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Conserved domains on  [gi|1398205115|ref|WP_110233191|]
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reverse transcriptase-like protein [Aurantimicrobium photophilum]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK07238 super family cl32201
bifunctional RNase H/acid phosphatase; Provisional
 3-133 2.02e-66

bifunctional RNase H/acid phosphatase; Provisional


The actual alignment was detected with superfamily member PRK07238:

Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 205.60  E-value: 2.02e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398205115   3 RQLIIEADGGSRGNPGIAAGGAVVIDGETQQVLASVGVYVGIATNNVAEYNGLLAGLIKAYDIDPGAlVHVRMDSKLVVE 82
Cdd:PRK07238    1 MKVVVEADGGSRGNPGPAGYGAVVWDADRGEVLAERAEAIGRATNNVAEYRGLIAGLEAAAELGATE-VEVRMDSKLVVE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1398205115  83 QMSGRWKIKHPDMAVLAAKAKDVIGN-RAVTYEWVPRLQNALADAAANKSMD 133
Cdd:PRK07238   80 QMSGRWKVKHPDMKPLAAQARELASQfGRVTYTWIPRARNAHADRLANEAMD 131
 
Name Accession Description Interval E-value
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
 3-133 2.02e-66

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 205.60  E-value: 2.02e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398205115   3 RQLIIEADGGSRGNPGIAAGGAVVIDGETQQVLASVGVYVGIATNNVAEYNGLLAGLIKAYDIDPGAlVHVRMDSKLVVE 82
Cdd:PRK07238    1 MKVVVEADGGSRGNPGPAGYGAVVWDADRGEVLAERAEAIGRATNNVAEYRGLIAGLEAAAELGATE-VEVRMDSKLVVE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1398205115  83 QMSGRWKIKHPDMAVLAAKAKDVIGN-RAVTYEWVPRLQNALADAAANKSMD 133
Cdd:PRK07238   80 QMSGRWKVKHPDMKPLAAQARELASQfGRVTYTWIPRARNAHADRLANEAMD 131
RNase_HI_like cd09279
RNAse HI family that includes archaeal, some bacterial as well as plant RNase HI; Ribonuclease ...
 5-133 9.05e-41

RNAse HI family that includes archaeal, some bacterial as well as plant RNase HI; Ribonuclease H (RNase H) is classified into two evolutionarily unrelated families, type 1 (prokaryotic RNase HI, eukaryotic RNase H1 and viral RNase H) and type 2 (prokaryotic RNase HII and HIII, and eukaryotic RNase H2). RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner. RNase H is involved in DNA replication, repair and transcription. RNase H is widely present in various organisms, including bacteria, archaea and eukaryotes and most prokaryotic and eukaryotic genomes contain multiple RNase H genes. Despite the lack of amino acid sequence homology, type 1 and type 2 RNase H share a main-chain fold and steric configurations of the four acidic active-site (DEDD) residues and have the same catalytic mechanism and functions in cells. One of the important functions of RNase H is to remove Okazaki fragments during DNA replication. Most archaeal genomes contain only type 2 RNase H (RNase HII); however, a few contain RNase HI as well. Although archaeal RNase HI sequences conserve the DEDD active-site motif, they lack other common features important for catalytic function, such as the basic protrusion region. Archaeal RNase HI homologs are more closely related to retroviral RNase HI than bacterial and eukaryotic type I RNase H in enzymatic properties.


Pssm-ID: 260011 [Multi-domain]  Cd Length: 128  Bit Score: 132.21  E-value: 9.05e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398205115   5 LIIEADGGSRGNPGIAAGGAVVIDGETQQvlASVGVYVGI-ATNNVAEYNGLLAGLIKAYDIDPGALVhVRMDSKLVVEQ 83
Cdd:cd09279     1 WTLYFDGASRGNPGPAGAGVVIYSPGGEV--LELSERLGFpATNNEAEYEALIAGLELALELGAEKLE-IYGDSQLVVNQ 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1398205115  84 MSGRWKIKHPDMAVLAAKAKDVIGN-RAVTYEWVPRLQNALADAAANKSMD 133
Cdd:cd09279    78 LNGEYKVKNERLKPLLEKVLELLAKfELVELKWIPREQNKEADALANQALD 128
RnhA COG0328
Ribonuclease HI [Replication, recombination and repair];
3-132 4.05e-33

Ribonuclease HI [Replication, recombination and repair];


Pssm-ID: 440097 [Multi-domain]  Cd Length: 136  Bit Score: 113.02  E-value: 4.05e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398205115   3 RQLIIEADGGSRGNPGIAAGGAVVIDGEtqqVLASVGVYVGIATNNVAEYNGLLAGLIKAYDIDPGAlVHVRMDSKLVVE 82
Cdd:COG0328     1 KMIEIYTDGACRGNPGPGGWGAVIRYGG---EEKELSGGLGDTTNNRAELTALIAALEALKELGPCE-VEIYTDSQYVVN 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1398205115  83 QMSG---RWK------IKHPDmavLAAKAKDVIGNRAVTYEWVPR----LQNALADAAANKSM 132
Cdd:COG0328    77 QITGwihGWKkngwkpVKNPD---LWQRLDELLARHKVTFEWVKGhaghPGNERADALANKAL 136
RNAseHI_Thmprot NF041175
ribonuclease HI;
16-134 2.53e-19

ribonuclease HI;


Pssm-ID: 469086 [Multi-domain]  Cd Length: 144  Bit Score: 78.09  E-value: 2.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398205115  16 NP-GIAAGGAVVIDGETQQV----LASVGVYVGiATNNVAEYNGLLAGLIKAYDIDPGAlVHVRMDSKLVVEQMSGRWKI 90
Cdd:NF041175   14 NPgGIATYGYVIYLDNKRKIegygLAAEPWSKD-STNNVAEYTGLICLLEKLLELGISE-VIIRGDSQLVIRQLNGEYKV 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1398205115  91 KHPDMAVLAAKAKDVIGN-RAVTYEWVPRLQNALADAAANKSMDL 134
Cdd:NF041175   92 KSPRIIPLYEKALELLSKfRSIEFEWVPREENKEADRLSRIAYEL 136
RVT_3 pfam13456
Reverse transcriptase-like; This domain is found in plants and appears to be part of a ...
 10-131 2.16e-13

Reverse transcriptase-like; This domain is found in plants and appears to be part of a retrotransposon.


Pssm-ID: 433223 [Multi-domain]  Cd Length: 123  Bit Score: 62.28  E-value: 2.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398205115  10 DGGSRGNPGIAAGGAVVIDGETQQVLASVGVYVGIATNNVAEYNGLLAGLIKAYD--IDPgalVHVRMDSKLVVEQMSGR 87
Cdd:pfam13456   3 DGAFKCDSGLAGAGVVIRDPNGNVLLAGQKKLGPGASVLEAEAQALIIGLQLAWKlgIRH---LIVEGDSATVVQLINGR 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1398205115  88 WKiKHPDMAVLAAKAKDVIGN-RAVTYEWVPRLQNALADAAANKS 131
Cdd:pfam13456  80 SP-KQSKLANLLDEIRKLLKRfESVSFEHIPREQNRVADTLAKMA 123
 
Name Accession Description Interval E-value
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
 3-133 2.02e-66

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 205.60  E-value: 2.02e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398205115   3 RQLIIEADGGSRGNPGIAAGGAVVIDGETQQVLASVGVYVGIATNNVAEYNGLLAGLIKAYDIDPGAlVHVRMDSKLVVE 82
Cdd:PRK07238    1 MKVVVEADGGSRGNPGPAGYGAVVWDADRGEVLAERAEAIGRATNNVAEYRGLIAGLEAAAELGATE-VEVRMDSKLVVE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1398205115  83 QMSGRWKIKHPDMAVLAAKAKDVIGN-RAVTYEWVPRLQNALADAAANKSMD 133
Cdd:PRK07238   80 QMSGRWKVKHPDMKPLAAQARELASQfGRVTYTWIPRARNAHADRLANEAMD 131
RNase_HI_like cd09279
RNAse HI family that includes archaeal, some bacterial as well as plant RNase HI; Ribonuclease ...
 5-133 9.05e-41

RNAse HI family that includes archaeal, some bacterial as well as plant RNase HI; Ribonuclease H (RNase H) is classified into two evolutionarily unrelated families, type 1 (prokaryotic RNase HI, eukaryotic RNase H1 and viral RNase H) and type 2 (prokaryotic RNase HII and HIII, and eukaryotic RNase H2). RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner. RNase H is involved in DNA replication, repair and transcription. RNase H is widely present in various organisms, including bacteria, archaea and eukaryotes and most prokaryotic and eukaryotic genomes contain multiple RNase H genes. Despite the lack of amino acid sequence homology, type 1 and type 2 RNase H share a main-chain fold and steric configurations of the four acidic active-site (DEDD) residues and have the same catalytic mechanism and functions in cells. One of the important functions of RNase H is to remove Okazaki fragments during DNA replication. Most archaeal genomes contain only type 2 RNase H (RNase HII); however, a few contain RNase HI as well. Although archaeal RNase HI sequences conserve the DEDD active-site motif, they lack other common features important for catalytic function, such as the basic protrusion region. Archaeal RNase HI homologs are more closely related to retroviral RNase HI than bacterial and eukaryotic type I RNase H in enzymatic properties.


Pssm-ID: 260011 [Multi-domain]  Cd Length: 128  Bit Score: 132.21  E-value: 9.05e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398205115   5 LIIEADGGSRGNPGIAAGGAVVIDGETQQvlASVGVYVGI-ATNNVAEYNGLLAGLIKAYDIDPGALVhVRMDSKLVVEQ 83
Cdd:cd09279     1 WTLYFDGASRGNPGPAGAGVVIYSPGGEV--LELSERLGFpATNNEAEYEALIAGLELALELGAEKLE-IYGDSQLVVNQ 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1398205115  84 MSGRWKIKHPDMAVLAAKAKDVIGN-RAVTYEWVPRLQNALADAAANKSMD 133
Cdd:cd09279    78 LNGEYKVKNERLKPLLEKVLELLAKfELVELKWIPREQNKEADALANQALD 128
RnhA COG0328
Ribonuclease HI [Replication, recombination and repair];
3-132 4.05e-33

Ribonuclease HI [Replication, recombination and repair];


Pssm-ID: 440097 [Multi-domain]  Cd Length: 136  Bit Score: 113.02  E-value: 4.05e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398205115   3 RQLIIEADGGSRGNPGIAAGGAVVIDGEtqqVLASVGVYVGIATNNVAEYNGLLAGLIKAYDIDPGAlVHVRMDSKLVVE 82
Cdd:COG0328     1 KMIEIYTDGACRGNPGPGGWGAVIRYGG---EEKELSGGLGDTTNNRAELTALIAALEALKELGPCE-VEIYTDSQYVVN 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1398205115  83 QMSG---RWK------IKHPDmavLAAKAKDVIGNRAVTYEWVPR----LQNALADAAANKSM 132
Cdd:COG0328    77 QITGwihGWKkngwkpVKNPD---LWQRLDELLARHKVTFEWVKGhaghPGNERADALANKAL 136
RNAseHI_Thmprot NF041175
ribonuclease HI;
16-134 2.53e-19

ribonuclease HI;


Pssm-ID: 469086 [Multi-domain]  Cd Length: 144  Bit Score: 78.09  E-value: 2.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398205115  16 NP-GIAAGGAVVIDGETQQV----LASVGVYVGiATNNVAEYNGLLAGLIKAYDIDPGAlVHVRMDSKLVVEQMSGRWKI 90
Cdd:NF041175   14 NPgGIATYGYVIYLDNKRKIegygLAAEPWSKD-STNNVAEYTGLICLLEKLLELGISE-VIIRGDSQLVIRQLNGEYKV 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1398205115  91 KHPDMAVLAAKAKDVIGN-RAVTYEWVPRLQNALADAAANKSMDL 134
Cdd:NF041175   92 KSPRIIPLYEKALELLSKfRSIEFEWVPREENKEADRLSRIAYEL 136
RNase_H_like cd06222
Ribonuclease H-like superfamily, including RNase H, HI, HII, HIII, and RNase-like domain IV of ...
 7-129 1.57e-18

Ribonuclease H-like superfamily, including RNase H, HI, HII, HIII, and RNase-like domain IV of spliceosomal protein Prp8; Ribonuclease H (RNase H) enzymes are divided into two major families, Type 1 and Type 2, based on amino acid sequence similarities and biochemical properties. RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner in the presence of divalent cations. It is widely present in various organisms, including bacteria, archaea, and eukaryotes. Most prokaryotic and eukaryotic genomes contain multiple RNase H genes. Despite the lack of amino acid sequence homology, type 1 and type 2 RNase H share a main-chain fold and steric configurations of the four acidic active-site residues and have the same catalytic mechanism and functions in cells. RNase H is involved in DNA replication, repair and transcription. An important RNase H function is to remove Okazaki fragments during DNA replication. RNase H inhibitors have been explored as anti-HIV drug targets since RNase H inactivation inhibits reverse transcription. This model also includes the Prp8 domain IV, which adopts the RNase fold but shows low sequence homology; domain IV is implicated in key spliceosomal interactions.


Pssm-ID: 259998 [Multi-domain]  Cd Length: 121  Bit Score: 75.43  E-value: 1.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398205115   7 IEADGGSRGNPGIAAGGAVVIDGETQqVLASVGVYVGIATNNVAEYNGLLAGLIKAydIDPGAL-VHVRMDSKLVVEQMS 85
Cdd:cd06222     1 INVDGSCRGNPGPAGIGGVLRDHEGG-WLGGFALKIGAPTALEAELLALLLALELA--LDLGYLkVIIESDSKYVVDLIN 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1398205115  86 GRWKIKHPDMAVLAAKAKDVIGNRAVTYEWVPRLQNALADAAAN 129
Cdd:cd06222    78 SGSFKWSPNILLIEDILLLLSRFWSVKISHVPREGNQVADALAK 121
RVT_3 pfam13456
Reverse transcriptase-like; This domain is found in plants and appears to be part of a ...
 10-131 2.16e-13

Reverse transcriptase-like; This domain is found in plants and appears to be part of a retrotransposon.


Pssm-ID: 433223 [Multi-domain]  Cd Length: 123  Bit Score: 62.28  E-value: 2.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398205115  10 DGGSRGNPGIAAGGAVVIDGETQQVLASVGVYVGIATNNVAEYNGLLAGLIKAYD--IDPgalVHVRMDSKLVVEQMSGR 87
Cdd:pfam13456   3 DGAFKCDSGLAGAGVVIRDPNGNVLLAGQKKLGPGASVLEAEAQALIIGLQLAWKlgIRH---LIVEGDSATVVQLINGR 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1398205115  88 WKiKHPDMAVLAAKAKDVIGN-RAVTYEWVPRLQNALADAAANKS 131
Cdd:pfam13456  80 SP-KQSKLANLLDEIRKLLKRfESVSFEHIPREQNRVADTLAKMA 123
RNase_HI_prokaryote_like cd09278
RNase HI family found mainly in prokaryotes; Ribonuclease H (RNase H) is classified into two ...
 4-133 1.25e-11

RNase HI family found mainly in prokaryotes; Ribonuclease H (RNase H) is classified into two evolutionarily unrelated families, type 1 (prokaryotic RNase HI, eukaryotic RNase H1 and viral RNase H) and type 2 (prokaryotic RNase HII and HIII, and eukaryotic RNase H2). RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner. RNase H is involved in DNA replication, repair and transcription. RNase H is widely present in various organisms, including bacteria, archaea and eukaryotes and most prokaryotic and eukaryotic genomes contain multiple RNase H genes. Despite the lack of amino acid sequence homology, type 1 and type 2 RNase H share a main-chain fold and steric configurations of the four acidic active-site (DEDD), residues and have the same catalytic mechanism and functions in cells. One of the important functions of RNase H is to remove Okazaki fragments during DNA replication. Prokaryotic RNase H varies greatly in domain structures and substrate specificities. Prokaryotes and some single-cell eukaryotes do not require RNase H for viability.


Pssm-ID: 260010 [Multi-domain]  Cd Length: 139  Bit Score: 57.88  E-value: 1.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398205115   4 QLIIEADGGSRGNPGIAAGGAVVIDGETQQVLAsvGVYVGiATNNVAEYNGLLAGLIKaydIDPGALVHVRMDSKLVVEQ 83
Cdd:cd09278     1 EIVIYTDGACLGNPGPGGWAAVIRYGDHEKELS--GGEPG-TTNNRMELTAAIEALEA---LKEPCPVTIYTDSQYVING 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398205115  84 MS---GRWK-----------IKHPD--MAVLAAKAKdvignRAVTYEWVP----RLQNALADAAANKSMD 133
Cdd:cd09278    75 ITkwiKGWKkngwktadgkpVKNRDlwQELDALLAG-----HKVTWEWVKghagHPGNERADRLANKAAD 139
rnhA PRK13907
ribonuclease H; Provisional
 10-132 3.45e-11

ribonuclease H; Provisional


Pssm-ID: 139967 [Multi-domain]  Cd Length: 128  Bit Score: 56.60  E-value: 3.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398205115  10 DGGSRGNPGiAAGGAVVIDGETQQVLASVGvyVGIATNNVAEYNGLLAGLikAYDIDPG-ALVHVRMDSKLvVEQMSGRW 88
Cdd:PRK13907    7 DGASKGNPG-PSGAGVFIKGVQPAVQLSLP--LGTMSNHEAEYHALLAAL--KYCTEHNyNIVSFRTDSQL-VERAVEKE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1398205115  89 KIKHPDMAVLAAKAKDVIGNRAVTY-EWVPRLQNALADAAANKSM 132
Cdd:PRK13907   81 YAKNKMFAPLLEEALQYIKSFDLFFiKWIPSSQNKVADELARKAI 125
RNase_H pfam00075
RNase H; RNase H digests the RNA strand of an RNA/DNA hybrid. Important enzyme in retroviral ...
 2-117 3.19e-07

RNase H; RNase H digests the RNA strand of an RNA/DNA hybrid. Important enzyme in retroviral replication cycle, and often found as a domain associated with reverse transcriptases. Structure is a mixed alpha+beta fold with three a/b/a layers.


Pssm-ID: 395028 [Multi-domain]  Cd Length: 141  Bit Score: 46.60  E-value: 3.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398205115   2 PRQLIIEADGGSRGNPGiAAGGAVVIDGETQQVLASvgvYVGIATNNVAEYNGLLAGLiKAYDIDPgaLVHVRMDSKLVV 81
Cdd:pfam00075   1 PKAVTVYTDGSCLGNPG-PGGAGAVLYRGHENISAP---LPGRTTNNRAELQAVIEAL-KALKSPS--KVNIYTDSQYVI 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1398205115  82 E---QMSGRWK------------IKHPDmavLAAKAKDVIGNRAVTYEWVP 117
Cdd:pfam00075  74 GgitQWVHGWKkngwpttsegkpVKNKD---LWQLLKALCKKHQVYWQWVK 121
PRK07708 PRK07708
hypothetical protein; Validated
 43-133 2.20e-04

hypothetical protein; Validated


Pssm-ID: 181088 [Multi-domain]  Cd Length: 219  Bit Score: 39.25  E-value: 2.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398205115  43 GIATNNVAEYNGLLAGLIKAYDIDPGAL-VHVRMDSKLVVEQMSGRWKIKHPDMAV----LAAKAKDVigNRAVTYEWVP 117
Cdd:PRK07708  114 GIYDNNEAEYAALYYAMQELEELGVKHEpVTFRGDSQVVLNQLAGEWPCYDEHLNHwldrIEQKLKQL--KLTPVYEPIS 191

                          90
                  ....*....|....*.
gi 1398205115 118 RLQNALADAAANKSMD 133
Cdd:PRK07708  192 RKQNKEADQLATQALE 207
 
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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