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Conserved domains on  [gi|1279769253|ref|XP_022937206|]
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polynucleotide 3'-phosphatase ZDP isoform X1 [Cucurbita moschata]

Protein Classification

polynucleotide 3'-phosphatase; HAD family hydrolase( domain architecture ID 12004038)

polynucleotide 3'-phosphatase dephosphorylates single-stranded as well as double-stranded 3'-phospho termini; it belongs to the HAD (haloacid dehalogenase) family of hydrolases, which includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates.; haloacid dehalogenase (HAD) family hydrolase containing a mannitol dehydrogenase domain, uses a nucleophilic aspartate in the phosphoryl transfer reaction; the HAD family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_PNP cd01625
polynucleotide 3'-phosphatase domain similar to the phosphatase domain of the bifunctional ...
 205-368 1.08e-67

polynucleotide 3'-phosphatase domain similar to the phosphatase domain of the bifunctional enzyme polynucleotide 5'-kinase/3'-phosphatase; Polynucleotide 3'-phosphatase (PNP) domain. This domain dephosphorylates single-stranded as well as double-stranded 3'-phospho termini. It is found in bifunctional enzyme polynucleotide kinase/phosphatase (PNKP) which contain both kinase and phosphatase domains. PNKP plays a key role in both base excision repair and non-homologous end-joining DNA repair pathway. DNA strand breaks can result from DNA damage by ionizing radiation and chemical agents, such as alkylating agents or anticancer agents. Such DNA damage often results in DNA strands with 5'-hydroxyl and 3'-phosphate termini. However, the repair of DNA damage by DNA polymerases and ligases requires 5'-phosphate and 3'-hydroxyl termini. PNKP acts as a 5'-kinase/3'-phosphatase to create 5'-phosphate/3'-hydroxyl termini, which are a necessary prerequisite for ligation during repair. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


:

Pssm-ID: 319766  Cd Length: 154  Bit Score: 210.28  E-value: 1.08e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279769253 205 KIAAFDFDGCLANTSVKRV---GAEAWSLMYPLIPHKLQSLYNEGYKLVIFTNESNIERWKNKRqvavDSKLGRLDSFIS 281
Cdd:cd01625     1 KVAAFDLDGTLIKTKSGKVfptNASDWQILYPSVPEKLKALHKDGYKIVIFTNQGGIVRGKLTP----EVFKGKIEAILE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279769253 282 RVNVPVQVFVACGIGggsgkseedPFRKPKPGMWQIMENHFNGGIPINLDQCFYVGDAAGRAKDHSDTDLRFAQAIGLKF 361
Cdd:cd01625    77 KLGVPIQVYAATKKG---------KYRKPVTGMWDHLKEDLNSGIPINLKDSFYVGDAAGRPKDFSDSDRLFAENVGLKF 147


                  ....*..
gi 1279769253 362 YVPEEFF 368
Cdd:cd01625   148 FTPEEFF 154
zf-PARP pfam00645
Poly(ADP-ribose) polymerase and DNA-Ligase Zn-finger region; Poly(ADP-ribose) polymerase is an ...
 50-125 1.82e-18

Poly(ADP-ribose) polymerase and DNA-Ligase Zn-finger region; Poly(ADP-ribose) polymerase is an important regulatory component of the cellular response to DNA damage. The amino-terminal region of Poly(ADP-ribose) polymerase consists of two PARP-type zinc fingers. This region acts as a DNA nick sensor.


:

Pssm-ID: 459887 [Multi-domain]  Cd Length: 87  Bit Score: 79.28  E-value: 1.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279769253  50 EYAKSNRSTCKNCSKTIPAKALRLG----FVSRDGRGFDMTRWFHSDC-------ASFGSDPVSSAEEINGFALLKGDDQ 118
Cdd:pfam00645   1 EYAKSGRAKCKGCKKKIEKGELRIGkvvdFVPSPFFDGGSKRWYHWGCftkkqlkNRKETKEIDDADDLDGFDELKDEDQ 80


                  ....*..
gi 1279769253 119 EALKKLV 125
Cdd:pfam00645  81 EKIRKAI 87
PLN03123 super family cl33639
poly [ADP-ribose] polymerase; Provisional
 42-204 1.33e-06

poly [ADP-ribose] polymerase; Provisional


The actual alignment was detected with superfamily member PLN03123:

Pssm-ID: 215590 [Multi-domain]  Cd Length: 981  Bit Score: 50.56  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279769253  42 TSAVKIVAEYAKSNRSTCKNCSKTIPAKALRLgFVSRDGRGFDMTRWFHSDC--ASFGSDPVssaEEINGFALLKGDDQE 119
Cdd:PLN03123  102 ASSFEYGIEVAKTSRATCRRCSEKILKGEVRI-SSKPEGQGYKGLAWHHAKCflEMSPSTPV---EKLSGWDTLSDSDQE 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279769253 120 ALKKLVSRSHESKVRKRDEDEEDGIEERDQKKVELSA--SSLLPKLDLVLTASNIKTKYKDATLLPKWKAFQTLIFLEQD 197
Cdd:PLN03123  178 AVLPLVKKSPSEAKEEKAEERKQESKKGAKRKKDASGddKSKKAKTDRDVSTSTAASQKKSSDLESKLEAQSKELWSLKD 257


                  ....*..
gi 1279769253 198 DGLHHSS 204
Cdd:PLN03123  258 DLKKHVS 264
 
Name Accession Description Interval E-value
HAD_PNP cd01625
polynucleotide 3'-phosphatase domain similar to the phosphatase domain of the bifunctional ...
 205-368 1.08e-67

polynucleotide 3'-phosphatase domain similar to the phosphatase domain of the bifunctional enzyme polynucleotide 5'-kinase/3'-phosphatase; Polynucleotide 3'-phosphatase (PNP) domain. This domain dephosphorylates single-stranded as well as double-stranded 3'-phospho termini. It is found in bifunctional enzyme polynucleotide kinase/phosphatase (PNKP) which contain both kinase and phosphatase domains. PNKP plays a key role in both base excision repair and non-homologous end-joining DNA repair pathway. DNA strand breaks can result from DNA damage by ionizing radiation and chemical agents, such as alkylating agents or anticancer agents. Such DNA damage often results in DNA strands with 5'-hydroxyl and 3'-phosphate termini. However, the repair of DNA damage by DNA polymerases and ligases requires 5'-phosphate and 3'-hydroxyl termini. PNKP acts as a 5'-kinase/3'-phosphatase to create 5'-phosphate/3'-hydroxyl termini, which are a necessary prerequisite for ligation during repair. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319766  Cd Length: 154  Bit Score: 210.28  E-value: 1.08e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279769253 205 KIAAFDFDGCLANTSVKRV---GAEAWSLMYPLIPHKLQSLYNEGYKLVIFTNESNIERWKNKRqvavDSKLGRLDSFIS 281
Cdd:cd01625     1 KVAAFDLDGTLIKTKSGKVfptNASDWQILYPSVPEKLKALHKDGYKIVIFTNQGGIVRGKLTP----EVFKGKIEAILE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279769253 282 RVNVPVQVFVACGIGggsgkseedPFRKPKPGMWQIMENHFNGGIPINLDQCFYVGDAAGRAKDHSDTDLRFAQAIGLKF 361
Cdd:cd01625    77 KLGVPIQVYAATKKG---------KYRKPVTGMWDHLKEDLNSGIPINLKDSFYVGDAAGRPKDFSDSDRLFAENVGLKF 147


                  ....*..
gi 1279769253 362 YVPEEFF 368
Cdd:cd01625   148 FTPEEFF 154
DNA-3'-Pase TIGR01664
DNA 3'-phosphatase; This model represents a family of proteins and protein domains which ...
 192-368 2.50e-63

DNA 3'-phosphatase; This model represents a family of proteins and protein domains which catalyze the dephosphorylation of DNA 3'-phosphates. It is believed that this activity is important for the repair of single-strand breaks in DNA caused by radiation or oxidative damage. This domain is often (TIGR01663), but not always linked to a DNA 5'-kinase domain. The central phosphatase domain is a member of the IIIA subfamily (TIGR01662) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. As is common in this superfamily, the enzyme is magnesium dependent. A difference between this enzyme and other HAD-superfamily phosphatases is in the third conserved catalytic motif which usually contains two conserved aspartate residues believed to be involved in binding the magnesium ion. Here, the second aspartate is usually replaced by an arginine residue which may indicate an interaction with the phosphate backbone of the substrate. Alternatively, there is an additional conserved aspartate downstream of the ususal site which may indicate slightly different fold in this region.


Pssm-ID: 211680  Cd Length: 166  Bit Score: 199.60  E-value: 2.50e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279769253 192 IFLEQDDGLHHSSKIAAFDFDGCLANTSVKRVG---AEAWSLMYPLIPHKLQSLYNEGYKLVIFTNESNIERWKnkrqVA 268
Cdd:TIGR01664   1 LFVFTADGPKPQSKVAAFDLDGTLITTRSGKVFptsASDWRFLYPEIPAKLQELDDEGYKIVIFTNQSGIGRGK----LS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279769253 269 VDSKLGRLDSFISRVNVPVQVFVACGIGggsgkseedPFRKPKPGMWQIMENHFNGgiPINLDQCFYVGDAAGRAKDHSD 348
Cdd:TIGR01664  77 AESFKNKIEAFLEKLKVPIQVLAATHAG---------LYRKPMTGMWEYLQSQYNS--PIKMTRSFYVGDAAGRKLDFSD 145

                         170       180
                  ....*....|....*....|
gi 1279769253 349 TDLRFAQAIGLKFYVPEEFF 368
Cdd:TIGR01664 146 ADIKFAKNLGLEFKYPEEFF 165
PNK3P pfam08645
Polynucleotide kinase 3 phosphatase; Polynucleotide kinase 3 phosphatases play a role in the ...
 205-368 1.31e-62

Polynucleotide kinase 3 phosphatase; Polynucleotide kinase 3 phosphatases play a role in the repair of single breaks in DNA induced by DNA-damaging agents such as gamma radiation and camptothecin.


Pssm-ID: 370030  Cd Length: 161  Bit Score: 197.48  E-value: 1.31e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279769253 205 KIAAFDFDGCLANTSVKRV---GAEAWSLMYPLIPHKLQSLYNEGYKLVIFTNESNIERWKNKRqvaVDSKLGRLDSFIS 281
Cdd:pfam08645   1 KIAAFDLDGTLIKTKSGKVfprNPDDWKWLYPSVPEKLKKLHEDGYKIVIFTNQGGIGRKGKKS---LEKFKNKIEAILK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279769253 282 RVNVPVQVFVACGigggsgkseEDPFRKPKPGMWQIMENHFNGGIPINLDQCFYVGDAAGRA------KDHSDTDLRFAQ 355
Cdd:pfam08645  78 KLGVPLQVYAATK---------KDIYRKPNTGMWDEMKKDYNDGVEIDLEKSFYVGDAAGRPydtrrkKDFSDSDRKFAL 148

                         170
                  ....*....|...
gi 1279769253 356 AIGLKFYVPEEFF 368
Cdd:pfam08645 149 NVGIKFKTPEEFF 161
zf-PARP pfam00645
Poly(ADP-ribose) polymerase and DNA-Ligase Zn-finger region; Poly(ADP-ribose) polymerase is an ...
 50-125 1.82e-18

Poly(ADP-ribose) polymerase and DNA-Ligase Zn-finger region; Poly(ADP-ribose) polymerase is an important regulatory component of the cellular response to DNA damage. The amino-terminal region of Poly(ADP-ribose) polymerase consists of two PARP-type zinc fingers. This region acts as a DNA nick sensor.


Pssm-ID: 459887 [Multi-domain]  Cd Length: 87  Bit Score: 79.28  E-value: 1.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279769253  50 EYAKSNRSTCKNCSKTIPAKALRLG----FVSRDGRGFDMTRWFHSDC-------ASFGSDPVSSAEEINGFALLKGDDQ 118
Cdd:pfam00645   1 EYAKSGRAKCKGCKKKIEKGELRIGkvvdFVPSPFFDGGSKRWYHWGCftkkqlkNRKETKEIDDADDLDGFDELKDEDQ 80


                  ....*..
gi 1279769253 119 EALKKLV 125
Cdd:pfam00645  81 EKIRKAI 87
PLN03123 PLN03123
poly [ADP-ribose] polymerase; Provisional
 49-125 2.47e-10

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215590 [Multi-domain]  Cd Length: 981  Bit Score: 62.12  E-value: 2.47e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1279769253  49 AEYAKSNRSTCKNCSKTIPAKALRLGFVSRDGRgFD--MTRWFHSDCASFGSDPVSSAEEINGFALLKGDDQEALKKLV 125
Cdd:PLN03123   10 AEYAKSSRSSCKTCKSPIDKDELRLGKMVQSTQ-FDgfMPMWNHASCILKKKNQIKSIDDVEGIDSLRWEDQQKIRKYV 87
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
232-362 4.25e-07

Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 50.31  E-value: 4.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279769253 232 YPLIPHKLQSLYNEGYKLVIFTnesnierwkNKRQVAVDSKLGR--LDSFISRVnvpvqvfvacgIGGgsgksEEDPFRK 309
Cdd:COG0546    86 FPGVRELLEALKARGIKLAVVT---------NKPREFAERLLEAlgLDDYFDAI-----------VGG-----DDVPPAK 140

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1279769253 310 PKPGM-WQIMENHfnggiPINLDQCFYVGDaagrakdhSDTDLRFAQAIGLKFY 362
Cdd:COG0546   141 PKPEPlLEALERL-----GLDPEEVLMVGD--------SPHDIEAARAAGVPFI 181
PLN03123 PLN03123
poly [ADP-ribose] polymerase; Provisional
 42-204 1.33e-06

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215590 [Multi-domain]  Cd Length: 981  Bit Score: 50.56  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279769253  42 TSAVKIVAEYAKSNRSTCKNCSKTIPAKALRLgFVSRDGRGFDMTRWFHSDC--ASFGSDPVssaEEINGFALLKGDDQE 119
Cdd:PLN03123  102 ASSFEYGIEVAKTSRATCRRCSEKILKGEVRI-SSKPEGQGYKGLAWHHAKCflEMSPSTPV---EKLSGWDTLSDSDQE 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279769253 120 ALKKLVSRSHESKVRKRDEDEEDGIEERDQKKVELSA--SSLLPKLDLVLTASNIKTKYKDATLLPKWKAFQTLIFLEQD 197
Cdd:PLN03123  178 AVLPLVKKSPSEAKEEKAEERKQESKKGAKRKKDASGddKSKKAKTDRDVSTSTAASQKKSSDLESKLEAQSKELWSLKD 257


                  ....*..
gi 1279769253 198 DGLHHSS 204
Cdd:PLN03123  258 DLKKHVS 264
 
Name Accession Description Interval E-value
HAD_PNP cd01625
polynucleotide 3'-phosphatase domain similar to the phosphatase domain of the bifunctional ...
 205-368 1.08e-67

polynucleotide 3'-phosphatase domain similar to the phosphatase domain of the bifunctional enzyme polynucleotide 5'-kinase/3'-phosphatase; Polynucleotide 3'-phosphatase (PNP) domain. This domain dephosphorylates single-stranded as well as double-stranded 3'-phospho termini. It is found in bifunctional enzyme polynucleotide kinase/phosphatase (PNKP) which contain both kinase and phosphatase domains. PNKP plays a key role in both base excision repair and non-homologous end-joining DNA repair pathway. DNA strand breaks can result from DNA damage by ionizing radiation and chemical agents, such as alkylating agents or anticancer agents. Such DNA damage often results in DNA strands with 5'-hydroxyl and 3'-phosphate termini. However, the repair of DNA damage by DNA polymerases and ligases requires 5'-phosphate and 3'-hydroxyl termini. PNKP acts as a 5'-kinase/3'-phosphatase to create 5'-phosphate/3'-hydroxyl termini, which are a necessary prerequisite for ligation during repair. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319766  Cd Length: 154  Bit Score: 210.28  E-value: 1.08e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279769253 205 KIAAFDFDGCLANTSVKRV---GAEAWSLMYPLIPHKLQSLYNEGYKLVIFTNESNIERWKNKRqvavDSKLGRLDSFIS 281
Cdd:cd01625     1 KVAAFDLDGTLIKTKSGKVfptNASDWQILYPSVPEKLKALHKDGYKIVIFTNQGGIVRGKLTP----EVFKGKIEAILE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279769253 282 RVNVPVQVFVACGIGggsgkseedPFRKPKPGMWQIMENHFNGGIPINLDQCFYVGDAAGRAKDHSDTDLRFAQAIGLKF 361
Cdd:cd01625    77 KLGVPIQVYAATKKG---------KYRKPVTGMWDHLKEDLNSGIPINLKDSFYVGDAAGRPKDFSDSDRLFAENVGLKF 147


                  ....*..
gi 1279769253 362 YVPEEFF 368
Cdd:cd01625   148 FTPEEFF 154
DNA-3'-Pase TIGR01664
DNA 3'-phosphatase; This model represents a family of proteins and protein domains which ...
 192-368 2.50e-63

DNA 3'-phosphatase; This model represents a family of proteins and protein domains which catalyze the dephosphorylation of DNA 3'-phosphates. It is believed that this activity is important for the repair of single-strand breaks in DNA caused by radiation or oxidative damage. This domain is often (TIGR01663), but not always linked to a DNA 5'-kinase domain. The central phosphatase domain is a member of the IIIA subfamily (TIGR01662) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. As is common in this superfamily, the enzyme is magnesium dependent. A difference between this enzyme and other HAD-superfamily phosphatases is in the third conserved catalytic motif which usually contains two conserved aspartate residues believed to be involved in binding the magnesium ion. Here, the second aspartate is usually replaced by an arginine residue which may indicate an interaction with the phosphate backbone of the substrate. Alternatively, there is an additional conserved aspartate downstream of the ususal site which may indicate slightly different fold in this region.


Pssm-ID: 211680  Cd Length: 166  Bit Score: 199.60  E-value: 2.50e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279769253 192 IFLEQDDGLHHSSKIAAFDFDGCLANTSVKRVG---AEAWSLMYPLIPHKLQSLYNEGYKLVIFTNESNIERWKnkrqVA 268
Cdd:TIGR01664   1 LFVFTADGPKPQSKVAAFDLDGTLITTRSGKVFptsASDWRFLYPEIPAKLQELDDEGYKIVIFTNQSGIGRGK----LS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279769253 269 VDSKLGRLDSFISRVNVPVQVFVACGIGggsgkseedPFRKPKPGMWQIMENHFNGgiPINLDQCFYVGDAAGRAKDHSD 348
Cdd:TIGR01664  77 AESFKNKIEAFLEKLKVPIQVLAATHAG---------LYRKPMTGMWEYLQSQYNS--PIKMTRSFYVGDAAGRKLDFSD 145

                         170       180
                  ....*....|....*....|
gi 1279769253 349 TDLRFAQAIGLKFYVPEEFF 368
Cdd:TIGR01664 146 ADIKFAKNLGLEFKYPEEFF 165
PNK3P pfam08645
Polynucleotide kinase 3 phosphatase; Polynucleotide kinase 3 phosphatases play a role in the ...
 205-368 1.31e-62

Polynucleotide kinase 3 phosphatase; Polynucleotide kinase 3 phosphatases play a role in the repair of single breaks in DNA induced by DNA-damaging agents such as gamma radiation and camptothecin.


Pssm-ID: 370030  Cd Length: 161  Bit Score: 197.48  E-value: 1.31e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279769253 205 KIAAFDFDGCLANTSVKRV---GAEAWSLMYPLIPHKLQSLYNEGYKLVIFTNESNIERWKNKRqvaVDSKLGRLDSFIS 281
Cdd:pfam08645   1 KIAAFDLDGTLIKTKSGKVfprNPDDWKWLYPSVPEKLKKLHEDGYKIVIFTNQGGIGRKGKKS---LEKFKNKIEAILK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279769253 282 RVNVPVQVFVACGigggsgkseEDPFRKPKPGMWQIMENHFNGGIPINLDQCFYVGDAAGRA------KDHSDTDLRFAQ 355
Cdd:pfam08645  78 KLGVPLQVYAATK---------KDIYRKPNTGMWDEMKKDYNDGVEIDLEKSFYVGDAAGRPydtrrkKDFSDSDRKFAL 148

                         170
                  ....*....|...
gi 1279769253 356 AIGLKFYVPEEFF 368
Cdd:pfam08645 149 NVGIKFKTPEEFF 161
PNK-3'Pase TIGR01663
polynucleotide 5'-kinase 3'-phosphatase; This model represents the metazoan 5 ...
 173-369 1.69e-40

polynucleotide 5'-kinase 3'-phosphatase; This model represents the metazoan 5'-polynucleotide-kinase-3'-phosphatase, PNKP, which is believed to be involved in repair of oxidative DNA damage. Removal of 3' phosphates is essential for the further processing of the break by DNA polymerases. The central phosphatase domain is a member of the IIIA subfamily (TIGR01662) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. As is common in this superfamily, the enzyme is magnesium dependent. A difference between this enzyme and other HAD-superfamily phosphatases is in the third conserved catalytic motif which usually contains two conserved aspartate residues believed to be involved in binding the magnesium ion. Here, the second aspartate is replaced by a conserved arginine residue which may indicate an interaction with the phosphate backbone of the substrate. Very close relatives of this domain are also found separate from the N- and C-terminal domains seen here, as in the 3'-phosphatase found in plants. The larger family of these domains is described by TIGR01664. Outside of the phosphatase domain is a P-loop ATP-binding motif associated with the kinase activity. The entry for the mouse homolog appears to be missing a large piece of sequence corresponding to the first conserved catalytic motif of the phosphatase domain as well as the conserved threonine of the second motif. Either this is a sequencing artifact or this may represent a pseudo- or non-functional gene. Note that the EC number for the kinase function is: 2.7.1.78


Pssm-ID: 130724 [Multi-domain]  Cd Length: 526  Bit Score: 149.79  E-value: 1.69e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279769253 173 KTKYKDATLLPKWKAFQTLIFLEQDdGLHHSSKIAAFDFDGCLANTSVKRV---GAEAWSLMYPLIPHKLQSLYNEGYKL 249
Cdd:TIGR01663 138 KPEKRDRKGNPGWENLEKLLIFTAA-GVKGQEKIAGFDLDGTIIKTKSGKVfpkGPDDWQIIFPEIPEKLKELEADGFKI 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279769253 250 VIFTNESNIERWKnkrqVAVDSKLGRLDSFISRVNVPVQVFVACGIGggsgkseedPFRKPKPGMWQIMENHFNGGIPIN 329
Cdd:TIGR01663 217 CIFTNQGGIARGK----INADDFKAKIEAIVAKLGVPFQVFIAIGAG---------FYRKPLTGMWDHLKEEANDGTEIQ 283

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1279769253 330 LDQCFYVGDAAGRA----------KDHSDTDLRFAQAIGLKFYVPEEFFV 369
Cdd:TIGR01663 284 EDDCFFVGDAAGRPangkaagkkkKDFSCADRLFAANLGIPFATPEEFFL 333
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 205-361 1.64e-33

HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class III subfamilies are characterized by the lack of any domains located between either between the first and second conserved catalytic motifs (as in the Class I subfamilies, TIGR01493, TIGR01509, TIGR01488 and TIGR01494) or between the second and third conserved catalytic motifs (as in the Class II subfamilies, TIGR01460 and TIGR01484) of the superfamily domain. The IIIA subfamily contains five major clades: histidinol-phosphatase (TIGR01261) and histidinol-phosphatase-related protein (TIGR00213) which together form a subfamily (TIGR01656), DNA 3'-phosphatase (TIGR01663, TIGR01664), YqeG (TIGR01668) and YrbI (TIGR01670). In the case of histidinol phosphatase and PNK-3'-phosphatase, this model represents a domain of a bifunctional system. In the histidinol phosphatase HisB, a C-terminal domain is an imidazoleglycerol-phosphate dehydratase which catalyzes a related step in histidine biosynthesis. In PNK-3'-phosphatase, N- and C-terminal domains constitute the polynucleotide kinase and DNA-binding components of the enzyme. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273742 [Multi-domain]  Cd Length: 135  Bit Score: 121.36  E-value: 1.64e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279769253 205 KIAAFDFDGCLaNTSVKRVGAEAWSLMYPLIPHKLQSLYNEGYKLVIFTNESNIERWKNKRQVAvdsklGRLDSFISRVN 284
Cdd:TIGR01662   1 KAVVLDLDGTL-TDDVPYVSDEDERILYPEVPDALAELKEAGYKVVIVTNQSGIGRGYFSRSFS-----GRVARRLEELG 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1279769253 285 VPVQVFVACGigggsgkseedPFRKPKPGMWQIMENHFNGgipINLDQCFYVGDAAGrakdhsdTDLRFAQAIGLKF 361
Cdd:TIGR01662  75 VPIDILYACP-----------GCRKPKPGMFLEALKRFNE---IDPEESVYVGDQDL-------TDLQAAKRVGLAT 130
zf-PARP pfam00645
Poly(ADP-ribose) polymerase and DNA-Ligase Zn-finger region; Poly(ADP-ribose) polymerase is an ...
 50-125 1.82e-18

Poly(ADP-ribose) polymerase and DNA-Ligase Zn-finger region; Poly(ADP-ribose) polymerase is an important regulatory component of the cellular response to DNA damage. The amino-terminal region of Poly(ADP-ribose) polymerase consists of two PARP-type zinc fingers. This region acts as a DNA nick sensor.


Pssm-ID: 459887 [Multi-domain]  Cd Length: 87  Bit Score: 79.28  E-value: 1.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279769253  50 EYAKSNRSTCKNCSKTIPAKALRLG----FVSRDGRGFDMTRWFHSDC-------ASFGSDPVSSAEEINGFALLKGDDQ 118
Cdd:pfam00645   1 EYAKSGRAKCKGCKKKIEKGELRIGkvvdFVPSPFFDGGSKRWYHWGCftkkqlkNRKETKEIDDADDLDGFDELKDEDQ 80


                  ....*..
gi 1279769253 119 EALKKLV 125
Cdd:pfam00645  81 EKIRKAI 87
PLN03123 PLN03123
poly [ADP-ribose] polymerase; Provisional
 49-125 2.47e-10

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215590 [Multi-domain]  Cd Length: 981  Bit Score: 62.12  E-value: 2.47e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1279769253  49 AEYAKSNRSTCKNCSKTIPAKALRLGFVSRDGRgFD--MTRWFHSDCASFGSDPVSSAEEINGFALLKGDDQEALKKLV 125
Cdd:PLN03123   10 AEYAKSSRSSCKTCKSPIDKDELRLGKMVQSTQ-FDgfMPMWNHASCILKKKNQIKSIDDVEGIDSLRWEDQQKIRKYV 87
HAD_HisB-N cd07503
histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal ...
 246-360 1.22e-07

histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal domain of the Escherichia coli bifunctional enzyme histidinol-phosphate phosphatase/imidazole-glycerol-phosphate dehydratase, HisB. The N-terminal histidinol-phosphate phosphatase domain catalyzes the dephosphorylation of histidinol phosphate, the eight step of L-histidine biosynthesis. This family also includes Escherichia coli GmhB phosphatase which is highly specific for D-glycero-D-manno-heptose-1,7-bisphosphate, it removes the C(7)phosphate and not the C(1)phosphate, and this is the third essential step of lipopolysaccharide heptose biosynthesis. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319806 [Multi-domain]  Cd Length: 142  Bit Score: 50.22  E-value: 1.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279769253 246 GYKLVIFTNESNIER----WKNKRQVavdskLGRLDSFISRVNVPVQVFVACgiggGSGKSEEDPFRKPKPGMWQIMENH 321
Cdd:cd07503    41 GYLVVVVTNQSGIARgyfsEADFEAL-----HDKMRELLASQGVEIDDIYYC----PHHPDDGCPCRKPKPGMLLDAAKE 111

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1279769253 322 FNggipINLDQCFYVGDaagrakdhSDTDLRFAQAIGLK 360
Cdd:cd07503   112 LG----IDLARSFVIGD--------RLSDIQAARNAGCK 138
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
232-362 4.25e-07

Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 50.31  E-value: 4.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279769253 232 YPLIPHKLQSLYNEGYKLVIFTnesnierwkNKRQVAVDSKLGR--LDSFISRVnvpvqvfvacgIGGgsgksEEDPFRK 309
Cdd:COG0546    86 FPGVRELLEALKARGIKLAVVT---------NKPREFAERLLEAlgLDDYFDAI-----------VGG-----DDVPPAK 140

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1279769253 310 PKPGM-WQIMENHfnggiPINLDQCFYVGDaagrakdhSDTDLRFAQAIGLKFY 362
Cdd:COG0546   141 PKPEPlLEALERL-----GLDPEEVLMVGD--------SPHDIEAARAAGVPFI 181
PLN03123 PLN03123
poly [ADP-ribose] polymerase; Provisional
 42-204 1.33e-06

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215590 [Multi-domain]  Cd Length: 981  Bit Score: 50.56  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279769253  42 TSAVKIVAEYAKSNRSTCKNCSKTIPAKALRLgFVSRDGRGFDMTRWFHSDC--ASFGSDPVssaEEINGFALLKGDDQE 119
Cdd:PLN03123  102 ASSFEYGIEVAKTSRATCRRCSEKILKGEVRI-SSKPEGQGYKGLAWHHAKCflEMSPSTPV---EKLSGWDTLSDSDQE 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279769253 120 ALKKLVSRSHESKVRKRDEDEEDGIEERDQKKVELSA--SSLLPKLDLVLTASNIKTKYKDATLLPKWKAFQTLIFLEQD 197
Cdd:PLN03123  178 AVLPLVKKSPSEAKEEKAEERKQESKKGAKRKKDASGddKSKKAKTDRDVSTSTAASQKKSSDLESKLEAQSKELWSLKD 257


                  ....*..
gi 1279769253 198 DGLHHSS 204
Cdd:PLN03123  258 DLKKHVS 264
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 225-360 3.55e-06

FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily (riboflavin biosynthesis) [Coenzyme transport and metabolism];


Pssm-ID: 440635 [Multi-domain]  Cd Length: 220  Bit Score: 47.33  E-value: 3.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279769253 225 AEAWSLMYPLIPH---KLQSLYNEGYKLVIFTNeSNIERWKNKRQvavdsKLGrLDSFISRvnvpvqVFVACGIGggsgk 301
Cdd:COG1011    85 LAALPELVEPYPDaleLLEALKARGYRLALLTN-GSAELQEAKLR-----RLG-LDDLFDA------VVSSEEVG----- 146

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1279769253 302 seedpFRKPKPGMWQIMENHFNggipINLDQCFYVGdaagrakDHSDTDLRFAQAIGLK 360
Cdd:COG1011   147 -----VRKPDPEIFELALERLG----VPPEEALFVG-------DSPETDVAGARAAGMR 189
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
 239-360 4.00e-06

Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino acid transport and metabolism]; Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 440011 [Multi-domain]  Cd Length: 176  Bit Score: 46.63  E-value: 4.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279769253 239 LQSLYNEGYKLVIFTNESNIER----WKnkrqvAVDSKLGRLDSFISRVNVPVQVFVACGigggSGKSEEDPFRKPKPGM 314
Cdd:COG0241    37 LARLNEAGYRLVVVTNQSGIGRglftEE-----DLNAVHAKMLELLAAEGGRIDAIYYCP----HHPDDNCDCRKPKPGM 107

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1279769253 315 -WQIMENHfnggiPINLDQCFYVGDaagrakdhSDTDLRFAQAIGLK 360
Cdd:COG0241   108 lLQAAERL-----GIDLSNSYMIGD--------RLSDLQAAKAAGCK 141
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 209-361 1.09e-03

Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily includes L-2-haloacid dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, and many others. This superfamily includes a variety of enzymes that catalyze the cleavage of substrate C-Cl, P-C, and P-OP bonds via nucleophilic substitution pathways. All of which use a nucleophilic aspartate in their phosphoryl transfer reaction. They catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. Members of this superfamily are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 38.15  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279769253 209 FDFDGCLantsvkrvgaeawslmypLIPHKLQSLYNEGYKLVIFTNESNIERWKNKRQvavdskLGRLDSFIsrvnvpvq 288
Cdd:cd01427     4 FDLDGTL------------------LAVELLKRLRAAGIKLAIVTNRSREALRALLEK------LGLGDLFD-------- 51

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1279769253 289 vFVACgigggsgkSEEDPFRKPKPGMWQIMENHFNggipINLDQCFYVGDaagrakdhSDTDLRFAQAIGLKF 361
Cdd:cd01427    52 -GIIG--------SDGGGTPKPKPKPLLLLLLKLG----VDPEEVLFVGD--------SENDIEAARAAGGRT 103
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 177-339 4.30e-03

haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or Dx(3-4)E; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions.The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)(D/E), (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 1 (this model) is found in the enzymes phosphoglycolate phosphatase (TIGR01449) and enolase-phosphatase. These three variant models (see also TIGR01493 and TIGR01509) were created withthe knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly relatedHAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273686 [Multi-domain]  Cd Length: 164  Bit Score: 37.76  E-value: 4.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279769253 177 KDATLLP----KWKAFQtLIFLEQDDGLHHsskIAAFDFDGCLANTSVKRVGAEAW-------------SLMYPLIPHK- 238
Cdd:TIGR01549   6 IDGTLVDikfaIRRAFP-QTFEEFGLDPAS---FKALKQAGGLAEEEWYRIATSALeelqgrfwseydaEEAYIRGAADl 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279769253 239 LQSLYNEGYKLVIFTNESnieRWKNKRqVAVDSKLGRLDSFISRvnvpvqvfvacgigggsgksEEDPFRKPKPGMWQIM 318
Cdd:TIGR01549  82 LARLKSAGIKLGIISNGS---LRAQKL-LLRLFGLGDYFELILV--------------------SDEPGSKPEPEIFLAA 137

                         170       180
                  ....*....|....*....|.
gi 1279769253 319 ENHFNGGipinlDQCFYVGDA 339
Cdd:TIGR01549 138 LESLGVP-----PEVLHVGDN 153
Histidinol-ppas TIGR01656
histidinol-phosphate phosphatase family domain; This domain is found in authentic ...
 209-360 7.87e-03

histidinol-phosphate phosphatase family domain; This domain is found in authentic histidinol-phosphate phosphatases which are sometimes found as stand-alone entities and sometimes as fusions with imidazoleglycerol-phosphate dehydratase (TIGR01261). Additionally, a family of proteins including YaeD from E. coli (TIGR00213) and various other proteins are closely related but may not have the same substrate specificity. This domain is a member of the haloacid-dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. This superfamily is distinguished by the presence of three motifs: an N-terminal motif containing the nucleophilic aspartate, a central motif containing an conserved serine or threonine, and a C-terminal motif containing a conserved lysine (or arginine) and conserved aspartates. More specifically, the domian modelled here is a member of subfamily III of the HAD-superfamily by virtue of lacking a "capping" domain in either of the two common positions, between motifs 1 and 2, or between motifs 2 and 3.


Pssm-ID: 273737  Cd Length: 147  Bit Score: 36.61  E-value: 7.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279769253 209 FDFDGCLANTSVKRVG--AEAWSLMYPLIPhKLQSLYNEGYKLVIFTNESNIERwKNKRQVAVDSKLGRLDSFISRVNVP 286
Cdd:TIGR01656   5 LDRDGVINEDTVSDYPrsLDDWQLRPGAVP-ALLTLRAAGYTVVVVTNQSGIGR-GYFSAEAFRAPNGRLLELLRQLGVA 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1279769253 287 VQVFVACGigggSGKSEEDPFRKPKPGMWqimeNHFNGGIPINLDQCFYVGDaagrakdhSDTDLRFAQAIGLK 360
Cdd:TIGR01656  83 VDGVLFCP----HHPADNCSCRKPKPGLI----LEALKRLGVDASRSLVVGD--------RLRDLQAARNAGAA 140
 
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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