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Conserved domains on  [gi|1700447656|ref|NP_001358263|]
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prostaglandin reductase 2 isoform 5 [Homo sapiens]

Protein Classification

MDR/zinc-dependent alcohol dehydrogenase-like family protein( domain architecture ID 94789)

medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family protein may catalyze the reversible NAD(P)(H)-dependent conversion of an alcohol to its corresponding aldehyde

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MDR super family cl16912
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1-117 2.33e-79

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


The actual alignment was detected with superfamily member cd08293:

Pssm-ID: 450120 [Multi-domain]  Cd Length: 345  Bit Score: 236.90  E-value: 2.33e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447656   1 MIVQRVVLNSRPGKNGNPVAENFRMEEVYLPDNINEGQVQVRTLYLSVDPYMRCRMNEDTGTDYITPWQLSQVVDGGGIG 80
Cdd:cd08293     1 MINKRVVLNSRPGKNGNPVAENFRVEECTLPDELNEGQVLVRTLYLSVDPYMRCRMNEDTGTDYLAPWQLSQVLDGGGVG 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1700447656  81 IIEESKHTNLTKGDFVTSFYWPWQTKVILDGNSLEKV 117
Cdd:cd08293    81 VVEESKHQKFAVGDIVTSFNWPWQTYAVLDGSSLEKV 117
 
Name Accession Description Interval E-value
PTGR2 cd08293
Prostaglandin reductase; Prostaglandins and related eicosanoids are metabolized by the ...
 1-117 2.33e-79

Prostaglandin reductase; Prostaglandins and related eicosanoids are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto-13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. These 15-PGDH and related enzymes are members of the medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176253 [Multi-domain]  Cd Length: 345  Bit Score: 236.90  E-value: 2.33e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447656   1 MIVQRVVLNSRPGKNGNPVAENFRMEEVYLPDNINEGQVQVRTLYLSVDPYMRCRMNEDTGTDYITPWQLSQVVDGGGIG 80
Cdd:cd08293     1 MINKRVVLNSRPGKNGNPVAENFRVEECTLPDELNEGQVLVRTLYLSVDPYMRCRMNEDTGTDYLAPWQLSQVLDGGGVG 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1700447656  81 IIEESKHTNLTKGDFVTSFYWPWQTKVILDGNSLEKV 117
Cdd:cd08293    81 VVEESKHQKFAVGDIVTSFNWPWQTYAVLDGSSLEKV 117
CurA COG2130
NADPH-dependent curcumin reductase CurA [Secondary metabolites biosynthesis, transport and ...
 1-117 6.77e-41

NADPH-dependent curcumin reductase CurA [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 441733 [Multi-domain]  Cd Length: 333  Bit Score: 137.88  E-value: 6.77e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447656   1 MIVQRVVLNSRPgkNGNPVAENFRMEEVYLPDnINEGQVQVRTLYLSVDPYMRCRMNEdtGTDYITPWQLSQVVDGGGIG 80
Cdd:COG2130     3 TTNRQIVLASRP--EGEPTPEDFRLEEVPVPE-PGDGEVLVRNLYLSVDPYMRGRMSD--AKSYAPPVELGEVMRGGAVG 77

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1700447656  81 IIEESKHTNLTKGDFVTSFyWPWQTKVILDGNSLEKV 117
Cdd:COG2130    78 EVVESRHPDFAVGDLVLGM-LGWQDYAVSDGAGLRKV 113
ADH_N_2 pfam16884
N-terminal domain of oxidoreductase; N-terminal region of oxidoreductase and prostaglandin ...
 5-117 7.81e-36

N-terminal domain of oxidoreductase; N-terminal region of oxidoreductase and prostaglandin reductase and alcohol dehydrogenase.


Pssm-ID: 465297 [Multi-domain]  Cd Length: 108  Bit Score: 118.46  E-value: 7.81e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447656   5 RVVLNSRPgkNGNPVAENFRMEEVYLPDnINEGQVQVRTLYLSVDPYMRCRMNEDTGtdYITPWQLSQVVDGGGIGIIEE 84
Cdd:pfam16884   2 QWLLAKRP--EGVPTPSDFELVEAELPE-LGDGEVLVRTLYLSVDPYMRGRMNDAKS--YVPPVELGDVMRGGAVGEVVE 76

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1700447656  85 SKHTNLTKGDFVTSFyWPWQTKVILDGNSLEKV 117
Cdd:pfam16884  77 SNNPDFPVGDLVLGM-LGWQDYAVSDGKGLTKV 108
B4_12hDH TIGR02825
leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase; Leukotriene B4 ...
 16-118 1.06e-10

leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase; Leukotriene B4 12-hydroxydehydrogenase is an NADP-dependent enzyme of arachidonic acid metabolism, responsible for converting leukotriene B4 to the much less active metabolite 12-oxo-leukotriene B4. The BRENDA database lists leukotriene B4 12-hydroxydehydrogenase as one of the synonyms of 2-alkenal reductase (EC 1.3.1.74), while 1.3.1.48 is 15-oxoprostaglandin 13-reductase.


Pssm-ID: 131872 [Multi-domain]  Cd Length: 325  Bit Score: 56.93  E-value: 1.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447656  16 GNPVAENFRMEEVYLPDnINEGQVQVRTLYLSVDPYMRCRMNEDTGTDYITPWQLSQVVdgggigiieESKHTNLTKGDF 95
Cdd:TIGR02825  12 GYPTDSDFELKTVELPP-LNNGEVLLEALFLSVDPYMRVAAKRLKEGDTMMGQQVARVV---------ESKNVALPKGTI 81

                          90       100
                  ....*....|....*....|...
gi 1700447656  96 VTSfYWPWQTKVILDGNSLEKVI 118
Cdd:TIGR02825  82 VLA-SPGWTSHSISDGKDLEKLL 103
PLN03154 PLN03154
putative allyl alcohol dehydrogenase; Provisional
 41-99 9.22e-09

putative allyl alcohol dehydrogenase; Provisional


Pssm-ID: 215606 [Multi-domain]  Cd Length: 348  Bit Score: 51.77  E-value: 9.22e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1700447656  41 VRTLYLSVDPYMRCRMNEDTGTdYITPWQLSQVVDGGGIGIIEESKHTNLTKGDFVTSF 99
Cdd:PLN03154   48 VKNLYLSCDPYMRGRMRDFHDS-YLPPFVPGQRIEGFGVSKVVDSDDPNFKPGDLISGI 105
 
Name Accession Description Interval E-value
PTGR2 cd08293
Prostaglandin reductase; Prostaglandins and related eicosanoids are metabolized by the ...
 1-117 2.33e-79

Prostaglandin reductase; Prostaglandins and related eicosanoids are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto-13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. These 15-PGDH and related enzymes are members of the medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176253 [Multi-domain]  Cd Length: 345  Bit Score: 236.90  E-value: 2.33e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447656   1 MIVQRVVLNSRPGKNGNPVAENFRMEEVYLPDNINEGQVQVRTLYLSVDPYMRCRMNEDTGTDYITPWQLSQVVDGGGIG 80
Cdd:cd08293     1 MINKRVVLNSRPGKNGNPVAENFRVEECTLPDELNEGQVLVRTLYLSVDPYMRCRMNEDTGTDYLAPWQLSQVLDGGGVG 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1700447656  81 IIEESKHTNLTKGDFVTSFYWPWQTKVILDGNSLEKV 117
Cdd:cd08293    81 VVEESKHQKFAVGDIVTSFNWPWQTYAVLDGSSLEKV 117
CurA COG2130
NADPH-dependent curcumin reductase CurA [Secondary metabolites biosynthesis, transport and ...
 1-117 6.77e-41

NADPH-dependent curcumin reductase CurA [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 441733 [Multi-domain]  Cd Length: 333  Bit Score: 137.88  E-value: 6.77e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447656   1 MIVQRVVLNSRPgkNGNPVAENFRMEEVYLPDnINEGQVQVRTLYLSVDPYMRCRMNEdtGTDYITPWQLSQVVDGGGIG 80
Cdd:COG2130     3 TTNRQIVLASRP--EGEPTPEDFRLEEVPVPE-PGDGEVLVRNLYLSVDPYMRGRMSD--AKSYAPPVELGEVMRGGAVG 77

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1700447656  81 IIEESKHTNLTKGDFVTSFyWPWQTKVILDGNSLEKV 117
Cdd:COG2130    78 EVVESRHPDFAVGDLVLGM-LGWQDYAVSDGAGLRKV 113
PGDH cd05288
Prostaglandin dehydrogenases; Prostaglandins and related eicosanoids are metabolized by the ...
 4-117 2.72e-37

Prostaglandin dehydrogenases; Prostaglandins and related eicosanoids are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto-13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. These 15-PGDH and related enzymes are members of the medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176190 [Multi-domain]  Cd Length: 329  Bit Score: 128.37  E-value: 2.72e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447656   4 QRVVLNSRPGknGNPVAENFRMEEVYLPDnINEGQVQVRTLYLSVDPYMRCRMNEdtGTDYITPWQLSQVVDGGGIGIIE 83
Cdd:cd05288     3 RQVVLAKRPE--GPPPPDDFELVEVPLPE-LKDGEVLVRTLYLSVDPYMRGWMSD--AKSYSPPVQLGEPMRGGGVGEVV 77

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1700447656  84 ESKHTNLTKGDFVTSFyWPWQTKVILDGNS-LEKV 117
Cdd:cd05288    78 ESRSPDFKVGDLVSGF-LGWQEYAVVDGASgLRKL 111
ADH_N_2 pfam16884
N-terminal domain of oxidoreductase; N-terminal region of oxidoreductase and prostaglandin ...
 5-117 7.81e-36

N-terminal domain of oxidoreductase; N-terminal region of oxidoreductase and prostaglandin reductase and alcohol dehydrogenase.


Pssm-ID: 465297 [Multi-domain]  Cd Length: 108  Bit Score: 118.46  E-value: 7.81e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447656   5 RVVLNSRPgkNGNPVAENFRMEEVYLPDnINEGQVQVRTLYLSVDPYMRCRMNEDTGtdYITPWQLSQVVDGGGIGIIEE 84
Cdd:pfam16884   2 QWLLAKRP--EGVPTPSDFELVEAELPE-LGDGEVLVRTLYLSVDPYMRGRMNDAKS--YVPPVELGDVMRGGAVGEVVE 76

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1700447656  85 SKHTNLTKGDFVTSFyWPWQTKVILDGNSLEKV 117
Cdd:pfam16884  77 SNNPDFPVGDLVLGM-LGWQDYAVSDGKGLTKV 108
double_bond_reductase_like cd08295
Arabidopsis alkenal double bond reductase and leukotriene B4 12-hydroxydehydrogenase; This ...
 15-117 2.04e-16

Arabidopsis alkenal double bond reductase and leukotriene B4 12-hydroxydehydrogenase; This group includes proteins identified as the Arabidopsis alkenal double bond reductase and leukotriene B4 12-hydroxydehydrogenase. The Arabidopsis enzyme, a member of the medium chain dehydrogenase/reductase family, catalyzes the reduction of 7-8-double bond of phenylpropanal substrates as a plant defense mechanism. Prostaglandins and related eicosanoids (lipid mediators involved in host defense and inflamation) are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto-13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. Leukotriene B4 (LTB4) can be metabolized by LTB4 20-hydroxylase in inflamatory cells, and in other cells by bifunctional LTB4 12-HD/PGR. These 15-PGDH and related enzymes are members of the medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of an beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176255 [Multi-domain]  Cd Length: 338  Bit Score: 73.12  E-value: 2.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447656  15 NGNPVAENFRMEEVYLP---DNINEGQVQVRTLYLSVDPYMRCRMNEDTGTDYITPWQLSQVVDGGGIGIIEESKHTNLT 91
Cdd:cd08295    13 TGFPKESDLELRTTKLTlkvPPGGSGDVLVKNLYLSCDPYMRGRMKGHDDSLYLPPFKPGEVITGYGVAKVVDSGNPDFK 92

                          90       100
                  ....*....|....*....|....*..
gi 1700447656  92 KGDFVTSFYwPWQTKVILD-GNSLEKV 117
Cdd:cd08295    93 VGDLVWGFT-GWEEYSLIPrGQDLRKI 118
B4_12hDH TIGR02825
leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase; Leukotriene B4 ...
 16-118 1.06e-10

leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase; Leukotriene B4 12-hydroxydehydrogenase is an NADP-dependent enzyme of arachidonic acid metabolism, responsible for converting leukotriene B4 to the much less active metabolite 12-oxo-leukotriene B4. The BRENDA database lists leukotriene B4 12-hydroxydehydrogenase as one of the synonyms of 2-alkenal reductase (EC 1.3.1.74), while 1.3.1.48 is 15-oxoprostaglandin 13-reductase.


Pssm-ID: 131872 [Multi-domain]  Cd Length: 325  Bit Score: 56.93  E-value: 1.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447656  16 GNPVAENFRMEEVYLPDnINEGQVQVRTLYLSVDPYMRCRMNEDTGTDYITPWQLSQVVdgggigiieESKHTNLTKGDF 95
Cdd:TIGR02825  12 GYPTDSDFELKTVELPP-LNNGEVLLEALFLSVDPYMRVAAKRLKEGDTMMGQQVARVV---------ESKNVALPKGTI 81

                          90       100
                  ....*....|....*....|...
gi 1700447656  96 VTSfYWPWQTKVILDGNSLEKVI 118
Cdd:TIGR02825  82 VLA-SPGWTSHSISDGKDLEKLL 103
leukotriene_B4_DH_like cd08294
13-PGR is a bifunctional enzyme with delta-13 15-prostaglandin reductase and leukotriene B4 12 ...
 15-111 1.12e-10

13-PGR is a bifunctional enzyme with delta-13 15-prostaglandin reductase and leukotriene B4 12 hydroxydehydrogenase activity; Prostaglandins and related eicosanoids are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto- 13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. These 15-PGDH and related enzymes are members of the medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176254 [Multi-domain]  Cd Length: 329  Bit Score: 56.89  E-value: 1.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447656  15 NGNPVAENFRMEEVYLPdNINEGQVQVRTLYLSVDPYMRCrmnedtgtdYITPWQLSQVVDGGGIGIIEESKHTNLTKGD 94
Cdd:cd08294    13 DGKPKESDFELVEEELP-PLKDGEVLCEALFLSVDPYMRP---------YSKRLNEGDTMIGTQVAKVIESKNSKFPVGT 82

                          90
                  ....*....|....*..
gi 1700447656  95 FVTSFYwPWQTKVILDG 111
Cdd:cd08294    83 IVVASF-GWRTHTVSDG 98
PLN03154 PLN03154
putative allyl alcohol dehydrogenase; Provisional
 41-99 9.22e-09

putative allyl alcohol dehydrogenase; Provisional


Pssm-ID: 215606 [Multi-domain]  Cd Length: 348  Bit Score: 51.77  E-value: 9.22e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1700447656  41 VRTLYLSVDPYMRCRMNEDTGTdYITPWQLSQVVDGGGIGIIEESKHTNLTKGDFVTSF 99
Cdd:PLN03154   48 VKNLYLSCDPYMRGRMRDFHDS-YLPPFVPGQRIEGFGVSKVVDSDDPNFKPGDLISGI 105
 
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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