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Conserved domains on  [gi|2022383188|ref|NP_001347367|]
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DNA cross-link repair 1A protein isoform 2 [Mus musculus]

Protein Classification

DNA cross-link repair protein( domain architecture ID 11039898)

DNA cross-link repair protein similar to Arabidopsis thaliana SNM1, which is involved in the repair of DNA lesions formed by oxidative stress

Gene Ontology:  GO:0006974|GO:0005634
PubMed:  12177301|20528238

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold super family cl23716
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 678-784 1.74e-62

mainly hydrolytic enzymes and related proteins which carry out various biological functions; MBL-fold metallohydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases which can catalyze the hydrolysis of a wide range of beta-lactam antibiotics, hydroxyacylglutathione hydrolases (also called glyoxalase II) which hydrolyze S-d-lactoylglutathione to d-lactate in the second step of the glycoxlase system, AHL lactonases which catalyze the hydrolysis and opening of the homoserine lactone rings of acyl homoserine lactones (AHLs), persulfide dioxygenase which catalyze the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria, flavodiiron proteins which catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J which has both 5'-3' exoribonucleolytic and endonucleolytic activity and ribonuclease Z which catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors, cyclic nucleotide phosphodiesterases which decompose cyclic adenosine and guanosine 3', 5'-monophosphate (cAMP and cGMP) respectively, insecticide hydrolases, and proteins required for natural transformation competence. The diversity of biological roles is reflected in variations in the active site metallo-chemistry, for example classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, human persulfide dioxygenase ETHE1 is a mono-iron binding member of the superfamily; Arabidopsis thaliana hydroxyacylglutathione hydrolases incorporates iron, manganese, and zinc in its dinuclear metal binding site, and flavodiiron proteins contains a diiron site.


The actual alignment was detected with superfamily member cd16298:

Pssm-ID: 451500 [Multi-domain]  Cd Length: 157  Bit Score: 208.91  E-value: 1.74e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022383188  678 SESSGAGEVRRTCPFYKRIPGTGFTVDAFQYGEIEGCTAYFLTHFHSDHYAGLSKDFTRPVYCSEITGNLLKKKLRVQEQ 757
Cdd:cd16298      1 SSTNGEGKRKKTCPFYKKIPGTGFTVDAFQYGVIEGCTAYFLTHFHSDHYCGLTKKFKFPIYCSKITGNLVKSKLKVEEQ 80

                           90       100
                   ....*....|....*....|....*..
gi 2022383188  758 YIRQLPMDTECVVDSVKVVLLDANHFP 784
Cdd:cd16298     81 YINVLPMNTECIVNGVKVVLLDANHCP 107
DRMBL pfam07522
DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence ...
 901-1007 7.88e-48

DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence motifs. The first four motifs are found in pfam00753 and are common to all metallo-beta-lactamases. The fifth motif appears to be specific to function. This entry represents the fifth motif from metallo-beta-lactamases involved in DNA repair.


:

Pssm-ID: 429512  Cd Length: 108  Bit Score: 165.53  E-value: 7.88e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022383188  901 PEVSSLITTDMCDSLVHLLPMMQINFKGLQSHLKKCGGKYDQILAFRPTGWTHSNNITS-TADIIPQTRGNISIYGIPYS 979
Cdd:pfam07522    1 PEILSLLTTDPLSTQIHVVPMPKLSYEALLDYLTARKDHFDSVLAIRPTGWTYRPPKTEvSDRIGPSIRGRITIYGVPYS 80

                           90       100
                   ....*....|....*....|....*...
gi 2022383188  980 EHSSYLEMKRFVQWLKPQKIIPTVNVGS 1007
Cdd:pfam07522   81 EHSSFDELKEFVQFLRPKKIIPTVNVGG 108
 
Name Accession Description Interval E-value
SNM1A-like_MBL-fold cd16298
5'-exonucleases human SNM1A and related proteins; MBL-fold metallo-hydrolase domain; Includes ...
 678-784 1.74e-62

5'-exonucleases human SNM1A and related proteins; MBL-fold metallo-hydrolase domain; Includes human SNM1A (SNM1 homolog A, also known as DNA cross-link repair 1A protein) which is a 5'-exonuclease and functions in interstrand cross-links (ICL) repair. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293856 [Multi-domain]  Cd Length: 157  Bit Score: 208.91  E-value: 1.74e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022383188  678 SESSGAGEVRRTCPFYKRIPGTGFTVDAFQYGEIEGCTAYFLTHFHSDHYAGLSKDFTRPVYCSEITGNLLKKKLRVQEQ 757
Cdd:cd16298      1 SSTNGEGKRKKTCPFYKKIPGTGFTVDAFQYGVIEGCTAYFLTHFHSDHYCGLTKKFKFPIYCSKITGNLVKSKLKVEEQ 80

                           90       100
                   ....*....|....*....|....*..
gi 2022383188  758 YIRQLPMDTECVVDSVKVVLLDANHFP 784
Cdd:cd16298     81 YINVLPMNTECIVNGVKVVLLDANHCP 107
DRMBL pfam07522
DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence ...
 901-1007 7.88e-48

DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence motifs. The first four motifs are found in pfam00753 and are common to all metallo-beta-lactamases. The fifth motif appears to be specific to function. This entry represents the fifth motif from metallo-beta-lactamases involved in DNA repair.


Pssm-ID: 429512  Cd Length: 108  Bit Score: 165.53  E-value: 7.88e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022383188  901 PEVSSLITTDMCDSLVHLLPMMQINFKGLQSHLKKCGGKYDQILAFRPTGWTHSNNITS-TADIIPQTRGNISIYGIPYS 979
Cdd:pfam07522    1 PEILSLLTTDPLSTQIHVVPMPKLSYEALLDYLTARKDHFDSVLAIRPTGWTYRPPKTEvSDRIGPSIRGRITIYGVPYS 80

                           90       100
                   ....*....|....*....|....*...
gi 2022383188  980 EHSSYLEMKRFVQWLKPQKIIPTVNVGS 1007
Cdd:pfam07522   81 EHSSFDELKEFVQFLRPKKIIPTVNVGG 108
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 718-782 4.73e-05

Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism];


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 46.04  E-value: 4.73e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2022383188  718 FLTHFHSDHYAGLsKDFTR-------PVYCSEITGNLLKKKLRVQEQY------IRQLPMDTECVVDSVKVVLLDANH 782
Cdd:COG1235     73 LLTHEHADHIAGL-DDLRPrygpnpiPVYATPGTLEALERRFPYLFAPypgkleFHEIEPGEPFEIGGLTVTPFPVPH 149
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 718-758 4.57e-03

Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 39.07  E-value: 4.57e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 2022383188   718 FLTHFHSDHYAG---LSKDFTRPVYCSEITGNLLKKKLRVQEQY 758
Cdd:smart00849   40 ILTHGHPDHIGGlpeLLEAPGAPVYAPEGTAELLKDLLALLGEL 83
 
Name Accession Description Interval E-value
SNM1A-like_MBL-fold cd16298
5'-exonucleases human SNM1A and related proteins; MBL-fold metallo-hydrolase domain; Includes ...
 678-784 1.74e-62

5'-exonucleases human SNM1A and related proteins; MBL-fold metallo-hydrolase domain; Includes human SNM1A (SNM1 homolog A, also known as DNA cross-link repair 1A protein) which is a 5'-exonuclease and functions in interstrand cross-links (ICL) repair. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293856 [Multi-domain]  Cd Length: 157  Bit Score: 208.91  E-value: 1.74e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022383188  678 SESSGAGEVRRTCPFYKRIPGTGFTVDAFQYGEIEGCTAYFLTHFHSDHYAGLSKDFTRPVYCSEITGNLLKKKLRVQEQ 757
Cdd:cd16298      1 SSTNGEGKRKKTCPFYKKIPGTGFTVDAFQYGVIEGCTAYFLTHFHSDHYCGLTKKFKFPIYCSKITGNLVKSKLKVEEQ 80

                           90       100
                   ....*....|....*....|....*..
gi 2022383188  758 YIRQLPMDTECVVDSVKVVLLDANHFP 784
Cdd:cd16298     81 YINVLPMNTECIVNGVKVVLLDANHCP 107
SNM1A-1C-like_MBL-fold cd16273
SNM1A , artemis/SNM1C, yeast Pso2p, and related proteins; MBL-fold metallo-hydrolase domain; ...
 687-784 9.98e-53

SNM1A , artemis/SNM1C, yeast Pso2p, and related proteins; MBL-fold metallo-hydrolase domain; Includes human SNM1A (SNM1 homolog A, also known as DNA cross-link repair 1A protein) and Saccharomyces cerevisiae Pso2 protein (PSOralen derivative sensitive 2, also known as SNM1, sensitive to nitrogen mustard 1), both proteins are 5'-exonucleases and function in interstrand cross-links (ICL) repair. Also includes the nuclease artemis (also known as SNM1C, SNM1 homolog C, SNM1-like protein, and DNA cross-link repair 1C protein) which plays a role in V(D)J recombination/DNA repair. Purified artemis protein possesses single-strand-specific 5' to 3' exonuclease activity. Upon complex formation with, and phosphorylation by, DNA-dependent protein kinase, artemis gains endonucleolytic activity on hairpins and 5' and 3' overhangs. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293831  Cd Length: 160  Bit Score: 181.58  E-value: 9.98e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022383188  687 RRTCPFYKRIPGTGFTVDAFQYGEIEGCTAYFLTHFHSDHYAGLSKDFTR-PVYCSEITGNLLKKKLRVQEQYIRQLPMD 765
Cdd:cd16273     10 KKPCPFYKIIPGTSFVVDAFKYGKIPGISAYFLSHFHSDHYGGLTKSWSHgPIYCSEITANLVKLKLKVDEEYIVVLPMN 89

                           90       100
                   ....*....|....*....|
gi 2022383188  766 TECVVDS-VKVVLLDANHFP 784
Cdd:cd16273     90 TPVEIDGdVSVTLLDANHCP 109
DRMBL pfam07522
DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence ...
 901-1007 7.88e-48

DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence motifs. The first four motifs are found in pfam00753 and are common to all metallo-beta-lactamases. The fifth motif appears to be specific to function. This entry represents the fifth motif from metallo-beta-lactamases involved in DNA repair.


Pssm-ID: 429512  Cd Length: 108  Bit Score: 165.53  E-value: 7.88e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022383188  901 PEVSSLITTDMCDSLVHLLPMMQINFKGLQSHLKKCGGKYDQILAFRPTGWTHSNNITS-TADIIPQTRGNISIYGIPYS 979
Cdd:pfam07522    1 PEILSLLTTDPLSTQIHVVPMPKLSYEALLDYLTARKDHFDSVLAIRPTGWTYRPPKTEvSDRIGPSIRGRITIYGVPYS 80

                           90       100
                   ....*....|....*....|....*...
gi 2022383188  980 EHSSYLEMKRFVQWLKPQKIIPTVNVGS 1007
Cdd:pfam07522   81 EHSSFDELKEFVQFLRPKKIIPTVNVGG 108
artemis-SNM1C-like_MBL-fold cd16297
artemis-SNM1C and related proteins; MBL-fold metallo-hydrolase domain; Includes the nuclease ...
 702-784 1.16e-05

artemis-SNM1C and related proteins; MBL-fold metallo-hydrolase domain; Includes the nuclease artemis (also known as SNM1C, SNM1 homolog C, SNM1-like protein and DNA cross-link repair 1C protein) which plays a role in V(D)J recombination/DNA repair. Purified artemis protein possesses single-strand-specific 5' to 3' exonuclease activity. Upon complex formation with, and phosphorylation by, DNA-dependent protein kinase, artemis gains endonucleolytic activity on hairpins and 5' and 3' overhangs. Inactivation of Artemis causes severe combined immunodeficiency (SCID). Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293855  Cd Length: 171  Bit Score: 46.73  E-value: 1.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022383188  702 TVDAFQYGEIEGcTAYFLTHFHSDHYAGLSKDFTRP---------VYCSEITGNLL--KKKLRVQEQYIRQLPMDTE--- 767
Cdd:cd16297     15 SIDRFDRENLRA-RAYFLSHCHKDHMKGLRAPGLKRrlkaslkvkLYCSPVTKELLltNPKYAFWENHIVSLEIDTPtqi 93

                           90       100
                   ....*....|....*....|....
gi 2022383188  768 CVVD-------SVKVVLLDANHFP 784
Cdd:cd16297     94 SLVDeatgekeDVVVTLLPAGHCP 117
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 718-782 4.73e-05

Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism];


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 46.04  E-value: 4.73e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2022383188  718 FLTHFHSDHYAGLsKDFTR-------PVYCSEITGNLLKKKLRVQEQY------IRQLPMDTECVVDSVKVVLLDANH 782
Cdd:COG1235     73 LLTHEHADHIAGL-DDLRPrygpnpiPVYATPGTLEALERRFPYLFAPypgkleFHEIEPGEPFEIGGLTVTPFPVPH 149
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
716-753 8.99e-04

mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 43.13  E-value: 8.99e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 2022383188  716 AYFLTHFHSDHYAGLS---KDFTRPVYCSEITGNLLKKKLR 753
Cdd:COG0595     66 GIVLTHGHEDHIGALPyllKELNVPVYGTPLTLALLEAKLK 106
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 696-749 2.20e-03

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized Enterococcus faecalis EF2904. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293818 [Multi-domain]  Cd Length: 202  Bit Score: 40.67  E-value: 2.20e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2022383188  696 IPGTGFTVDAFQYGEIEG---CTAYFLTHFHSDHYAGLSK-DFTRPVYCSEITGNLLK 749
Cdd:cd07732     55 IVGLYRDPLLLGGLRSEEdpsVDAVLLSHAHLDHYGLLNYlRPDIPVYMGEATKRILK 112
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 718-795 4.42e-03

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry. Some members of this subgroup are named as octanoyltransferase (also known as lipoate-protein ligase B).


Pssm-ID: 293837 [Multi-domain]  Cd Length: 193  Bit Score: 39.38  E-value: 4.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022383188  718 FLTHFHSDHYAGLS--KDFTR------PVYCSEITGNLLKKKLRVQEQY----------IRQLPMDTECVVDSVKVVLLD 779
Cdd:cd16279     71 LLTHAHADHIHGLDdlRPFNRlqqrpiPVYASEETLDDLKRRFPYFFAAtggggvpkldLHIIEPDEPFTIGGLEITPLP 150

                           90       100
                   ....*....|....*....|....*....
gi 2022383188  780 ANHFPTV--------LSYCT-----PETS 795
Cdd:cd16279    151 VLHGKLPslgfrfgdFAYLTdvseiPEES 179
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 718-758 4.57e-03

Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 39.07  E-value: 4.57e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 2022383188   718 FLTHFHSDHYAG---LSKDFTRPVYCSEITGNLLKKKLRVQEQY 758
Cdd:smart00849   40 ILTHGHPDHIGGlpeLLEAPGAPVYAPEGTAELLKDLLALLGEL 83
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 675-782 6.20e-03

RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 40.17  E-value: 6.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022383188  675 MNISESSGAGEVRRTCpFYKRIPGTGFTVDA--FQYGEIEGCTAY----------FLTHFHSDHyAGL-----SKDFTRP 737
Cdd:COG1236      1 MKLTFLGAAGEVTGSC-YLLETGGTRILIDCglFQGGKERNWPPFpfrpsdvdavVLTHAHLDH-SGAlpllvKEGFRGP 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2022383188  738 VYCS----EITGNLLKKKLRVQE------------------QYIRQLPMDTECVVDSVKVVLLDANH 782
Cdd:COG1236     79 IYATpataDLARILLGDSAKIQEeeaeaeplyteedaeralELFQTVDYGEPFEIGGVRVTFHPAGH 145
 
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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