NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|575771899|ref|NP_001276522|]
View 

kynureninase isoform 2 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
kynureninase super family cl31141
kynureninase; This model describes kynureninase, a pyridoxal-phosphate enzyme. Kynurinine is a ...
31-426 0e+00

kynureninase; This model describes kynureninase, a pyridoxal-phosphate enzyme. Kynurinine is a Trp breakdown product and a precursor for NAD. In Chlamydia psittaci, an obligate intracellular pathogen, kynureninase makes anthranilate, a Trp precursor, from kynurenine. This counters the tryptophan hydrolysis that occurs in the host cell in response to the pathogen. [Energy metabolism, Amino acids and amines]


The actual alignment was detected with superfamily member TIGR01814:

Pssm-ID: 130873 [Multi-domain]  Cd Length: 406  Bit Score: 548.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771899   31 ALRLDEEDKLSHFRNCFYIPKMRDlpsidlslvseDDDAIYFLGNSLGLQPKMVRTYLEEELDKWAKMGAYGHDVGKRPW 110
Cdd:TIGR01814   1 ALELDEADPLRALRDEFHLPKIGD-----------ENAVIYLDGNSLGLMPKAARNALKEELDKWAKIAIRGHNTGKAPW 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771899  111 IVGDESIVSLMKdiVGAHEKEIALMNALTINLHLLLLSFFKPTPKRHKILLEAKAFPSDHYAIESQIQLHGLDVEKSMRM 190
Cdd:TIGR01814  70 FTLDESLLKLRL--VGAKEDEVVVMNTLTINLHLLLASFYKPTPKRYKILLEAKAFPSDHYAIESQLQLHGLTVEESMVQ 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771899  191 VKPREgEETLRMEDILEVIEEEGDSIAVILFSGLHFYTGQLFNIPAITKAGHAKGCFVGFDLAHAVGNVELRLHDWGVDF 270
Cdd:TIGR01814 148 IEPRE-EETLRLEDILDTIEKNGDDIAVILLSGVQYYTGQLFDMAAITRAAHAKGALVGFDLAHAVGNVPLDLHDWGVDF 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771899  271 ACWCSYKYLNsgAGGLAGAFVHEKHAHTVKPALVGWFGHDLSTRFNMDNKLQLIPgaNGFRISNPPILLVCSLHASLEVF 350
Cdd:TIGR01814 227 ACWCTYKYLN--AGPGAGAFVHEKHAHTERPRLAGWWGHARPTRFKMDNTLGLIP--CGFRISNPPILSVAALRGSLDIF 302
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 575771899  351 QQATMTALRRKSILLTGYLEYMLKHYHSKDntenkgPIVNIITPSRAEERGCQLTLTFSIPKKSVFKELEKRGVVV 426
Cdd:TIGR01814 303 DQAGMEALRKKSLLLTDYLEELIKARCGGP------PVLTIITPRDHAQRGCQLSLTHPVPGKAVFQALIKRGVIG 372
 
Name Accession Description Interval E-value
kynureninase TIGR01814
kynureninase; This model describes kynureninase, a pyridoxal-phosphate enzyme. Kynurinine is a ...
31-426 0e+00

kynureninase; This model describes kynureninase, a pyridoxal-phosphate enzyme. Kynurinine is a Trp breakdown product and a precursor for NAD. In Chlamydia psittaci, an obligate intracellular pathogen, kynureninase makes anthranilate, a Trp precursor, from kynurenine. This counters the tryptophan hydrolysis that occurs in the host cell in response to the pathogen. [Energy metabolism, Amino acids and amines]


Pssm-ID: 130873 [Multi-domain]  Cd Length: 406  Bit Score: 548.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771899   31 ALRLDEEDKLSHFRNCFYIPKMRDlpsidlslvseDDDAIYFLGNSLGLQPKMVRTYLEEELDKWAKMGAYGHDVGKRPW 110
Cdd:TIGR01814   1 ALELDEADPLRALRDEFHLPKIGD-----------ENAVIYLDGNSLGLMPKAARNALKEELDKWAKIAIRGHNTGKAPW 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771899  111 IVGDESIVSLMKdiVGAHEKEIALMNALTINLHLLLLSFFKPTPKRHKILLEAKAFPSDHYAIESQIQLHGLDVEKSMRM 190
Cdd:TIGR01814  70 FTLDESLLKLRL--VGAKEDEVVVMNTLTINLHLLLASFYKPTPKRYKILLEAKAFPSDHYAIESQLQLHGLTVEESMVQ 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771899  191 VKPREgEETLRMEDILEVIEEEGDSIAVILFSGLHFYTGQLFNIPAITKAGHAKGCFVGFDLAHAVGNVELRLHDWGVDF 270
Cdd:TIGR01814 148 IEPRE-EETLRLEDILDTIEKNGDDIAVILLSGVQYYTGQLFDMAAITRAAHAKGALVGFDLAHAVGNVPLDLHDWGVDF 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771899  271 ACWCSYKYLNsgAGGLAGAFVHEKHAHTVKPALVGWFGHDLSTRFNMDNKLQLIPgaNGFRISNPPILLVCSLHASLEVF 350
Cdd:TIGR01814 227 ACWCTYKYLN--AGPGAGAFVHEKHAHTERPRLAGWWGHARPTRFKMDNTLGLIP--CGFRISNPPILSVAALRGSLDIF 302
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 575771899  351 QQATMTALRRKSILLTGYLEYMLKHYHSKDntenkgPIVNIITPSRAEERGCQLTLTFSIPKKSVFKELEKRGVVV 426
Cdd:TIGR01814 303 DQAGMEALRKKSLLLTDYLEELIKARCGGP------PVLTIITPRDHAQRGCQLSLTHPVPGKAVFQALIKRGVIG 372
Bna5 COG3844
Kynureninase [Amino acid transport and metabolism];
31-426 3.67e-153

Kynureninase [Amino acid transport and metabolism];


Pssm-ID: 443054 [Multi-domain]  Cd Length: 420  Bit Score: 439.94  E-value: 3.67e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771899  31 ALRLDEEDKLSHFRNCFYIPkmrdlpsidlslvseDDDAIYFLGNSLGLQPKMVRTYLEEEL-DKWAKMGAYGHDvgKRP 109
Cdd:COG3844    8 ARALDAADPLAAFRDRFHLP---------------DDGVIYLDGNSLGLLPKAAAARLAEVLeEEWGELLIRGWN--EAP 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771899 110 WI-----VGDesivsLMKDIVGAHEKEIALMNALTINLHLLLLSFFKPTPKRHKILLEAKAFPSDHYAIESQIQLHGLDV 184
Cdd:COG3844   71 WFdlperLGD-----KLARLVGAAPGEVVVMDSTTVNLHKLLVAAYRPRPGRTKILSEADNFPTDRYALEGQARLHGLDE 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771899 185 EksMRMVKPREGEeTLRMEDILEVIEEEgdsIAVILFSGLHFYTGQLFNIPAITKAGHAKGCFVGFDLAHAVGNVELRLH 264
Cdd:COG3844  146 E--LRLVEPRDGE-TLRPEDIEAALDDD---VALVLLSHVNYRTGQLFDMAAITAAAHAAGALVGWDLAHSAGAVPVDLH 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771899 265 DWGVDFACWCSYKYLNSGAGGLAGAFVHEKHAHTVKPALVGWFGHDlsTRFNMDNKLQLIPGANGFRISNPPILLVCSLH 344
Cdd:COG3844  220 DWGVDFAVGCTYKYLNGGPGAPAFLYVHERHQDRLLQPLAGWWGHA--TPFAMEPGYEPAPGARRFQLGTPPILSMAALE 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771899 345 ASLEVFQQATMTALRRKSILLTGYLEYMLKHyhskdntENKGPIVNIITPSRAEERGCQLTLTfsIPK-KSVFKELEKRG 423
Cdd:COG3844  298 ASLDLFEEAGMDALRAKSLALTDYLIFLVEE-------RLAPLGLELITPRDPARRGSQVSLR--HPEaYAIFQALIERG 368

                 ...
gi 575771899 424 VVV 426
Cdd:COG3844  369 VIG 371
AGAT_like cd06451
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ...
180-348 1.62e-05

Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to alanine-glyoxylate aminotransferase (AGAT), serine-glyoxylate aminotransferase (SGAT), and 3-hydroxykynurenine transaminase (HKT). AGAT is a homodimeric protein, which catalyses the transamination of glyoxylate to glycine, and SGAT converts serine and glyoxylate to hydroxypyruvate and glycine. HKT catalyzes the PLP-dependent transamination of 3-hydroxykynurenine, a potentially toxic metabolite of the kynurenine pathway.


Pssm-ID: 99744 [Multi-domain]  Cd Length: 356  Bit Score: 46.51  E-value: 1.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771899 180 HGLDVE----KSMRMVKPREGEETLRMEDILEVIEEEGDSiavilfsglhfYTGQLFNIPAITKAGHAKGCFVGFDLAHA 255
Cdd:cd06451   96 YGADVDvvekPWGEAVSPEEIAEALEQHDIKAVTLTHNET-----------STGVLNPLEGIGALAKKHDALLIVDAVSS 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771899 256 VGNVELRLHDWGVDFACWCSYKYLNSGAGGLAGAFVHEkhahtvkpALVGWFGHDLSTRFNMDNKLQLIP-GANGFRISN 334
Cdd:cd06451  165 LGGEPFRMDEWGVDVAYTGSQKALGAPPGLGPIAFSER--------ALERIKKKTKPKGFYFDLLLLLKYwGEGYSYPHT 236
                        170
                 ....*....|....
gi 575771899 335 PPILLVCSLHASLE 348
Cdd:cd06451  237 PPVNLLYALREALD 250
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
228-370 7.43e-04

Aminotransferase class-V; This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.


Pssm-ID: 425567 [Multi-domain]  Cd Length: 368  Bit Score: 41.46  E-value: 7.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771899  228 TGQLFNIPAITKAGHAKGCFVGFDLAHAVGNVELRLHDWGVDFACWCSYKYLnsGAGGLAGAFVHEKHAHTVKPALVGwf 307
Cdd:pfam00266 152 TGTIQPVPEIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLY--GPTGIGVLYGRRDLLEKMPPLLGG-- 227
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 575771899  308 GHDLSTRFNMDNKLQLIPgaNGFRISNPPILLVCSLHASLEVFQQATMTALRRKSILLTGYLE 370
Cdd:pfam00266 228 GGMIETVSLQESTFADAP--WKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLY 288
 
Name Accession Description Interval E-value
kynureninase TIGR01814
kynureninase; This model describes kynureninase, a pyridoxal-phosphate enzyme. Kynurinine is a ...
31-426 0e+00

kynureninase; This model describes kynureninase, a pyridoxal-phosphate enzyme. Kynurinine is a Trp breakdown product and a precursor for NAD. In Chlamydia psittaci, an obligate intracellular pathogen, kynureninase makes anthranilate, a Trp precursor, from kynurenine. This counters the tryptophan hydrolysis that occurs in the host cell in response to the pathogen. [Energy metabolism, Amino acids and amines]


Pssm-ID: 130873 [Multi-domain]  Cd Length: 406  Bit Score: 548.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771899   31 ALRLDEEDKLSHFRNCFYIPKMRDlpsidlslvseDDDAIYFLGNSLGLQPKMVRTYLEEELDKWAKMGAYGHDVGKRPW 110
Cdd:TIGR01814   1 ALELDEADPLRALRDEFHLPKIGD-----------ENAVIYLDGNSLGLMPKAARNALKEELDKWAKIAIRGHNTGKAPW 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771899  111 IVGDESIVSLMKdiVGAHEKEIALMNALTINLHLLLLSFFKPTPKRHKILLEAKAFPSDHYAIESQIQLHGLDVEKSMRM 190
Cdd:TIGR01814  70 FTLDESLLKLRL--VGAKEDEVVVMNTLTINLHLLLASFYKPTPKRYKILLEAKAFPSDHYAIESQLQLHGLTVEESMVQ 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771899  191 VKPREgEETLRMEDILEVIEEEGDSIAVILFSGLHFYTGQLFNIPAITKAGHAKGCFVGFDLAHAVGNVELRLHDWGVDF 270
Cdd:TIGR01814 148 IEPRE-EETLRLEDILDTIEKNGDDIAVILLSGVQYYTGQLFDMAAITRAAHAKGALVGFDLAHAVGNVPLDLHDWGVDF 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771899  271 ACWCSYKYLNsgAGGLAGAFVHEKHAHTVKPALVGWFGHDLSTRFNMDNKLQLIPgaNGFRISNPPILLVCSLHASLEVF 350
Cdd:TIGR01814 227 ACWCTYKYLN--AGPGAGAFVHEKHAHTERPRLAGWWGHARPTRFKMDNTLGLIP--CGFRISNPPILSVAALRGSLDIF 302
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 575771899  351 QQATMTALRRKSILLTGYLEYMLKHYHSKDntenkgPIVNIITPSRAEERGCQLTLTFSIPKKSVFKELEKRGVVV 426
Cdd:TIGR01814 303 DQAGMEALRKKSLLLTDYLEELIKARCGGP------PVLTIITPRDHAQRGCQLSLTHPVPGKAVFQALIKRGVIG 372
Bna5 COG3844
Kynureninase [Amino acid transport and metabolism];
31-426 3.67e-153

Kynureninase [Amino acid transport and metabolism];


Pssm-ID: 443054 [Multi-domain]  Cd Length: 420  Bit Score: 439.94  E-value: 3.67e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771899  31 ALRLDEEDKLSHFRNCFYIPkmrdlpsidlslvseDDDAIYFLGNSLGLQPKMVRTYLEEEL-DKWAKMGAYGHDvgKRP 109
Cdd:COG3844    8 ARALDAADPLAAFRDRFHLP---------------DDGVIYLDGNSLGLLPKAAAARLAEVLeEEWGELLIRGWN--EAP 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771899 110 WI-----VGDesivsLMKDIVGAHEKEIALMNALTINLHLLLLSFFKPTPKRHKILLEAKAFPSDHYAIESQIQLHGLDV 184
Cdd:COG3844   71 WFdlperLGD-----KLARLVGAAPGEVVVMDSTTVNLHKLLVAAYRPRPGRTKILSEADNFPTDRYALEGQARLHGLDE 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771899 185 EksMRMVKPREGEeTLRMEDILEVIEEEgdsIAVILFSGLHFYTGQLFNIPAITKAGHAKGCFVGFDLAHAVGNVELRLH 264
Cdd:COG3844  146 E--LRLVEPRDGE-TLRPEDIEAALDDD---VALVLLSHVNYRTGQLFDMAAITAAAHAAGALVGWDLAHSAGAVPVDLH 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771899 265 DWGVDFACWCSYKYLNSGAGGLAGAFVHEKHAHTVKPALVGWFGHDlsTRFNMDNKLQLIPGANGFRISNPPILLVCSLH 344
Cdd:COG3844  220 DWGVDFAVGCTYKYLNGGPGAPAFLYVHERHQDRLLQPLAGWWGHA--TPFAMEPGYEPAPGARRFQLGTPPILSMAALE 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771899 345 ASLEVFQQATMTALRRKSILLTGYLEYMLKHyhskdntENKGPIVNIITPSRAEERGCQLTLTfsIPK-KSVFKELEKRG 423
Cdd:COG3844  298 ASLDLFEEAGMDALRAKSLALTDYLIFLVEE-------RLAPLGLELITPRDPARRGSQVSLR--HPEaYAIFQALIERG 368

                 ...
gi 575771899 424 VVV 426
Cdd:COG3844  369 VIG 371
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
199-426 1.11e-06

Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 50.52  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771899 199 TLRMEDILEVIeeeGDSIAVILFSGLHFYTGQLFNIPAITKAGHAKGCFVGFDLAHAVGNVELRLHDWGVDFACWCSYK- 277
Cdd:COG0520  141 ELDLEALEALL---TPRTKLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKl 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771899 278 YLNSGAGGLagaFVHEKHAHTVKPALVGWFghdlSTRFNMDNKLQLIPGANGFRISNPPILLVCSLHASLEVFQQATMTA 357
Cdd:COG0520  218 YGPTGIGVL---YGKRELLEALPPFLGGGG----MIEWVSFDGTTYADLPRRFEAGTPNIAGAIGLGAAIDYLEAIGMEA 290
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 575771899 358 LRRKSILLTGYLEYMLKhyhskdntENKGpiVNIITPSRAEERGCqlTLTFSIPKKS---VFKELEKRGVVV 426
Cdd:COG0520  291 IEARERELTAYALEGLA--------AIPG--VRILGPADPEDRSG--IVSFNVDGVHphdVAALLDDEGIAV 350
AGAT_like cd06451
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ...
180-348 1.62e-05

Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to alanine-glyoxylate aminotransferase (AGAT), serine-glyoxylate aminotransferase (SGAT), and 3-hydroxykynurenine transaminase (HKT). AGAT is a homodimeric protein, which catalyses the transamination of glyoxylate to glycine, and SGAT converts serine and glyoxylate to hydroxypyruvate and glycine. HKT catalyzes the PLP-dependent transamination of 3-hydroxykynurenine, a potentially toxic metabolite of the kynurenine pathway.


Pssm-ID: 99744 [Multi-domain]  Cd Length: 356  Bit Score: 46.51  E-value: 1.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771899 180 HGLDVE----KSMRMVKPREGEETLRMEDILEVIEEEGDSiavilfsglhfYTGQLFNIPAITKAGHAKGCFVGFDLAHA 255
Cdd:cd06451   96 YGADVDvvekPWGEAVSPEEIAEALEQHDIKAVTLTHNET-----------STGVLNPLEGIGALAKKHDALLIVDAVSS 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771899 256 VGNVELRLHDWGVDFACWCSYKYLNSGAGGLAGAFVHEkhahtvkpALVGWFGHDLSTRFNMDNKLQLIP-GANGFRISN 334
Cdd:cd06451  165 LGGEPFRMDEWGVDVAYTGSQKALGAPPGLGPIAFSER--------ALERIKKKTKPKGFYFDLLLLLKYwGEGYSYPHT 236
                        170
                 ....*....|....
gi 575771899 335 PPILLVCSLHASLE 348
Cdd:cd06451  237 PPVNLLYALREALD 250
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
228-370 7.43e-04

Aminotransferase class-V; This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.


Pssm-ID: 425567 [Multi-domain]  Cd Length: 368  Bit Score: 41.46  E-value: 7.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771899  228 TGQLFNIPAITKAGHAKGCFVGFDLAHAVGNVELRLHDWGVDFACWCSYKYLnsGAGGLAGAFVHEKHAHTVKPALVGwf 307
Cdd:pfam00266 152 TGTIQPVPEIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLY--GPTGIGVLYGRRDLLEKMPPLLGG-- 227
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 575771899  308 GHDLSTRFNMDNKLQLIPgaNGFRISNPPILLVCSLHASLEVFQQATMTALRRKSILLTGYLE 370
Cdd:pfam00266 228 GGMIETVSLQESTFADAP--WKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLY 288
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH