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Conserved domains on  [gi|1655140092|ref|WP_137624623|]
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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
SCOP:  4000436

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 ...
4-132 2.01e-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: 240.07  E-value: 2.01e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140092   4 IYFLCTGNSCRSQMAEGFARELLAPSWEVASAGVEMHGLNANAVAVMAEVGIDISAQYSKLIDTEYLNQCDVVVTLCGDA 83
Cdd:TIGR02691   1 IYFLCTGNSCRSQMAEGWGKKYLGDEWEVYSAGIEAHGLNPNAVKAMKEVGIDISNQTSDLIDLDILNKADLVVTLCGDA 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1655140092  84 RDKCPVTPPSVKKLHWPLPDPAQATGSEDEQLAVFREVRDQIRRNVETL 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 2.01e-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: 240.07  E-value: 2.01e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140092   4 IYFLCTGNSCRSQMAEGFARELLAPSWEVASAGVEMHGLNANAVAVMAEVGIDISAQYSKLIDTEYLNQCDVVVTLCGDA 83
Cdd:TIGR02691   1 IYFLCTGNSCRSQMAEGWGKKYLGDEWEVYSAGIEAHGLNPNAVKAMKEVGIDISNQTSDLIDLDILNKADLVVTLCGDA 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1655140092  84 RDKCPVTPPSVKKLHWPLPDPAQATGSEDEQLAVFREVRDQIRRNVETL 132
Cdd:TIGR02691  81 RDKCPATPPHVKREHWGLDDPARAEGTEEEKWAVFRRVRDEIKERVKDF 129
LMWP_ArsC cd16345
Arsenate reductase of the LMWP family; Arsenate reductase plays an important role in the ...
3-133 2.09e-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: 222.71  E-value: 2.09e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140092   3 KIYFLCTGNSCRSQMAEGFARELLAPSWEVASAGVEMHGLNANAVAVMAEVGIDISAQYSKLIDTEYLNQCDVVVTLCGD 82
Cdd:cd16345     1 KVLFLCTGNSARSQMAEALLRHLGGDRFEAYSAGSEPAGVNPLAIEVMKEIGIDISGQRSKSLDEFLGQEFDYVITVCDN 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1655140092  83 ARDKCPVTPPSVKKLHWPLPDPAQATGSEDEQLAVFREVRDQIRRNVETLI 133
Cdd:cd16345    81 AAEVCPVFPGAVKRLHWGFPDPAAAEGSEEEKLEAFRRVRDEIKERIEALL 131
PRK13530 PRK13530
arsenate reductase (thioredoxin);
2-131 2.25e-65

arsenate reductase (thioredoxin);


Pssm-ID: 237415  Cd Length: 133  Bit Score: 194.58  E-value: 2.25e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140092   2 KKIYFLCTGNSCRSQMAEGFARELLAPSWEVASAGVEMHGLNANAVAVMAEVGIDISAQYSKLIDTEYLNQCDVVVTLCG 81
Cdd:PRK13530    4 KTIYFLCTGNSCRSQMAEGWGKQYLGDKWNVYSAGIEAHGVNPNAIKAMKEVGIDISNQTSDIIDNDILNNADLVVTLCS 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1655140092  82 DARDKCPVTPPSVKKLHWPLPDPAQAtgsedeQLAVFREVRDQIRRNVET 131
Cdd:PRK13530   84 HADDVCPSTPPHVKRVHWGFDDPAGK------EWSEFQRVRDEIGERIKR 127
Wzb COG0394
Protein-tyrosine-phosphatase [Signal transduction mechanisms];
1-133 8.54e-51

Protein-tyrosine-phosphatase [Signal transduction mechanisms];


Pssm-ID: 440163  Cd Length: 137  Bit Score: 158.02  E-value: 8.54e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140092   1 MKKIYFLCTGNSCRSQMAEGFARELLAPSWEVASAGVEMHG-LNANAVAVMAEVGIDISAQYSKLIDTEYLNQCDVVVTL 79
Cdd:COG0394     3 PKRVLFVCTGNICRSPMAEALLRHLAGGRVEVDSAGTEPGGpVDPRAVAVLAERGIDLSGHRSRQLDEEDLPEFDLVITM 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1655140092  80 CGDARDK-CPVTPPSVKKL-HWPLPDPAQATgsedeqLAVFREVRDQIRRNVETLI 133
Cdd:COG0394    83 CDSAAEElCPLFPGAAKLLlHWDVPDPYYGG------LEAFREVRDEIERRIEALL 132
LMWPc smart00226
Low molecular weight phosphatase family;
4-125 6.09e-31

Low molecular weight phosphatase family;


Pssm-ID: 197586  Cd Length: 134  Bit Score: 107.56  E-value: 6.09e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140092    4 IYFLCTGNSCRSQMAEGFARELLAPSWEVASAGVEM---HGLNANAVAVMAEVGIDISAQYSKlIDTEYLNQCDVVVTLC 80
Cdd:smart00226   1 ILFVCTGNICRSPMAEALFKAYVGDRVKIDSAGTGAwvgGGADPRAVKVLKEHGIDLSHHASQ-LTSSDFKNADLVLAMD 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1655140092   81 GD-ARDKCPVTPPS-VKKLHW----PLPDPAQatGSEDeqlaVFREVRDQI 125
Cdd:smart00226  80 GShLRNICRLKPPSrAKVELFghyvDVDDPYY--GGID----GFERVYDEL 124
LMWPc pfam01451
Low molecular weight phosphotyrosine protein phosphatase;
4-132 1.44e-28

Low molecular weight phosphotyrosine protein phosphatase;


Pssm-ID: 460216  Cd Length: 142  Bit Score: 101.68  E-value: 1.44e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140092   4 IYFLCTGNSCRSQMAEGFAREL-----LAPSWEVASAGVEM---HGLNANAVAVMAEVGIDISAQYSKLIDTEYLNQCDV 75
Cdd:pfam01451   1 ILFVCTGNICRSPMAEAIFRRElekagLGDKVEVDSAGTGAwpgNPADPRAVEVLKEHGIDLSGHYARQLSTEDFASFDL 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655140092  76 VVTLCGD-ARDKCPVTP----PSVKKL-----HWPLPDPAqatGSEDEQlavFREVRDQIRRNVETL 132
Cdd:pfam01451  81 ILAMDSEhKRDLCPLAPeryrAKVMLLgeygeQLDIPDPY---YGSIDA---FEEVRDLIERRCRQL 141
 
Name Accession Description Interval E-value
arsC_pI258_fam TIGR02691
arsenate reductase (thioredoxin); This family describes the well-studied thioredoxin-dependent ...
4-132 2.01e-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: 240.07  E-value: 2.01e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140092   4 IYFLCTGNSCRSQMAEGFARELLAPSWEVASAGVEMHGLNANAVAVMAEVGIDISAQYSKLIDTEYLNQCDVVVTLCGDA 83
Cdd:TIGR02691   1 IYFLCTGNSCRSQMAEGWGKKYLGDEWEVYSAGIEAHGLNPNAVKAMKEVGIDISNQTSDLIDLDILNKADLVVTLCGDA 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1655140092  84 RDKCPVTPPSVKKLHWPLPDPAQATGSEDEQLAVFREVRDQIRRNVETL 132
Cdd:TIGR02691  81 RDKCPATPPHVKREHWGLDDPARAEGTEEEKWAVFRRVRDEIKERVKDF 129
LMWP_ArsC cd16345
Arsenate reductase of the LMWP family; Arsenate reductase plays an important role in the ...
3-133 2.09e-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: 222.71  E-value: 2.09e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140092   3 KIYFLCTGNSCRSQMAEGFARELLAPSWEVASAGVEMHGLNANAVAVMAEVGIDISAQYSKLIDTEYLNQCDVVVTLCGD 82
Cdd:cd16345     1 KVLFLCTGNSARSQMAEALLRHLGGDRFEAYSAGSEPAGVNPLAIEVMKEIGIDISGQRSKSLDEFLGQEFDYVITVCDN 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1655140092  83 ARDKCPVTPPSVKKLHWPLPDPAQATGSEDEQLAVFREVRDQIRRNVETLI 133
Cdd:cd16345    81 AAEVCPVFPGAVKRLHWGFPDPAAAEGSEEEKLEAFRRVRDEIKERIEALL 131
PRK13530 PRK13530
arsenate reductase (thioredoxin);
2-131 2.25e-65

arsenate reductase (thioredoxin);


Pssm-ID: 237415  Cd Length: 133  Bit Score: 194.58  E-value: 2.25e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140092   2 KKIYFLCTGNSCRSQMAEGFARELLAPSWEVASAGVEMHGLNANAVAVMAEVGIDISAQYSKLIDTEYLNQCDVVVTLCG 81
Cdd:PRK13530    4 KTIYFLCTGNSCRSQMAEGWGKQYLGDKWNVYSAGIEAHGVNPNAIKAMKEVGIDISNQTSDIIDNDILNNADLVVTLCS 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1655140092  82 DARDKCPVTPPSVKKLHWPLPDPAQAtgsedeQLAVFREVRDQIRRNVET 131
Cdd:PRK13530   84 HADDVCPSTPPHVKRVHWGFDDPAGK------EWSEFQRVRDEIGERIKR 127
Wzb COG0394
Protein-tyrosine-phosphatase [Signal transduction mechanisms];
1-133 8.54e-51

Protein-tyrosine-phosphatase [Signal transduction mechanisms];


Pssm-ID: 440163  Cd Length: 137  Bit Score: 158.02  E-value: 8.54e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140092   1 MKKIYFLCTGNSCRSQMAEGFARELLAPSWEVASAGVEMHG-LNANAVAVMAEVGIDISAQYSKLIDTEYLNQCDVVVTL 79
Cdd:COG0394     3 PKRVLFVCTGNICRSPMAEALLRHLAGGRVEVDSAGTEPGGpVDPRAVAVLAERGIDLSGHRSRQLDEEDLPEFDLVITM 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1655140092  80 CGDARDK-CPVTPPSVKKL-HWPLPDPAQATgsedeqLAVFREVRDQIRRNVETLI 133
Cdd:COG0394    83 CDSAAEElCPLFPGAAKLLlHWDVPDPYYGG------LEAFREVRDEIERRIEALL 132
LMWP cd00115
Low molecular weight phosphatase family; Low molecular weight phosphatases (LMWPs) are a group ...
4-125 3.29e-37

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: 123.75  E-value: 3.29e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140092   4 IYFLCTGNSCRSQMAEGFARELLAPSWEVASAGVEMH---GLNANAVAVMAEVGIDISaQYSKLIDTEYLNQCDVVVTLC 80
Cdd:cd00115     2 ILFICTGNICRSPMAEAIFKQLLGDEWKVDSAGTGAHhgeGADPRAVRVLKEVGIDIS-HRSDQIKSEHLDNYDLVLVMD 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1655140092  81 GDARDKCP---------VTPPSVKKLHWPLPDPAQAtgsedeQLAVFREVRDQI 125
Cdd:cd00115    81 GSNLDKIPrifpeargkTWLPHVKLEHGEIDDPYRG------DIEDFRRVRDEL 128
LMWPc smart00226
Low molecular weight phosphatase family;
4-125 6.09e-31

Low molecular weight phosphatase family;


Pssm-ID: 197586  Cd Length: 134  Bit Score: 107.56  E-value: 6.09e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140092    4 IYFLCTGNSCRSQMAEGFARELLAPSWEVASAGVEM---HGLNANAVAVMAEVGIDISAQYSKlIDTEYLNQCDVVVTLC 80
Cdd:smart00226   1 ILFVCTGNICRSPMAEALFKAYVGDRVKIDSAGTGAwvgGGADPRAVKVLKEHGIDLSHHASQ-LTSSDFKNADLVLAMD 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1655140092   81 GD-ARDKCPVTPPS-VKKLHW----PLPDPAQatGSEDeqlaVFREVRDQI 125
Cdd:smart00226  80 GShLRNICRLKPPSrAKVELFghyvDVDDPYY--GGID----GFERVYDEL 124
LMWPc pfam01451
Low molecular weight phosphotyrosine protein phosphatase;
4-132 1.44e-28

Low molecular weight phosphotyrosine protein phosphatase;


Pssm-ID: 460216  Cd Length: 142  Bit Score: 101.68  E-value: 1.44e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140092   4 IYFLCTGNSCRSQMAEGFAREL-----LAPSWEVASAGVEM---HGLNANAVAVMAEVGIDISAQYSKLIDTEYLNQCDV 75
Cdd:pfam01451   1 ILFVCTGNICRSPMAEAIFRRElekagLGDKVEVDSAGTGAwpgNPADPRAVEVLKEHGIDLSGHYARQLSTEDFASFDL 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655140092  76 VVTLCGD-ARDKCPVTP----PSVKKL-----HWPLPDPAqatGSEDEQlavFREVRDQIRRNVETL 132
Cdd:pfam01451  81 ILAMDSEhKRDLCPLAPeryrAKVMLLgeygeQLDIPDPY---YGSIDA---FEEVRDLIERRCRQL 141
LMWPAP cd16344
low molecular weight protein arginine phosphatase; Low molecular weight protein arginine ...
2-78 1.36e-25

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: 94.04  E-value: 1.36e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140092   2 KKIYFLCTGNSCRSQMAEGFARELLAPS-WEVASAGV-EMHGLNA--NAVAVMAEVGIDISAQYSKLIDTEYLNQCDVVV 77
Cdd:cd16344     1 MKILFVCTGNTCRSPMAEAILKKLLEELdVEVKSAGIfAVDGSPAspNAVEVLKEKGIDLSGHRSQQLTEELLEWADLIL 80

                  .
gi 1655140092  78 T 78
Cdd:cd16344    81 T 81
LMWPTP cd16343
Low molecular weight protein tyrosine phosphatase; Low molecular weight protein tyrosine ...
2-133 3.39e-16

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: 70.16  E-value: 3.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140092   2 KKIYFLCTGNSCRSQMAEGFARELLA----PSWEVASAGVE-MHGLN---ANAVAVMAEVGIDISAQYSKLIDTEYLNQC 73
Cdd:cd16343     1 KKILFVCLGNICRSPMAEAVLRHLLPkaggDDVEVDSAGTSaWHGGEppdPRARAVLKEHGIDLSGHRARQLTAEDFDEF 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655140092  74 DVVVTL----CGDARDKCPVTPPS-VKKL-HWplpDPAQATGSED---EQLAVFREVRDQIRRNVETLI 133
Cdd:cd16343    81 DLILAMdesnLRDLRRLAPAEARGkVFLLgDF---DPEGGKDVPDpyyGGREGFEEVYDLIERACEGLL 146
etp PRK11391
phosphotyrosine-protein phosphatase; Provisional
4-79 2.35e-06

phosphotyrosine-protein phosphatase; Provisional


Pssm-ID: 138553  Cd Length: 144  Bit Score: 44.24  E-value: 2.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140092   4 IYFLCTGNSCRSQMAEGFARELLaPSWEVASAGVemHGL-----NANAVAVMAEVGIDISAQYSKLIDTEYLNQCDVVVT 78
Cdd:PRK11391    5 ILVVCTGNICRSPIGERLLRKRL-PGVKVKSAGV--HGLvkhpaDATAADVAANHGVSLEGHAGRKLTAEMARNYDLILA 81

                  .
gi 1655140092  79 L 79
Cdd:PRK11391   82 M 82
PRK10126 PRK10126
low molecular weight protein-tyrosine-phosphatase Wzb;
3-104 1.25e-03

low molecular weight protein-tyrosine-phosphatase Wzb;


Pssm-ID: 182256  Cd Length: 147  Bit Score: 36.81  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140092   3 KIYFLCTGNSCRSQMAEGFARELLaPSWEVASAGVEM---HGLNANAVAVMAEVGIDISAQYSKLIDTEYLNQCDVVVTL 79
Cdd:PRK10126    4 NILVVCVGNICRSPTAERLLQRYH-PELKVESAGLGAlvgKGADPTAISVAAEHQLSLEGHCARQISRRLCRNYDLILTM 82
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1655140092  80 --CGDARdKCPVTPPSVKKL----HW----PLPDP 104
Cdd:PRK10126   83 ekRHIER-LCEMAPEMRGKVmlfgHWdnecEIPDP 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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