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Conserved domains on  [gi|7592876|dbj|BAA94443|]
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ribulose-1,5-bisphosphate carboxylase/oxygenase form II large subunit, partial [uncultured deep-sea autotrophic bacterium ORII-1]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RuBisCO_large super family cl08232
Ribulose bisphosphate carboxylase large chain; Ribulose bisphosphate carboxylase (Rubisco) ...
 1-112 4.68e-80

Ribulose bisphosphate carboxylase large chain; Ribulose bisphosphate carboxylase (Rubisco) plays an important role in the Calvin reductive pentose phosphate pathway. It catalyzes the primary CO2 fixation step. Rubisco is activated by carbamylation of an active site lysine, stabilized by a divalent cation, which then catalyzes the proton abstraction from the substrate ribulose 1,5 bisphosphate (RuBP) and leads to the formation of two molecules of 3-phosphoglycerate. Members of the Rubisco family can be divided into 4 subgroups, Form I-IV, which differ in their taxonomic distribution and subunit composition. Form I-III have Rubisco activity, while Form IV, also called Rubisco-like proteins (RLP), are missing critical active site residues and therefore do not catalyze CO2 fixation. They are believed to utilize a related enzymatic mechanism, but have divergent functions.


The actual alignment was detected with superfamily member PRK13475:

Pssm-ID: 471793  Cd Length: 443  Bit Score: 241.16  E-value: 4.68e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7592876     1 QPFAKAAYDFWLGGDFIKNDEPQGNQVFAPLKETITAVADAMRRAQDDTGEAKLFSANITADDYREMIARGEFILETFAE 80
Cdd:PRK13475 174 EPFAEACYDFWLGGDFIKNDEPQGNQVFAPLKKTVPLVADAMKRAQDETGEAKLFSANITADDHYEMIARGEYILETFGE 253

                         90       100       110
                 ....*....|....*....|....*....|..
gi 7592876    81 NADHVAFLVDGYVAGTAAITTARRQFPNQYLH 112
Cdd:PRK13475 254 NADHVAFLVDGYVAGPGAVTTARRQYPDQYLH 285
 
Name Accession Description Interval E-value
PRK13475 PRK13475
ribulose-bisphosphate carboxylase;
1-112 4.68e-80

ribulose-bisphosphate carboxylase;


Pssm-ID: 184072  Cd Length: 443  Bit Score: 241.16  E-value: 4.68e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7592876     1 QPFAKAAYDFWLGGDFIKNDEPQGNQVFAPLKETITAVADAMRRAQDDTGEAKLFSANITADDYREMIARGEFILETFAE 80
Cdd:PRK13475 174 EPFAEACYDFWLGGDFIKNDEPQGNQVFAPLKKTVPLVADAMKRAQDETGEAKLFSANITADDHYEMIARGEYILETFGE 253

                         90       100       110
                 ....*....|....*....|....*....|..
gi 7592876    81 NADHVAFLVDGYVAGTAAITTARRQFPNQYLH 112
Cdd:PRK13475 254 NADHVAFLVDGYVAGPGAVTTARRQYPDQYLH 285
RuBisCO_large_II cd08211
Ribulose bisphosphate carboxylase large chain, Form II; Ribulose bisphosphate carboxylase ...
 1-112 1.30e-69

Ribulose bisphosphate carboxylase large chain, Form II; Ribulose bisphosphate carboxylase (Rubisco) plays an important role in the Calvin reductive pentose phosphate pathway. It catalyzes the primary CO2 fixation step. Rubisco is activated by carbamylation of an active site lysine, stabilized by a divalent cation, which then catalyzes the proton abstraction from the substrate ribulose 1,5 bisphosphate (RuBP) and leads to the formation of two molecules of 3-phosphoglycerate. Members of the Rubisco family can be divided into 4 subgroups, Form I-IV , which differ in their taxonomic distribution and subunit composition. Form II is mainly found in bacteria, and forms large subunit oligomers (dimers, tetramers, etc.) that do not include small subunits.


Pssm-ID: 173976  Cd Length: 439  Bit Score: 214.29  E-value: 1.30e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7592876    1 QPFAKAAYDFWLGGDFIKNDEPQGNQVFAPLKETITAVADAMRRAQDDTGEAKLFSANITADDYREMIARGEFILETFAE 80
Cdd:cd08211 173 KPFAEACYAFWLGGDFIKNDEPQANQPFCPLKKVIPLVADAMRRAQDETGEAKLFSANITADDPDEMIARGEYILEAFGP 252

                        90       100       110
                ....*....|....*....|....*....|..
gi 7592876   81 NADHVAFLVDGYVAGTAAITTARRQFPNQYLH 112
Cdd:cd08211 253 NAGHVAFLVDGYVAGPAAVTTARRRFPDQFLH 284
RuBisCO_large pfam00016
Ribulose bisphosphate carboxylase large chain, catalytic domain; The C-terminal domain of ...
 1-112 8.46e-53

Ribulose bisphosphate carboxylase large chain, catalytic domain; The C-terminal domain of RuBisCO large chain is the catalytic domain adopting a TIM barrel fold.


Pssm-ID: 459631  Cd Length: 292  Bit Score: 167.15  E-value: 8.46e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7592876      1 QPFAKAAYDFWLGG-DFIKNDEPQGNQVFAPLKETITAVADAMRRAQDDTGEAKLFSANITADDYREMIARGEFILETFA 79
Cdd:pfam00016  29 KNYARAVYEFLLGGlDFIKDDENINSQPFMPWRDRFLFVAEAIDRAQDETGEAKGHYLNITADDMEEMYRRAEFAKETGG 108

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 7592876     80 EnadhvAFLVDGYVAGTAAITTARRQFPNQ--YLH 112
Cdd:pfam00016 109 V-----AVMVDGLVIGPTAITTLRRWFRDNgvILH 138
RbcL COG1850
Ribulose 1,5-bisphosphate carboxylase, large subunit, or a RuBisCO-like protein [Carbohydrate ...
 2-112 5.08e-38

Ribulose 1,5-bisphosphate carboxylase, large subunit, or a RuBisCO-like protein [Carbohydrate transport and metabolism];


Pssm-ID: 441455  Cd Length: 417  Bit Score: 131.83  E-value: 5.08e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7592876    2 PFAKAAYDFWLGG-DFIKNDEPQGNQVFAPLKETITAVADAMRRAQDDTGEAKLFSANITaDDYREMIARGEFILETFAE 80
Cdd:COG1850 164 ETAELVYELALGGvDFIKDDENLADQPFCPFEDRVRAVMEAIDRAEEETGEKKMYAFNIT-ADTDEMLRRADLAVELGAN 242

                        90       100       110
                ....*....|....*....|....*....|..
gi 7592876   81 nadhvAFLVDGYVAGTAAITTARRQFPNQYLH 112
Cdd:COG1850 243 -----AVMVDVNTVGLSAVQTLREEHIGLPIH 269
 
Name Accession Description Interval E-value
PRK13475 PRK13475
ribulose-bisphosphate carboxylase;
1-112 4.68e-80

ribulose-bisphosphate carboxylase;


Pssm-ID: 184072  Cd Length: 443  Bit Score: 241.16  E-value: 4.68e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7592876     1 QPFAKAAYDFWLGGDFIKNDEPQGNQVFAPLKETITAVADAMRRAQDDTGEAKLFSANITADDYREMIARGEFILETFAE 80
Cdd:PRK13475 174 EPFAEACYDFWLGGDFIKNDEPQGNQVFAPLKKTVPLVADAMKRAQDETGEAKLFSANITADDHYEMIARGEYILETFGE 253

                         90       100       110
                 ....*....|....*....|....*....|..
gi 7592876    81 NADHVAFLVDGYVAGTAAITTARRQFPNQYLH 112
Cdd:PRK13475 254 NADHVAFLVDGYVAGPGAVTTARRQYPDQYLH 285
RuBisCO_large_II cd08211
Ribulose bisphosphate carboxylase large chain, Form II; Ribulose bisphosphate carboxylase ...
 1-112 1.30e-69

Ribulose bisphosphate carboxylase large chain, Form II; Ribulose bisphosphate carboxylase (Rubisco) plays an important role in the Calvin reductive pentose phosphate pathway. It catalyzes the primary CO2 fixation step. Rubisco is activated by carbamylation of an active site lysine, stabilized by a divalent cation, which then catalyzes the proton abstraction from the substrate ribulose 1,5 bisphosphate (RuBP) and leads to the formation of two molecules of 3-phosphoglycerate. Members of the Rubisco family can be divided into 4 subgroups, Form I-IV , which differ in their taxonomic distribution and subunit composition. Form II is mainly found in bacteria, and forms large subunit oligomers (dimers, tetramers, etc.) that do not include small subunits.


Pssm-ID: 173976  Cd Length: 439  Bit Score: 214.29  E-value: 1.30e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7592876    1 QPFAKAAYDFWLGGDFIKNDEPQGNQVFAPLKETITAVADAMRRAQDDTGEAKLFSANITADDYREMIARGEFILETFAE 80
Cdd:cd08211 173 KPFAEACYAFWLGGDFIKNDEPQANQPFCPLKKVIPLVADAMRRAQDETGEAKLFSANITADDPDEMIARGEYILEAFGP 252

                        90       100       110
                ....*....|....*....|....*....|..
gi 7592876   81 NADHVAFLVDGYVAGTAAITTARRQFPNQYLH 112
Cdd:cd08211 253 NAGHVAFLVDGYVAGPAAVTTARRRFPDQFLH 284
RuBisCO_large pfam00016
Ribulose bisphosphate carboxylase large chain, catalytic domain; The C-terminal domain of ...
 1-112 8.46e-53

Ribulose bisphosphate carboxylase large chain, catalytic domain; The C-terminal domain of RuBisCO large chain is the catalytic domain adopting a TIM barrel fold.


Pssm-ID: 459631  Cd Length: 292  Bit Score: 167.15  E-value: 8.46e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7592876      1 QPFAKAAYDFWLGG-DFIKNDEPQGNQVFAPLKETITAVADAMRRAQDDTGEAKLFSANITADDYREMIARGEFILETFA 79
Cdd:pfam00016  29 KNYARAVYEFLLGGlDFIKDDENINSQPFMPWRDRFLFVAEAIDRAQDETGEAKGHYLNITADDMEEMYRRAEFAKETGG 108

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 7592876     80 EnadhvAFLVDGYVAGTAAITTARRQFPNQ--YLH 112
Cdd:pfam00016 109 V-----AVMVDGLVIGPTAITTLRRWFRDNgvILH 138
RuBisCO_large_I_II_III cd08206
Ribulose bisphosphate carboxylase large chain, Form I,II,III; Ribulose bisphosphate ...
 2-112 2.74e-48

Ribulose bisphosphate carboxylase large chain, Form I,II,III; Ribulose bisphosphate carboxylase (Rubisco) plays an important role in the Calvin reductive pentose phosphate pathway. It catalyzes the primary CO2 fixation step. Rubisco is activated by carbamylation of an active site lysine, stabilized by a divalent cation, which then catalyzes the proton abstraction from the substrate ribulose 1,5 bisphosphate (RuBP) and leads to the formation of two molecules of 3-phosphoglycerate. Members of the Rubisco family can be divided into 4 subgroups, Form I-IV, which differ in their taxonomic distribution and subunit composition. Form I-III have Rubisco activity, while Form IV, also called Rubico-like proteins (RLP), are missing critical active site residues.


Pssm-ID: 173971  Cd Length: 414  Bit Score: 158.55  E-value: 2.74e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7592876    2 PFAKAAYDFWLGG-DFIKNDEPQGNQVFAPLKETITAVADAMRRAQDDTGEAKLFSANITADDYREMIARGEFILETFae 80
Cdd:cd08206 149 EYARVVYEALRGGlDFVKDDENQNSQPFMRFEDRILFVAEAMDKAEAETGEAKGHYLNITADTPEEMIKRAEFAKELG-- 226

                        90       100       110
                ....*....|....*....|....*....|....
gi 7592876   81 nadHVAFLVDGYVAGTAAITTARRQFPN--QYLH 112
Cdd:cd08206 227 ---SVIVMVDGVTAGWTAIQSARRWCPDngLALH 257
RbcL COG1850
Ribulose 1,5-bisphosphate carboxylase, large subunit, or a RuBisCO-like protein [Carbohydrate ...
 2-112 5.08e-38

Ribulose 1,5-bisphosphate carboxylase, large subunit, or a RuBisCO-like protein [Carbohydrate transport and metabolism];


Pssm-ID: 441455  Cd Length: 417  Bit Score: 131.83  E-value: 5.08e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7592876    2 PFAKAAYDFWLGG-DFIKNDEPQGNQVFAPLKETITAVADAMRRAQDDTGEAKLFSANITaDDYREMIARGEFILETFAE 80
Cdd:COG1850 164 ETAELVYELALGGvDFIKDDENLADQPFCPFEDRVRAVMEAIDRAEEETGEKKMYAFNIT-ADTDEMLRRADLAVELGAN 242

                        90       100       110
                ....*....|....*....|....*....|..
gi 7592876   81 nadhvAFLVDGYVAGTAAITTARRQFPNQYLH 112
Cdd:COG1850 243 -----AVMVDVNTVGLSAVQTLREEHIGLPIH 269
RuBisCO_large cd08148
Ribulose bisphosphate carboxylase large chain; Ribulose bisphosphate carboxylase (Rubisco) ...
 2-108 1.94e-35

Ribulose bisphosphate carboxylase large chain; Ribulose bisphosphate carboxylase (Rubisco) plays an important role in the Calvin reductive pentose phosphate pathway. It catalyzes the primary CO2 fixation step. Rubisco is activated by carbamylation of an active site lysine, stabilized by a divalent cation, which then catalyzes the proton abstraction from the substrate ribulose 1,5 bisphosphate (RuBP) and leads to the formation of two molecules of 3-phosphoglycerate. Members of the Rubisco family can be divided into 4 subgroups, Form I-IV, which differ in their taxonomic distribution and subunit composition. Form I-III have Rubisco activity, while Form IV, also called Rubisco-like proteins (RLP), are missing critical active site residues and therefore do not catalyze CO2 fixation. They are believed to utilize a related enzymatic mechanism, but have divergent functions.


Pssm-ID: 173969  Cd Length: 366  Bit Score: 124.08  E-value: 1.94e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7592876    2 PFAKAAYDFWLGG-DFIKNDEPQGNQVFAPLKETITAVADAMRRAQDDTGEAKLFSANITADDYrEMIARGEFILETFae 80
Cdd:cd08148 144 YTAEAAYAAALGGlDLIKDDETLTDQPFCPLRDRITEVAAALDRVQEETGEKKLYAVNVTAGTF-EIIERAERALELG-- 220

                        90       100
                ....*....|....*....|....*...
gi 7592876   81 nadHVAFLVDGYVAGTAAITTARRQFPN 108
Cdd:cd08148 221 ---ANMLMVDVLTAGFSALQALAEDFEI 245
rbcL PRK04208
ribulose bisophosphate carboxylase; Reviewed
 3-104 5.53e-18

ribulose bisophosphate carboxylase; Reviewed


Pssm-ID: 179787  Cd Length: 468  Bit Score: 77.64  E-value: 5.53e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7592876     3 FAKAAYDFWLGG-DFIKNDEPQGNQVFAPLKETITAVADAMRRAQDDTGEAKLFSANITADDYREMIARGEFILEtfaEN 81
Cdd:PRK04208 178 YGRVVYEALRGGlDFTKDDENLNSQPFNRWRDRFLFVMEAIDKAEAETGERKGHYLNVTAPTMEEMYKRAEFAKE---LG 254

                         90       100
                 ....*....|....*....|...
gi 7592876    82 ADHVafLVDGYVAGTAAITTARR 104
Cdd:PRK04208 255 SPIV--MIDVVTAGWTALQSLRE 275
RuBisCO_IV_RLP cd08205
Ribulose bisphosphate carboxylase like proteins, Rubisco-Form IV; Ribulose bisphosphate ...
 3-76 8.84e-17

Ribulose bisphosphate carboxylase like proteins, Rubisco-Form IV; Ribulose bisphosphate carboxylase (Rubisco) plays an important role in the Calvin reductive pentose phosphate pathway. It catalyzes the primary CO2 fixation step. Rubisco is activated by carbamylation of an active site lysine, stabilized by a divalent cation, which then catalyzes the proton abstraction from the substrate ribulose 1,5 bisphosphate (RuBP) and leads to the formation of two molecules of 3-phosphoglycerate. Members of the Rubisco family can be divided into 4 subgroups, Form I-IV, which differ in their taxonomic distribution and subunit composition. Form I-III have Rubisco activity, while Form IV, also called Rubisco-like proteins (RLP), are missing critical active site residues and therefore do not catalyze CO2 fixation. They are believed to utilize a related enzymatic mechanism, but have divergent functions, like for example 2,3-diketo-5-methylthiopentyl-1-phosphate enolase or 5-methylthio-d-ribulose 1-phosphate isomerase.


Pssm-ID: 173970  Cd Length: 367  Bit Score: 73.72  E-value: 8.84e-17
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7592876    3 FAKAAYDFWLGG-DFIKNDEPQGNQVFAPLKETITAVADAMRRAQDDTGEAKLFSANITaDDYREMIARGEFILE 76
Cdd:cd08205 148 LAELAYELALGGiDLIKDDELLADQPYAPFEERVRACMEAVRRANEETGRKTLYAPNIT-GDPDELRRRADRAVE 221
RuBisCO_large_III cd08213
Ribulose bisphosphate carboxylase large chain, Form III; Ribulose bisphosphate carboxylase ...
 3-103 1.91e-16

Ribulose bisphosphate carboxylase large chain, Form III; Ribulose bisphosphate carboxylase (Rubisco) plays an important role in the Calvin reductive pentose phosphate pathway. It catalyzes the primary CO2 fixation step. Rubisco is activated by carbamylation of an active site lysine, stabilized by a divalent cation, which then catalyzes the proton abstraction from the substrate ribulose 1,5 bisphosphate (RuBP) and leads to the formation of two molecules of 3-phosphoglycerate. Members of the Rubisco family can be divided into 4 subgroups, Form I-IV , which differ in their taxonomic distribution and subunit composition. Form III is only found in archaea and forms large subunit oligomers (dimers or decamers) that do not include small subunits.


Pssm-ID: 173978  Cd Length: 412  Bit Score: 73.19  E-value: 1.91e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7592876    3 FAKAAYDFWLGG-DFIKNDEPQGNQVFAPLKETITAVADAMRRAQDDTGEAKLFSANITAdDYREMIARGEFILEtfaEN 81
Cdd:cd08213 149 HAEVAYEALVGGvDLVKDDENLTSQPFNRFEERAKESLKARDKAEAETGERKAYLANITA-PVREMERRAELVAD---LG 224

                        90       100
                ....*....|....*....|..
gi 7592876   82 ADHVafLVDGYVAGTAAITTAR 103
Cdd:cd08213 225 GKYV--MIDVVVAGWSALQYLR 244
RLP_RrRLP cd08210
Ribulose bisphosphate carboxylase like proteins (RLPs) similar to R.rubrum RLP; RLP from ...
 3-107 6.60e-13

Ribulose bisphosphate carboxylase like proteins (RLPs) similar to R.rubrum RLP; RLP from Rhodospirillum rubrum plays a role in an uncharacterized sulfur salvage pathway and has been shown to catalyze a novel isomerization reaction that converts 5-methylthio-d-ribulose 1-phosphate to a 3:1 mixture of 1-methylthioxylulose 5-phosphate and 1-methylthioribulose 5-phosphate.


Pssm-ID: 173975  Cd Length: 364  Bit Score: 63.03  E-value: 6.60e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7592876    3 FAKAAYDFWLGG-DFIKNDEPQGNQVFAPLKETITAVADAMRRAQDDTGEAKLFSANITAdDYREMIARGEfiletFAEN 81
Cdd:cd08210 143 LAELAYAFALGGiDIIKDDHGLADQPFAPFEERVKACQEAVAEANAETGGRTLYAPNVTG-PPTQLLERAR-----FAKE 216

                        90       100
                ....*....|....*....|....*.
gi 7592876   82 ADHVAFLVDGYVAGTAAITTARRQFP 107
Cdd:cd08210 217 AGAGGVLIAPGLTGLDTFRELAEDFD 242
RLP_Photo cd08208
Ribulose bisphosphate carboxylase like proteins from phototrophic bacteria; Ribulose ...
 1-60 1.27e-09

Ribulose bisphosphate carboxylase like proteins from phototrophic bacteria; Ribulose bisphosphate carboxylase (Rubisco) plays an important role in the Calvin reductive pentose phosphate pathway. It catalyzes the primary CO2 fixation step. Rubisco is activated by carbamylation of an active site lysine, stabilized by a divalent cation, which then catalyzes the proton abstraction from the substrate ribulose 1,5 bisphosphate (RuBP) and leads to the formation of two molecules of 3-phosphoglycerate. Members of the Rubisco family can be divided into 4 subgroups, Form I-IV, which differ in their taxonomic distribution and subunit composition. Form I-III have Rubisco activity, while Form IV, also called Rubisco-like proteins (RLP), are missing critical active site residues and therefore do not catalyze CO2 fixation. They are believed to utilize a related enzymatic mechanism, but have divergent functions. The specific function of this subgroup is unknown.


Pssm-ID: 173973  Cd Length: 424  Bit Score: 53.75  E-value: 1.27e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7592876    1 QPFAKAAYDFWLGG-DFIKNDEPQGNQVFAPLKETITAVADAMRRAQDDTGEAKLFSANIT 60
Cdd:cd08208 176 GEFAELGYQSWLGGlDIAKDDEMLADVDWCPLEERAALLGKARRRAEAETGVPKIYLANIT 236
RuBisCO_large_I cd08212
Ribulose bisphosphate carboxylase large chain, Form I; Ribulose bisphosphate carboxylase ...
 3-101 3.41e-09

Ribulose bisphosphate carboxylase large chain, Form I; Ribulose bisphosphate carboxylase (Rubisco) plays an important role in the Calvin reductive pentose phosphate pathway. It catalyzes the primary CO2 fixation step. Rubisco is activated by carbamylation of an active site lysine, stabilized by a divalent cation, which then catalyzes the proton abstraction from the substrate ribulose 1,5 bisphosphate (RuBP) and leads to the formation of two molecules of 3-phosphoglycerate. Members of the Rubisco family can be divided into 4 subgroups, Form I-IV , which differ in their taxonomic distribution and subunit composition. Form I is the most abundant class, present in plants, algae, and bacteria, and forms large complexes composed of 8 large and 8 small subunits.


Pssm-ID: 173977  Cd Length: 450  Bit Score: 52.43  E-value: 3.41e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7592876    3 FAKAAYDFWLGG-DFIKNDEPQGNQVFAPLKETITAVADAMRRAQDDTGEAKLFSANITADDYREMIARGEfiletFAEN 81
Cdd:cd08212 163 YGRVVYECLRGGlDFTKDDENINSQPFMRWRDRFLFVAEAVNKAQAETGEVKGHYLNVTAGTMEEMYKRAE-----FAKE 237

                        90       100
                ....*....|....*....|
gi 7592876   82 ADHVAFLVDgYVAGTAAITT 101
Cdd:cd08212 238 LGSPIIMHD-LLTGFTAIQS 256
rbcL CHL00040
ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit
 3-101 1.78e-08

ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit


Pssm-ID: 176981  Cd Length: 475  Bit Score: 50.47  E-value: 1.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7592876     3 FAKAAYDFWLGG-DFIKNDEPQGNQVFAPLKETITAVADAMRRAQDDTGEAKLFSANITADDYREMIARGEfiletFAEN 81
Cdd:CHL00040 185 YGRAVYECLRGGlDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTCEEMYKRAV-----FARE 259

                         90       100
                 ....*....|....*....|
gi 7592876    82 ADHVAFLVDGYVAGTAAITT 101
Cdd:CHL00040 260 LGVPIVMHDYLTGGFTANTS 279
 
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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