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Conserved domains on  [gi|334186182|ref|NP_001190152|]
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cysteine synthase C1 [Arabidopsis thaliana]

Protein Classification

PALP domain-containing protein( domain architecture ID 751)

PALP domain-containing protein belonging to the tryptophan synthase beta superfamily (fold type II) that consists of pyridoxal phosphate (PLP)-dependent enzymes that catalyze beta-replacement and beta-elimination reactions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Trp-synth-beta_II super family cl00342
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 1-247 2.74e-175

Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP)-dependent enzymes catalyzes beta-replacement and beta-elimination reactions. This CD corresponds to aminocyclopropane-1-carboxylate deaminase (ACCD), tryptophan synthase beta chain (Trp-synth_B), cystathionine beta-synthase (CBS), O-acetylserine sulfhydrylase (CS), serine dehydratase (Ser-dehyd), threonine dehydratase (Thr-dehyd), diaminopropionate ammonia lyase (DAL), and threonine synthase (Thr-synth). ACCD catalyzes the conversion of 1-aminocyclopropane-1-carboxylate to alpha-ketobutyrate and ammonia. Tryptophan synthase folds into a tetramer, where the beta chain is the catalytic PLP-binding subunit and catalyzes the formation of L-tryptophan from indole and L-serine. CBS is a tetrameric hemeprotein that catalyzes condensation of serine and homocysteine to cystathionine. CS is a homodimer that catalyzes the formation of L-cysteine from O-acetyl-L-serine. Ser-dehyd catalyzes the conversion of L- or D-serine to pyruvate and ammonia. Thr-dehyd is active as a homodimer and catalyzes the conversion of L-threonine to 2-oxobutanoate and ammonia. DAL is also a homodimer and catalyzes the alpha, beta-elimination reaction of both L- and D-alpha, beta-diaminopropionate to form pyruvate and ammonia. Thr-synth catalyzes the formation of threonine and inorganic phosphate from O-phosphohomoserine.


The actual alignment was detected with superfamily member PLN02556:

Pssm-ID: 444852 [Multi-domain]  Cd Length: 368  Bit Score: 486.77  E-value: 2.74e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182   1 MGISLAFMAAMKGYRIIMTMPSYTSLERRVTMRSFGAELVLTDPAKGMGGTVKKAYDLLDSTPDAFMCQQFANPANTQIH 80
Cdd:PLN02556 122 MGISLAFMAAMKGYKMILTMPSYTSLERRVTMRAFGAELVLTDPTKGMGGTVKKAYELLESTPDAFMLQQFSNPANTQVH 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182  81 FDTTGPEIWEDTLGNVDIFVMGIGSGGTVSGVGRYLKSKNPNVKIYGVEPAESNILNGGKPGPHAITGNGVGFKPEILDM 160
Cdd:PLN02556 202 FETTGPEIWEDTLGQVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEPAESNVLNGGKPGPHHITGNGVGFKPDILDM 281

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182 161 DVMESVLEVSSEDAIKMARELALKEGLMVGISSGANTVAAIRLAKMPENKGKLIVTIHASFGERYLSSVLFDELRKEAEE 240
Cdd:PLN02556 282 DVMEKVLEVSSEDAVNMARELALKEGLMVGISSGANTVAALRLAKMPENKGKLIVTVHPSFGERYLSSVLFQELRKEAEN 361


                 ....*..
gi 334186182 241 MKPVSVD 247
Cdd:PLN02556 362 MQPVSVD 368
 
Name Accession Description Interval E-value
PLN02556 PLN02556
cysteine synthase/L-3-cyanoalanine synthase
 1-247 2.74e-175

cysteine synthase/L-3-cyanoalanine synthase


Pssm-ID: 178171 [Multi-domain]  Cd Length: 368  Bit Score: 486.77  E-value: 2.74e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182   1 MGISLAFMAAMKGYRIIMTMPSYTSLERRVTMRSFGAELVLTDPAKGMGGTVKKAYDLLDSTPDAFMCQQFANPANTQIH 80
Cdd:PLN02556 122 MGISLAFMAAMKGYKMILTMPSYTSLERRVTMRAFGAELVLTDPTKGMGGTVKKAYELLESTPDAFMLQQFSNPANTQVH 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182  81 FDTTGPEIWEDTLGNVDIFVMGIGSGGTVSGVGRYLKSKNPNVKIYGVEPAESNILNGGKPGPHAITGNGVGFKPEILDM 160
Cdd:PLN02556 202 FETTGPEIWEDTLGQVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEPAESNVLNGGKPGPHHITGNGVGFKPDILDM 281

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182 161 DVMESVLEVSSEDAIKMARELALKEGLMVGISSGANTVAAIRLAKMPENKGKLIVTIHASFGERYLSSVLFDELRKEAEE 240
Cdd:PLN02556 282 DVMEKVLEVSSEDAVNMARELALKEGLMVGISSGANTVAALRLAKMPENKGKLIVTVHPSFGERYLSSVLFQELRKEAEN 361


                 ....*..
gi 334186182 241 MKPVSVD 247
Cdd:PLN02556 362 MQPVSVD 368
cysK TIGR01139
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ...
 1-231 1.05e-110

cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine synthase B (CysM). CysM differs in having a broader specificity that also allows the use of thiosulfate to produce cysteine thiosulfonate. [Amino acid biosynthesis, Serine family]


Pssm-ID: 273465  Cd Length: 298  Bit Score: 320.47  E-value: 1.05e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182    1 MGISLAFMAAMKGYRIIMTMPSYTSLERRVTMRSFGAELVLTDPAKGMGGTVKKAYDLLDSTPDA-FMCQQFANPANTQI 79
Cdd:TIGR01139  68 TGIALAMVAAARGYKLILTMPETMSIERRKLLKAYGAELVLTPGAEGMKGAIAKAEEIAASTPNSyFMLQQFENPANPEI 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182   80 HFDTTGPEIWEDTLGNVDIFVMGIGSGGTVSGVGRYLKSKNPNVKIYGVEPAESNILNGGKPGPHAITGNGVGFKPEILD 159
Cdd:TIGR01139 148 HRKTTGPEIWRDTDGKLDAFVAGVGTGGTITGVGEVLKEQKPNIKIVAVEPAESPVLSGGKPGPHKIQGIGAGFIPKNLN 227

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334186182  160 MDVMESVLEVSSEDAIKMARELALKEGLMVGISSGANTVAAIRLAKMPEnKGKLIVTIHASFGERYLSSVLF 231
Cdd:TIGR01139 228 RSVIDEVITVSDEEAIETARRLAAEEGILVGISSGAAVAAALKLAKRPE-PDKLIVVILPSTGERYLSTPLF 298
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
 2-228 1.01e-104

Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 439802 [Multi-domain]  Cd Length: 301  Bit Score: 305.05  E-value: 1.01e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182   2 GISLAFMAAMKGYRIIMTMPSYTSLERRVTMRSFGAELVLTDPAKGMGGTVKKAYDLLDSTPDAFMCQQFANPANTQIHF 81
Cdd:COG0031   76 GIGLAMVAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEGMKGAIDKAEELAAETPGAFWPNQFENPANPEAHY 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182  82 DTTGPEIWEDTLGNVDIFV---------MGIgsggtvsgvGRYLKSKNPNVKIYGVEPAESNILNGGKPGPHAITGNGVG 152
Cdd:COG0031  156 ETTGPEIWEQTDGKVDAFVagvgtggtiTGV---------GRYLKERNPDIKIVAVEPEGSPLLSGGEPGPHKIEGIGAG 226

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334186182 153 FKPEILDMDVMESVLEVSSEDAIKMARELALKEGLMVGISSGANTVAAIRLAKMpENKGKLIVTIHASFGERYLSS 228
Cdd:COG0031  227 FVPKILDPSLIDEVITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKR-LGPGKTIVTILPDSGERYLST 301
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 1-227 1.40e-102

CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS is a unique heme-containing enzyme that catalyzes a pyridoxal 5'-phosphate (PLP)-dependent condensation of serine and homocysteine to give cystathionine. Deficiency of CBS leads to homocystinuria, an inherited disease of sulfur metabolism characterized by increased levels of the toxic metabolite homocysteine. Cysteine synthase on the other hand catalyzes the last step of cysteine biosynthesis. This subgroup also includes an O-Phosphoserine sulfhydrylase found in hyperthermophilic archaea which produces L-cysteine from sulfide and the more thermostable O-phospho-L-serine.


Pssm-ID: 107204 [Multi-domain]  Cd Length: 291  Bit Score: 299.43  E-value: 1.40e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182   1 MGISLAFMAAMKGYRIIMTMPSYTSLERRVTMRSFGAELVLTDPAK--GMGGTVKKAYDLLDSTPDAFMCQQFANPANTQ 78
Cdd:cd01561   64 TGIGLAMVAAAKGYRFIIVMPETMSEEKRKLLRALGAEVILTPEAEadGMKGAIAKARELAAETPNAFWLNQFENPANPE 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182  79 IHFDTTGPEIWEDTLGNVDIFV---------MGIgsggtvsgvGRYLKSKNPNVKIYGVEPAESNILNGGKPGPHAITGN 149
Cdd:cd01561  144 AHYETTAPEIWEQLDGKVDAFVagvgtggtiTGV---------ARYLKEKNPNVRIVGVDPVGSVLFSGGPPGPHKIEGI 214

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334186182 150 GVGFKPEILDMDVMESVLEVSSEDAIKMARELALKEGLMVGISSGANTVAAIRLAKMPEnKGKLIVTIHASFGERYLS 227
Cdd:cd01561  215 GAGFIPENLDRSLIDEVVRVSDEEAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLG-PGKTIVTILPDSGERYLS 291
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 1-218 2.18e-44

Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate dependent enzymes. This family includes: serine dehydratase EC:4.2.1.13 P20132, threonine dehydratase EC:4.2.1.16, tryptophan synthase beta chain EC:4.2.1.20, threonine synthase EC:4.2.99.2, cysteine synthase EC:4.2.99.8 P11096, cystathionine beta-synthase EC:4.2.1.22, 1-aminocyclopropane-1-carboxylate deaminase EC:4.1.99.4.


Pssm-ID: 459749 [Multi-domain]  Cd Length: 295  Bit Score: 150.92  E-value: 2.18e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182    1 MGISLAFMAAMKGYRIIMTMPSYTSLERRVTMRSFGAELVLTDPakGMGGTVKKAYDLLDSTPDAFMCQQFANPANTQIH 80
Cdd:pfam00291  66 HGRALAAAAARLGLKVTIVVPEDAPPGKLLLMRALGAEVVLVGG--DYDEAVAAARELAAEGPGAYYINQYDNPLNIEGY 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182   81 FdTTGPEIWEDTLGNVDIFVMGIGSGGTVSGVGRYLKSKNPNVKIYGVEPAESNILNGG---------KPGPHAITGNGV 151
Cdd:pfam00291 144 G-TIGLEILEQLGGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSlaagrpvpvPVADTIADGLGV 222

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334186182  152 GFKPEILDMDVME----SVLEVSSEDAIKMARELALKEGLMVGISSGANtVAAIRLAKMPE-NKGKLIVTIH 218
Cdd:pfam00291 223 GDEPGALALDLLDeyvgEVVTVSDEEALEAMRLLARREGIVVEPSSAAA-LAALKLALAGElKGGDRVVVVL 293
 
Name Accession Description Interval E-value
PLN02556 PLN02556
cysteine synthase/L-3-cyanoalanine synthase
 1-247 2.74e-175

cysteine synthase/L-3-cyanoalanine synthase


Pssm-ID: 178171 [Multi-domain]  Cd Length: 368  Bit Score: 486.77  E-value: 2.74e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182   1 MGISLAFMAAMKGYRIIMTMPSYTSLERRVTMRSFGAELVLTDPAKGMGGTVKKAYDLLDSTPDAFMCQQFANPANTQIH 80
Cdd:PLN02556 122 MGISLAFMAAMKGYKMILTMPSYTSLERRVTMRAFGAELVLTDPTKGMGGTVKKAYELLESTPDAFMLQQFSNPANTQVH 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182  81 FDTTGPEIWEDTLGNVDIFVMGIGSGGTVSGVGRYLKSKNPNVKIYGVEPAESNILNGGKPGPHAITGNGVGFKPEILDM 160
Cdd:PLN02556 202 FETTGPEIWEDTLGQVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEPAESNVLNGGKPGPHHITGNGVGFKPDILDM 281

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182 161 DVMESVLEVSSEDAIKMARELALKEGLMVGISSGANTVAAIRLAKMPENKGKLIVTIHASFGERYLSSVLFDELRKEAEE 240
Cdd:PLN02556 282 DVMEKVLEVSSEDAVNMARELALKEGLMVGISSGANTVAALRLAKMPENKGKLIVTVHPSFGERYLSSVLFQELRKEAEN 361


                 ....*..
gi 334186182 241 MKPVSVD 247
Cdd:PLN02556 362 MQPVSVD 368
PLN02565 PLN02565
cysteine synthase
 2-242 2.31e-118

cysteine synthase


Pssm-ID: 166206  Cd Length: 322  Bit Score: 340.75  E-value: 2.31e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182   2 GISLAFMAAMKGYRIIMTMPSYTSLERRVTMRSFGAELVLTDPAKGMGGTVKKAYDLLDSTPDAFMCQQFANPANTQIHF 81
Cdd:PLN02565  79 GIGLAFMAAAKGYKLIITMPASMSLERRIILLAFGAELVLTDPAKGMKGAVQKAEEILAKTPNSYILQQFENPANPKIHY 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182  82 DTTGPEIWEDTLGNVDIFVMGIGSGGTVSGVGRYLKSKNPNVKIYGVEPAESNILNGGKPGPHAITGNGVGFKPEILDMD 161
Cdd:PLN02565 159 ETTGPEIWKGTGGKVDAFVSGIGTGGTITGAGKYLKEQNPDIKLYGVEPVESAVLSGGKPGPHKIQGIGAGFIPGVLDVD 238

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182 162 VMESVLEVSSEDAIKMARELALKEGLMVGISSGANTVAAIRLAKMPENKGKLIVTIHASFGERYLSSVLFDELRKEAEEM 241
Cdd:PLN02565 239 LLDEVVQVSSDEAIETAKLLALKEGLLVGISSGAAAAAAIKIAKRPENAGKLIVVIFPSFGERYLSSVLFESVKKEAENM 318


                 .
gi 334186182 242 K 242
Cdd:PLN02565 319 V 319
cysK TIGR01139
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ...
 1-231 1.05e-110

cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine synthase B (CysM). CysM differs in having a broader specificity that also allows the use of thiosulfate to produce cysteine thiosulfonate. [Amino acid biosynthesis, Serine family]


Pssm-ID: 273465  Cd Length: 298  Bit Score: 320.47  E-value: 1.05e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182    1 MGISLAFMAAMKGYRIIMTMPSYTSLERRVTMRSFGAELVLTDPAKGMGGTVKKAYDLLDSTPDA-FMCQQFANPANTQI 79
Cdd:TIGR01139  68 TGIALAMVAAARGYKLILTMPETMSIERRKLLKAYGAELVLTPGAEGMKGAIAKAEEIAASTPNSyFMLQQFENPANPEI 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182   80 HFDTTGPEIWEDTLGNVDIFVMGIGSGGTVSGVGRYLKSKNPNVKIYGVEPAESNILNGGKPGPHAITGNGVGFKPEILD 159
Cdd:TIGR01139 148 HRKTTGPEIWRDTDGKLDAFVAGVGTGGTITGVGEVLKEQKPNIKIVAVEPAESPVLSGGKPGPHKIQGIGAGFIPKNLN 227

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334186182  160 MDVMESVLEVSSEDAIKMARELALKEGLMVGISSGANTVAAIRLAKMPEnKGKLIVTIHASFGERYLSSVLF 231
Cdd:TIGR01139 228 RSVIDEVITVSDEEAIETARRLAAEEGILVGISSGAAVAAALKLAKRPE-PDKLIVVILPSTGERYLSTPLF 298
cysKM TIGR01136
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ...
 1-231 2.56e-107

cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and CysM) from cystathionine beta-synthase, a protein found primarily in eukaryotes and carrying a C-terminal CBS domain lacking from this protein. Bacterial proteins lacking the CBS domain but otherwise showing resemblamnce to cystathionine beta-synthases and considerable phylogenetic distance from known cysteine synthases were excluded from the seed and score below the trusted cutoff. [Amino acid biosynthesis, Serine family]


Pssm-ID: 273463  Cd Length: 299  Bit Score: 311.91  E-value: 2.56e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182    1 MGISLAFMAAMKGYRIIMTMPSYTSLERRVTMRSFGAELVLTDPAKGMGGTVKKAYDLLDSTPDAFMCQQFANPANTQIH 80
Cdd:TIGR01136  69 TGIALAMVAAARGYKLILTMPETMSLERRKLLRAYGAELILTPGEEGMKGAIDKAEELAAETNKYVMLDQFENPANPEAH 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182   81 FDTTGPEIWEDTLGNVDIFVMGIGSGGTVSGVGRYLKSKNPNVKIYGVEPAESNILNGGKPGPHAITGNGVGFKPEILDM 160
Cdd:TIGR01136 149 YKTTGPEIWRDTDGRIDHFVAGVGTGGTITGVGRYLKEQNPNIQIVAVEPAESPVLSGGEPGPHKIQGIGAGFIPKILDL 228

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334186182  161 DVMESVLEVSSEDAIKMARELALKEGLMVGISSGANTVAAIRLAKMPENKGKLIVTIHASFGERYLSSVLF 231
Cdd:TIGR01136 229 SLIDEVITVSDEDAIETARRLAREEGILVGISSGAAVAAALKLAKRLENADKVIVAILPDTGERYLSTGLF 299
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
 2-228 1.01e-104

Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 439802 [Multi-domain]  Cd Length: 301  Bit Score: 305.05  E-value: 1.01e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182   2 GISLAFMAAMKGYRIIMTMPSYTSLERRVTMRSFGAELVLTDPAKGMGGTVKKAYDLLDSTPDAFMCQQFANPANTQIHF 81
Cdd:COG0031   76 GIGLAMVAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEGMKGAIDKAEELAAETPGAFWPNQFENPANPEAHY 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182  82 DTTGPEIWEDTLGNVDIFV---------MGIgsggtvsgvGRYLKSKNPNVKIYGVEPAESNILNGGKPGPHAITGNGVG 152
Cdd:COG0031  156 ETTGPEIWEQTDGKVDAFVagvgtggtiTGV---------GRYLKERNPDIKIVAVEPEGSPLLSGGEPGPHKIEGIGAG 226

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334186182 153 FKPEILDMDVMESVLEVSSEDAIKMARELALKEGLMVGISSGANTVAAIRLAKMpENKGKLIVTIHASFGERYLSS 228
Cdd:COG0031  227 FVPKILDPSLIDEVITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKR-LGPGKTIVTILPDSGERYLST 301
PLN03013 PLN03013
cysteine synthase
 2-243 1.88e-104

cysteine synthase


Pssm-ID: 178587 [Multi-domain]  Cd Length: 429  Bit Score: 309.40  E-value: 1.88e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182   2 GISLAFMAAMKGYRIIMTMPSYTSLERRVTMRSFGAELVLTDPAKGMGGTVKKAYDLLDSTPDAFMCQQFANPANTQIHF 81
Cdd:PLN03013 187 GIGLAFIAASRGYRLILTMPASMSMERRVLLKAFGAELVLTDPAKGMTGAVQKAEEILKNTPDAYMLQQFDNPANPKIHY 266

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182  82 DTTGPEIWEDTLGNVDIFVMGIGSGGTVSGVGRYLKSKNPNVKIYGVEPAESNILNGGKPGPHAITGNGVGFKPEILDMD 161
Cdd:PLN03013 267 ETTGPEIWDDTKGKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEPTESDILSGGKPGPHKIQGIGAGFIPKNLDQK 346

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182 162 VMESVLEVSSEDAIKMARELALKEGLMVGISSGANTVAAIRLAKMPENKGKLIVTIHASFGeRYLSSVLFDELRKEAEEM 241
Cdd:PLN03013 347 IMDEVIAISSEEAIETAKQLALKEGLMVGISSGAAAAAAIKVAKRPENAGKLIAVSLFASG-RDIYTPRCSSLSGKRWRK 425


                 ..
gi 334186182 242 KP 243
Cdd:PLN03013 426 CS 427
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 1-227 1.40e-102

CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS is a unique heme-containing enzyme that catalyzes a pyridoxal 5'-phosphate (PLP)-dependent condensation of serine and homocysteine to give cystathionine. Deficiency of CBS leads to homocystinuria, an inherited disease of sulfur metabolism characterized by increased levels of the toxic metabolite homocysteine. Cysteine synthase on the other hand catalyzes the last step of cysteine biosynthesis. This subgroup also includes an O-Phosphoserine sulfhydrylase found in hyperthermophilic archaea which produces L-cysteine from sulfide and the more thermostable O-phospho-L-serine.


Pssm-ID: 107204 [Multi-domain]  Cd Length: 291  Bit Score: 299.43  E-value: 1.40e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182   1 MGISLAFMAAMKGYRIIMTMPSYTSLERRVTMRSFGAELVLTDPAK--GMGGTVKKAYDLLDSTPDAFMCQQFANPANTQ 78
Cdd:cd01561   64 TGIGLAMVAAAKGYRFIIVMPETMSEEKRKLLRALGAEVILTPEAEadGMKGAIAKARELAAETPNAFWLNQFENPANPE 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182  79 IHFDTTGPEIWEDTLGNVDIFV---------MGIgsggtvsgvGRYLKSKNPNVKIYGVEPAESNILNGGKPGPHAITGN 149
Cdd:cd01561  144 AHYETTAPEIWEQLDGKVDAFVagvgtggtiTGV---------ARYLKEKNPNVRIVGVDPVGSVLFSGGPPGPHKIEGI 214

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334186182 150 GVGFKPEILDMDVMESVLEVSSEDAIKMARELALKEGLMVGISSGANTVAAIRLAKMPEnKGKLIVTIHASFGERYLS 227
Cdd:cd01561  215 GAGFIPENLDRSLIDEVVRVSDEEAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLG-PGKTIVTILPDSGERYLS 291
PLN00011 PLN00011
cysteine synthase
 2-241 8.86e-98

cysteine synthase


Pssm-ID: 177651  Cd Length: 323  Bit Score: 288.44  E-value: 8.86e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182   2 GISLAFMAAMKGYRIIMTMPSYTSLERRVTMRSFGAELVLTDPAKGMGGTVKKAYDLLDSTPDAFMCQQFANPANTQIHF 81
Cdd:PLN00011  81 GIGLACIGAARGYKVILVMPSTMSLERRIILRALGAEVHLTDQSIGLKGMLEKAEEILSKTPGGYIPQQFENPANPEIHY 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182  82 DTTGPEIWEDTLGNVDIFVMGIGSGGTVSGVGRYLKSKNPNVKIYGVEPAESNILNGGKPGPHAITGNGVGFKPEILDMD 161
Cdd:PLN00011 161 RTTGPEIWRDSAGKVDILVAGVGTGGTATGVGKFLKEKNKDIKVCVVEPVESAVLSGGQPGPHLIQGIGSGIIPFNLDLT 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182 162 VMESVLEVSSEDAIKMARELALKEGLMVGISSGANTVAAIRLAKMPENKGKLIVTIHASFGERYLSSVLFDELRKEAEEM 241
Cdd:PLN00011 241 IVDEIIQVTGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRPENAGKLIVVIFPSGGERYLSTKLFESVRYEAENL 320
cysM PRK11761
cysteine synthase CysM;
2-233 5.89e-65

cysteine synthase CysM;


Pssm-ID: 236972  Cd Length: 296  Bit Score: 203.95  E-value: 5.89e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182   2 GISLAFMAAMKGYRIIMTMPSYTSLERRVTMRSFGAELVLTDPAKGMGGtvkkAYDLLDSTPDA---FMCQQFANPANTQ 78
Cdd:PRK11761  75 GIALAMIAAIKGYRMKLIMPENMSQERRAAMRAYGAELILVPKEQGMEG----ARDLALQMQAEgegKVLDQFANPDNPL 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182  79 IHFDTTGPEIWEDTLGNVDIFV---------MGIgsggtvsgvGRYLKSKNPNVKIYGVEPAE-SNIlnggkPG----PH 144
Cdd:PRK11761 151 AHYETTGPEIWRQTEGRITHFVssmgttgtiMGV---------SRYLKEQNPAVQIVGLQPEEgSSI-----PGirrwPE 216

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182 145 AitgngvgFKPEILDMDVMESVLEVSSEDAIKMARELALKEGLMVGISSGANTVAAIRLAKmpENKGKLIVTIHASFGER 224
Cdd:PRK11761 217 E-------YLPKIFDASRVDRVLDVSQQEAENTMRRLAREEGIFCGVSSGGAVAAALRIAR--ENPNAVIVAIICDRGDR 287


                 ....*....
gi 334186182 225 YLSSVLFDE 233
Cdd:PRK11761 288 YLSTGVFPA 296
PRK10717 PRK10717
cysteine synthase A; Provisional
 2-237 3.31e-61

cysteine synthase A; Provisional


Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 195.47  E-value: 3.31e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182   2 GISLAFMAAMKGYRIIMTMPSYTSLERRVTMRSFGAELVLT------DPAKGMGGTVKKAYDLLDSTPD-AFMCQQFANP 74
Cdd:PRK10717  76 GIGLALVAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVpaapyaNPNNYVKGAGRLAEELVASEPNgAIWANQFDNP 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182  75 ANTQIHFDTTGPEIWEDTLGNVDIFVMGIGSGGTVSGVGRYLKSKNPNVKIYGVEPAESNI----LNG--GKPGPHAITG 148
Cdd:PRK10717 156 ANREAHYETTGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGSALysyyKTGelKAEGSSITEG 235

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182 149 NGVGFKPEILDMDVMESVLEVSSEDAIKMARELALKEGLMVGISSGANTVAAIRLAKmPENKGKLIVTIHASFGERYLSS 228
Cdd:PRK10717 236 IGQGRITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLAR-ELGPGHTIVTILCDSGERYQSK 314


                 ....*....
gi 334186182 229 VLFDELRKE 237
Cdd:PRK10717 315 LFNPDFLRE 323
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 1-218 2.18e-44

Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate dependent enzymes. This family includes: serine dehydratase EC:4.2.1.13 P20132, threonine dehydratase EC:4.2.1.16, tryptophan synthase beta chain EC:4.2.1.20, threonine synthase EC:4.2.99.2, cysteine synthase EC:4.2.99.8 P11096, cystathionine beta-synthase EC:4.2.1.22, 1-aminocyclopropane-1-carboxylate deaminase EC:4.1.99.4.


Pssm-ID: 459749 [Multi-domain]  Cd Length: 295  Bit Score: 150.92  E-value: 2.18e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182    1 MGISLAFMAAMKGYRIIMTMPSYTSLERRVTMRSFGAELVLTDPakGMGGTVKKAYDLLDSTPDAFMCQQFANPANTQIH 80
Cdd:pfam00291  66 HGRALAAAAARLGLKVTIVVPEDAPPGKLLLMRALGAEVVLVGG--DYDEAVAAARELAAEGPGAYYINQYDNPLNIEGY 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182   81 FdTTGPEIWEDTLGNVDIFVMGIGSGGTVSGVGRYLKSKNPNVKIYGVEPAESNILNGG---------KPGPHAITGNGV 151
Cdd:pfam00291 144 G-TIGLEILEQLGGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSlaagrpvpvPVADTIADGLGV 222

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334186182  152 GFKPEILDMDVME----SVLEVSSEDAIKMARELALKEGLMVGISSGANtVAAIRLAKMPE-NKGKLIVTIH 218
Cdd:pfam00291 223 GDEPGALALDLLDeyvgEVVTVSDEEALEAMRLLARREGIVVEPSSAAA-LAALKLALAGElKGGDRVVVVL 293
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 2-218 3.33e-39

Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP)-dependent enzymes catalyzes beta-replacement and beta-elimination reactions. This CD corresponds to aminocyclopropane-1-carboxylate deaminase (ACCD), tryptophan synthase beta chain (Trp-synth_B), cystathionine beta-synthase (CBS), O-acetylserine sulfhydrylase (CS), serine dehydratase (Ser-dehyd), threonine dehydratase (Thr-dehyd), diaminopropionate ammonia lyase (DAL), and threonine synthase (Thr-synth). ACCD catalyzes the conversion of 1-aminocyclopropane-1-carboxylate to alpha-ketobutyrate and ammonia. Tryptophan synthase folds into a tetramer, where the beta chain is the catalytic PLP-binding subunit and catalyzes the formation of L-tryptophan from indole and L-serine. CBS is a tetrameric hemeprotein that catalyzes condensation of serine and homocysteine to cystathionine. CS is a homodimer that catalyzes the formation of L-cysteine from O-acetyl-L-serine. Ser-dehyd catalyzes the conversion of L- or D-serine to pyruvate and ammonia. Thr-dehyd is active as a homodimer and catalyzes the conversion of L-threonine to 2-oxobutanoate and ammonia. DAL is also a homodimer and catalyzes the alpha, beta-elimination reaction of both L- and D-alpha, beta-diaminopropionate to form pyruvate and ammonia. Thr-synth catalyzes the formation of threonine and inorganic phosphate from O-phosphohomoserine.


Pssm-ID: 107202 [Multi-domain]  Cd Length: 244  Bit Score: 136.11  E-value: 3.33e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182   2 GISLAFMAAMKGYRIIMTMPSYTSLERRVTMRSFGAELVLTDPakGMGGTVKKAYDLLDSTPDAFMCQQFANPANTQIHF 81
Cdd:cd00640   62 GIALAAAAARLGLKCTIVMPEGASPEKVAQMRALGAEVVLVPG--DFDDAIALAKELAEEDPGAYYVNQFDNPANIAGQG 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182  82 dTTGPEIWEDTLG-NVDIFV---------MGIgsggtvsgvGRYLKSKNPNVKIYGVEPAesnilnggkpgphaitgngv 151
Cdd:cd00640  140 -TIGLEILEQLGGqKPDAVVvpvggggniAGI---------ARALKELLPNVKVIGVEPE-------------------- 189

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334186182 152 gfkpeildmdvmesVLEVSSEDAIKMARELALKEGLMVGISSGANTVAAIRLAKmPENKGKLIVTIH 218
Cdd:cd00640  190 --------------VVTVSDEEALEAIRLLAREEGILVEPSSAAALAAALKLAK-KLGKGKTVVVIL 241
PLN02356 PLN02356
phosphateglycerate kinase
 52-227 1.03e-21

phosphateglycerate kinase


Pssm-ID: 215204  Cd Length: 423  Bit Score: 92.75  E-value: 1.03e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182  52 VKKAYDLLDSTPDAFMCQQFANPANTQIHFDTTGPEIWEDTLGNVDIFVMGIGSGGTVSGVGRYLKSKNPNVKIYGVEPA 131
Cdd:PLN02356 207 EKENSLFSSSCTGGFFADQFENLANFRAHYEGTGPEIWEQTQGNLDAFVAAAGTGGTLAGVSRFLQEKNPNIKCFLIDPP 286

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182 132 ESNILNGGKPG---------------PHAITGNGVGFK--PEILDMDVMESVLEVSSEDAIKMARELALKEGLMVGISSG 194
Cdd:PLN02356 287 GSGLFNKVTRGvmytreeaegrrlknPFDTITEGIGINrlTQNFLMAKLDGAFRGTDKEAVEMSRYLLKNDGLFVGSSSA 366

                        170       180       190
                 ....*....|....*....|....*....|...
gi 334186182 195 ANTVAAIRLAKmPENKGKLIVTIHASFGERYLS 227
Cdd:PLN02356 367 MNCVGAVRVAQ-SLGPGHTIVTILCDSGMRHLS 398
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 2-217 2.21e-08

Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 440784 [Multi-domain]  Cd Length: 327  Bit Score: 53.50  E-value: 2.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182   2 GISLAFMAAMKGYRIIMTMPSYTSLERRVTMRSFGAELVLTDpakgmggtvkkaydllDSTPDAF-MCQQFANPAN-TQI 79
Cdd:COG1171   84 AQGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHG----------------DTYDDAEaAAAELAEEEGaTFV 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182  80 H-FD---------TTGPEIWEDtLGNVD-IFV--------MGIGSggtvsgvgrYLKSKNPNVKIYGVEPAESN------ 134
Cdd:COG1171  148 HpFDdpdviagqgTIALEILEQ-LPDLDaVFVpvggggliAGVAA---------ALKALSPDIRVIGVEPEGAAamyrsl 217

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182 135 -------------I---LNGGKPGPHAitgngvgFkpEILDMDVMESVLeVsSEDAIKMA-RELALKEGLMVGiSSGANT 197
Cdd:COG1171  218 aagepvtlpgvdtIadgLAVGRPGELT-------F--EILRDLVDDIVT-V-SEDEIAAAmRLLLERTKIVVE-PAGAAA 285

                        250       260
                 ....*....|....*....|
gi 334186182 198 VAAIrLAKMPENKGKLIVTI 217
Cdd:COG1171  286 LAAL-LAGKERLKGKRVVVV 304
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
 2-217 1.65e-07

Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. Although the nitrogen atoms of most amino acids are transferred to alpha-ketoglutarate before removal, the alpha-amino group of threonine can be directly converted into NH4+. The direct deamination is catalyzed by threonine dehydratase, in which pyridoxal phosphate (PLP) is the prosthetic group. Threonine dehydratase is widely distributed in all three major phylogenetic divisions.


Pssm-ID: 107205 [Multi-domain]  Cd Length: 304  Bit Score: 50.95  E-value: 1.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182   2 GISLAFMAAMKGYRIIMTMPSYTSLERRVTMRSFGAELVLTDpakgmggtvkkaydllDSTPDAF-MCQQFANPAN-TQI 79
Cdd:cd01562   77 AQGVAYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYG----------------EDFDEAEaKARELAEEEGlTFI 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182  80 H-FD---------TTGPEIWEDtLGNVD-IFV--------MGIGSggtvsgvgrYLKSKNPNVKIYGVEPAESNI----L 136
Cdd:cd01562  141 HpFDdpdviagqgTIGLEILEQ-VPDLDaVFVpvggggliAGIAT---------AVKALSPNTKVIGVEPEGAPAmaqsL 210

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186182 137 NGGKPGPHAITGN---GVGFK------PEILdMDVMESVLEVsSEDAIKMA-RELALKEGLMV-GisSGANTVAAIrLAK 205
Cdd:cd01562  211 AAGKPVTLPEVDTiadGLAVKrpgeltFEII-RKLVDDVVTV-SEDEIAAAmLLLFEREKLVAeP--AGALALAAL-LSG 285

                        250
                 ....*....|..
gi 334186182 206 MPENKGKLIVTI 217
Cdd:cd01562  286 KLDLKGKKVVVV 297
PBP1_As_SBP-like cd06330
periplasmic substrate-binding domain of active transport proteins; Periplasmic ...
 170-220 1.89e-04

periplasmic substrate-binding domain of active transport proteins; Periplasmic substrate-binding domain of active transport proteins found in bacteria and Archaea that is predicted to be involved in the efflux of toxic compounds. Members of this subgroup include proteins from Herminiimonas arsenicoxydans, which is resistant to arsenic (As) and various heavy metals such as cadmium and zinc. Moreover, they show significant sequence similarity to the cluster of AmiC and active transport systems for short-chain amides and urea (FmdDEF), and thus are likely to exhibit a ligand-binding mode similar to that of the amide sensor protein AmiC from Pseudomonas aeruginosa.


Pssm-ID: 380553 [Multi-domain]  Cd Length: 342  Bit Score: 41.78  E-value: 1.89e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 334186182 170 SSEDAIKMARELALKEG--LMVGISSGANTVAAIRLAKmpENKGKLIVTIHAS 220
Cdd:cd06330   51 KPDEAVRAARELVLQEGvdFLIGTISSGVALAVAPVAE--ELKVLFIATDAAT 101
 
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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