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Conserved domains on  [gi|635596048|dbj|BAO81205|]
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penicillin V acylase and related amidase [Serpentinimonas raichei]

Protein Classification

PRK13377 family protein( domain architecture ID 10014217)

PRK13377 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK13377 PRK13377
protocatechuate 4,5-dioxygenase subunit alpha; Provisional
 1-129 9.17e-91

protocatechuate 4,5-dioxygenase subunit alpha; Provisional


:

Pssm-ID: 184013 [Multi-domain]  Cd Length: 129  Bit Score: 258.96  E-value: 9.17e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635596048   1 MPLDKPYLDVPGTIIFDAEQSRKGYWLNQFCMSLMQAANRARFKADERAYLDQWPMTEEQKQAVLARDLNWCMRTGGNIY 80
Cdd:PRK13377   1 MALDKPYLDIPGTTIFDADMSRKGYHLNQFCMSLMKAENRERFKADERAYLDEWPMTEEQKQAVLARDLNRCIALGGNIY 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 635596048  81 FLAKIGATDGKSFQQMAGSMTGMSEQEYRDMMIKGGRSIQGNRYLGEDG 129
Cdd:PRK13377  81 FLAKIGATDGKSFQQMAGSMTGMTEEEYRQMMLGGGRSPEGNRYIGEKG 129
 
Name Accession Description Interval E-value
PRK13377 PRK13377
protocatechuate 4,5-dioxygenase subunit alpha; Provisional
 1-129 9.17e-91

protocatechuate 4,5-dioxygenase subunit alpha; Provisional


Pssm-ID: 184013 [Multi-domain]  Cd Length: 129  Bit Score: 258.96  E-value: 9.17e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635596048   1 MPLDKPYLDVPGTIIFDAEQSRKGYWLNQFCMSLMQAANRARFKADERAYLDQWPMTEEQKQAVLARDLNWCMRTGGNIY 80
Cdd:PRK13377   1 MALDKPYLDIPGTTIFDADMSRKGYHLNQFCMSLMKAENRERFKADERAYLDEWPMTEEQKQAVLARDLNRCIALGGNIY 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 635596048  81 FLAKIGATDGKSFQQMAGSMTGMSEQEYRDMMIKGGRSIQGNRYLGEDG 129
Cdd:PRK13377  81 FLAKIGATDGKSFQQMAGSMTGMTEEEYRQMMLGGGRSPEGNRYIGEKG 129
PCA_45_Doxase_A cd07924
The A subunit of Protocatechuate 4,5-dioxygenase (LigAB) is the smaller, non-catalytic subunit; ...
 4-124 4.96e-78

The A subunit of Protocatechuate 4,5-dioxygenase (LigAB) is the smaller, non-catalytic subunit; The A subunit is the non-catalytic subunit of Protocatechuate (PCA) 4,5-dioxygenase (LigAB), which is composed of A and B subunits that form a tetramer. PCA 4,5-dioxygenase catalyzes the oxidization and subsequent ring-opening of PCA (or 3,4-dihydroxybenzoic acid), which is an intermediate in the breakdown of lignin and other compounds. PCA 4,5-dioxygenase is one of the aromatic ring opening dioxygenases which play key roles in the degradation of aromatic compounds. As a member of the Class III extradiol dioxygenase family, LigAB uses a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon.


Pssm-ID: 153394 [Multi-domain]  Cd Length: 121  Bit Score: 226.51  E-value: 4.96e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635596048   4 DKPYLDVPGTIIFDAEQSRKGYWLNQFCMSLMQAANRARFKADERAYLDQWPMTEEQKQAVLARDLNWCMRTGGNIYFLA 83
Cdd:cd07924    1 DKPYDDIPGTYVFDAERARKGYHLNQFCMSLMKAENRERFKADERAYLDKWPMTEEQKQAVLARDYNRMLALGGNIYYLA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 635596048  84 KIGATDGKSFQQMAGSMTGMSEQEYRDMMIKGGRSIQGNRY 124
Cdd:cd07924   81 KIGATDGLSFQQAAGSMTGMSMEEYRQMMVDGGRSPEGNRS 121
PCA_ligA TIGR02792
protocatechuate 4,5-dioxygenase, alpha subunit; Protocatechuate (PCA) 4,5-dioxygenase is the ...
 7-123 8.70e-76

protocatechuate 4,5-dioxygenase, alpha subunit; Protocatechuate (PCA) 4,5-dioxygenase is the first enzyme in the PCA 4,5-cleavage pathway that is an alternative to PCA 3,4-cleavage and PCA 2,3 cleavage pathways. PCA is an intermediate in the breakdown of lignin (hence the gene symbol ligA) and other compounds. Members of this family are the alpha chain of PCA 4,5-dioxygenase, or the equivalent domain of a fusion protein. [Energy metabolism, Aerobic]


Pssm-ID: 131839 [Multi-domain]  Cd Length: 117  Bit Score: 220.58  E-value: 8.70e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635596048    7 YLDVPGTIIFDAEQSRKGYWLNQFCMSLMQAANRARFKADERAYLDQWPMTEEQKQAVLARDLNWCMRTGGNIYFLAKIG 86
Cdd:TIGR02792   1 YDDVPGTRIFDAQQARKGYNLNQFCMSLMKAENRERFKADESAYLDEWNLTPAQKQAVLARDLNACIDEGGNIYFLAKIG 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 635596048   87 ATDGKSFQQMAGSMTGMSEQEYRDMMIKGGRSIQGNR 123
Cdd:TIGR02792  81 ATDGKSFQQMAGSMTGMTEEEYRQMMIGGGRSPEGNR 117
LigA pfam07746
Aromatic-ring-opening dioxygenase LigAB, LigA subunit; This is a family of aromatic ring ...
 27-112 2.55e-41

Aromatic-ring-opening dioxygenase LigAB, LigA subunit; This is a family of aromatic ring opening dioxygenases which catalyze the ring-opening reaction of protocatechuate and related compounds.


Pssm-ID: 429632 [Multi-domain]  Cd Length: 87  Bit Score: 132.34  E-value: 2.55e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635596048   27 LNQFCMSLMQAANRARFKADERAYLDQWPMTEEQKQAVLARDLNWCMRTGGNIYFLAKIGATDGKSFQQMAGSMTGMSEQ 106
Cdd:pfam07746   1 LNKFCMSLNDPENRERFLADEEAYLDEYGLTEEQKDAVLARDWLGLIRLGGNIYYLEKLAAVDGLSMQDVGAAMTGMTVE 80


                  ....*.
gi 635596048  107 EYRDMM 112
Cdd:pfam07746  81 EFQAMM 86
 
Name Accession Description Interval E-value
PRK13377 PRK13377
protocatechuate 4,5-dioxygenase subunit alpha; Provisional
 1-129 9.17e-91

protocatechuate 4,5-dioxygenase subunit alpha; Provisional


Pssm-ID: 184013 [Multi-domain]  Cd Length: 129  Bit Score: 258.96  E-value: 9.17e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635596048   1 MPLDKPYLDVPGTIIFDAEQSRKGYWLNQFCMSLMQAANRARFKADERAYLDQWPMTEEQKQAVLARDLNWCMRTGGNIY 80
Cdd:PRK13377   1 MALDKPYLDIPGTTIFDADMSRKGYHLNQFCMSLMKAENRERFKADERAYLDEWPMTEEQKQAVLARDLNRCIALGGNIY 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 635596048  81 FLAKIGATDGKSFQQMAGSMTGMSEQEYRDMMIKGGRSIQGNRYLGEDG 129
Cdd:PRK13377  81 FLAKIGATDGKSFQQMAGSMTGMTEEEYRQMMLGGGRSPEGNRYIGEKG 129
pcmA PRK13372
protocatechuate 4,5-dioxygenase subunit alpha/beta;
1-141 7.48e-87

protocatechuate 4,5-dioxygenase subunit alpha/beta;


Pssm-ID: 106330 [Multi-domain]  Cd Length: 444  Bit Score: 259.96  E-value: 7.48e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635596048   1 MPLDKPYLDVPGTIIFDAEQSRKGYWLNQFCMSLMQAANRARFKADERAYLDQWPMTEEQKQAVLARDLNWCMRTGGNIY 80
Cdd:PRK13372   1 MSLDKPYKDVPGTIIFDADQARKGYNLNQFCMSLMKADNRARFKADEGAYLDEWALNEAQKQAVLAIDLNQCIAEGGNIY 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 635596048  81 FLAKIGATDGKSFQQMAGSMTGMSEQEYRDMMIKGGRSIQGNRYLGEDGDAQPQ----RQPQGKR 141
Cdd:PRK13372  81 FLAKIGATDGKSFQQMAGSMTGLSEAAYRDMMIGGGRPAEGLRLKDEDGATPPEpaekAEPTGAQ 145
PCA_45_Doxase_A cd07924
The A subunit of Protocatechuate 4,5-dioxygenase (LigAB) is the smaller, non-catalytic subunit; ...
 4-124 4.96e-78

The A subunit of Protocatechuate 4,5-dioxygenase (LigAB) is the smaller, non-catalytic subunit; The A subunit is the non-catalytic subunit of Protocatechuate (PCA) 4,5-dioxygenase (LigAB), which is composed of A and B subunits that form a tetramer. PCA 4,5-dioxygenase catalyzes the oxidization and subsequent ring-opening of PCA (or 3,4-dihydroxybenzoic acid), which is an intermediate in the breakdown of lignin and other compounds. PCA 4,5-dioxygenase is one of the aromatic ring opening dioxygenases which play key roles in the degradation of aromatic compounds. As a member of the Class III extradiol dioxygenase family, LigAB uses a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon.


Pssm-ID: 153394 [Multi-domain]  Cd Length: 121  Bit Score: 226.51  E-value: 4.96e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635596048   4 DKPYLDVPGTIIFDAEQSRKGYWLNQFCMSLMQAANRARFKADERAYLDQWPMTEEQKQAVLARDLNWCMRTGGNIYFLA 83
Cdd:cd07924    1 DKPYDDIPGTYVFDAERARKGYHLNQFCMSLMKAENRERFKADERAYLDKWPMTEEQKQAVLARDYNRMLALGGNIYYLA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 635596048  84 KIGATDGKSFQQMAGSMTGMSEQEYRDMMIKGGRSIQGNRY 124
Cdd:cd07924   81 KIGATDGLSFQQAAGSMTGMSMEEYRQMMVDGGRSPEGNRS 121
PCA_ligA TIGR02792
protocatechuate 4,5-dioxygenase, alpha subunit; Protocatechuate (PCA) 4,5-dioxygenase is the ...
 7-123 8.70e-76

protocatechuate 4,5-dioxygenase, alpha subunit; Protocatechuate (PCA) 4,5-dioxygenase is the first enzyme in the PCA 4,5-cleavage pathway that is an alternative to PCA 3,4-cleavage and PCA 2,3 cleavage pathways. PCA is an intermediate in the breakdown of lignin (hence the gene symbol ligA) and other compounds. Members of this family are the alpha chain of PCA 4,5-dioxygenase, or the equivalent domain of a fusion protein. [Energy metabolism, Aerobic]


Pssm-ID: 131839 [Multi-domain]  Cd Length: 117  Bit Score: 220.58  E-value: 8.70e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635596048    7 YLDVPGTIIFDAEQSRKGYWLNQFCMSLMQAANRARFKADERAYLDQWPMTEEQKQAVLARDLNWCMRTGGNIYFLAKIG 86
Cdd:TIGR02792   1 YDDVPGTRIFDAQQARKGYNLNQFCMSLMKAENRERFKADESAYLDEWNLTPAQKQAVLARDLNACIDEGGNIYFLAKIG 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 635596048   87 ATDGKSFQQMAGSMTGMSEQEYRDMMIKGGRSIQGNR 123
Cdd:TIGR02792  81 ATDGKSFQQMAGSMTGMTEEEYRQMMIGGGRSPEGNR 117
PCA_45_Doxase_A_like cd07921
Subunit A of the Class III Extradiol dioxygenase, Protocatechuate 4,5-dioxygenase, and similar ...
 12-117 2.87e-50

Subunit A of the Class III Extradiol dioxygenase, Protocatechuate 4,5-dioxygenase, and similar enzymes; This subfamily includes the A subunit of protocatechuate (PCA) 4,5-dioxygenase (LigAB) and two subfamilies of unknown function. The A subunit is the smaller, non-catalytic subunit of LigAB. PCA 4,5-dioxygenase catalyzes the oxidization and subsequent ring-opening of PCA (or 3,4-dihydroxybenzoic acid), which is an intermediate in the breakdown of lignin and other compounds. PCA 4,5-dioxygenase is one of the aromatic ring opening dioxygenases which play key roles in the degradation of aromatic compounds. As members of the Class III extradiol dioxygenase family, the enzymes use a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon. LigAB-like class III enzymes are usually composed of two subunits, designated A and B, which form a tetramer composed of two copies of each subunit.


Pssm-ID: 153391 [Multi-domain]  Cd Length: 106  Bit Score: 155.70  E-value: 2.87e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635596048  12 GTIIFDAEQSRKGYWLNQFCMSLMQAANRARFKADERAYLDQWPMTEEQKQAVLARDLNWCMRTGGNIYFLAKIGATDGK 91
Cdd:cd07921    1 GTYVFDAERSRKGYALNKMCMSLNKAENREAFKADEEAYCDKFGLTEEQKQAVLDRDWLRLLELGGNIYYLLKLAAIDGK 80

                         90       100
                 ....*....|....*....|....*.
gi 635596048  92 SFQQMAGSMTGMSEQEYRDMMIKGGR 117
Cdd:cd07921   81 SMQDIGAQMTGMTEEEFRAMMVAGGR 106
LigA pfam07746
Aromatic-ring-opening dioxygenase LigAB, LigA subunit; This is a family of aromatic ring ...
 27-112 2.55e-41

Aromatic-ring-opening dioxygenase LigAB, LigA subunit; This is a family of aromatic ring opening dioxygenases which catalyze the ring-opening reaction of protocatechuate and related compounds.


Pssm-ID: 429632 [Multi-domain]  Cd Length: 87  Bit Score: 132.34  E-value: 2.55e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635596048   27 LNQFCMSLMQAANRARFKADERAYLDQWPMTEEQKQAVLARDLNWCMRTGGNIYFLAKIGATDGKSFQQMAGSMTGMSEQ 106
Cdd:pfam07746   1 LNKFCMSLNDPENRERFLADEEAYLDEYGLTEEQKDAVLARDWLGLIRLGGNIYYLEKLAAVDGLSMQDVGAAMTGMTVE 80


                  ....*.
gi 635596048  107 EYRDMM 112
Cdd:pfam07746  81 EFQAMM 86
LigA_like_1 cd07925
The A subunit of Uncharacterized proteins with similarity to Protocatechuate 4,5-dioxygenase ...
 12-117 8.85e-40

The A subunit of Uncharacterized proteins with similarity to Protocatechuate 4,5-dioxygenase (LigAB); The proteins of unknown function in this subfamily are similar to the A subunit of the Protocatechuate (PCA) 4,5-dioxygenase (LigAB). LigAB belongs to the class III extradiol dioxygenase family, composed of enzymes which use a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon. Dioxygenases play key roles in the degradation of aromatic compounds. PCA 4,5-dioxygenase catalyzes the oxidization and subsequent ring-opening of PCA (or 3,4-dihydroxybenzoic acid), which is an intermediate in the breakdown of lignin and other compounds.


Pssm-ID: 153395 [Multi-domain]  Cd Length: 106  Bit Score: 129.08  E-value: 8.85e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635596048  12 GTIIFDAEQSRKGYWLNQFCMSLMQAANRARFKADERAYLDQWPMTEEQKQAVLARDLNWCMRTGGNIYFLAKIGATDGK 91
Cdd:cd07925    1 GTTLFDGEMARKGYALNKMCFSFNDAANREAFLADEEAYCEKFGLTPEQKQAVRNRDVLRMLEAGGNIYYLAKLAGILGL 80

                         90       100
                 ....*....|....*....|....*.
gi 635596048  92 SFQQMAGSMTGMSEQEYRDMMIKGGR 117
Cdd:cd07925   81 NMQDIGGLQTGMSTEEFKAMLVAQGR 106
PRK13378 PRK13378
protocatechuate 4,5-dioxygenase subunit alpha; Provisional
 1-117 3.44e-33

protocatechuate 4,5-dioxygenase subunit alpha; Provisional


Pssm-ID: 139527 [Multi-domain]  Cd Length: 117  Bit Score: 112.91  E-value: 3.44e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635596048   1 MPLDKPYLDVPGTIIFDAEQSRKGYWLNQFCMSLMQAANRARFKADERAYLDQWPMTEEQKQAVLARDLNWCMRTGGNIY 80
Cdd:PRK13378   1 MAATSAKREIPGTTIFDGEQARKGYALNKMCFSFNDAANRAAFLADEAAYCRKYGLNEEQKEAIRNRDVLQLLAAGGNAY 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 635596048  81 FLAKIGATDGKSFQQMAGSMTGMSEQEYRDMMIKGGR 117
Cdd:PRK13378  81 YLAKFAGIFGLDMQDIGAQQTGMTKEEFKAKLLAAGR 117
PRK13367 PRK13367
gallate dioxygenase;
11-108 3.24e-12

gallate dioxygenase;


Pssm-ID: 184006  Cd Length: 420  Bit Score: 62.45  E-value: 3.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635596048  11 PGTIIFDAEQSRKGYWLNQFCMSLMQAANRARFKADERAYLDQWPMTEEQKQAVLARDLNWCMRTGGNIYFLAKIGATDG 90
Cdd:PRK13367 305 PGTYPFTLERSLKAYRINRFLHRLIEPAWRERFLADPEALYDEAGLSEEERDLIRRRDWRGLIHYGVSFFLLEKLGAVVG 384

                         90
                 ....*....|....*...
gi 635596048  91 KSFQQMAGSMTGMSEQEY 108
Cdd:PRK13367 385 VSNLHIYAAMRGQTLEAF 402
Gallate_dioxygenase_C cd07923
The C-terminal domain of Gallate Dioxygenase, which catalyzes the oxidization and subsequent ...
 20-108 8.69e-10

The C-terminal domain of Gallate Dioxygenase, which catalyzes the oxidization and subsequent ring-opening of gallate; Gallate Dioxygenase catalyzes the oxidization and subsequent ring-opening of gallate, an intermediate in the degradation of the aromatic compound, syringate. The reaction product of gallate dioxygenase is 4-oxalomesaconate. The amino acid sequence of the N-terminal and C-terminal regions of gallate dioxygenase exhibits homology with the sequence of the PCA 4,5-dioxygenase B (catalytic) and A subunits, respectively. This model represents the C-terminal domain, which is similar to the A subunit of PCA 4,5-dioxygenase (or LigAB). The enzyme is estimated to be a homodimer according to the Escherichia coli enzyme. Since enzymes in this subfamily have fused A and B subunits, the dimer interface may resemble the tetramer interface of classical LigAB enzymes. This enzyme belongs to the class III extradiol dioxygenase family, composed of enzymes which use a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon.


Pssm-ID: 153393 [Multi-domain]  Cd Length: 94  Bit Score: 52.05  E-value: 8.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635596048  20 QSRKGYWLNQFCMSLMQAANRARFKADERAYLDQWPMTEEQKQAVLARDLNWCMRTGGNIYFLAKIGATDGKSFQQMAGS 99
Cdd:cd07923    1 RSVRAYRINRFLHRLIEPAHRERFLEDPEALFDEAGLTEEERTLIRNRDWIGMIRYGVIFFVLEKLAAVVGVSNLHVYAA 80


                 ....*....
gi 635596048 100 MTGMSEQEY 108
Cdd:cd07923   81 MRGESLEEF 89
Extradiol_Dioxygenase_3A_like cd07321
Subunit A of Class III extradiol dioxygenases; Extradiol dioxygenases catalyze the ...
 21-82 2.59e-09

Subunit A of Class III extradiol dioxygenases; Extradiol dioxygenases catalyze the incorporation of both atoms of molecular oxygen into substrates using a variety of reaction mechanisms, resulting in the cleavage of aromatic rings. There are two major groups of dioxygenases according to the cleavage site of the aromatic ring. Intradiol enzymes cleave the aromatic ring between two hydroxyl groups, whereas extradiol enzymes cleave the aromatic ring between a hydroxylated carbon and an adjacent non-hydroxylated carbon. Extradiol dioxygenases can be divided into three classes. Class I and II enzymes are evolutionary related and show sequence similarity, with the two domain class II enzymes evolving from the class I enzyme through gene duplication. Class III enzymes are different in sequence and structure and usually have two subunits, designated A and B, which form a tetramer composed of two copies of each subunit. This model represents subunit A of class III extradiol dioxygenase enzymes. The A subunit is the smaller, non-catalytic subunit. Enzymes that belong to this family include Protocatechuate 4,5-dioxygenase (LigAB) A subunit, 2'-aminobiphenyl-2,3-diol 1,2-dioxygenase (CarB) A subunit, Gallate Dioxygenase and proteins of unknown function.


Pssm-ID: 153390 [Multi-domain]  Cd Length: 77  Bit Score: 50.39  E-value: 2.59e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 635596048  21 SRKGYwLNQFCMSLMQAANRARFKADERAYLDQWPMTEEQKQAVLARDLNWCMRTGGNIYFL 82
Cdd:cd07321    1 SRYEL-EKLLEQLLVKPEVKERFKADPEAVLAEYGLTPEEKAALLARDVGALYVLGVNPMLL 61
PRK13379 PRK13379
protocatechuate 4,5-dioxygenase subunit alpha; Provisional
 1-108 2.40e-07

protocatechuate 4,5-dioxygenase subunit alpha; Provisional


Pssm-ID: 184014 [Multi-domain]  Cd Length: 119  Bit Score: 46.47  E-value: 2.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635596048   1 MPLDKPYLDVPG-TIIFDAEQSRKGYWLNQFCMSLMQAANRARFKADERAYLDQWPMTEEQKQAVLARDLNWCMRTGGNI 79
Cdd:PRK13379   1 MNPQVQGMEQLGgTYVFDLRTSNRALRLNRFFWHMIRAPWRDRFLQDAEALMQEAGLTEQEKELIRARDWLGLVQYGANF 80

                         90       100
                 ....*....|....*....|....*....
gi 635596048  80 YFLAKIGATDGKSFQQMAGSMTGMSEQEY 108
Cdd:PRK13379  81 FVIEKFARVVRMTNLQVYAIMRGETFEEF 109
 
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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