTNRAARAYAAYEGRTEVTVEDIQ 279
Cdd:COG1239   270 ELCIALGVDGHRADIVIARAARALAALEGRTEVTAEDIR 308
BchI-ChlI TIGR02030
magnesium chelatase ATPase subunit I; This model represents one of two ATPase subunits of the ...
1-279 5.74e-143

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: 405.04  E-value: 5.74e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899041   1 IGGVIIMGDRGTGKSTTIRAITDILPEIQIVEDDPFNSDPTDLELMSDEVRRSIENGEDIKVTSTKVPMVDLPLGATEDR 80
Cdd:TIGR02030  25 IGGVMVMGDRGTGKSTAVRALAALLPEIKAVAGCPFNSSPSDPEMMCEEVRIRVDSQEPLSIIKKPVPVVDLPLGATEDR 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899041  81 VCGTIDIEKALTEGVKAFEPGLLAKANRGLLYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPE 160
Cdd:TIGR02030 105 VCGTLDIERALTEGVKAFEPGLLARANRGILYIDEVNLLEDHLVDVLLDVAASGWNVVEREGISIRHPARFVLVGSGNPE 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899041 161 EGELRPQLLDRFGMHSEIRTVRDPELRVQIVEQRSDFDKNPEECLTRYQEQQDNFKKTITEAQKLLSQTNIDYALRVKIS 240
Cdd:TIGR02030 185 EGELRPQLLDRFGLHAEIRTVRDVELRVEIVERRTEYDADPHAFCEKWQTEQEALQAKIVNAQNLLPQVTIPYDVLVKVA 264
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1557899041 241 QVCGELDVDGLRGDIVTNRAARAYAAYEGRTEVTVEDIQ 279
Cdd:TIGR02030 265 ELCAELDVDGLRGELTLNRAAKALAAFEGRTEVTVDDIR 303
MCM cd17706
MCM helicase family; MCM helicases are a family of helicases that play an important role in ...
4-228 1.39e-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: 39.63  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899041   4 VIIMGDRGTGKSTTIRAITDILPeiqiveddpfnsdptdlelmsdevrRSIengediKVTSTKVPMVDLPLGATEDRVCG 83
Cdd:cd17706    44 ILLVGDPGTAKSQILKYVLKIAP-------------------------RGV------YTSGKGSSGAGLTAAVVRDSETG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899041  84 TIdiekaltegvkAFEPGLLAKANRGLLYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPEEG- 162
Cdd:cd17706    93 EW-----------YLEAGALVLADGGVCCIDEFDKMKELDRTALHEAMEQQTISIAKAGIVTTLNARCSILAAANPKGGr 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899041 163 -----------ELRPQLLDRFGMHSEIRTVRDPE----------------LRVQIVEQRSDFDKNPEECLTRYQEQQDNF 215
Cdd:cd17706   162 ynpklspieniNLPSPLLSRFDLIFVIRDDPDEErdeelaehiidlhrgsDPEEQVKPEEDGIPIDIELLRKYILYARQI 241
                         250
                  ....*....|....
gi 1557899041 216 KKTIT-EAQKLLSQ 228
Cdd:cd17706   242 HPKISeEAREKLVR 255
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
2-182 2.71e-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: 37.35  E-value: 2.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899041    2 GGVIIMGDRGTGKSTTIRAItdilpeiqiveddpfnsdptdlelmsdeVRRSIENGEDIKVTStkvpMVDLPLGATEDRV 81
Cdd:smart00382   3 EVILIVGPPGSGKTTLARAL----------------------------ARELGPPGGGVIYID----GEDILEEVLDQLL 50
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899041   82 CGTIDIEKALTEGVKAFEpGLLAKANR---GLLYVDEVNLLDDHLVDILLDSAAsgwntVEREGISIRHPARFVLVGSGN 158
Cdd:smart00382  51 LIIVGGKKASGSGELRLR-LALALARKlkpDVLILDEITSLLDAEQEALLLLLE-----ELRLLLLLKSEKNLTVILTTN 124
                          170       180
                   ....*....|....*....|....
gi 1557899041  159 PEEGELRPQLLDRFGMHSEIRTVR 182
Cdd:smart00382 125 DEKDLGPALLRRRFDRRIVLLLIL 148
 
Name Accession Description Interval E-value
chlI CHL00081
Mg-protoporyphyrin IX chelatase
1-279 0e+00

Mg-protoporyphyrin IX chelatase


Pssm-ID: 177020 [Multi-domain]  Cd Length: 350  Bit Score: 551.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899041   1 IGGVIIMGDRGTGKSTTIRAITDILPEIQIVEDDPFNSDPTDLELMSDEVRRSIENGEDIKVTSTKVPMVDLPLGATEDR 80
Cdd:CHL00081   38 IGGVMIMGDRGTGKSTTIRALVDLLPEIEVVKDDPFNSHPSDPELMSDEVREAIQNGETIETEKIKIPMVDLPLGATEDR 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899041  81 VCGTIDIEKALTEGVKAFEPGLLAKANRGLLYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPE 160
Cdd:CHL00081  118 VCGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPE 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899041 161 EGELRPQLLDRFGMHSEIRTVRDPELRVQIVEQRSDFDKNPEECLTRYQEQQDNFKKTITEAQKLLSQTNIDYALRVKIS 240
Cdd:CHL00081  198 EGELRPQLLDRFGMHAEIRTVKDPELRVKIVEQRTSFDKNPQEFREKYEESQEELRSKIVAAQNLLPKVEIDYDLRVKIS 277
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1557899041 241 QVCGELDVDGLRGDIVTNRAARAYAAYEGRTEVTVEDIQ 279
Cdd:CHL00081  278 QICSELDVDGLRGDIVTNRAAKALAAFEGRTEVTPKDIF 316
ChlI COG1239
Mg-chelatase subunit ChlI [Coenzyme transport and metabolism];
1-279 2.34e-160

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


Pssm-ID: 440852 [Multi-domain]  Cd Length: 344  Bit Score: 449.20  E-value: 2.34e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899041   1 IGGVIIMGDRGTGKSTTIRAITDILPEIQIVEDDPFNSDPTDLELMSDEVRRSIENGEDIKVTSTKVPMVDLPLGATEDR 80
Cdd:COG1239    30 IGGVLIRGEKGTAKSTAVRALAALLPPIEVVKGCPYNCDPDDPDELCPDCRERLAAGEELPTETRPVPVVELPLGATEDR 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899041  81 VCGTIDIEKALTEGVKAFEPGLLAKANRGLLYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPE 160
Cdd:COG1239   110 VVGSLDLEKALKEGEKAFEPGLLARAHRGILYVDEVNLLDDHLVDVLLDAAAMGRNTVEREGVSVSHPARFVLVGTMNPE 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899041 161 EGELRPQLLDRFGMHSEIRTVRDPELRVQIVEQRSDFDKNPEECLTRYQEQQDNFKKTITEAQKLLSQTNIDYALRVKIS 240
Cdd:COG1239   190 EGELRPQLLDRFGLSVEVEGPRDPEERVEIVRRRLAFEADPEAFAAEYAEEQAELRERIAAARELLPEVTIPDELLRYIA 269
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1557899041 241 QVCGELDVDGLRGDIVTNRAARAYAAYEGRTEVTVEDIQ 279
Cdd:COG1239   270 ELCIALGVDGHRADIVIARAARALAALEGRTEVTAEDIR 308
BchI-ChlI TIGR02030
magnesium chelatase ATPase subunit I; This model represents one of two ATPase subunits of the ...
1-279 5.74e-143

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: 405.04  E-value: 5.74e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899041   1 IGGVIIMGDRGTGKSTTIRAITDILPEIQIVEDDPFNSDPTDLELMSDEVRRSIENGEDIKVTSTKVPMVDLPLGATEDR 80
Cdd:TIGR02030  25 IGGVMVMGDRGTGKSTAVRALAALLPEIKAVAGCPFNSSPSDPEMMCEEVRIRVDSQEPLSIIKKPVPVVDLPLGATEDR 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899041  81 VCGTIDIEKALTEGVKAFEPGLLAKANRGLLYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPE 160
Cdd:TIGR02030 105 VCGTLDIERALTEGVKAFEPGLLARANRGILYIDEVNLLEDHLVDVLLDVAASGWNVVEREGISIRHPARFVLVGSGNPE 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899041 161 EGELRPQLLDRFGMHSEIRTVRDPELRVQIVEQRSDFDKNPEECLTRYQEQQDNFKKTITEAQKLLSQTNIDYALRVKIS 240
Cdd:TIGR02030 185 EGELRPQLLDRFGLHAEIRTVRDVELRVEIVERRTEYDADPHAFCEKWQTEQEALQAKIVNAQNLLPQVTIPYDVLVKVA 264
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1557899041 241 QVCGELDVDGLRGDIVTNRAARAYAAYEGRTEVTVEDIQ 279
Cdd:TIGR02030 265 ELCAELDVDGLRGELTLNRAAKALAAFEGRTEVTVDDIR 303
Cob-chelat-sub TIGR02442
cobaltochelatase subunit; Cobaltochelatase is responsible for the insertion of cobalt into the ...
1-279 3.20e-117

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: 349.76  E-value: 3.20e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899041   1 IGGVIIMGDRGTGKSTTIRAITDILPEIQIVEDDPFNSDPTDLELMSDEVRRSIENGEdikvtSTKVPMVDLPLGATEDR 80
Cdd:TIGR02442  25 IGGVLIRGEKGTAKSTAARGLAALLPPIDVVAGCPFSCDPDDPEEWCEECRRKYRPSE-----QRPVPFVNLPLGATEDR 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899041  81 VCGTIDIEKALTEGVKAFEPGLLAKANRGLLYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPE 160
Cdd:TIGR02442 100 VVGSLDIERALREGEKAFQPGLLAEAHRGILYIDEVNLLDDHLVDVLLDAAAMGVNRVEREGLSVSHPARFVLIGTMNPE 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899041 161 EGELRPQLLDRFGMHSEIRTVRDPELRVQIVEQRSDFDKNPEECLTRYQEQQDNFKKTITEAQKLLSQTNIDYALRVKIS 240
Cdd:TIGR02442 180 EGDLRPQLLDRFGLCVDVAAPRDPEERVEIIRRRLAFDADPEAFAARWAAEQEELRNRIARARSLLPSVRISDSLIRFIS 259
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1557899041 241 QVCGELDVDGLRGDIVTNRAARAYAAYEGRTEVTVEDIQ 279
Cdd:TIGR02442 260 ELCIEFGVDGHRADIVMARAARALAALDGRRRVTAEDVR 298
bchD PRK13406
magnesium chelatase subunit D; Provisional
68-278 2.09e-10

magnesium chelatase subunit D; Provisional


Pssm-ID: 237378 [Multi-domain]  Cd Length: 584  Bit Score: 60.81  E-value: 2.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899041  68 PMVDLPLGATEDRVCGTIDIEKALTEGVKAFEPGLLAKANRGLLYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRH 147
Cdd:PRK13406   54 PLRRLPPGIADDRLLGGLDLAATLRAGRPVAQRGLLAEADGGVLVLAMAERLEPGTAARLAAALDTGEVRLERDGLALRL 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899041 148 PARFVLVG--SGNPEEGELRPQLLDRFGMHSEIRTVRDPELRvqiveqrsDFDKNPEEcltryqeqqdnfkktITEAQKL 225
Cdd:PRK13406  134 PARFGLVAldEGAEEDERAPAALADRLAFHLDLDGLALRDAR--------EIPIDADD---------------IAAARAR 190
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1557899041 226 LSQTNIDYALRVKISQVCGELDVDGLRGDIVTNRAARAYAAYEGRTEVTVEDI 278
Cdd:PRK13406  191 LPAVGPPPEAIAALCAAAAALGIASLRAPLLALRAARAAAALAGRTAVEEEDL 243
PRK09862 PRK09862
ATP-dependent protease;
99-178 6.08e-05

ATP-dependent protease;


Pssm-ID: 182120 [Multi-domain]  Cd Length: 506  Bit Score: 44.20  E-value: 6.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899041  99 EPGLLAKANRGLLYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPEE----------------- 161
Cdd:PRK09862  286 GPGEISLAHNGVLFLDELPEFERRTLDALREPIESGQIHLSRTRAKITYPARFQLVAAMNPSPtghyqgnhnrctpeqtl 365
                          90       100
                  ....*....|....*....|
gi 1557899041 162 ---GELRPQLLDRFGMHSEI 178
Cdd:PRK09862  366 rylNRLSGPFLDRFDLSLEI 385
MCM cd17706
MCM helicase family; MCM helicases are a family of helicases that play an important role in ...
4-228 1.39e-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: 39.63  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899041   4 VIIMGDRGTGKSTTIRAITDILPeiqiveddpfnsdptdlelmsdevrRSIengediKVTSTKVPMVDLPLGATEDRVCG 83
Cdd:cd17706    44 ILLVGDPGTAKSQILKYVLKIAP-------------------------RGV------YTSGKGSSGAGLTAAVVRDSETG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899041  84 TIdiekaltegvkAFEPGLLAKANRGLLYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPEEG- 162
Cdd:cd17706    93 EW-----------YLEAGALVLADGGVCCIDEFDKMKELDRTALHEAMEQQTISIAKAGIVTTLNARCSILAAANPKGGr 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899041 163 -----------ELRPQLLDRFGMHSEIRTVRDPE----------------LRVQIVEQRSDFDKNPEECLTRYQEQQDNF 215
Cdd:cd17706   162 ynpklspieniNLPSPLLSRFDLIFVIRDDPDEErdeelaehiidlhrgsDPEEQVKPEEDGIPIDIELLRKYILYARQI 241
                         250
                  ....*....|....
gi 1557899041 216 KKTIT-EAQKLLSQ 228
Cdd:cd17706   242 HPKISeEAREKLVR 255
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
2-182 2.71e-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: 37.35  E-value: 2.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899041    2 GGVIIMGDRGTGKSTTIRAItdilpeiqiveddpfnsdptdlelmsdeVRRSIENGEDIKVTStkvpMVDLPLGATEDRV 81
Cdd:smart00382   3 EVILIVGPPGSGKTTLARAL----------------------------ARELGPPGGGVIYID----GEDILEEVLDQLL 50
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899041   82 CGTIDIEKALTEGVKAFEpGLLAKANR---GLLYVDEVNLLDDHLVDILLDSAAsgwntVEREGISIRHPARFVLVGSGN 158
Cdd:smart00382  51 LIIVGGKKASGSGELRLR-LALALARKlkpDVLILDEITSLLDAEQEALLLLLE-----ELRLLLLLKSEKNLTVILTTN 124
                          170       180
                   ....*....|....*....|....
gi 1557899041  159 PEEGELRPQLLDRFGMHSEIRTVR 182
Cdd:smart00382 125 DEKDLGPALLRRRFDRRIVLLLIL 148
 
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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