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Conserved domains on  [gi|489737577|ref|WP_003641672|]
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MULTISPECIES: arsenate reductase (thioredoxin) [Lactobacillaceae]

Protein Classification

arsenate reductase (thioredoxin)( domain architecture ID 10798604)

arsenate reductase (thioredoxin) catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)]

CATH:  3.40.50.2300
EC:  1.20.4.4
Gene Ontology:  GO:0030612
SCOP:  4000436

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
arsC_pI258_fam TIGR02691
arsenate reductase (thioredoxin); This family describes the well-studied thioredoxin-dependent ...
 4-132 3.57e-90

arsenate reductase (thioredoxin); This family describes the well-studied thioredoxin-dependent arsenate reductase of Staphylococcus aureaus plasmid pI258 and other mechanistically similar arsenate reductases. The mechanism involves an intramolecular disulfide bond cascade, and aligned members of this family have four absolutely conserved Cys residues. This group of arsenate reductases belongs to the low-molecular weight protein-tyrosine phosphatase family (pfam01451), as does a group of glutathione/glutaredoxin type arsenate reductases (TIGR02689). At least two other, non-homologous groups of arsenate reductases involved in arsenical resistance are also known. This enzyme reduces arsenate to arsenite, which may be more toxic but which is more easily exported. [Cellular processes, Detoxification]


:

Pssm-ID: 131738  Cd Length: 129  Bit Score: 257.40  E-value: 3.57e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737577    4 IYFLCTGNACRSQMAEGFAQQLLGPNWQVASAGVETHGLNPLAVQVMSEVGIDISDQVSKLIDLTYLNQCAVVVTLCGDA 83
Cdd:TIGR02691   1 IYFLCTGNSCRSQMAEGWGKKYLGDEWEVYSAGIEAHGLNPNAVKAMKEVGIDISNQTSDLIDLDILNKADLVVTLCGDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 489737577   84 RDRCPVTPATVTRLHWPLPDPARTTGSVSDQLLVFRQVRDQIKARVIDL 132
Cdd:TIGR02691  81 RDKCPATPPHVKREHWGLDDPARAEGTEEEKWAVFRRVRDEIKERVKDF 129
 
Name Accession Description Interval E-value
arsC_pI258_fam TIGR02691
arsenate reductase (thioredoxin); This family describes the well-studied thioredoxin-dependent ...
 4-132 3.57e-90

arsenate reductase (thioredoxin); This family describes the well-studied thioredoxin-dependent arsenate reductase of Staphylococcus aureaus plasmid pI258 and other mechanistically similar arsenate reductases. The mechanism involves an intramolecular disulfide bond cascade, and aligned members of this family have four absolutely conserved Cys residues. This group of arsenate reductases belongs to the low-molecular weight protein-tyrosine phosphatase family (pfam01451), as does a group of glutathione/glutaredoxin type arsenate reductases (TIGR02689). At least two other, non-homologous groups of arsenate reductases involved in arsenical resistance are also known. This enzyme reduces arsenate to arsenite, which may be more toxic but which is more easily exported. [Cellular processes, Detoxification]


Pssm-ID: 131738  Cd Length: 129  Bit Score: 257.40  E-value: 3.57e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737577    4 IYFLCTGNACRSQMAEGFAQQLLGPNWQVASAGVETHGLNPLAVQVMSEVGIDISDQVSKLIDLTYLNQCAVVVTLCGDA 83
Cdd:TIGR02691   1 IYFLCTGNSCRSQMAEGWGKKYLGDEWEVYSAGIEAHGLNPNAVKAMKEVGIDISNQTSDLIDLDILNKADLVVTLCGDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 489737577   84 RDRCPVTPATVTRLHWPLPDPARTTGSVSDQLLVFRQVRDQIKARVIDL 132
Cdd:TIGR02691  81 RDKCPATPPHVKREHWGLDDPARAEGTEEEKWAVFRRVRDEIKERVKDF 129
LMWP_ArsC cd16345
Arsenate reductase of the LMWP family; Arsenate reductase plays an important role in the ...
 3-132 2.81e-73

Arsenate reductase of the LMWP family; Arsenate reductase plays an important role in the reduction of intracellular arsenate to arsenite, an important step in arsenic detoxification. The reduction involves three different thiolate nucleophiles. In arsenate reductases of the LMWP family, reduction can be coupled with thioredoxin (Trx)/thioredoxin reductase (TrxR) or glutathione (GSH)/glutaredoxin (Grx).


Pssm-ID: 319973  Cd Length: 132  Bit Score: 214.62  E-value: 2.81e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737577   3 KIYFLCTGNACRSQMAEGFAQQLLGPNWQVASAGVETHGLNPLAVQVMSEVGIDISDQVSKLIDLTYLNQCAVVVTLCGD 82
Cdd:cd16345    1 KVLFLCTGNSARSQMAEALLRHLGGDRFEAYSAGSEPAGVNPLAIEVMKEIGIDISGQRSKSLDEFLGQEFDYVITVCDN 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 489737577  83 ARDRCPVTPATVTRLHWPLPDPARTTGSVSDQLLVFRQVRDQIKARVIDL 132
Cdd:cd16345   81 AAEVCPVFPGAVKRLHWGFPDPAAAEGSEEEKLEAFRRVRDEIKERIEAL 130
PRK13530 PRK13530
arsenate reductase (thioredoxin);
4-135 2.28e-64

arsenate reductase (thioredoxin);


Pssm-ID: 237415  Cd Length: 133  Bit Score: 192.27  E-value: 2.28e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737577   4 IYFLCTGNACRSQMAEGFAQQLLGPNWQVASAGVETHGLNPLAVQVMSEVGIDISDQVSKLIDLTYLNQCAVVVTLCGDA 83
Cdd:PRK13530   6 IYFLCTGNSCRSQMAEGWGKQYLGDKWNVYSAGIEAHGVNPNAIKAMKEVGIDISNQTSDIIDNDILNNADLVVTLCSHA 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489737577  84 RDRCPVTPATVTRLHWPLPDPARTtgsvsdQLLVFRQVRDQIKARVIDLART 135
Cdd:PRK13530  86 DDVCPSTPPHVKRVHWGFDDPAGK------EWSEFQRVRDEIGERIKRFAET 131
Wzb COG0394
Protein-tyrosine-phosphatase [Signal transduction mechanisms];
1-136 2.61e-50

Protein-tyrosine-phosphatase [Signal transduction mechanisms];


Pssm-ID: 440163  Cd Length: 137  Bit Score: 156.86  E-value: 2.61e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737577   1 MPKIYFLCTGNACRSQMAEGFAQQLLGPNWQVASAGVETHG-LNPLAVQVMSEVGIDISDQVSKLIDLTYLNQCAVVVTL 79
Cdd:COG0394    3 PKRVLFVCTGNICRSPMAEALLRHLAGGRVEVDSAGTEPGGpVDPRAVAVLAERGIDLSGHRSRQLDEEDLPEFDLVITM 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489737577  80 CGDARDR-CPVTP-ATVTRLHWPLPDPARTTgsvsdqLLVFRQVRDQIKARVIDLARTL 136
Cdd:COG0394   83 CDSAAEElCPLFPgAAKLLLHWDVPDPYYGG------LEAFREVRDEIERRIEALLAKL 135
LMWPc smart00226
Low molecular weight phosphatase family;
4-135 3.97e-29

Low molecular weight phosphatase family;


Pssm-ID: 197586  Cd Length: 134  Bit Score: 102.94  E-value: 3.97e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737577     4 IYFLCTGNACRSQMAEGFAQQLLGPNWQVASAGVET---HGLNPLAVQVMSEVGIDISDQVSKlIDLTYLNQCAVVVTLC 80
Cdd:smart00226   1 ILFVCTGNICRSPMAEALFKAYVGDRVKIDSAGTGAwvgGGADPRAVKVLKEHGIDLSHHASQ-LTSSDFKNADLVLAMD 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489737577    81 GD-ARDRCPVTP--ATVTRL--HWP-LPDPARttGSVSdqllVFRQVRDQIKARVIDLART 135
Cdd:smart00226  80 GShLRNICRLKPpsRAKVELfgHYVdVDDPYY--GGID----GFERVYDELENALQEFLKQ 134
LMWPc pfam01451
Low molecular weight phosphotyrosine protein phosphatase;
4-133 5.75e-26

Low molecular weight phosphotyrosine protein phosphatase;


Pssm-ID: 460216  Cd Length: 142  Bit Score: 95.13  E-value: 5.75e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737577    4 IYFLCTGNACRSQMAEGFAQQL-----LGPNWQVASAGVET---HGLNPLAVQVMSEVGIDISDQVSKLIDLTYLNQCAV 75
Cdd:pfam01451   1 ILFVCTGNICRSPMAEAIFRRElekagLGDKVEVDSAGTGAwpgNPADPRAVEVLKEHGIDLSGHYARQLSTEDFASFDL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489737577   76 VVTLCGD-ARDRCPVTPAT----VTRL-----HWPLPDPARttGSVSDqllvFRQVRDQIKARVIDLA 133
Cdd:pfam01451  81 ILAMDSEhKRDLCPLAPERyrakVMLLgeygeQLDIPDPYY--GSIDA----FEEVRDLIERRCRQLL 142
 
Name Accession Description Interval E-value
arsC_pI258_fam TIGR02691
arsenate reductase (thioredoxin); This family describes the well-studied thioredoxin-dependent ...
 4-132 3.57e-90

arsenate reductase (thioredoxin); This family describes the well-studied thioredoxin-dependent arsenate reductase of Staphylococcus aureaus plasmid pI258 and other mechanistically similar arsenate reductases. The mechanism involves an intramolecular disulfide bond cascade, and aligned members of this family have four absolutely conserved Cys residues. This group of arsenate reductases belongs to the low-molecular weight protein-tyrosine phosphatase family (pfam01451), as does a group of glutathione/glutaredoxin type arsenate reductases (TIGR02689). At least two other, non-homologous groups of arsenate reductases involved in arsenical resistance are also known. This enzyme reduces arsenate to arsenite, which may be more toxic but which is more easily exported. [Cellular processes, Detoxification]


Pssm-ID: 131738  Cd Length: 129  Bit Score: 257.40  E-value: 3.57e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737577    4 IYFLCTGNACRSQMAEGFAQQLLGPNWQVASAGVETHGLNPLAVQVMSEVGIDISDQVSKLIDLTYLNQCAVVVTLCGDA 83
Cdd:TIGR02691   1 IYFLCTGNSCRSQMAEGWGKKYLGDEWEVYSAGIEAHGLNPNAVKAMKEVGIDISNQTSDLIDLDILNKADLVVTLCGDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 489737577   84 RDRCPVTPATVTRLHWPLPDPARTTGSVSDQLLVFRQVRDQIKARVIDL 132
Cdd:TIGR02691  81 RDKCPATPPHVKREHWGLDDPARAEGTEEEKWAVFRRVRDEIKERVKDF 129
LMWP_ArsC cd16345
Arsenate reductase of the LMWP family; Arsenate reductase plays an important role in the ...
 3-132 2.81e-73

Arsenate reductase of the LMWP family; Arsenate reductase plays an important role in the reduction of intracellular arsenate to arsenite, an important step in arsenic detoxification. The reduction involves three different thiolate nucleophiles. In arsenate reductases of the LMWP family, reduction can be coupled with thioredoxin (Trx)/thioredoxin reductase (TrxR) or glutathione (GSH)/glutaredoxin (Grx).


Pssm-ID: 319973  Cd Length: 132  Bit Score: 214.62  E-value: 2.81e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737577   3 KIYFLCTGNACRSQMAEGFAQQLLGPNWQVASAGVETHGLNPLAVQVMSEVGIDISDQVSKLIDLTYLNQCAVVVTLCGD 82
Cdd:cd16345    1 KVLFLCTGNSARSQMAEALLRHLGGDRFEAYSAGSEPAGVNPLAIEVMKEIGIDISGQRSKSLDEFLGQEFDYVITVCDN 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 489737577  83 ARDRCPVTPATVTRLHWPLPDPARTTGSVSDQLLVFRQVRDQIKARVIDL 132
Cdd:cd16345   81 AAEVCPVFPGAVKRLHWGFPDPAAAEGSEEEKLEAFRRVRDEIKERIEAL 130
PRK13530 PRK13530
arsenate reductase (thioredoxin);
4-135 2.28e-64

arsenate reductase (thioredoxin);


Pssm-ID: 237415  Cd Length: 133  Bit Score: 192.27  E-value: 2.28e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737577   4 IYFLCTGNACRSQMAEGFAQQLLGPNWQVASAGVETHGLNPLAVQVMSEVGIDISDQVSKLIDLTYLNQCAVVVTLCGDA 83
Cdd:PRK13530   6 IYFLCTGNSCRSQMAEGWGKQYLGDKWNVYSAGIEAHGVNPNAIKAMKEVGIDISNQTSDIIDNDILNNADLVVTLCSHA 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489737577  84 RDRCPVTPATVTRLHWPLPDPARTtgsvsdQLLVFRQVRDQIKARVIDLART 135
Cdd:PRK13530  86 DDVCPSTPPHVKRVHWGFDDPAGK------EWSEFQRVRDEIGERIKRFAET 131
Wzb COG0394
Protein-tyrosine-phosphatase [Signal transduction mechanisms];
1-136 2.61e-50

Protein-tyrosine-phosphatase [Signal transduction mechanisms];


Pssm-ID: 440163  Cd Length: 137  Bit Score: 156.86  E-value: 2.61e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737577   1 MPKIYFLCTGNACRSQMAEGFAQQLLGPNWQVASAGVETHG-LNPLAVQVMSEVGIDISDQVSKLIDLTYLNQCAVVVTL 79
Cdd:COG0394    3 PKRVLFVCTGNICRSPMAEALLRHLAGGRVEVDSAGTEPGGpVDPRAVAVLAERGIDLSGHRSRQLDEEDLPEFDLVITM 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489737577  80 CGDARDR-CPVTP-ATVTRLHWPLPDPARTTgsvsdqLLVFRQVRDQIKARVIDLARTL 136
Cdd:COG0394   83 CDSAAEElCPLFPgAAKLLLHWDVPDPYYGG------LEAFREVRDEIERRIEALLAKL 135
LMWP cd00115
Low molecular weight phosphatase family; Low molecular weight phosphatases (LMWPs) are a group ...
 4-133 2.92e-32

Low molecular weight phosphatase family; Low molecular weight phosphatases (LMWPs) are a group of small soluble enzymes that are characterized by a highly conserved active site motif (V/I)CXGNXCRS and share no sequence similarity with other types of protein tyrosine phosphatases (PTPs). This family includes protein tyrosine phosphatases, arginine phosphatases and arsenate reductases.


Pssm-ID: 319970  Cd Length: 137  Bit Score: 111.04  E-value: 2.92e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737577   4 IYFLCTGNACRSQMAEGFAQQLLGPNWQVASAGVETH---GLNPLAVQVMSEVGIDISdQVSKLIDLTYLNQCAVVVTLC 80
Cdd:cd00115    2 ILFICTGNICRSPMAEAIFKQLLGDEWKVDSAGTGAHhgeGADPRAVRVLKEVGIDIS-HRSDQIKSEHLDNYDLVLVMD 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489737577  81 GDARDRCP---------VTPATVTRLHWPLPDPARTtgsvsdQLLVFRQVRDQIKARVIDLA 133
Cdd:cd00115   81 GSNLDKIPrifpeargkTWLPHVKLEHGEIDDPYRG------DIEDFRRVRDELENASKRFA 136
LMWPc smart00226
Low molecular weight phosphatase family;
4-135 3.97e-29

Low molecular weight phosphatase family;


Pssm-ID: 197586  Cd Length: 134  Bit Score: 102.94  E-value: 3.97e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737577     4 IYFLCTGNACRSQMAEGFAQQLLGPNWQVASAGVET---HGLNPLAVQVMSEVGIDISDQVSKlIDLTYLNQCAVVVTLC 80
Cdd:smart00226   1 ILFVCTGNICRSPMAEALFKAYVGDRVKIDSAGTGAwvgGGADPRAVKVLKEHGIDLSHHASQ-LTSSDFKNADLVLAMD 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489737577    81 GD-ARDRCPVTP--ATVTRL--HWP-LPDPARttGSVSdqllVFRQVRDQIKARVIDLART 135
Cdd:smart00226  80 GShLRNICRLKPpsRAKVELfgHYVdVDDPYY--GGID----GFERVYDELENALQEFLKQ 134
LMWPc pfam01451
Low molecular weight phosphotyrosine protein phosphatase;
4-133 5.75e-26

Low molecular weight phosphotyrosine protein phosphatase;


Pssm-ID: 460216  Cd Length: 142  Bit Score: 95.13  E-value: 5.75e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737577    4 IYFLCTGNACRSQMAEGFAQQL-----LGPNWQVASAGVET---HGLNPLAVQVMSEVGIDISDQVSKLIDLTYLNQCAV 75
Cdd:pfam01451   1 ILFVCTGNICRSPMAEAIFRRElekagLGDKVEVDSAGTGAwpgNPADPRAVEVLKEHGIDLSGHYARQLSTEDFASFDL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489737577   76 VVTLCGD-ARDRCPVTPAT----VTRL-----HWPLPDPARttGSVSDqllvFRQVRDQIKARVIDLA 133
Cdd:pfam01451  81 ILAMDSEhKRDLCPLAPERyrakVMLLgeygeQLDIPDPYY--GSIDA----FEEVRDLIERRCRQLL 142
LMWPAP cd16344
low molecular weight protein arginine phosphatase; Low molecular weight protein arginine ...
 3-66 1.64e-19

low molecular weight protein arginine phosphatase; Low molecular weight protein arginine phosphatases are part of the low molecular weight phosphatase (LMWP) family. They share a highly conserved active site motif (V/I)CXGNTCRS. It has been shown that the conserved threonine, which in many LMWPTPs is an isoleucine, confers specificity to phosphoarginine over phosphotyrosine.


Pssm-ID: 319972  Cd Length: 142  Bit Score: 78.63  E-value: 1.64e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489737577   3 KIYFLCTGNACRSQMAEGFAQQLLGP-NWQVASAGVETH-GL--NPLAVQVMSEVGIDISDQVSKLID 66
Cdd:cd16344    2 KILFVCTGNTCRSPMAEAILKKLLEElDVEVKSAGIFAVdGSpaSPNAVEVLKEKGIDLSGHRSQQLT 69
LMWPTP cd16343
Low molecular weight protein tyrosine phosphatase; Low molecular weight protein tyrosine ...
 3-66 4.74e-14

Low molecular weight protein tyrosine phosphatase; Low molecular weight protein tyrosine phosphatases (LMW-PTP) are a family of small soluble single-domain enzymes that are characterized by a highly conserved active site motif (V/I)CXGNXCRS and share no sequence similarity with other types of protein tyrosine phosphatases (PTPs). LMW-PTPs play important roles in many biological processes and are widely distributed in prokaryotes and eukaryotes.


Pssm-ID: 319971  Cd Length: 147  Bit Score: 64.38  E-value: 4.74e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489737577   3 KIYFLCTGNACRSQMAEGFAQQLL----GPNWQVASAGveTHGLN------PLAVQVMSEVGIDISDQVSKLID 66
Cdd:cd16343    2 KILFVCLGNICRSPMAEAVLRHLLpkagGDDVEVDSAG--TSAWHggeppdPRARAVLKEHGIDLSGHRARQLT 73
etp PRK11391
phosphotyrosine-protein phosphatase; Provisional
 4-42 5.07e-04

phosphotyrosine-protein phosphatase; Provisional


Pssm-ID: 138553  Cd Length: 144  Bit Score: 37.69  E-value: 5.07e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 489737577   4 IYFLCTGNACRSQMAEGFAQQLLgPNWQVASAGVetHGL 42
Cdd:PRK11391   5 ILVVCTGNICRSPIGERLLRKRL-PGVKVKSAGV--HGL 40
PRK10126 PRK10126
low molecular weight protein-tyrosine-phosphatase Wzb;
3-106 6.95e-04

low molecular weight protein-tyrosine-phosphatase Wzb;


Pssm-ID: 182256  Cd Length: 147  Bit Score: 37.58  E-value: 6.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737577   3 KIYFLCTGNACRSQMAEGFAQQLLgPNWQVASAGVET---HGLNPLAVQVMSEVGIDISDQVSKLI--------DLTYLN 71
Cdd:PRK10126   4 NILVVCVGNICRSPTAERLLQRYH-PELKVESAGLGAlvgKGADPTAISVAAEHQLSLEGHCARQIsrrlcrnyDLILTM 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 489737577  72 QCAVVVTLCgdarDRCPVTPATVTRL-HW----PLPDPAR 106
Cdd:PRK10126  83 EKRHIERLC----EMAPEMRGKVMLFgHWdnecEIPDPYR 118
 
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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