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Conserved domains on  [gi|447206356|ref|WP_001283612|]
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MULTISPECIES: redox-sensing transcriptional repressor Rex [Staphylococcus]

Protein Classification

redox-sensing transcriptional repressor Rex( domain architecture ID 11481021)

redox-sensing transcriptional repressor Rex modulates transcription in response to changes in cellular NADH/NAD(+) redox state

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK05472 PRK05472
redox-sensing transcriptional repressor Rex; Provisional
 1-211 1.68e-107

redox-sensing transcriptional repressor Rex; Provisional


:

Pssm-ID: 235486 [Multi-domain]  Cd Length: 213  Bit Score: 307.43  E-value: 1.68e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206356   1 MSDQVKIPRATLKRLPLYYRFVSSLKSKGIDRVNSKAISDALQIDSATIRRDFSYFGELGKKGYGYNIDSLLDFFKSELS 80
Cdd:PRK05472   1 MMKQKKIPEATIKRLPLYYRYLKELKEEGVERVSSKELAEALGVDSAQIRKDLSYFGEFGKRGVGYNVEELLEFIEKILG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206356  81 ESDMIKIAIVGVGNLGKALLTYNFSIHDDMTITEAFDVKEDVIGQKIGNVIVKDNDELITTLKKEEIDVVILTTPERVAQ 160
Cdd:PRK05472  81 LDRTWNVALVGAGNLGRALLNYNGFEKRGFKIVAAFDVDPEKIGTKIGGIPVYHIDELEEVVKENDIEIGILTVPAEAAQ 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 447206356 161 KVADELVQAGVKGILNFTPGRINTPSDVQVHQIDLGIELQSLLFFMKNYSE 211
Cdd:PRK05472 161 EVADRLVEAGIKGILNFAPVRLSVPEDVIVRNVDLTVELQTLSYFLNNYEL 211
 
Name Accession Description Interval E-value
PRK05472 PRK05472
redox-sensing transcriptional repressor Rex; Provisional
 1-211 1.68e-107

redox-sensing transcriptional repressor Rex; Provisional


Pssm-ID: 235486 [Multi-domain]  Cd Length: 213  Bit Score: 307.43  E-value: 1.68e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206356   1 MSDQVKIPRATLKRLPLYYRFVSSLKSKGIDRVNSKAISDALQIDSATIRRDFSYFGELGKKGYGYNIDSLLDFFKSELS 80
Cdd:PRK05472   1 MMKQKKIPEATIKRLPLYYRYLKELKEEGVERVSSKELAEALGVDSAQIRKDLSYFGEFGKRGVGYNVEELLEFIEKILG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206356  81 ESDMIKIAIVGVGNLGKALLTYNFSIHDDMTITEAFDVKEDVIGQKIGNVIVKDNDELITTLKKEEIDVVILTTPERVAQ 160
Cdd:PRK05472  81 LDRTWNVALVGAGNLGRALLNYNGFEKRGFKIVAAFDVDPEKIGTKIGGIPVYHIDELEEVVKENDIEIGILTVPAEAAQ 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 447206356 161 KVADELVQAGVKGILNFTPGRINTPSDVQVHQIDLGIELQSLLFFMKNYSE 211
Cdd:PRK05472 161 EVADRLVEAGIKGILNFAPVRLSVPEDVIVRNVDLTVELQTLSYFLNNYEL 211
Rex COG2344
NADH/NAD ratio-sensing transcriptional regulator Rex [Transcription];
1-211 1.01e-100

NADH/NAD ratio-sensing transcriptional regulator Rex [Transcription];


Pssm-ID: 441913 [Multi-domain]  Cd Length: 214  Bit Score: 290.45  E-value: 1.01e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206356   1 MSDQVKIPRATLKRLPLYYRFVSSLKSKGIDRVNSKAISDALQIDSATIRRDFSYFGELGKKGYGYNIDSLLDFFKSELS 80
Cdd:COG2344    1 MMKKKKIPEATIKRLPLYLRYLEELKEEGVERISSKELAEALGVTAAQVRKDLSYFGEFGKRGVGYNVEELIEEIEKILG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206356  81 ESDMIKIAIVGVGNLGKALLTYNFSIHDDMTITEAFDVKEDVIGQKIGNVIVKDNDELITTLKKEEIDVVILTTPERVAQ 160
Cdd:COG2344   81 LDREWNVALVGAGNLGQALANYNGFEKRGFKIVAAFDVDPEKIGTKIGGIPVYHIDELEEVVKENKIEIAIITVPAEAAQ 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 447206356 161 KVADELVQAGVKGILNFTPGRINTPSDVQVHQIDLGIELQSLLFFMKNYSE 211
Cdd:COG2344  161 EVADRLVEAGIKGILNFAPVRLKVPEDVVVENVDLSVELQTLSYFLNNKEE 211
CoA_binding pfam02629
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
 84-180 2.58e-29

CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.


Pssm-ID: 396961 [Multi-domain]  Cd Length: 97  Bit Score: 104.60  E-value: 2.58e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206356   84 MIKIAIVGVGNLGKALLTYNFSIHDDMTITEAFDVKEDVIGQKIGNVIVKDN-DELIttlKKEEIDVVILTTPERVAQKV 162
Cdd:pfam02629   3 DTKVIVIGAGGLGIQGLNYHFIQMLGYGIKMVFGVNPGKGGTEILGIPVYNSvDELE---EKTGVDVAVITVPAPFAQEA 79

                          90
                  ....*....|....*...
gi 447206356  163 ADELVQAGVKGILNFTPG 180
Cdd:pfam02629  80 IDELVDAGIKGIVNITPG 97
CoA_binding smart00881
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
 86-181 4.17e-18

CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.


Pssm-ID: 214881 [Multi-domain]  Cd Length: 100  Bit Score: 76.01  E-value: 4.17e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206356    86 KIAIVGV-GNLGK-ALLTYNFSIHDDMTIteAFDVKEDVIGQKIGNVIVKDN-DELIttlKKEEIDVVILTTPERVAQKV 162
Cdd:smart00881   7 SVAVVGAsGNLGSfGLAVMRNLLEYGTKF--VGGVYPGKVGPKVDGVPVYDSvAEAP---EETGVDVAVIFVPAEAAPDA 81

                           90
                   ....*....|....*....
gi 447206356   163 ADELVQAGVKGILNFTPGR 181
Cdd:smart00881  82 IDEAIEAGIKGIVVITEGI 100
nat-AmDH_N_like cd24146
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ...
 85-174 3.14e-07

N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) and similar proteins; The family corresponds to a group of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) that catalyze the reductive amination of ketone and aldehyde substrates using NAD(P)H as the hydride source. nat-AmDHs can naturally catalyze the amination of 'neutral' carbonyl compounds using ammonia. They possess tremendous potential for the efficient asymmetric synthesis of alpha-chiral amines. The family also contains 2,4-diaminopentanoate dehydrogenase (DAPDH) and similar proteins. DAPDH, also known as ORD, is involved in the ornithine fermentation pathway. It catalyzes the oxidative deamination of (2R,4S)-2,4-diaminopentanoate ((2R,4S)-DAP) to yield 2-amino-4-ketopentanoate (AKP). Although DAPDH is more efficient with (2R,4S)-DAP, the diastereoisomer (2R,4R)-DAP can also be metabolized. Different forms of DAPDH exist which utilize NAD(+) (EC 1.4.1.26) or NAD(+)/NADP(+) (EC 1.4.1.12). Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.


Pssm-ID: 467616 [Multi-domain]  Cd Length: 157  Bit Score: 48.31  E-value: 3.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206356  85 IKIAIVGVGNLGKALLTYnFSIHDDMTITEAFDVKEDVIGQKIGNVIVKDN------DELITTLKKEEIDVVILTTPERV 158
Cdd:cd24146    1 IRVVVWGLGAMGRGIARY-LLEKPGLEIVGAVDRDPAKVGKDLGELGGGAPlgvkvtDDLDAVLAATKPDVVVHATTSFL 79

                         90
                 ....*....|....*.
gi 447206356 159 AQkVADELVQAGVKGI 174
Cdd:cd24146   80 AD-VAPQIERLLEAGL 94
 
Name Accession Description Interval E-value
PRK05472 PRK05472
redox-sensing transcriptional repressor Rex; Provisional
 1-211 1.68e-107

redox-sensing transcriptional repressor Rex; Provisional


Pssm-ID: 235486 [Multi-domain]  Cd Length: 213  Bit Score: 307.43  E-value: 1.68e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206356   1 MSDQVKIPRATLKRLPLYYRFVSSLKSKGIDRVNSKAISDALQIDSATIRRDFSYFGELGKKGYGYNIDSLLDFFKSELS 80
Cdd:PRK05472   1 MMKQKKIPEATIKRLPLYYRYLKELKEEGVERVSSKELAEALGVDSAQIRKDLSYFGEFGKRGVGYNVEELLEFIEKILG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206356  81 ESDMIKIAIVGVGNLGKALLTYNFSIHDDMTITEAFDVKEDVIGQKIGNVIVKDNDELITTLKKEEIDVVILTTPERVAQ 160
Cdd:PRK05472  81 LDRTWNVALVGAGNLGRALLNYNGFEKRGFKIVAAFDVDPEKIGTKIGGIPVYHIDELEEVVKENDIEIGILTVPAEAAQ 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 447206356 161 KVADELVQAGVKGILNFTPGRINTPSDVQVHQIDLGIELQSLLFFMKNYSE 211
Cdd:PRK05472 161 EVADRLVEAGIKGILNFAPVRLSVPEDVIVRNVDLTVELQTLSYFLNNYEL 211
Rex COG2344
NADH/NAD ratio-sensing transcriptional regulator Rex [Transcription];
1-211 1.01e-100

NADH/NAD ratio-sensing transcriptional regulator Rex [Transcription];


Pssm-ID: 441913 [Multi-domain]  Cd Length: 214  Bit Score: 290.45  E-value: 1.01e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206356   1 MSDQVKIPRATLKRLPLYYRFVSSLKSKGIDRVNSKAISDALQIDSATIRRDFSYFGELGKKGYGYNIDSLLDFFKSELS 80
Cdd:COG2344    1 MMKKKKIPEATIKRLPLYLRYLEELKEEGVERISSKELAEALGVTAAQVRKDLSYFGEFGKRGVGYNVEELIEEIEKILG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206356  81 ESDMIKIAIVGVGNLGKALLTYNFSIHDDMTITEAFDVKEDVIGQKIGNVIVKDNDELITTLKKEEIDVVILTTPERVAQ 160
Cdd:COG2344   81 LDREWNVALVGAGNLGQALANYNGFEKRGFKIVAAFDVDPEKIGTKIGGIPVYHIDELEEVVKENKIEIAIITVPAEAAQ 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 447206356 161 KVADELVQAGVKGILNFTPGRINTPSDVQVHQIDLGIELQSLLFFMKNYSE 211
Cdd:COG2344  161 EVADRLVEAGIKGILNFAPVRLKVPEDVVVENVDLSVELQTLSYFLNNKEE 211
CoA_binding pfam02629
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
 84-180 2.58e-29

CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.


Pssm-ID: 396961 [Multi-domain]  Cd Length: 97  Bit Score: 104.60  E-value: 2.58e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206356   84 MIKIAIVGVGNLGKALLTYNFSIHDDMTITEAFDVKEDVIGQKIGNVIVKDN-DELIttlKKEEIDVVILTTPERVAQKV 162
Cdd:pfam02629   3 DTKVIVIGAGGLGIQGLNYHFIQMLGYGIKMVFGVNPGKGGTEILGIPVYNSvDELE---EKTGVDVAVITVPAPFAQEA 79

                          90
                  ....*....|....*...
gi 447206356  163 ADELVQAGVKGILNFTPG 180
Cdd:pfam02629  80 IDELVDAGIKGIVNITPG 97
Put_DNA-bind_N pfam06971
Putative DNA-binding protein N-terminus; This family represents the N-terminus (approximately ...
 6-54 2.05e-21

Putative DNA-binding protein N-terminus; This family represents the N-terminus (approximately 50 residues) of a number of putative bacterial DNA-binding proteins.


Pssm-ID: 429222 [Multi-domain]  Cd Length: 49  Bit Score: 82.88  E-value: 2.05e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 447206356    6 KIPRATLKRLPLYYRFVSSLKSKGIDRVNSKAISDALQIDSATIRRDFS 54
Cdd:pfam06971   1 KIPEATIRRLPLYLRYLEELEEEGVERISSTELAEALGVTAAQVRKDLS 49
CoA_binding smart00881
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
 86-181 4.17e-18

CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.


Pssm-ID: 214881 [Multi-domain]  Cd Length: 100  Bit Score: 76.01  E-value: 4.17e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206356    86 KIAIVGV-GNLGK-ALLTYNFSIHDDMTIteAFDVKEDVIGQKIGNVIVKDN-DELIttlKKEEIDVVILTTPERVAQKV 162
Cdd:smart00881   7 SVAVVGAsGNLGSfGLAVMRNLLEYGTKF--VGGVYPGKVGPKVDGVPVYDSvAEAP---EETGVDVAVIFVPAEAAPDA 81

                           90
                   ....*....|....*....
gi 447206356   163 ADELVQAGVKGILNFTPGR 181
Cdd:smart00881  82 IDEAIEAGIKGIVVITEGI 100
MviM COG0673
Predicted dehydrogenase [General function prediction only];
82-155 2.31e-07

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 49.92  E-value: 2.31e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447206356  82 SDMIKIAIVGVGNLGKALLTyNFSIHDDMTITEAFDVKEDV---IGQKIGNVIVKDNDELittLKKEEIDVVILTTP 155
Cdd:COG0673    1 MDKLRVGIIGAGGIGRAHAP-ALAALPGVELVAVADRDPERaeaFAEEYGVRVYTDYEEL---LADPDIDAVVIATP 73
nat-AmDH_N_like cd24146
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ...
 85-174 3.14e-07

N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) and similar proteins; The family corresponds to a group of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) that catalyze the reductive amination of ketone and aldehyde substrates using NAD(P)H as the hydride source. nat-AmDHs can naturally catalyze the amination of 'neutral' carbonyl compounds using ammonia. They possess tremendous potential for the efficient asymmetric synthesis of alpha-chiral amines. The family also contains 2,4-diaminopentanoate dehydrogenase (DAPDH) and similar proteins. DAPDH, also known as ORD, is involved in the ornithine fermentation pathway. It catalyzes the oxidative deamination of (2R,4S)-2,4-diaminopentanoate ((2R,4S)-DAP) to yield 2-amino-4-ketopentanoate (AKP). Although DAPDH is more efficient with (2R,4S)-DAP, the diastereoisomer (2R,4R)-DAP can also be metabolized. Different forms of DAPDH exist which utilize NAD(+) (EC 1.4.1.26) or NAD(+)/NADP(+) (EC 1.4.1.12). Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.


Pssm-ID: 467616 [Multi-domain]  Cd Length: 157  Bit Score: 48.31  E-value: 3.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206356  85 IKIAIVGVGNLGKALLTYnFSIHDDMTITEAFDVKEDVIGQKIGNVIVKDN------DELITTLKKEEIDVVILTTPERV 158
Cdd:cd24146    1 IRVVVWGLGAMGRGIARY-LLEKPGLEIVGAVDRDPAKVGKDLGELGGGAPlgvkvtDDLDAVLAATKPDVVVHATTSFL 79

                         90
                 ....*....|....*.
gi 447206356 159 AQkVADELVQAGVKGI 174
Cdd:cd24146   80 AD-VAPQIERLLEAGL 94
COG5495 COG5495
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ...
 84-171 8.09e-05

Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains [General function prediction only];


Pssm-ID: 444246 [Multi-domain]  Cd Length: 286  Bit Score: 42.49  E-value: 8.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206356  84 MIKIAIVGVGNLGKALLTYnFSiHDDMTITEAFDVKED---VIGQKIGNVIVKDNDELIttlkkEEIDVVILTTPERVAQ 160
Cdd:COG5495    3 RMKIGIIGAGRVGTALAAA-LR-AAGHEVVGVYSRSPAsaeRAAALLGAVPALDLEELA-----AEADLVLLAVPDDAIA 75

                         90
                 ....*....|.
gi 447206356 161 KVADELVQAGV 171
Cdd:COG5495   76 EVAAGLAAAGA 86
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 83-171 9.23e-04

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 38.97  E-value: 9.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206356  83 DMIKIAIVGVGNLGKALLT---YNFSIHDDMTITEAFDVKEDVIGQKIGNVIVKDNDELIttlkkEEIDVVILTT-P--- 155
Cdd:PRK11880   1 MMKKIGFIGGGNMASAIIGgllASGVPAKDIIVSDPSPEKRAALAEEYGVRAATDNQEAA-----QEADVVVLAVkPqvm 75

                         90       100
                 ....*....|....*....|..
gi 447206356 156 ERVAQKVADEL------VQAGV 171
Cdd:PRK11880  76 EEVLSELKGQLdklvvsIAAGV 97
Semialdhyde_dh pfam01118
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ...
 86-172 1.06e-03

Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: N-acetyl-glutamine semialdehyde dehydrogenase (AgrC) Aspartate-semialdehyde dehydrogenase


Pssm-ID: 426059 [Multi-domain]  Cd Length: 121  Bit Score: 37.50  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206356   86 KIAIVGV-GNLGKALLTYnFSIHDDMTITEAFdVKEDVIGQKIG----------NVIVKDNDELITtlkkEEIDVVILTT 154
Cdd:pfam01118   1 KVAIVGAtGYVGQELLRL-LEEHPPVELVVLF-ASSRSAGKKLAfvhpileggkDLVVEDVDPEDF----KDVDIVFFAL 74

                          90
                  ....*....|....*...
gi 447206356  155 PERVAQKVADELVQAGVK 172
Cdd:pfam01118  75 PGGVSKEIAPKLAEAGAK 92
meso-DAPDH_N cd02270
N-terminal NAD(P)-binding domain of meso-diaminopimelate D-dehydrogenase (meso-DAPDH) and ...
 85-157 1.17e-03

N-terminal NAD(P)-binding domain of meso-diaminopimelate D-dehydrogenase (meso-DAPDH) and similar proteins; Meso-DAPDH (EC 1.4.1.16), also called diaminopimelate dehydrogenase, or meso-DAP dehydrogenase, probably plays a role in lysine biosynthesis. It catalyzes the reversible NADP(H)-dependent reductive amination of L-2-amino-6-oxopimelate, the acyclic form of L-tetrahydrodipicolinate, to generate the meso compound, D,L-2,6-diaminopimelate. DAPDH is a homodimer which is highly specific for meso-DAP and NADP(+) as substrates. Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.


Pssm-ID: 467610 [Multi-domain]  Cd Length: 151  Bit Score: 37.94  E-value: 1.17e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447206356  85 IKIAIVGVGNLGKALLTynfSI--HDDMTITEAFDVKEDVIGQKIGNVIVKDNDELITtlKKEEIDVVILTTPER 157
Cdd:cd02270    1 IRVAIVGYGNLGRGVEE---AIqaNPDMELVGVFRRRDPKSTKELTPVVVVSVVEHIS--ELDKVDVAILCGGSA 70
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
 85-171 3.12e-03

Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.


Pssm-ID: 426248 [Multi-domain]  Cd Length: 120  Bit Score: 36.42  E-value: 3.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206356   85 IKIAIVGVGNLGKALLTYNFSIHDDMTITEAFDV---KEDVIGQKIGNVIVKDNDELittLKKEEIDVVILTTPERVAQK 161
Cdd:pfam01408   1 IRVGIIGAGKIGSKHARALNASQPGAELVAILDPnseRAEAVAESFGVEVYSDLEEL---LNDPEIDAVIVATPNGLHYD 77

                          90
                  ....*....|
gi 447206356  162 VADELVQAGV 171
Cdd:pfam01408  78 LAIAALEAGK 87
FlaA1 COG1086
NDP-sugar epimerase, includes UDP-GlcNAc-inverting 4,6-dehydratase FlaA1 and capsular ...
 83-172 7.84e-03

NDP-sugar epimerase, includes UDP-GlcNAc-inverting 4,6-dehydratase FlaA1 and capsular polysaccharide biosynthesis protein EpsC [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440703 [Multi-domain]  Cd Length: 121  Bit Score: 35.29  E-value: 7.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206356  83 DMIKIAIVGVGNLGKALLTY-NFSIHDDMTITEAFDVKEDVIGQKIGNV-IVKDNDELITTLKKEEIDVVILTTP---ER 157
Cdd:COG1086   20 NKRRVLIVGAGEAGRQLARAlRRNPDLGYRVVGFVDDDPDKRGRRIEGVpVLGTLDDLPELVRRLGVDEVIIALPsasRE 99

                         90
                 ....*....|....*
gi 447206356 158 VAQKVADELVQAGVK 172
Cdd:COG1086  100 RLRELLEQLEDLGVK 114
 
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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