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Conserved domains on  [gi|1655140894|ref|WP_137625401|]
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arsenate reductase (thioredoxin) [Lactiplantibacillus pingfangensis]

Protein Classification

low molecular weight phosphatase family protein( domain architecture ID 435)

low molecular weight phosphatase (LMWP) family protein similar to arsenate reductase that plays an important role in the reduction of intracellular arsenate to arsenite, an important step in arsenic detoxification

CATH:  3.40.50.2300

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LMWP super family cl00105
Low molecular weight phosphatase family; Low molecular weight phosphatases (LMWPs) are a group ...
 7-135 1.34e-83

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.


The actual alignment was detected with superfamily member TIGR02691:

Pssm-ID: 469616  Cd Length: 129  Bit Score: 240.84  E-value: 1.34e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140894   7 LYFLCTGNACRSQMAEGFAKQLLPANWTIQSAGVETHGLNPTAVKVMAEVGIDISGQQSKLIEPTYLQQCDLVITLCGDA 86
Cdd:TIGR02691   1 IYFLCTGNSCRSQMAEGWGKKYLGDEWEVYSAGIEAHGLNPNAVKAMKEVGIDISNQTSDLIDLDILNKADLVVTLCGDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1655140894  87 RDRCPVTPATVQKLHWPLPDPAQATGTPAAQLAVFRQVRDEIKRRVLTL 135
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 ...
 7-135 1.34e-83

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: 240.84  E-value: 1.34e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140894   7 LYFLCTGNACRSQMAEGFAKQLLPANWTIQSAGVETHGLNPTAVKVMAEVGIDISGQQSKLIEPTYLQQCDLVITLCGDA 86
Cdd:TIGR02691   1 IYFLCTGNSCRSQMAEGWGKKYLGDEWEVYSAGIEAHGLNPNAVKAMKEVGIDISNQTSDLIDLDILNKADLVVTLCGDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1655140894  87 RDRCPVTPATVQKLHWPLPDPAQATGTPAAQLAVFRQVRDEIKRRVLTL 135
Cdd:TIGR02691  81 RDKCPATPPHVKREHWGLDDPARAEGTEEEKWAVFRRVRDEIKERVKDF 129
LMWP_ArsC cd16345
Arsenate reductase of the LMWP family; Arsenate reductase plays an important role in the ...
 8-137 3.84e-76

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: 221.94  E-value: 3.84e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140894   8 YFLCTGNACRSQMAEGFAKQLLPANWTIQSAGVETHGLNPTAVKVMAEVGIDISGQQSKLIEPTYLQQCDLVITLCGDAR 87
Cdd:cd16345     3 LFLCTGNSARSQMAEALLRHLGGDRFEAYSAGSEPAGVNPLAIEVMKEIGIDISGQRSKSLDEFLGQEFDYVITVCDNAA 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1655140894  88 DRCPVTPATVQKLHWPLPDPAQATGTPAAQLAVFRQVRDEIKRRVLTLVP 137
Cdd:cd16345    83 EVCPVFPGAVKRLHWGFPDPAAAEGSEEEKLEAFRRVRDEIKERIEALLA 132
PRK13530 PRK13530
arsenate reductase (thioredoxin);
5-132 2.17e-65

arsenate reductase (thioredoxin);


Pssm-ID: 237415  Cd Length: 133  Bit Score: 194.96  E-value: 2.17e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140894   5 KQLYFLCTGNACRSQMAEGFAKQLLPANWTIQSAGVETHGLNPTAVKVMAEVGIDISGQQSKLIEPTYLQQCDLVITLCG 84
Cdd:PRK13530    4 KTIYFLCTGNSCRSQMAEGWGKQYLGDKWNVYSAGIEAHGVNPNAIKAMKEVGIDISNQTSDIIDNDILNNADLVVTLCS 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1655140894  85 DARDRCPVTPATVQKLHWPLPDPAQatgtpaAQLAVFRQVRDEIKRRV 132
Cdd:PRK13530   84 HADDVCPSTPPHVKRVHWGFDDPAG------KEWSEFQRVRDEIGERI 125
Wzb COG0394
Protein-tyrosine-phosphatase [Signal transduction mechanisms];
3-138 1.16e-51

Protein-tyrosine-phosphatase [Signal transduction mechanisms];


Pssm-ID: 440163  Cd Length: 137  Bit Score: 160.33  E-value: 1.16e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140894   3 KSKQLYFLCTGNACRSQMAEGFAKQLLPANWTIQSAGVETHG-LNPTAVKVMAEVGIDISGQQSKLIEPTYLQQCDLVIT 81
Cdd:COG0394     2 MPKRVLFVCTGNICRSPMAEALLRHLAGGRVEVDSAGTEPGGpVDPRAVAVLAERGIDLSGHRSRQLDEEDLPEFDLVIT 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1655140894  82 LCGDARDR-CPVTPATVQKL-HWPLPDPAQATgtpaaqLAVFRQVRDEIKRRVLTLVPA 138
Cdd:COG0394    82 MCDSAAEElCPLFPGAAKLLlHWDVPDPYYGG------LEAFREVRDEIERRIEALLAK 134
LMWPc smart00226
Low molecular weight phosphatase family;
7-128 1.35e-30

Low molecular weight phosphatase family;


Pssm-ID: 197586  Cd Length: 134  Bit Score: 106.79  E-value: 1.35e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140894    7 LYFLCTGNACRSQMAEGFAKQLLPANWTIQSAGVET---HGLNPTAVKVMAEVGIDISGQQSKLIEpTYLQQCDLVITLC 83
Cdd:smart00226   1 ILFVCTGNICRSPMAEALFKAYVGDRVKIDSAGTGAwvgGGADPRAVKVLKEHGIDLSHHASQLTS-SDFKNADLVLAMD 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1655140894   84 GD-ARDRCPVTPATVQKL----HWP-LPDPAQATgtpaaqLAVFRQVRDEI 128
Cdd:smart00226  80 GShLRNICRLKPPSRAKVelfgHYVdVDDPYYGG------IDGFERVYDEL 124
LMWPc pfam01451
Low molecular weight phosphotyrosine protein phosphatase;
9-132 1.19e-28

Low molecular weight phosphotyrosine protein phosphatase;


Pssm-ID: 460216  Cd Length: 142  Bit Score: 102.07  E-value: 1.19e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140894   9 FLCTGNACRSQMAEGFAKQLLP-----ANWTIQSAGVET---HGLNPTAVKVMAEVGIDISGQQSKLIEPTYLQQCDLVI 80
Cdd:pfam01451   3 FVCTGNICRSPMAEAIFRRELEkaglgDKVEVDSAGTGAwpgNPADPRAVEVLKEHGIDLSGHYARQLSTEDFASFDLIL 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655140894  81 TLCGD-ARDRCPVTPATVQ---------KLHWPLPDPAQatgtpaAQLAVFRQVRDEIKRRV 132
Cdd:pfam01451  83 AMDSEhKRDLCPLAPERYRakvmllgeyGEQLDIPDPYY------GSIDAFEEVRDLIERRC 138
 
Name Accession Description Interval E-value
arsC_pI258_fam TIGR02691
arsenate reductase (thioredoxin); This family describes the well-studied thioredoxin-dependent ...
 7-135 1.34e-83

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: 240.84  E-value: 1.34e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140894   7 LYFLCTGNACRSQMAEGFAKQLLPANWTIQSAGVETHGLNPTAVKVMAEVGIDISGQQSKLIEPTYLQQCDLVITLCGDA 86
Cdd:TIGR02691   1 IYFLCTGNSCRSQMAEGWGKKYLGDEWEVYSAGIEAHGLNPNAVKAMKEVGIDISNQTSDLIDLDILNKADLVVTLCGDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1655140894  87 RDRCPVTPATVQKLHWPLPDPAQATGTPAAQLAVFRQVRDEIKRRVLTL 135
Cdd:TIGR02691  81 RDKCPATPPHVKREHWGLDDPARAEGTEEEKWAVFRRVRDEIKERVKDF 129
LMWP_ArsC cd16345
Arsenate reductase of the LMWP family; Arsenate reductase plays an important role in the ...
 8-137 3.84e-76

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: 221.94  E-value: 3.84e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140894   8 YFLCTGNACRSQMAEGFAKQLLPANWTIQSAGVETHGLNPTAVKVMAEVGIDISGQQSKLIEPTYLQQCDLVITLCGDAR 87
Cdd:cd16345     3 LFLCTGNSARSQMAEALLRHLGGDRFEAYSAGSEPAGVNPLAIEVMKEIGIDISGQRSKSLDEFLGQEFDYVITVCDNAA 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1655140894  88 DRCPVTPATVQKLHWPLPDPAQATGTPAAQLAVFRQVRDEIKRRVLTLVP 137
Cdd:cd16345    83 EVCPVFPGAVKRLHWGFPDPAAAEGSEEEKLEAFRRVRDEIKERIEALLA 132
PRK13530 PRK13530
arsenate reductase (thioredoxin);
5-132 2.17e-65

arsenate reductase (thioredoxin);


Pssm-ID: 237415  Cd Length: 133  Bit Score: 194.96  E-value: 2.17e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140894   5 KQLYFLCTGNACRSQMAEGFAKQLLPANWTIQSAGVETHGLNPTAVKVMAEVGIDISGQQSKLIEPTYLQQCDLVITLCG 84
Cdd:PRK13530    4 KTIYFLCTGNSCRSQMAEGWGKQYLGDKWNVYSAGIEAHGVNPNAIKAMKEVGIDISNQTSDIIDNDILNNADLVVTLCS 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1655140894  85 DARDRCPVTPATVQKLHWPLPDPAQatgtpaAQLAVFRQVRDEIKRRV 132
Cdd:PRK13530   84 HADDVCPSTPPHVKRVHWGFDDPAG------KEWSEFQRVRDEIGERI 125
Wzb COG0394
Protein-tyrosine-phosphatase [Signal transduction mechanisms];
3-138 1.16e-51

Protein-tyrosine-phosphatase [Signal transduction mechanisms];


Pssm-ID: 440163  Cd Length: 137  Bit Score: 160.33  E-value: 1.16e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140894   3 KSKQLYFLCTGNACRSQMAEGFAKQLLPANWTIQSAGVETHG-LNPTAVKVMAEVGIDISGQQSKLIEPTYLQQCDLVIT 81
Cdd:COG0394     2 MPKRVLFVCTGNICRSPMAEALLRHLAGGRVEVDSAGTEPGGpVDPRAVAVLAERGIDLSGHRSRQLDEEDLPEFDLVIT 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1655140894  82 LCGDARDR-CPVTPATVQKL-HWPLPDPAQATgtpaaqLAVFRQVRDEIKRRVLTLVPA 138
Cdd:COG0394    82 MCDSAAEElCPLFPGAAKLLlHWDVPDPYYGG------LEAFREVRDEIERRIEALLAK 134
LMWP cd00115
Low molecular weight phosphatase family; Low molecular weight phosphatases (LMWPs) are a group ...
 7-131 1.81e-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: 111.81  E-value: 1.81e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140894   7 LYFLCTGNACRSQMAEGFAKQLLPANWTIQSAGVETH---GLNPTAVKVMAEVGIDISgQQSKLIEPTYLQQCDLVITLC 83
Cdd:cd00115     2 ILFICTGNICRSPMAEAIFKQLLGDEWKVDSAGTGAHhgeGADPRAVRVLKEVGIDIS-HRSDQIKSEHLDNYDLVLVMD 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1655140894  84 GDARDRCP---------VTPATVQKLHWPLPDPAQatgtpaAQLAVFRQVRDEIKRR 131
Cdd:cd00115    81 GSNLDKIPrifpeargkTWLPHVKLEHGEIDDPYR------GDIEDFRRVRDELENA 131
LMWPc smart00226
Low molecular weight phosphatase family;
7-128 1.35e-30

Low molecular weight phosphatase family;


Pssm-ID: 197586  Cd Length: 134  Bit Score: 106.79  E-value: 1.35e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140894    7 LYFLCTGNACRSQMAEGFAKQLLPANWTIQSAGVET---HGLNPTAVKVMAEVGIDISGQQSKLIEpTYLQQCDLVITLC 83
Cdd:smart00226   1 ILFVCTGNICRSPMAEALFKAYVGDRVKIDSAGTGAwvgGGADPRAVKVLKEHGIDLSHHASQLTS-SDFKNADLVLAMD 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1655140894   84 GD-ARDRCPVTPATVQKL----HWP-LPDPAQATgtpaaqLAVFRQVRDEI 128
Cdd:smart00226  80 GShLRNICRLKPPSRAKVelfgHYVdVDDPYYGG------IDGFERVYDEL 124
LMWPc pfam01451
Low molecular weight phosphotyrosine protein phosphatase;
9-132 1.19e-28

Low molecular weight phosphotyrosine protein phosphatase;


Pssm-ID: 460216  Cd Length: 142  Bit Score: 102.07  E-value: 1.19e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140894   9 FLCTGNACRSQMAEGFAKQLLP-----ANWTIQSAGVET---HGLNPTAVKVMAEVGIDISGQQSKLIEPTYLQQCDLVI 80
Cdd:pfam01451   3 FVCTGNICRSPMAEAIFRRELEkaglgDKVEVDSAGTGAwpgNPADPRAVEVLKEHGIDLSGHYARQLSTEDFASFDLIL 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655140894  81 TLCGD-ARDRCPVTPATVQ---------KLHWPLPDPAQatgtpaAQLAVFRQVRDEIKRRV 132
Cdd:pfam01451  83 AMDSEhKRDLCPLAPERYRakvmllgeyGEQLDIPDPYY------GSIDAFEEVRDLIERRC 138
LMWPAP cd16344
low molecular weight protein arginine phosphatase; Low molecular weight protein arginine ...
 5-81 1.57e-22

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: 86.33  E-value: 1.57e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140894   5 KQLYFLCTGNACRSQMAEGFAKQLLP-ANWTIQSAGVETH-GLNPT--AVKVMAEVGIDISGQQSKLIEPTYLQQCDLVI 80
Cdd:cd16344     1 MKILFVCTGNTCRSPMAEAILKKLLEeLDVEVKSAGIFAVdGSPASpnAVEVLKEKGIDLSGHRSQQLTEELLEWADLIL 80


                  .
gi 1655140894  81 T 81
Cdd:cd16344    81 T 81
LMWPTP cd16343
Low molecular weight protein tyrosine phosphatase; Low molecular weight protein tyrosine ...
 9-81 1.79e-17

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: 73.63  E-value: 1.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140894   9 FLCTGNACRSQMAEGFAKQLLPA----NWTIQSAGveTHGLN------PTAVKVMAEVGIDISGQQSKLIEPTYLQQCDL 78
Cdd:cd16343     5 FVCLGNICRSPMAEAVLRHLLPKaggdDVEVDSAG--TSAWHggeppdPRARAVLKEHGIDLSGHRARQLTAEDFDEFDL 82


                  ...
gi 1655140894  79 VIT 81
Cdd:cd16343    83 ILA 85
etp PRK11391
phosphotyrosine-protein phosphatase; Provisional
 10-82 1.25e-06

phosphotyrosine-protein phosphatase; Provisional


Pssm-ID: 138553  Cd Length: 144  Bit Score: 45.01  E-value: 1.25e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655140894  10 LCTGNACRSQMAEGFAKQLLPAnWTIQSAGVE---THGLNPTAVKVMAEVGIDISGQQSKLIEPTYLQQCDLVITL 82
Cdd:PRK11391    8 VCTGNICRSPIGERLLRKRLPG-VKVKSAGVHglvKHPADATAADVAANHGVSLEGHAGRKLTAEMARNYDLILAM 82
PRK10126 PRK10126
low molecular weight protein-tyrosine-phosphatase Wzb;
10-107 3.65e-06

low molecular weight protein-tyrosine-phosphatase Wzb;


Pssm-ID: 182256  Cd Length: 147  Bit Score: 43.74  E-value: 3.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140894  10 LCTGNACRSQMAEGFAKQLLPaNWTIQSAGVET---HGLNPTAVKVMAEVGIDISGQQSKLIEPTYLQQCDLVITLCGDA 86
Cdd:PRK10126    8 VCVGNICRSPTAERLLQRYHP-ELKVESAGLGAlvgKGADPTAISVAAEHQLSLEGHCARQISRRLCRNYDLILTMEKRH 86

                          90       100       110
                  ....*....|....*....|....*....|
gi 1655140894  87 RDR-CPVTPATVQKL----HW----PLPDP 107
Cdd:PRK10126   87 IERlCEMAPEMRGKVmlfgHWdnecEIPDP 116
 
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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