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Conserved domains on  [gi|704266018|ref|XP_010152547|]
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PREDICTED: heme oxygenase 2-like, partial [Eurypyga helias]

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

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List of domain hits

 Name Accession Description Interval E-value
Heme_oxygenase pfam01126
Heme oxygenase;
30-231 3.88e-97

Heme oxygenase;


:

Pssm-ID: 395895  Cd Length: 204  Bit Score: 281.94  E-value: 3.88e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704266018   30 TDLSELLKEGTKESHDRAENTQFVKDFLKGRIKKELFKLATVALYFTYSALEEEMDCNKDSPVFAPLYFPlELHRKEALA 109
Cdd:pfam01126   1 LNLAKRLREATKDVHVMAENLVFVKDFLKGVVDKDAYAKLLANLYFVYSALEEELERNRDSPVAAPIYFP-ELNRKAALE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704266018  110 KDLKYFYGEDWKEKVQCSEATQHYVDRIHHVGQHEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPStEEGIQFYVFD 189
Cdd:pfam01126  80 RDLAYLYGADWRADIQDSPATQEYVPRIREIGNESPELLVAHAYTRYLGDLSGGQLLKKIAQRALGLPP-GEGTAFYEFE 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 704266018  190 NVSNAQQFKQLYRARMNALDLDKDTKERIVEEANRAFRFNMQ 231
Cdd:pfam01126 159 GISDRKVFKQEYREALNALELDDEARARAVEEANDAFALNIQ 200
 
Name Accession Description Interval E-value
Heme_oxygenase pfam01126
Heme oxygenase;
30-231 3.88e-97

Heme oxygenase;


Pssm-ID: 395895  Cd Length: 204  Bit Score: 281.94  E-value: 3.88e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704266018   30 TDLSELLKEGTKESHDRAENTQFVKDFLKGRIKKELFKLATVALYFTYSALEEEMDCNKDSPVFAPLYFPlELHRKEALA 109
Cdd:pfam01126   1 LNLAKRLREATKDVHVMAENLVFVKDFLKGVVDKDAYAKLLANLYFVYSALEEELERNRDSPVAAPIYFP-ELNRKAALE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704266018  110 KDLKYFYGEDWKEKVQCSEATQHYVDRIHHVGQHEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPStEEGIQFYVFD 189
Cdd:pfam01126  80 RDLAYLYGADWRADIQDSPATQEYVPRIREIGNESPELLVAHAYTRYLGDLSGGQLLKKIAQRALGLPP-GEGTAFYEFE 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 704266018  190 NVSNAQQFKQLYRARMNALDLDKDTKERIVEEANRAFRFNMQ 231
Cdd:pfam01126 159 GISDRKVFKQEYREALNALELDDEARARAVEEANDAFALNIQ 200
COG5398 COG5398
Heme oxygenase [Coenzyme transport and metabolism];
30-231 6.37e-97

Heme oxygenase [Coenzyme transport and metabolism];


Pssm-ID: 444157  Cd Length: 211  Bit Score: 281.33  E-value: 6.37e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704266018  30 TDLSELLKEGTKESHDRAENTQFVKDFLKGRIKKELFKLATVALYFTYSALEEEMDCNKDSPVFAPLYFPlELHRKEALA 109
Cdd:COG5398    1 SPLSTALREGTAKAHTAAENSGFMKALLKGRLDRDAYVALLAQLYFVYSALEEALERHRDHPVVGPFYFP-ELNRLPALE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704266018 110 KDLKYFYGEDWKEKVQCSEATQHYVDRIHHVGQHEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPsTEEGIQFYVFD 189
Cdd:COG5398   80 ADLAFLYGPDWRDQITPLPATRAYVARIREVAAEWPELLVAHHYTRYLGDLSGGQIIKRILQRAYGLP-DGEGTAFYEFD 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 704266018 190 NVSNAQQFKQLYRARMNALDLDKDTKERIVEEANRAFRFNMQ 231
Cdd:COG5398  159 EIPDPKAFKDRYRAALDALPLDEAERERIVDEANLAFRLNTA 200
pbsA CHL00168
heme oxygenase; Provisional
 30-231 1.66e-84

heme oxygenase; Provisional


Pssm-ID: 214383  Cd Length: 238  Bit Score: 250.86  E-value: 1.66e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704266018  30 TDLSELLKEGTKESHDRAENTQFVKDFLKGRIKKELFKLATVALYFTYSALEEEMDCNKDSPVFAPLYFPlELHRKEALA 109
Cdd:CHL00168   3 TNLATQLREGTTKSHSMAENVSFVKSFLGGVIDKKSYRKLVANLYFVYSAIEEEIEKNKEHPLIKPIYFQ-ELNRKESLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704266018 110 KDLKYFYGEDWKEKVQCSEATQHYVDRIHHVGQHEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPStEEGIQFYVFD 189
Cdd:CHL00168  82 KDLNYYYGDDWKSIIEPSPATKIYVDRIHKISAKKPELLIAHAYTRYLGDLSGGQILKKIAQRAMNLSD-SGGLAFYDFD 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 704266018 190 NVSNAQQFKQLYRARMNALDLDKDTKERIVEEANRAFRFNMQ 231
Cdd:CHL00168 161 NIEDDQEFKQIYKAALDNLPLSDDQIQNIIAEANIAFNLNMK 202
HemeO cd19165
heme oxygenase in eukaryotes and some bacteria; This subfamily contains heme oxygenase (HO, EC ...
 31-231 3.97e-80

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: 238.65  E-value: 3.97e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704266018  31 DLSELLKEGTKESHDRAENTQFVKDFLKGRIKKELFKLATVALYFTYSALEEEMDCNKDSPVFAPLYFPLELHRKEALAK 110
Cdd:cd19165    1 PLSERLREATRKLHTAAERSIFAKLLLAGPLDREAYARLLVQLYFVYEALEEALDRLADDPVLAAALYDPELERSEALEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704266018 111 DLKYFYGEDWKEKVQCSEATQHYVDRIHHVGQHEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPStEEGIQFYVFDN 190
Cdd:cd19165   81 DLAFLLGPDWREPIPPSPATAAYVARIRELAEEKPHLLLAHAYVRYLGDLSGGQIIRRKLAKAYGLFG-GEGLSFYDFDG 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 704266018 191 VSNAQQFKQLYRARMNALDLDKDTKERIVEEANRAFRFNMQ 231
Cdd:cd19165  160 IGDGKDLKDEYRARLDALELTEEEKDAIVEEAKLAFELNIA 200
 
Name Accession Description Interval E-value
Heme_oxygenase pfam01126
Heme oxygenase;
30-231 3.88e-97

Heme oxygenase;


Pssm-ID: 395895  Cd Length: 204  Bit Score: 281.94  E-value: 3.88e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704266018   30 TDLSELLKEGTKESHDRAENTQFVKDFLKGRIKKELFKLATVALYFTYSALEEEMDCNKDSPVFAPLYFPlELHRKEALA 109
Cdd:pfam01126   1 LNLAKRLREATKDVHVMAENLVFVKDFLKGVVDKDAYAKLLANLYFVYSALEEELERNRDSPVAAPIYFP-ELNRKAALE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704266018  110 KDLKYFYGEDWKEKVQCSEATQHYVDRIHHVGQHEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPStEEGIQFYVFD 189
Cdd:pfam01126  80 RDLAYLYGADWRADIQDSPATQEYVPRIREIGNESPELLVAHAYTRYLGDLSGGQLLKKIAQRALGLPP-GEGTAFYEFE 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 704266018  190 NVSNAQQFKQLYRARMNALDLDKDTKERIVEEANRAFRFNMQ 231
Cdd:pfam01126 159 GISDRKVFKQEYREALNALELDDEARARAVEEANDAFALNIQ 200
COG5398 COG5398
Heme oxygenase [Coenzyme transport and metabolism];
30-231 6.37e-97

Heme oxygenase [Coenzyme transport and metabolism];


Pssm-ID: 444157  Cd Length: 211  Bit Score: 281.33  E-value: 6.37e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704266018  30 TDLSELLKEGTKESHDRAENTQFVKDFLKGRIKKELFKLATVALYFTYSALEEEMDCNKDSPVFAPLYFPlELHRKEALA 109
Cdd:COG5398    1 SPLSTALREGTAKAHTAAENSGFMKALLKGRLDRDAYVALLAQLYFVYSALEEALERHRDHPVVGPFYFP-ELNRLPALE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704266018 110 KDLKYFYGEDWKEKVQCSEATQHYVDRIHHVGQHEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPsTEEGIQFYVFD 189
Cdd:COG5398   80 ADLAFLYGPDWRDQITPLPATRAYVARIREVAAEWPELLVAHHYTRYLGDLSGGQIIKRILQRAYGLP-DGEGTAFYEFD 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 704266018 190 NVSNAQQFKQLYRARMNALDLDKDTKERIVEEANRAFRFNMQ 231
Cdd:COG5398  159 EIPDPKAFKDRYRAALDALPLDEAERERIVDEANLAFRLNTA 200
pbsA CHL00168
heme oxygenase; Provisional
 30-231 1.66e-84

heme oxygenase; Provisional


Pssm-ID: 214383  Cd Length: 238  Bit Score: 250.86  E-value: 1.66e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704266018  30 TDLSELLKEGTKESHDRAENTQFVKDFLKGRIKKELFKLATVALYFTYSALEEEMDCNKDSPVFAPLYFPlELHRKEALA 109
Cdd:CHL00168   3 TNLATQLREGTTKSHSMAENVSFVKSFLGGVIDKKSYRKLVANLYFVYSAIEEEIEKNKEHPLIKPIYFQ-ELNRKESLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704266018 110 KDLKYFYGEDWKEKVQCSEATQHYVDRIHHVGQHEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPStEEGIQFYVFD 189
Cdd:CHL00168  82 KDLNYYYGDDWKSIIEPSPATKIYVDRIHKISAKKPELLIAHAYTRYLGDLSGGQILKKIAQRAMNLSD-SGGLAFYDFD 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 704266018 190 NVSNAQQFKQLYRARMNALDLDKDTKERIVEEANRAFRFNMQ 231
Cdd:CHL00168 161 NIEDDQEFKQIYKAALDNLPLSDDQIQNIIAEANIAFNLNMK 202
HemeO cd19165
heme oxygenase in eukaryotes and some bacteria; This subfamily contains heme oxygenase (HO, EC ...
 31-231 3.97e-80

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: 238.65  E-value: 3.97e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704266018  31 DLSELLKEGTKESHDRAENTQFVKDFLKGRIKKELFKLATVALYFTYSALEEEMDCNKDSPVFAPLYFPLELHRKEALAK 110
Cdd:cd19165    1 PLSERLREATRKLHTAAERSIFAKLLLAGPLDREAYARLLVQLYFVYEALEEALDRLADDPVLAAALYDPELERSEALEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704266018 111 DLKYFYGEDWKEKVQCSEATQHYVDRIHHVGQHEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPStEEGIQFYVFDN 190
Cdd:cd19165   81 DLAFLLGPDWREPIPPSPATAAYVARIRELAEEKPHLLLAHAYVRYLGDLSGGQIIRRKLAKAYGLFG-GEGLSFYDFDG 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 704266018 191 VSNAQQFKQLYRARMNALDLDKDTKERIVEEANRAFRFNMQ 231
Cdd:cd19165  160 IGDGKDLKDEYRARLDALELTEEEKDAIVEEAKLAFELNIA 200
HemeO-like cd00232
heme oxygenase; Heme oxygenase (HO, EC 1.14.14.18) catalyzes the rate limiting step in the ...
 32-231 1.33e-52

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: 168.57  E-value: 1.33e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704266018  32 LSELLKEGTKESHDRAENTQFVKDFlKGRIKKELFKLATVALYFTYSALEEEMDCNKDSPVFAPLYFPLELHRKEALAKD 111
Cdd:cd00232    1 LSKRLKKATREVHNVSESLVNSRLP-ALFVSKDNYAKFLACQYYFFVALEAAYDEALLKGDFDKDPLLEGLARADAFKQD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704266018 112 LKYFYGEDWKEKVQCSEATQHYVDRIHHVGQHEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPStEEGIQFYVFDNV 191
Cdd:cd00232   80 LADLGGPTWQADLGTKSQAKDYEAHLAELGRSSPALLLAHLYTQELSMLSGGQFLKKWAQKLFQLPD-DVGAAHFAYPGE 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 704266018 192 SNAqQFKQLYRARMNALDLDKDTKERIVEEANRAFRFNMQ 231
Cdd:cd00232  159 SRN-KLWSAFVKQLDELELTPELEDQAISEALAAFGHNNA 197
HemeO-bac cd19166
heme oxygenase found in pathogenic bacteria; This subfamily contains bacterial heme oxygenase ...
 32-228 2.20e-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: 37.61  E-value: 2.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704266018  32 LSELLKEGTKESHDRAENTQFVKDFLKGRikkELFKLATVALYFTYSALEEEMDcnkdSPVFAPLYFPLELHRK-EALAK 110
Cdd:cd19166    1 LRARLRAATRAAHERLEALLGLLDLFLTL---ADYARFLAAQYGFYAPLEAALA----AALLAALLPDLAARRRlPLLAA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704266018 111 DLKYFygedwkeKVQCSEATQHYVDRIHHVGQhepelLVAHAYTrymgdL--S--GGQVLKKVAQRALKLPstEEGIQFY 186
Cdd:cd19166   74 DLAAL-------GLAPPAPAAAPLPALPSLAA-----ALGALYV-----LegStlGGRVIARRLAKLLGLA--DFGARFL 134

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 704266018 187 VFDNVSNAQQFKQLyRARMNALDLDKDTKERIVEEANRAFRF 228
Cdd:cd19166  135 AGYGEGTGARWRAF-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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