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Conserved domains on  [gi|17137186|ref|NP_477154|]
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cytochrome b5-related, isoform A [Drosophila melanogaster]

Protein Classification

cytochrome b5-like heme/steroid binding domain-containing protein; FMN-dependent alpha-hydroxy acid dehydrogenase( domain architecture ID 11989345)

cytochrome b5-like heme/steroid binding domain-containing protein such as cytochrome b5, a membrane-bound hemoprotein that functions as an electron carrier for several membrane-bound oxygenases and Arabidopsis thaliana steroid-binding proteins| FMN-dependent alpha-hydroxy acid dehydrogenase containing a cytochrome b5-like heme/steroid binding domain, similar to Saccharomyces cerevisiae L-lactate dehydrogenase (cytochrome) that catalyzes the oxidation of (S)-lactate (L-lactate) to pyruvate with subsequent transfer of electrons to cytochrome c

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
 34-100 1.89e-16

Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from a diverse range of proteins. This family also includes proteins that bind to steroids. The family includes progesterone receptors. Many members of this subfamily are membrane anchored by an N-terminal transmembrane alpha helix. This family also includes a domain in some chitin synthases. There is no known ligand for this domain in the chitin synthases.


:

Pssm-ID: 459698 [Multi-domain]  Cd Length: 74  Bit Score: 73.81  E-value: 1.89e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17137186    34 RQDDGAEGLWRINDG-IYDFTSFIDKHPGGPFWIRETKGTDITEAFEA-HHLTTAPEKMIAKYKVRDAA 100
Cdd:pfam00173   6 SKHNGDGDCWVAINGkVYDVTKFLKEHPGGEDVILSAAGKDATDAFEAiGHSEDAAEKLLKKYRIGELA 74
DesA super family cl34570
Fatty acid desaturase [Lipid transport and metabolism];
106-424 3.01e-12

Fatty acid desaturase [Lipid transport and metabolism];


The actual alignment was detected with superfamily member COG3239:

Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 67.06  E-value: 3.01e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137186 106 TLTLEEGGFYKTLKERVREQLKTIDKRpkkksDLIHLGLVVSLYLLGIASAKYN--SLLALVLASVALCWTVIVSHNYFH 183
Cdd:COG3239   6 PLTPADEAELRALRARLRALLGRRDWR-----YLLKLALTLALLAALWLLLSWSwlALLAALLLGLALAGLFSLGHDAGH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137186 184 ------RRDN-WQMYAFNLGM-MNFAAWRVSHaLSHHIYPNS-YFDLELsmfepllcwVPNPHIKSKLMRYVSWVTEPVA 254
Cdd:COG3239  81 gslfrsRWLNdLLGRLLGLPLgTPYDAWRRSH-NRHHAYTNDpGKDPDI---------GYGVQAWRPLYLFQHLLRFFLL 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137186 255 YALAFFIQMGTRIFYSLRHTNILYWH-DLLPLTIPIAIYLGTGGSLGIWICVRQWLAMTSIASFSFCLIglNAAHHDPEI 333
Cdd:COG3239 151 GLGGLYWLLALDFLPLRGRLELKERRlEALLLLLFLAALLALLLALGWWAVLLFWLLPLLVAGLLLGLR--FYLEHRGED 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137186 334 YHEGDANRedrdwglfQVDTIIDRGDLKWSQFLVLtHFGDHVLHHLFPTLDHGLLPALYPVLYQTLDEFKGHLRECNhIE 413
Cdd:COG3239 229 TGDGEYRD--------QLLGSRNIRGGRLLRWLFG-NLNYHIEHHLFPSIPWYRLPEAHRILKELCPEYGLPYTEGS-LL 298

                       330
                ....*....|.
gi 17137186 414 HMIGQHKQLLR 424
Cdd:COG3239 299 RSYREVLRLLR 309
 
Name Accession Description Interval E-value
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
 34-100 1.89e-16

Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from a diverse range of proteins. This family also includes proteins that bind to steroids. The family includes progesterone receptors. Many members of this subfamily are membrane anchored by an N-terminal transmembrane alpha helix. This family also includes a domain in some chitin synthases. There is no known ligand for this domain in the chitin synthases.


Pssm-ID: 459698 [Multi-domain]  Cd Length: 74  Bit Score: 73.81  E-value: 1.89e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17137186    34 RQDDGAEGLWRINDG-IYDFTSFIDKHPGGPFWIRETKGTDITEAFEA-HHLTTAPEKMIAKYKVRDAA 100
Cdd:pfam00173   6 SKHNGDGDCWVAINGkVYDVTKFLKEHPGGEDVILSAAGKDATDAFEAiGHSEDAAEKLLKKYRIGELA 74
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
106-424 3.01e-12

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 67.06  E-value: 3.01e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137186 106 TLTLEEGGFYKTLKERVREQLKTIDKRpkkksDLIHLGLVVSLYLLGIASAKYN--SLLALVLASVALCWTVIVSHNYFH 183
Cdd:COG3239   6 PLTPADEAELRALRARLRALLGRRDWR-----YLLKLALTLALLAALWLLLSWSwlALLAALLLGLALAGLFSLGHDAGH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137186 184 ------RRDN-WQMYAFNLGM-MNFAAWRVSHaLSHHIYPNS-YFDLELsmfepllcwVPNPHIKSKLMRYVSWVTEPVA 254
Cdd:COG3239  81 gslfrsRWLNdLLGRLLGLPLgTPYDAWRRSH-NRHHAYTNDpGKDPDI---------GYGVQAWRPLYLFQHLLRFFLL 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137186 255 YALAFFIQMGTRIFYSLRHTNILYWH-DLLPLTIPIAIYLGTGGSLGIWICVRQWLAMTSIASFSFCLIglNAAHHDPEI 333
Cdd:COG3239 151 GLGGLYWLLALDFLPLRGRLELKERRlEALLLLLFLAALLALLLALGWWAVLLFWLLPLLVAGLLLGLR--FYLEHRGED 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137186 334 YHEGDANRedrdwglfQVDTIIDRGDLKWSQFLVLtHFGDHVLHHLFPTLDHGLLPALYPVLYQTLDEFKGHLRECNhIE 413
Cdd:COG3239 229 TGDGEYRD--------QLLGSRNIRGGRLLRWLFG-NLNYHIEHHLFPSIPWYRLPEAHRILKELCPEYGLPYTEGS-LL 298

                       330
                ....*....|.
gi 17137186 414 HMIGQHKQLLR 424
Cdd:COG3239 299 RSYREVLRLLR 309
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 161-408 2.82e-10

Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a double bond at the delta position of fatty acids. There seem to be two distinct families of fatty acid desaturases which do not seem to be evolutionary related: Family 1 composed of Stearoyl-CoA desaturases (SCD) and Family 2 composed of Bacterial fatty acid desaturases, Plant stearoyl-acyl-carrier-protein desaturase and Cyanobacterial DesA. Members of this entry are ER integral membrane proteins that share the same mushroom-shaped fold consisting of four transmembrane helices (TM1-TM4) which anchor them to the membrane, capped by a cytosolic domain containing a unique 9-10 histidine- coordinating di metal (di-iron) catalytic centre. The structure of mouse stearoyl-CoA desaturase (SDC) revealed that TM2 and TM4 are longer than TM1 and TM3 and protrude into the cytosolic domain, providing three of the nine histidine residues that coordinate the two metal ions, while the other histidine residues are provided by the soluble domain in this enzyme.


Pssm-ID: 425713 [Multi-domain]  Cd Length: 252  Bit Score: 60.44  E-value: 2.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137186   161 LLALVLASVALCWTVIVSHNYFHR------------RDNWQMYAFNLGMMNFAAWRVSHaLSHHIYPNSYF-DLELSMFE 227
Cdd:pfam00487   6 LLALLLGLFLLGITGSLAHEASHGalfkkrrlnrwlNDLLGRLAGLPLGISYSAWRIAH-LVHHRYTNGPDkDPDTAPLA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137186   228 PLLCWVPNPHIKSKLMRYV-SWVTEPVAYALAFFIqMGTRIFYSLRHTNILYWHDLLPLTIPIAIYLGTGGSLGIWICVr 306
Cdd:pfam00487  85 SRFRGLLRYLLRWLLGLLVlAWLLALVLPLWLRRL-ARRKRPIKSRRRRWRLIAWLLLLAAWLGLWLGFLGLGGLLLLL- 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137186   307 qWLAMTSIASFSFCLIGLNAAHHDpeiyhegdanredRDWGLFQVDTIIDRGDLKWSQFLVLTHFGDHVLHHLFPTLDHG 386
Cdd:pfam00487 163 -WLLPLLVFGFLLALIFNYLEHYG-------------GDWGERPVETTRSIRSPNWWLNLLTGNLNYHIEHHLFPGVPWY 228

                         250       260
                  ....*....|....*....|..
gi 17137186   387 LLPALYPVLYQTLDEFKGHLRE 408
Cdd:pfam00487 229 RLPKLHRRLREALPEHGLPYRS 250
PLN03198 PLN03198
delta6-acyl-lipid desaturase; Provisional
 45-393 1.26e-07

delta6-acyl-lipid desaturase; Provisional


Pssm-ID: 178739 [Multi-domain]  Cd Length: 526  Bit Score: 53.93  E-value: 1.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137186   45 INDGIYDFTSFIDKHPGGPFwIRETKGTDITEAFEAHHLTTApEKMIAKYKVRDA--AEPriytlTLEEGGFYKTLKER- 121
Cdd:PLN03198 124 IKNKVYDVSDFAAEHPGGSV-ISTYFGRDGTDAFSSFHAAST-WKILQDFYIGDVdnVEP-----TPELLKDFRDLRALf 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137186  122 VREQLktidKRPKKKSDLIHLGLVVSLYLLGIASAKYNSLLALVLAS---VALCWTVI--VSHNYFHRR---DNW--QMY 191
Cdd:PLN03198 197 LREQL----FKSSKLYYVFKLLTNIAIFAASIAIICCSKSISAVLASacmMALCFQQCgwLSHDFLHNQvfeTRWlnEVV 272

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137186  192 AFNLG--MMNFAA--WRVSHALsHHIYPNSYFDLELSMFE-----PLLCWVPN--PHIKSKLMRYVSWVTEPVAYALAFF 260
Cdd:PLN03198 273 GYLIGnaVLGFSTgwWKEKHNL-HHAAPNECDQLYQPIDEdidtlPLIAWSKDilATVENKTFLRILQYQHLFFMALLFF 351

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137186  261 IQmGTRIFYSLRHTNILYWHDLLPLT------------IPIAIYLGTGGSLGIWICVRQwLAMTSIASFSFCLiglnaAH 328
Cdd:PLN03198 352 AR-GSWLFWSWRYTSTAKLAPADRLLekgtilfhyfwfIGTACYLLPGWKPLVWMAVTE-LMCGMLLGFVFVL-----SH 424

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17137186  329 HDPEIYhegDANREdrdwglFQVDTIIDRGDLKWSQF--LVLTHFGDHVLHHLFPTLDHGLLPALYP 393
Cdd:PLN03198 425 NGMEVY---NKSKE------FVNAQIVSTRDIKANIFndWFTGGLNRQIEHHLFPTMPRHNLNKIAP 482
PLN02252 PLN02252
nitrate reductase [NADPH]
 7-98 2.17e-07

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 53.14  E-value: 2.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137186    7 KKSGIATKFPTYRNSALITTHSWQKGKRQDDGaeglWRI-NDGIYDFTSFIDKHPGGPFWIRETKGTDITEAFEAHHLTT 85
Cdd:PLN02252 503 KKSVSTPFMNTNTGSKQYTMSEVRKHNSEDSC----WIVvHGHVYDCTRFLKDHPGGADSILINAGTDCTEEFDAIHSDK 578

                         90
                 ....*....|...
gi 17137186   86 ApEKMIAKYKVRD 98
Cdd:PLN02252 579 A-KKMLEDYRIGE 590
 
Name Accession Description Interval E-value
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
 34-100 1.89e-16

Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from a diverse range of proteins. This family also includes proteins that bind to steroids. The family includes progesterone receptors. Many members of this subfamily are membrane anchored by an N-terminal transmembrane alpha helix. This family also includes a domain in some chitin synthases. There is no known ligand for this domain in the chitin synthases.


Pssm-ID: 459698 [Multi-domain]  Cd Length: 74  Bit Score: 73.81  E-value: 1.89e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17137186    34 RQDDGAEGLWRINDG-IYDFTSFIDKHPGGPFWIRETKGTDITEAFEA-HHLTTAPEKMIAKYKVRDAA 100
Cdd:pfam00173   6 SKHNGDGDCWVAINGkVYDVTKFLKEHPGGEDVILSAAGKDATDAFEAiGHSEDAAEKLLKKYRIGELA 74
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
106-424 3.01e-12

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 67.06  E-value: 3.01e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137186 106 TLTLEEGGFYKTLKERVREQLKTIDKRpkkksDLIHLGLVVSLYLLGIASAKYN--SLLALVLASVALCWTVIVSHNYFH 183
Cdd:COG3239   6 PLTPADEAELRALRARLRALLGRRDWR-----YLLKLALTLALLAALWLLLSWSwlALLAALLLGLALAGLFSLGHDAGH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137186 184 ------RRDN-WQMYAFNLGM-MNFAAWRVSHaLSHHIYPNS-YFDLELsmfepllcwVPNPHIKSKLMRYVSWVTEPVA 254
Cdd:COG3239  81 gslfrsRWLNdLLGRLLGLPLgTPYDAWRRSH-NRHHAYTNDpGKDPDI---------GYGVQAWRPLYLFQHLLRFFLL 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137186 255 YALAFFIQMGTRIFYSLRHTNILYWH-DLLPLTIPIAIYLGTGGSLGIWICVRQWLAMTSIASFSFCLIglNAAHHDPEI 333
Cdd:COG3239 151 GLGGLYWLLALDFLPLRGRLELKERRlEALLLLLFLAALLALLLALGWWAVLLFWLLPLLVAGLLLGLR--FYLEHRGED 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137186 334 YHEGDANRedrdwglfQVDTIIDRGDLKWSQFLVLtHFGDHVLHHLFPTLDHGLLPALYPVLYQTLDEFKGHLRECNhIE 413
Cdd:COG3239 229 TGDGEYRD--------QLLGSRNIRGGRLLRWLFG-NLNYHIEHHLFPSIPWYRLPEAHRILKELCPEYGLPYTEGS-LL 298

                       330
                ....*....|.
gi 17137186 414 HMIGQHKQLLR 424
Cdd:COG3239 299 RSYREVLRLLR 309
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 161-408 2.82e-10

Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a double bond at the delta position of fatty acids. There seem to be two distinct families of fatty acid desaturases which do not seem to be evolutionary related: Family 1 composed of Stearoyl-CoA desaturases (SCD) and Family 2 composed of Bacterial fatty acid desaturases, Plant stearoyl-acyl-carrier-protein desaturase and Cyanobacterial DesA. Members of this entry are ER integral membrane proteins that share the same mushroom-shaped fold consisting of four transmembrane helices (TM1-TM4) which anchor them to the membrane, capped by a cytosolic domain containing a unique 9-10 histidine- coordinating di metal (di-iron) catalytic centre. The structure of mouse stearoyl-CoA desaturase (SDC) revealed that TM2 and TM4 are longer than TM1 and TM3 and protrude into the cytosolic domain, providing three of the nine histidine residues that coordinate the two metal ions, while the other histidine residues are provided by the soluble domain in this enzyme.


Pssm-ID: 425713 [Multi-domain]  Cd Length: 252  Bit Score: 60.44  E-value: 2.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137186   161 LLALVLASVALCWTVIVSHNYFHR------------RDNWQMYAFNLGMMNFAAWRVSHaLSHHIYPNSYF-DLELSMFE 227
Cdd:pfam00487   6 LLALLLGLFLLGITGSLAHEASHGalfkkrrlnrwlNDLLGRLAGLPLGISYSAWRIAH-LVHHRYTNGPDkDPDTAPLA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137186   228 PLLCWVPNPHIKSKLMRYV-SWVTEPVAYALAFFIqMGTRIFYSLRHTNILYWHDLLPLTIPIAIYLGTGGSLGIWICVr 306
Cdd:pfam00487  85 SRFRGLLRYLLRWLLGLLVlAWLLALVLPLWLRRL-ARRKRPIKSRRRRWRLIAWLLLLAAWLGLWLGFLGLGGLLLLL- 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137186   307 qWLAMTSIASFSFCLIGLNAAHHDpeiyhegdanredRDWGLFQVDTIIDRGDLKWSQFLVLTHFGDHVLHHLFPTLDHG 386
Cdd:pfam00487 163 -WLLPLLVFGFLLALIFNYLEHYG-------------GDWGERPVETTRSIRSPNWWLNLLTGNLNYHIEHHLFPGVPWY 228

                         250       260
                  ....*....|....*....|..
gi 17137186   387 LLPALYPVLYQTLDEFKGHLRE 408
Cdd:pfam00487 229 RLPKLHRRLREALPEHGLPYRS 250
PLN03198 PLN03198
delta6-acyl-lipid desaturase; Provisional
 45-393 1.26e-07

delta6-acyl-lipid desaturase; Provisional


Pssm-ID: 178739 [Multi-domain]  Cd Length: 526  Bit Score: 53.93  E-value: 1.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137186   45 INDGIYDFTSFIDKHPGGPFwIRETKGTDITEAFEAHHLTTApEKMIAKYKVRDA--AEPriytlTLEEGGFYKTLKER- 121
Cdd:PLN03198 124 IKNKVYDVSDFAAEHPGGSV-ISTYFGRDGTDAFSSFHAAST-WKILQDFYIGDVdnVEP-----TPELLKDFRDLRALf 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137186  122 VREQLktidKRPKKKSDLIHLGLVVSLYLLGIASAKYNSLLALVLAS---VALCWTVI--VSHNYFHRR---DNW--QMY 191
Cdd:PLN03198 197 LREQL----FKSSKLYYVFKLLTNIAIFAASIAIICCSKSISAVLASacmMALCFQQCgwLSHDFLHNQvfeTRWlnEVV 272

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137186  192 AFNLG--MMNFAA--WRVSHALsHHIYPNSYFDLELSMFE-----PLLCWVPN--PHIKSKLMRYVSWVTEPVAYALAFF 260
Cdd:PLN03198 273 GYLIGnaVLGFSTgwWKEKHNL-HHAAPNECDQLYQPIDEdidtlPLIAWSKDilATVENKTFLRILQYQHLFFMALLFF 351

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137186  261 IQmGTRIFYSLRHTNILYWHDLLPLT------------IPIAIYLGTGGSLGIWICVRQwLAMTSIASFSFCLiglnaAH 328
Cdd:PLN03198 352 AR-GSWLFWSWRYTSTAKLAPADRLLekgtilfhyfwfIGTACYLLPGWKPLVWMAVTE-LMCGMLLGFVFVL-----SH 424

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17137186  329 HDPEIYhegDANREdrdwglFQVDTIIDRGDLKWSQF--LVLTHFGDHVLHHLFPTLDHGLLPALYP 393
Cdd:PLN03198 425 NGMEVY---NKSKE------FVNAQIVSTRDIKANIFndWFTGGLNRQIEHHLFPTMPRHNLNKIAP 482
PLN02252 PLN02252
nitrate reductase [NADPH]
 7-98 2.17e-07

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 53.14  E-value: 2.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137186    7 KKSGIATKFPTYRNSALITTHSWQKGKRQDDGaeglWRI-NDGIYDFTSFIDKHPGGPFWIRETKGTDITEAFEAHHLTT 85
Cdd:PLN02252 503 KKSVSTPFMNTNTGSKQYTMSEVRKHNSEDSC----WIVvHGHVYDCTRFLKDHPGGADSILINAGTDCTEEFDAIHSDK 578

                         90
                 ....*....|...
gi 17137186   86 ApEKMIAKYKVRD 98
Cdd:PLN02252 579 A-KKMLEDYRIGE 590
 
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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