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Conserved domains on  [gi|2113639204|ref|XP_044159752|]
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heme oxygenase 2 isoform X1 [Bufo gargarizans]

Protein Classification

biliverdin-producing heme oxygenase( domain architecture ID 10471538)

biliverdin-producing heme oxygenase cleaves the heme ring at the alpha-methene bridge to form biliverdin, which is subsequently converted to bilirubin by biliverdin reductase

CATH:  1.20.910.10
EC:  1.14.14.18
Gene Ontology:  GO:0004392|GO:0046872|GO:0006788
PubMed:  12230872|11281297
SCOP:  3001676

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
Heme_oxygenase pfam01126
Heme oxygenase;
159-364 3.98e-97

Heme oxygenase;


:

Pssm-ID: 395895  Cd Length: 204  Bit Score: 289.65  E-value: 3.98e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113639204 159 TDLSELLKEGTKESHEKAENTKFVKDFLKGRIKRELFKLATGALYYTYSALEEELDRNKENPAITALYFPqELHRAEALK 238
Cdd:pfam01126   1 LNLAKRLREATKDVHVMAENLVFVKDFLKGVVDKDAYAKLLANLYFVYSALEEELERNRDSPVAAPIYFP-ELNRKAALE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113639204 239 KDVAYFYGEDWEDTIQCSEATQAYVDRIHHLGRHKPELLVAHAYTRYMGDLSGGQVLKKVAQRALHLPGtGEGIQFYLFD 318
Cdd:pfam01126  80 RDLAYLYGADWRADIQDSPATQEYVPRIREIGNESPELLVAHAYTRYLGDLSGGQLLKKIAQRALGLPP-GEGTAFYEFE 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2113639204 319 NVTNAQQFKQLYRARLNTLELSDEAKKSIVEEANKAFQFNMNVFEE 364
Cdd:pfam01126 159 GISDRKVFKQEYREALNALELDDEARARAVEEANDAFALNIQVFRE 204
 
Name Accession Description Interval E-value
Heme_oxygenase pfam01126
Heme oxygenase;
159-364 3.98e-97

Heme oxygenase;


Pssm-ID: 395895  Cd Length: 204  Bit Score: 289.65  E-value: 3.98e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113639204 159 TDLSELLKEGTKESHEKAENTKFVKDFLKGRIKRELFKLATGALYYTYSALEEELDRNKENPAITALYFPqELHRAEALK 238
Cdd:pfam01126   1 LNLAKRLREATKDVHVMAENLVFVKDFLKGVVDKDAYAKLLANLYFVYSALEEELERNRDSPVAAPIYFP-ELNRKAALE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113639204 239 KDVAYFYGEDWEDTIQCSEATQAYVDRIHHLGRHKPELLVAHAYTRYMGDLSGGQVLKKVAQRALHLPGtGEGIQFYLFD 318
Cdd:pfam01126  80 RDLAYLYGADWRADIQDSPATQEYVPRIREIGNESPELLVAHAYTRYLGDLSGGQLLKKIAQRALGLPP-GEGTAFYEFE 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2113639204 319 NVTNAQQFKQLYRARLNTLELSDEAKKSIVEEANKAFQFNMNVFEE 364
Cdd:pfam01126 159 GISDRKVFKQEYREALNALELDDEARARAVEEANDAFALNIQVFRE 204
COG5398 COG5398
Heme oxygenase [Coenzyme transport and metabolism];
159-366 4.22e-93

Heme oxygenase [Coenzyme transport and metabolism];


Pssm-ID: 444157  Cd Length: 211  Bit Score: 279.79  E-value: 4.22e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113639204 159 TDLSELLKEGTKESHEKAENTKFVKDFLKGRIKRELFKLATGALYYTYSALEEELDRNKENPAITALYFPqELHRAEALK 238
Cdd:COG5398     1 SPLSTALREGTAKAHTAAENSGFMKALLKGRLDRDAYVALLAQLYFVYSALEEALERHRDHPVVGPFYFP-ELNRLPALE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113639204 239 KDVAYFYGEDWEDTIQCSEATQAYVDRIHHLGRHKPELLVAHAYTRYMGDLSGGQVLKKVAQRALHLPGtGEGIQFYLFD 318
Cdd:COG5398    80 ADLAFLYGPDWRDQITPLPATRAYVARIREVAAEWPELLVAHHYTRYLGDLSGGQIIKRILQRAYGLPD-GEGTAFYEFD 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2113639204 319 NVTNAQQFKQLYRARLNTLELSDEAKKSIVEEANKAFQFNMNVFEELD 366
Cdd:COG5398   159 EIPDPKAFKDRYRAALDALPLDEAERERIVDEANLAFRLNTAVFAELE 206
pbsA CHL00168
heme oxygenase; Provisional
159-366 6.92e-91

heme oxygenase; Provisional


Pssm-ID: 214383  Cd Length: 238  Bit Score: 275.12  E-value: 6.92e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113639204 159 TDLSELLKEGTKESHEKAENTKFVKDFLKGRIKRELFKLATGALYYTYSALEEELDRNKENPAITALYFpQELHRAEALK 238
Cdd:CHL00168    3 TNLATQLREGTTKSHSMAENVSFVKSFLGGVIDKKSYRKLVANLYFVYSAIEEEIEKNKEHPLIKPIYF-QELNRKESLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113639204 239 KDVAYFYGEDWEDTIQCSEATQAYVDRIHHLGRHKPELLVAHAYTRYMGDLSGGQVLKKVAQRALHLPGTGeGIQFYLFD 318
Cdd:CHL00168   82 KDLNYYYGDDWKSIIEPSPATKIYVDRIHKISAKKPELLIAHAYTRYLGDLSGGQILKKIAQRAMNLSDSG-GLAFYDFD 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2113639204 319 NVTNAQQFKQLYRARLNTLELSDEAKKSIVEEANKAFQFNMNVFEELD 366
Cdd:CHL00168  161 NIEDDQEFKQIYKAALDNLPLSDDQIQNIIAEANIAFNLNMKMFQELN 208
HemeO cd19165
heme oxygenase in eukaryotes and some bacteria; This subfamily contains heme oxygenase (HO, EC ...
160-365 3.43e-83

heme oxygenase in eukaryotes and some bacteria; This subfamily contains heme oxygenase (HO, EC 1.14.14.18) found in eukaryotes as well as some proteobacteria, including cyanobacteria. Heme oxygenase (HO) catalyzes the rate limiting step in the degradation of heme to biliverdin in a multi-step reaction. HO is essential for recycling of iron from heme which is used as a substrate and cofactor for its own degradation to biliverdin, iron, and carbon monoxide. In vertebrates, HO plays a role in heme homeostasis and oxidative stress response, and cellular signaling in mammals that include isoforms HO-1, HO-2 and HO-3. HO-1 is ubiquitously expressed after induction while HO-2 expression is constitutive, mostly limited to certain organs, such as the brain, testes, and the vascular system. HO-3 is non-functional in humans, suggesting that the Hmox3 gene is a pseudogene derived from HO-2 transcripts. In higher plants and cyanobacteria, heme oxygenase is required for the synthesis of light-harvesting pigments, which contain tetrapyrrols derived from biliverdin. Candida albicans expresses a heme oxygenase that is required for the utilization of heme as a nutritional iron source, whereas Saccharomyces cerevisiae responds to iron deprivation by increasing Hmx1p transcription, which is controlled by the major iron-dependent transcription factor, Aft1p, and promotes both the re-utilization of heme iron and the regulation of heme-dependent transcription during periods of iron scarcity. In pathogenic bacteria, HO is part of a pathway for iron acquisition from host heme. In Leptospira interrogans, a pathogenic spirochete that causes leptospirosis, HO is required for iron utilization when hemoglobin is the sole iron source, thus making HO an interesting target for novel antimicrobial agents. HO shares tertiary structure similarity to methane monooxygenase (EC 1.14.13.25), ribonucleotide reductase (EC 1.17.4.1) and thiaminase II (EC 3.5.99.2), but shares little sequence homology.


Pssm-ID: 350856  Cd Length: 205  Bit Score: 254.06  E-value: 3.43e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113639204 160 DLSELLKEGTKESHEKAENTKFVKDFLKGRIKRELFKLATGALYYTYSALEEELDRNKENPAITALYFPQELHRAEALKK 239
Cdd:cd19165     1 PLSERLREATRKLHTAAERSIFAKLLLAGPLDREAYARLLVQLYFVYEALEEALDRLADDPVLAAALYDPELERSEALEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113639204 240 DVAYFYGEDWEDTIQCSEATQAYVDRIHHLGRHKPELLVAHAYTRYMGDLSGGQVLKKVAQRALHLPGtGEGIQFYLFDN 319
Cdd:cd19165    81 DLAFLLGPDWREPIPPSPATAAYVARIRELAEEKPHLLLAHAYVRYLGDLSGGQIIRRKLAKAYGLFG-GEGLSFYDFDG 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2113639204 320 VTNAQQFKQLYRARLNTLELSDEAKKSIVEEANKAFQFNMNVFEEL 365
Cdd:cd19165   160 IGDGKDLKDEYRARLDALELTEEEKDAIVEEAKLAFELNIALFEEL 205
 
Name Accession Description Interval E-value
Heme_oxygenase pfam01126
Heme oxygenase;
159-364 3.98e-97

Heme oxygenase;


Pssm-ID: 395895  Cd Length: 204  Bit Score: 289.65  E-value: 3.98e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113639204 159 TDLSELLKEGTKESHEKAENTKFVKDFLKGRIKRELFKLATGALYYTYSALEEELDRNKENPAITALYFPqELHRAEALK 238
Cdd:pfam01126   1 LNLAKRLREATKDVHVMAENLVFVKDFLKGVVDKDAYAKLLANLYFVYSALEEELERNRDSPVAAPIYFP-ELNRKAALE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113639204 239 KDVAYFYGEDWEDTIQCSEATQAYVDRIHHLGRHKPELLVAHAYTRYMGDLSGGQVLKKVAQRALHLPGtGEGIQFYLFD 318
Cdd:pfam01126  80 RDLAYLYGADWRADIQDSPATQEYVPRIREIGNESPELLVAHAYTRYLGDLSGGQLLKKIAQRALGLPP-GEGTAFYEFE 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2113639204 319 NVTNAQQFKQLYRARLNTLELSDEAKKSIVEEANKAFQFNMNVFEE 364
Cdd:pfam01126 159 GISDRKVFKQEYREALNALELDDEARARAVEEANDAFALNIQVFRE 204
COG5398 COG5398
Heme oxygenase [Coenzyme transport and metabolism];
159-366 4.22e-93

Heme oxygenase [Coenzyme transport and metabolism];


Pssm-ID: 444157  Cd Length: 211  Bit Score: 279.79  E-value: 4.22e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113639204 159 TDLSELLKEGTKESHEKAENTKFVKDFLKGRIKRELFKLATGALYYTYSALEEELDRNKENPAITALYFPqELHRAEALK 238
Cdd:COG5398     1 SPLSTALREGTAKAHTAAENSGFMKALLKGRLDRDAYVALLAQLYFVYSALEEALERHRDHPVVGPFYFP-ELNRLPALE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113639204 239 KDVAYFYGEDWEDTIQCSEATQAYVDRIHHLGRHKPELLVAHAYTRYMGDLSGGQVLKKVAQRALHLPGtGEGIQFYLFD 318
Cdd:COG5398    80 ADLAFLYGPDWRDQITPLPATRAYVARIREVAAEWPELLVAHHYTRYLGDLSGGQIIKRILQRAYGLPD-GEGTAFYEFD 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2113639204 319 NVTNAQQFKQLYRARLNTLELSDEAKKSIVEEANKAFQFNMNVFEELD 366
Cdd:COG5398   159 EIPDPKAFKDRYRAALDALPLDEAERERIVDEANLAFRLNTAVFAELE 206
pbsA CHL00168
heme oxygenase; Provisional
159-366 6.92e-91

heme oxygenase; Provisional


Pssm-ID: 214383  Cd Length: 238  Bit Score: 275.12  E-value: 6.92e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113639204 159 TDLSELLKEGTKESHEKAENTKFVKDFLKGRIKRELFKLATGALYYTYSALEEELDRNKENPAITALYFpQELHRAEALK 238
Cdd:CHL00168    3 TNLATQLREGTTKSHSMAENVSFVKSFLGGVIDKKSYRKLVANLYFVYSAIEEEIEKNKEHPLIKPIYF-QELNRKESLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113639204 239 KDVAYFYGEDWEDTIQCSEATQAYVDRIHHLGRHKPELLVAHAYTRYMGDLSGGQVLKKVAQRALHLPGTGeGIQFYLFD 318
Cdd:CHL00168   82 KDLNYYYGDDWKSIIEPSPATKIYVDRIHKISAKKPELLIAHAYTRYLGDLSGGQILKKIAQRAMNLSDSG-GLAFYDFD 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2113639204 319 NVTNAQQFKQLYRARLNTLELSDEAKKSIVEEANKAFQFNMNVFEELD 366
Cdd:CHL00168  161 NIEDDQEFKQIYKAALDNLPLSDDQIQNIIAEANIAFNLNMKMFQELN 208
HemeO cd19165
heme oxygenase in eukaryotes and some bacteria; This subfamily contains heme oxygenase (HO, EC ...
160-365 3.43e-83

heme oxygenase in eukaryotes and some bacteria; This subfamily contains heme oxygenase (HO, EC 1.14.14.18) found in eukaryotes as well as some proteobacteria, including cyanobacteria. Heme oxygenase (HO) catalyzes the rate limiting step in the degradation of heme to biliverdin in a multi-step reaction. HO is essential for recycling of iron from heme which is used as a substrate and cofactor for its own degradation to biliverdin, iron, and carbon monoxide. In vertebrates, HO plays a role in heme homeostasis and oxidative stress response, and cellular signaling in mammals that include isoforms HO-1, HO-2 and HO-3. HO-1 is ubiquitously expressed after induction while HO-2 expression is constitutive, mostly limited to certain organs, such as the brain, testes, and the vascular system. HO-3 is non-functional in humans, suggesting that the Hmox3 gene is a pseudogene derived from HO-2 transcripts. In higher plants and cyanobacteria, heme oxygenase is required for the synthesis of light-harvesting pigments, which contain tetrapyrrols derived from biliverdin. Candida albicans expresses a heme oxygenase that is required for the utilization of heme as a nutritional iron source, whereas Saccharomyces cerevisiae responds to iron deprivation by increasing Hmx1p transcription, which is controlled by the major iron-dependent transcription factor, Aft1p, and promotes both the re-utilization of heme iron and the regulation of heme-dependent transcription during periods of iron scarcity. In pathogenic bacteria, HO is part of a pathway for iron acquisition from host heme. In Leptospira interrogans, a pathogenic spirochete that causes leptospirosis, HO is required for iron utilization when hemoglobin is the sole iron source, thus making HO an interesting target for novel antimicrobial agents. HO shares tertiary structure similarity to methane monooxygenase (EC 1.14.13.25), ribonucleotide reductase (EC 1.17.4.1) and thiaminase II (EC 3.5.99.2), but shares little sequence homology.


Pssm-ID: 350856  Cd Length: 205  Bit Score: 254.06  E-value: 3.43e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113639204 160 DLSELLKEGTKESHEKAENTKFVKDFLKGRIKRELFKLATGALYYTYSALEEELDRNKENPAITALYFPQELHRAEALKK 239
Cdd:cd19165     1 PLSERLREATRKLHTAAERSIFAKLLLAGPLDREAYARLLVQLYFVYEALEEALDRLADDPVLAAALYDPELERSEALEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113639204 240 DVAYFYGEDWEDTIQCSEATQAYVDRIHHLGRHKPELLVAHAYTRYMGDLSGGQVLKKVAQRALHLPGtGEGIQFYLFDN 319
Cdd:cd19165    81 DLAFLLGPDWREPIPPSPATAAYVARIRELAEEKPHLLLAHAYVRYLGDLSGGQIIRRKLAKAYGLFG-GEGLSFYDFDG 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2113639204 320 VTNAQQFKQLYRARLNTLELSDEAKKSIVEEANKAFQFNMNVFEEL 365
Cdd:cd19165   160 IGDGKDLKDEYRARLDALELTEEEKDAIVEEAKLAFELNIALFEEL 205
HemeO-like cd00232
heme oxygenase; Heme oxygenase (HO, EC 1.14.14.18) catalyzes the rate limiting step in the ...
161-364 1.65e-56

heme oxygenase; Heme oxygenase (HO, EC 1.14.14.18) catalyzes the rate limiting step in the degradation of heme to biliverdin in a multi-step reaction. HO is essential for recycling iron from heme which is used as a substrate and cofactor for its own degradation to biliverdin, iron, and carbon monoxide. This family serves a variety of specific needs in different branches of life: in vertebrates, HO plays a role in heme homeostasis and oxidative stress response, and cellular signaling in mammals that include isoforms HO-1 and HO-2; in photosynthetic organisms including cyanobacteria, algae, and higher plants, biliverdin is used for photosynthetic pigment formation or light-sensing; and, in pathogenic bacteria, HO is part of a pathway for iron acquisition from host heme and heme products. HO shares tertiary structure similarity to methane monooxygenase (EC 1.14.13.25), ribonucleotide reductase (EC 1.17.4.1) and thiaminase II (EC 3.5.99.2), but shares little sequence homology.


Pssm-ID: 350855  Cd Length: 201  Bit Score: 185.52  E-value: 1.65e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113639204 161 LSELLKEGTKESHEKAENTKFVKDFlKGRIKRELFKLATGALYYTYSALEEELDRNKENPAITALYFPQELHRAEALKKD 240
Cdd:cd00232     1 LSKRLKKATREVHNVSESLVNSRLP-ALFVSKDNYAKFLACQYYFFVALEAAYDEALLKGDFDKDPLLEGLARADAFKQD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113639204 241 VAYFYGEDWEDTIQCSEATQAYVDRIHHLGRHKPELLVAHAYTRYMGDLSGGQVLKKVAQRALHLPGtGEGIQFYLFDNV 320
Cdd:cd00232    80 LADLGGPTWQADLGTKSQAKDYEAHLAELGRSSPALLLAHLYTQELSMLSGGQFLKKWAQKLFQLPD-DVGAAHFAYPGE 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2113639204 321 TNAqQFKQLYRARLNTLELSDEAKKSIVEEANKAFQFNMNVFEE 364
Cdd:cd00232   159 SRN-KLWSAFVKQLDELELTPELEDQAISEALAAFGHNNALLEE 201
HemeO-bac cd19166
heme oxygenase found in pathogenic bacteria; This subfamily contains bacterial heme oxygenase ...
161-357 1.09e-03

heme oxygenase found in pathogenic bacteria; This subfamily contains bacterial heme oxygenase (HO, EC 1.14.14.18), where HO is part of a pathway for iron acquisition from host heme and heme products. Most of these proteins have yet to be characterized. HO catalyzes the rate limiting step in the degradation of heme to biliverdin in a multi-step reaction. HO is essential for recycling of iron from heme which is used as a substrate and cofactor for its own degradation to biliverdin, iron, and carbon monoxide. This family includes heme oxygenase (pa-HO) from Pseudomonas aeruginosa, an opportunistic pathogen that causes a variety of systemic infections, particularly in those afflicted with cystic fibrosis, as well as cancer and AIDS patients who are immunosuppressed. Pa-HO, expressed by the PigA gene, is critical for the acquisition of host iron since there is essentially no free iron in mammals, and is unusual since it hydroxylates heme predominantly at the delta-meso heme carbon, while all other well-studied HOs hydroxylate the alpha-meso carbon. Also included in this family is Neisseria meningitidis HO which is substantially different from the human HO, with the reaction product being ferric biliverdin IXalpha rather than reduced iron and free biliverdin IXalpha. HO shares tertiary structure similarity to methane monooxygenase (EC 1.14.13.25), ribonucleotide reductase (EC 1.17.4.1) and thiaminase II (EC 3.5.99.2), but shares little sequence homology.


Pssm-ID: 350857 [Multi-domain]  Cd Length: 182  Bit Score: 39.92  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113639204 161 LSELLKEGTKESHEKAENTKFVKDFLkgrIKRELFKLATGALYYTYSALEEELDRNKENPAITALyfpQELHRAEALKKD 240
Cdd:cd19166     1 LRARLRAATRAAHERLEALLGLLDLF---LTLADYARFLAAQYGFYAPLEAALAAALLAALLPDL---AARRRLPLLAAD 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113639204 241 vayfygedwedtiqcseatqayvdrIHHLGRHKPELLVAHAYTryMGDLS--------------GGQVLKKVAQRALHLP 306
Cdd:cd19166    75 -------------------------LAALGLAPPAPAAAPLPA--LPSLAaalgalyvlegstlGGRVIARRLAKLLGLA 127
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2113639204 307 GtgEGIQFYLFDNVTNAQQFKQLyRARLNTLELSDEAKKSIVEEANKAFQF 357
Cdd:cd19166   128 D--FGARFLAGYGEGTGARWRAF-LAALEAAALTPADEDAAVAGARATFAL 175
 
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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