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Conserved domains on  [gi|22760516|dbj|BAC11229|]
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unnamed protein product [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
218-469 5.68e-69

The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: delta-4, delta-5, delta-6, delta-8, delta-8-sphingolipid, and delta-11 desaturases found in vertebrates, higher plants, fungi, and bacteria. These desaturases are required for the synthesis of highly unsaturated fatty acids (HUFAs), which are mainly esterified into phospholipids and contribute to maintaining membrane fluidity. While HUFAs may be required for cold tolerance in bacteria, plants and fish, the primary role of HUFAs in mammals is cell signaling. These enzymes are described as front-end desaturases because they introduce a double bond between the pre-exiting double bond and the carboxyl (front) end of the fatty acid. Various substrates are involved, with both acyl-coenzyme A (CoA) and acyl-lipid desaturases present in this CD. Acyl-lipid desaturases are localized in the membranes of cyanobacterial thylakoid, plant endoplasmic reticulum (ER), and plastid; and acyl-CoA desaturases are present in ER membrane. ER-bound plant acyl-lipid desaturases and acyl-CoA desaturases require cytochrome b5 as an electron donor. Most of the eukaryotic desaturase domains have an adjacent N-terminal cytochrome b5-like domain. This domain family has extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of sequences also reveals the existence of three regions of conserved histidine cluster motifs that contain the residues: HXXXH, HXX(X)HH, and Q/HXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within the homolog, stearoyl CoA desaturase.


:

Pssm-ID: 239583  Cd Length: 204  Bit Score: 219.44  E-value: 5.68e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516 218 LLCAVLLSAVQAQAGWLQHDFGHLSVFSTSKWNHLLHHFVIGhLKGAPASWWNHMHFQHHAKPNCFRKDPDINMHPFFFA 297
Cdd:cd03506   1 LLLAILLGLFWAQGGFLAHDAGHGQVFKNRWLNKLLGLTVGN-LLGASAGWWKNKHNVHHAYTNILGHDPDIDTLPLLAR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516 298 LGKILsvelGKQKKKYMPYNHQHKYFFLIGPPALLplyfqwyifyfviqrkkwvdlawmitfyvrffltyvpllglkafl 377
Cdd:cd03506  80 SEPAF----GKDQKKRFLHRYQHFYFFPLLALLLL--------------------------------------------- 110
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516 378 gLFFIVRFLESNWFVWVTQMNHIPMHIDH---DRNMDWVSTQLQATCNVHKSAFNDWFSGHLNSQIEHHLFPTMPRHNYH 454
Cdd:cd03506 111 -AFLVVQLAGGLWLAVVFQLNHFGMPVEDppgESKNDWLERQVLTTRNITGSPFLDWLHGGLNYQIEHHLFPTMPRHNYP 189
                       250
                ....*....|....*
gi 22760516 455 KVAPLVQSLCAKHGI 469
Cdd:cd03506 190 KVAPLVRELCKKHGL 204
PLN03199 super family cl31982
delta6-acyl-lipid desaturase-like protein; Provisional
74-487 1.80e-48

delta6-acyl-lipid desaturase-like protein; Provisional


The actual alignment was detected with superfamily member PLN03199:

Pssm-ID: 178740 [Multi-domain]  Cd Length: 485  Bit Score: 173.69  E-value: 1.80e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516   74 PRYFTWDEVAQRSGCEERWLVIDRKVYNISEFtRRHPGGSRVISHyAGQDATDPFVAFHI--NKGLVKKYMnsllIGELS 151
Cdd:PLN03199  23 PQKISWQEVKKHASPDDAWIIHQNKVYDVSNW-HDHPGGAVIFTH-AGDDMTDIFAAFHApgSQALMKKFY----IGDLI 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516  152 PEQPSFEPTKNKELTDEFRELRATVERMGLMKANHVFFLLYLLHilllDGAAWL---TLWVFGTSFLPFLLCAVLLSAVQ 228
Cdd:PLN03199  97 PESTEHKDPQQIAFEKGYRDLRAKLIMMGMFKSNKMFYAYKCLF----NMAIWAaacALVFYSDRFAMHIASALLLGLFF 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516  229 AQAGWLQHDFGHLSVFSTSKWNHLLHHFVIGHLKGAPASWWNHMHFQHHAKPNCFRK-------DPDINMHPFF-FALGK 300
Cdd:PLN03199 173 QQCGWLAHDFLHHQVFKKRKHGDLGGIFWGDLMQGFSMQWWKNKHNGHHAVPNLHCSsadaqdgDPDIDTMPLLaWSLKQ 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516  301 ILSV-ELGKQKK-----KYMPYNHQHKYFfligpPALLPLYFQWYIFYF-------------VIQRKK------------ 349
Cdd:PLN03199 253 AQSFrEINADGKdsgfvKFAIKFQAFFYF-----PILLLARISWLNESFkcafglgaasenaALELEAkglqypllekag 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516  350 -WVDLAWMITF---YVRFFLTYVPLLGLKAFL--GLFFIVRFlesnwfvwvtQMNHIPMHI-DHDRNMDWVSTQLQATCN 422
Cdd:PLN03199 328 iLLHYAWMFTLssgFGRFSFAYSAFYFFTATAscGFFLAIVF----------GLGHNGMATyDADARPDFWKLQVTTTRN 397
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516  423 V-----HKSAFNDWFSGHLNSQIEHHLFPTMPRHNYHKVAPLVQSLCAKHGIEYQSKPLLSAFADIIHSL 487
Cdd:PLN03199 398 IigghgFPQAFVDWFCGGLQYQVDHHLFPMLPRHNIAKCHALVESFCKEWGVKYHEADLVDGTMEVLHHL 467
PRK07003 super family cl35530
DNA polymerase III subunits gamma and tau; Validated
3-75 5.79e-04

DNA polymerase III subunits gamma and tau; Validated


The actual alignment was detected with superfamily member PRK07003:

Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 42.53  E-value: 5.79e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22760516    3 TRAARPAglPCGAENPARRRLALGARQQIHSWSPRTPSTRLTAPAGPARGVARPAMAPDPVAAETAAQGPTPR 75
Cdd:PRK07003 530 PEARPPT--PAAAAPAARAGGAAAALDVLRNAGMRVSSDRGARAAAAAKPAAAPAAAPKPAAPRVAVQVPTPR 600
 
Name Accession Description Interval E-value
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
218-469 5.68e-69

The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: delta-4, delta-5, delta-6, delta-8, delta-8-sphingolipid, and delta-11 desaturases found in vertebrates, higher plants, fungi, and bacteria. These desaturases are required for the synthesis of highly unsaturated fatty acids (HUFAs), which are mainly esterified into phospholipids and contribute to maintaining membrane fluidity. While HUFAs may be required for cold tolerance in bacteria, plants and fish, the primary role of HUFAs in mammals is cell signaling. These enzymes are described as front-end desaturases because they introduce a double bond between the pre-exiting double bond and the carboxyl (front) end of the fatty acid. Various substrates are involved, with both acyl-coenzyme A (CoA) and acyl-lipid desaturases present in this CD. Acyl-lipid desaturases are localized in the membranes of cyanobacterial thylakoid, plant endoplasmic reticulum (ER), and plastid; and acyl-CoA desaturases are present in ER membrane. ER-bound plant acyl-lipid desaturases and acyl-CoA desaturases require cytochrome b5 as an electron donor. Most of the eukaryotic desaturase domains have an adjacent N-terminal cytochrome b5-like domain. This domain family has extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of sequences also reveals the existence of three regions of conserved histidine cluster motifs that contain the residues: HXXXH, HXX(X)HH, and Q/HXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within the homolog, stearoyl CoA desaturase.


Pssm-ID: 239583  Cd Length: 204  Bit Score: 219.44  E-value: 5.68e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516 218 LLCAVLLSAVQAQAGWLQHDFGHLSVFSTSKWNHLLHHFVIGhLKGAPASWWNHMHFQHHAKPNCFRKDPDINMHPFFFA 297
Cdd:cd03506   1 LLLAILLGLFWAQGGFLAHDAGHGQVFKNRWLNKLLGLTVGN-LLGASAGWWKNKHNVHHAYTNILGHDPDIDTLPLLAR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516 298 LGKILsvelGKQKKKYMPYNHQHKYFFLIGPPALLplyfqwyifyfviqrkkwvdlawmitfyvrffltyvpllglkafl 377
Cdd:cd03506  80 SEPAF----GKDQKKRFLHRYQHFYFFPLLALLLL--------------------------------------------- 110
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516 378 gLFFIVRFLESNWFVWVTQMNHIPMHIDH---DRNMDWVSTQLQATCNVHKSAFNDWFSGHLNSQIEHHLFPTMPRHNYH 454
Cdd:cd03506 111 -AFLVVQLAGGLWLAVVFQLNHFGMPVEDppgESKNDWLERQVLTTRNITGSPFLDWLHGGLNYQIEHHLFPTMPRHNYP 189
                       250
                ....*....|....*
gi 22760516 455 KVAPLVQSLCAKHGI 469
Cdd:cd03506 190 KVAPLVRELCKKHGL 204
PLN03198 PLN03198
delta6-acyl-lipid desaturase; Provisional
81-489 2.79e-56

delta6-acyl-lipid desaturase; Provisional


Pssm-ID: 178739 [Multi-domain]  Cd Length: 526  Bit Score: 195.68  E-value: 2.79e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516   81 EVAQRSGCEERWLVIDRKVYNISEFTRRHPGGSrVISHYAGQDATDPFVAFHinKGLVKKYMNSLLIGELSpeqpSFEPT 160
Cdd:PLN03198 110 EVAAHNKPNDCWIVIKNKVYDVSDFAAEHPGGS-VISTYFGRDGTDAFSSFH--AASTWKILQDFYIGDVD----NVEPT 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516  161 KnkELTDEFRELRATVERMGLMKANHVFFLLYLLHILLLDGAAwLTLWVFGTSFLPFLLCAVLLSAVQAQAGWLQHDFGH 240
Cdd:PLN03198 183 P--ELLKDFRDLRALFLREQLFKSSKLYYVFKLLTNIAIFAAS-IAIICCSKSISAVLASACMMALCFQQCGWLSHDFLH 259
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516  241 LSVFSTSKWNHLLHHFVIGHLKGAPASWWNHMHFQHHAKPN-CFRK----DPDINMHPFFFALGKILSVELGKQKKKYMP 315
Cdd:PLN03198 260 NQVFETRWLNEVVGYLIGNAVLGFSTGWWKEKHNLHHAAPNeCDQLyqpiDEDIDTLPLIAWSKDILATVENKTFLRILQ 339
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516  316 YNHqhkyffligppallpLYFQWYIFYfviQRKKWVDLAWMITFYVRffLTYVPLLGLKAFLgLFFIVRFLESNWF---- 391
Cdd:PLN03198 340 YQH---------------LFFMALLFF---ARGSWLFWSWRYTSTAK--LAPADRLLEKGTI-LFHYFWFIGTACYllpg 398
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516  392 ----VW--VTQM------------NHIPMHIdHDRNMDWVSTQLQATCNVHKSAFNDWFSGHLNSQIEHHLFPTMPRHNY 453
Cdd:PLN03198 399 wkplVWmaVTELmcgmllgfvfvlSHNGMEV-YNKSKEFVNAQIVSTRDIKANIFNDWFTGGLNRQIEHHLFPTMPRHNL 477
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 22760516  454 HKVAPLVQSLCAKHGIEYQSKPLLSAFADIIHSLEE 489
Cdd:PLN03198 478 NKIAPQVEAFCIKHGLVYEDVSIAAGTCKVLKALKE 513
PLN03199 PLN03199
delta6-acyl-lipid desaturase-like protein; Provisional
74-487 1.80e-48

delta6-acyl-lipid desaturase-like protein; Provisional


Pssm-ID: 178740 [Multi-domain]  Cd Length: 485  Bit Score: 173.69  E-value: 1.80e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516   74 PRYFTWDEVAQRSGCEERWLVIDRKVYNISEFtRRHPGGSRVISHyAGQDATDPFVAFHI--NKGLVKKYMnsllIGELS 151
Cdd:PLN03199  23 PQKISWQEVKKHASPDDAWIIHQNKVYDVSNW-HDHPGGAVIFTH-AGDDMTDIFAAFHApgSQALMKKFY----IGDLI 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516  152 PEQPSFEPTKNKELTDEFRELRATVERMGLMKANHVFFLLYLLHilllDGAAWL---TLWVFGTSFLPFLLCAVLLSAVQ 228
Cdd:PLN03199  97 PESTEHKDPQQIAFEKGYRDLRAKLIMMGMFKSNKMFYAYKCLF----NMAIWAaacALVFYSDRFAMHIASALLLGLFF 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516  229 AQAGWLQHDFGHLSVFSTSKWNHLLHHFVIGHLKGAPASWWNHMHFQHHAKPNCFRK-------DPDINMHPFF-FALGK 300
Cdd:PLN03199 173 QQCGWLAHDFLHHQVFKKRKHGDLGGIFWGDLMQGFSMQWWKNKHNGHHAVPNLHCSsadaqdgDPDIDTMPLLaWSLKQ 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516  301 ILSV-ELGKQKK-----KYMPYNHQHKYFfligpPALLPLYFQWYIFYF-------------VIQRKK------------ 349
Cdd:PLN03199 253 AQSFrEINADGKdsgfvKFAIKFQAFFYF-----PILLLARISWLNESFkcafglgaasenaALELEAkglqypllekag 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516  350 -WVDLAWMITF---YVRFFLTYVPLLGLKAFL--GLFFIVRFlesnwfvwvtQMNHIPMHI-DHDRNMDWVSTQLQATCN 422
Cdd:PLN03199 328 iLLHYAWMFTLssgFGRFSFAYSAFYFFTATAscGFFLAIVF----------GLGHNGMATyDADARPDFWKLQVTTTRN 397
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516  423 V-----HKSAFNDWFSGHLNSQIEHHLFPTMPRHNYHKVAPLVQSLCAKHGIEYQSKPLLSAFADIIHSL 487
Cdd:PLN03199 398 IigghgFPQAFVDWFCGGLQYQVDHHLFPMLPRHNIAKCHALVESFCKEWGVKYHEADLVDGTMEVLHHL 467
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
78-150 1.35e-23

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: 306642 [Multi-domain]  Cd Length: 74  Bit Score: 93.84  E-value: 1.35e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22760516    78 TWDEVAQRSGCEERWLVIDRKVYNISEFTRRHPGGSRVISHYAGQDATDPFVAFHINKGLVKKYMNSLLIGEL 150
Cdd:pfam00173   1 TLEELAKHNGDGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDATDAFEAIVHSEDAAEKLLKKYRIGEL 73
FA_desaturase pfam00487
Fatty acid desaturase;
214-475 1.87e-21

Fatty acid desaturase;


Pssm-ID: 334106 [Multi-domain]  Cd Length: 248  Bit Score: 93.17  E-value: 1.87e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516   214 FLPFLLCAVLLSAVQAQAGWLQHDFGHLSVFSTSKWNHLLHHFVIGHLKGAPASWWNHMHFQHHAKPNCFRKDPDINMHP 293
Cdd:pfam00487   1 WLALLLALLLGLFLLGILGVLAHEASHGALFRRRNRWLNDLLGLAGLPLGISYSAWRIAHLVHHRYTNGPDEDPDTAPLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516   294 FFFAlgkilsvELGKQKKKYMPYNHQHKYFFLIGPPALLPLYFQWYIFYFVIQRKkWVDLAWMItFYVRFFLTYVPLLGL 373
Cdd:pfam00487  81 SRFR-------GLLRYLLRWLLGLLVLAWLLALLLGLWLRRLARRKRPIKSRRRR-WRLIAWLL-LLAAWLGLWLGFLGL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516   374 KAFLGLFFIVRFLESNWF--VWVTQMNHIPMhidhdrnmDWVSTQLQATCNVHK-SAFNDWFSGHLNSQIEHHLFPTMPR 450
Cdd:pfam00487 152 GGLLLLLWLLPLLVAGFLlaLIFNYLEHYGG--------DWGERPVETTRSIRSpNWWLNLLTGNLNYHIEHHLFPGVPW 223
                         250       260
                  ....*....|....*....|....*
gi 22760516   451 HNYHKVAPLVQSLCAKHGIEYQSKP 475
Cdd:pfam00487 224 YRLPKLHRRLREALPEHGLPYRSLA 248
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
202-464 1.49e-16

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 225779 [Multi-domain]  Cd Length: 343  Bit Score: 80.60  E-value: 1.49e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516 202 AAWLTLWVFGTSFLPFLLCAVLLSAVQAQAGWLQHDFGHLSVFSTSKWNHLLHHFVIGhLKGAPASWWNHMHFQHHAKPN 281
Cdd:COG3239  49 ALLALSLAYWPSWWLLPLALLLAGLLLTGLFSVGHDCGHGSFFKNRWINDLIGHLAAA-LLLAPPVFWRISHNQHHAHTN 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516 282 CFRKDPDInmhpfffalgkilSVELGKQKKKympynhqhkyffligPPALLPLYFQWYIFYFVIQRKKWVDLAWMITFY- 360
Cdd:COG3239 128 ILDDDPET-------------YVSYPEQLRR---------------GPLRFQLIRLPWLAFGFGPRWALLHFELLEKLFk 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516 361 ----------VRFFLTYVPLLGLKAFLGLFFIVRFLESN-WFVWVTQMNH----IPMHIDHDrnMDWVSTQLQATCNVHK 425
Cdd:COG3239 180 rsgkapkaaaLATLLAAIGLAALLALAFFWGLIPLLLVGlWLVLVLFVHHtfdlLPHHGLED--WQWSDRALNARSNVDA 257
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 22760516 426 SAFNDWFSGHLNSQIEHHLFPTMPRHNYHKVAPLVQSLC 464
Cdd:COG3239 258 PPLLRFLTGNINYHVEHHLFPDVPWYRLPRAHRLIKEAL 296
CYB5 COG5274
Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport ...
72-162 1.58e-11

Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport and metabolism];


Pssm-ID: 227599 [Multi-domain]  Cd Length: 164  Bit Score: 62.53  E-value: 1.58e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516  72 PTPRYFTWDEVAQRSGCEERWLVIDRKVYNISEFTRRHPGGSRVISHYAGQDATDPFVAFH----INKGLVKKYMNSLLI 147
Cdd:COG5274  47 ESPKPITAEEVAKHNKSEDCWIVINGKVYDVSQFLDEHPGGEDIIKDTAGKDATKAFNFLHhshqIGNLLKDVYVDQVHR 126
                        90
                ....*....|....*..
gi 22760516 148 --GELSPEQPSFEPTKN 162
Cdd:COG5274 127 peEELPLFKTAWYPLKV 143
PRK07003 PRK07003
DNA polymerase III subunits gamma and tau; Validated
3-75 5.79e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 42.53  E-value: 5.79e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22760516    3 TRAARPAglPCGAENPARRRLALGARQQIHSWSPRTPSTRLTAPAGPARGVARPAMAPDPVAAETAAQGPTPR 75
Cdd:PRK07003 530 PEARPPT--PAAAAPAARAGGAAAALDVLRNAGMRVSSDRGARAAAAAKPAAAPAAAPKPAAPRVAVQVPTPR 600
 
Name Accession Description Interval E-value
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
218-469 5.68e-69

The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: delta-4, delta-5, delta-6, delta-8, delta-8-sphingolipid, and delta-11 desaturases found in vertebrates, higher plants, fungi, and bacteria. These desaturases are required for the synthesis of highly unsaturated fatty acids (HUFAs), which are mainly esterified into phospholipids and contribute to maintaining membrane fluidity. While HUFAs may be required for cold tolerance in bacteria, plants and fish, the primary role of HUFAs in mammals is cell signaling. These enzymes are described as front-end desaturases because they introduce a double bond between the pre-exiting double bond and the carboxyl (front) end of the fatty acid. Various substrates are involved, with both acyl-coenzyme A (CoA) and acyl-lipid desaturases present in this CD. Acyl-lipid desaturases are localized in the membranes of cyanobacterial thylakoid, plant endoplasmic reticulum (ER), and plastid; and acyl-CoA desaturases are present in ER membrane. ER-bound plant acyl-lipid desaturases and acyl-CoA desaturases require cytochrome b5 as an electron donor. Most of the eukaryotic desaturase domains have an adjacent N-terminal cytochrome b5-like domain. This domain family has extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of sequences also reveals the existence of three regions of conserved histidine cluster motifs that contain the residues: HXXXH, HXX(X)HH, and Q/HXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within the homolog, stearoyl CoA desaturase.


Pssm-ID: 239583  Cd Length: 204  Bit Score: 219.44  E-value: 5.68e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516 218 LLCAVLLSAVQAQAGWLQHDFGHLSVFSTSKWNHLLHHFVIGhLKGAPASWWNHMHFQHHAKPNCFRKDPDINMHPFFFA 297
Cdd:cd03506   1 LLLAILLGLFWAQGGFLAHDAGHGQVFKNRWLNKLLGLTVGN-LLGASAGWWKNKHNVHHAYTNILGHDPDIDTLPLLAR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516 298 LGKILsvelGKQKKKYMPYNHQHKYFFLIGPPALLplyfqwyifyfviqrkkwvdlawmitfyvrffltyvpllglkafl 377
Cdd:cd03506  80 SEPAF----GKDQKKRFLHRYQHFYFFPLLALLLL--------------------------------------------- 110
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516 378 gLFFIVRFLESNWFVWVTQMNHIPMHIDH---DRNMDWVSTQLQATCNVHKSAFNDWFSGHLNSQIEHHLFPTMPRHNYH 454
Cdd:cd03506 111 -AFLVVQLAGGLWLAVVFQLNHFGMPVEDppgESKNDWLERQVLTTRNITGSPFLDWLHGGLNYQIEHHLFPTMPRHNYP 189
                       250
                ....*....|....*
gi 22760516 455 KVAPLVQSLCAKHGI 469
Cdd:cd03506 190 KVAPLVRELCKKHGL 204
PLN03198 PLN03198
delta6-acyl-lipid desaturase; Provisional
81-489 2.79e-56

delta6-acyl-lipid desaturase; Provisional


Pssm-ID: 178739 [Multi-domain]  Cd Length: 526  Bit Score: 195.68  E-value: 2.79e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516   81 EVAQRSGCEERWLVIDRKVYNISEFTRRHPGGSrVISHYAGQDATDPFVAFHinKGLVKKYMNSLLIGELSpeqpSFEPT 160
Cdd:PLN03198 110 EVAAHNKPNDCWIVIKNKVYDVSDFAAEHPGGS-VISTYFGRDGTDAFSSFH--AASTWKILQDFYIGDVD----NVEPT 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516  161 KnkELTDEFRELRATVERMGLMKANHVFFLLYLLHILLLDGAAwLTLWVFGTSFLPFLLCAVLLSAVQAQAGWLQHDFGH 240
Cdd:PLN03198 183 P--ELLKDFRDLRALFLREQLFKSSKLYYVFKLLTNIAIFAAS-IAIICCSKSISAVLASACMMALCFQQCGWLSHDFLH 259
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516  241 LSVFSTSKWNHLLHHFVIGHLKGAPASWWNHMHFQHHAKPN-CFRK----DPDINMHPFFFALGKILSVELGKQKKKYMP 315
Cdd:PLN03198 260 NQVFETRWLNEVVGYLIGNAVLGFSTGWWKEKHNLHHAAPNeCDQLyqpiDEDIDTLPLIAWSKDILATVENKTFLRILQ 339
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516  316 YNHqhkyffligppallpLYFQWYIFYfviQRKKWVDLAWMITFYVRffLTYVPLLGLKAFLgLFFIVRFLESNWF---- 391
Cdd:PLN03198 340 YQH---------------LFFMALLFF---ARGSWLFWSWRYTSTAK--LAPADRLLEKGTI-LFHYFWFIGTACYllpg 398
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516  392 ----VW--VTQM------------NHIPMHIdHDRNMDWVSTQLQATCNVHKSAFNDWFSGHLNSQIEHHLFPTMPRHNY 453
Cdd:PLN03198 399 wkplVWmaVTELmcgmllgfvfvlSHNGMEV-YNKSKEFVNAQIVSTRDIKANIFNDWFTGGLNRQIEHHLFPTMPRHNL 477
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 22760516  454 HKVAPLVQSLCAKHGIEYQSKPLLSAFADIIHSLEE 489
Cdd:PLN03198 478 NKIAPQVEAFCIKHGLVYEDVSIAAGTCKVLKALKE 513
PLN03199 PLN03199
delta6-acyl-lipid desaturase-like protein; Provisional
74-487 1.80e-48

delta6-acyl-lipid desaturase-like protein; Provisional


Pssm-ID: 178740 [Multi-domain]  Cd Length: 485  Bit Score: 173.69  E-value: 1.80e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516   74 PRYFTWDEVAQRSGCEERWLVIDRKVYNISEFtRRHPGGSRVISHyAGQDATDPFVAFHI--NKGLVKKYMnsllIGELS 151
Cdd:PLN03199  23 PQKISWQEVKKHASPDDAWIIHQNKVYDVSNW-HDHPGGAVIFTH-AGDDMTDIFAAFHApgSQALMKKFY----IGDLI 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516  152 PEQPSFEPTKNKELTDEFRELRATVERMGLMKANHVFFLLYLLHilllDGAAWL---TLWVFGTSFLPFLLCAVLLSAVQ 228
Cdd:PLN03199  97 PESTEHKDPQQIAFEKGYRDLRAKLIMMGMFKSNKMFYAYKCLF----NMAIWAaacALVFYSDRFAMHIASALLLGLFF 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516  229 AQAGWLQHDFGHLSVFSTSKWNHLLHHFVIGHLKGAPASWWNHMHFQHHAKPNCFRK-------DPDINMHPFF-FALGK 300
Cdd:PLN03199 173 QQCGWLAHDFLHHQVFKKRKHGDLGGIFWGDLMQGFSMQWWKNKHNGHHAVPNLHCSsadaqdgDPDIDTMPLLaWSLKQ 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516  301 ILSV-ELGKQKK-----KYMPYNHQHKYFfligpPALLPLYFQWYIFYF-------------VIQRKK------------ 349
Cdd:PLN03199 253 AQSFrEINADGKdsgfvKFAIKFQAFFYF-----PILLLARISWLNESFkcafglgaasenaALELEAkglqypllekag 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516  350 -WVDLAWMITF---YVRFFLTYVPLLGLKAFL--GLFFIVRFlesnwfvwvtQMNHIPMHI-DHDRNMDWVSTQLQATCN 422
Cdd:PLN03199 328 iLLHYAWMFTLssgFGRFSFAYSAFYFFTATAscGFFLAIVF----------GLGHNGMATyDADARPDFWKLQVTTTRN 397
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516  423 V-----HKSAFNDWFSGHLNSQIEHHLFPTMPRHNYHKVAPLVQSLCAKHGIEYQSKPLLSAFADIIHSL 487
Cdd:PLN03199 398 IigghgFPQAFVDWFCGGLQYQVDHHLFPMLPRHNIAKCHALVESFCKEWGVKYHEADLVDGTMEVLHHL 467
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
78-150 1.35e-23

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: 306642 [Multi-domain]  Cd Length: 74  Bit Score: 93.84  E-value: 1.35e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22760516    78 TWDEVAQRSGCEERWLVIDRKVYNISEFTRRHPGGSRVISHYAGQDATDPFVAFHINKGLVKKYMNSLLIGEL 150
Cdd:pfam00173   1 TLEELAKHNGDGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDATDAFEAIVHSEDAAEKLLKKYRIGEL 73
FA_desaturase pfam00487
Fatty acid desaturase;
214-475 1.87e-21

Fatty acid desaturase;


Pssm-ID: 334106 [Multi-domain]  Cd Length: 248  Bit Score: 93.17  E-value: 1.87e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516   214 FLPFLLCAVLLSAVQAQAGWLQHDFGHLSVFSTSKWNHLLHHFVIGHLKGAPASWWNHMHFQHHAKPNCFRKDPDINMHP 293
Cdd:pfam00487   1 WLALLLALLLGLFLLGILGVLAHEASHGALFRRRNRWLNDLLGLAGLPLGISYSAWRIAHLVHHRYTNGPDEDPDTAPLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516   294 FFFAlgkilsvELGKQKKKYMPYNHQHKYFFLIGPPALLPLYFQWYIFYFVIQRKkWVDLAWMItFYVRFFLTYVPLLGL 373
Cdd:pfam00487  81 SRFR-------GLLRYLLRWLLGLLVLAWLLALLLGLWLRRLARRKRPIKSRRRR-WRLIAWLL-LLAAWLGLWLGFLGL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516   374 KAFLGLFFIVRFLESNWF--VWVTQMNHIPMhidhdrnmDWVSTQLQATCNVHK-SAFNDWFSGHLNSQIEHHLFPTMPR 450
Cdd:pfam00487 152 GGLLLLLWLLPLLVAGFLlaLIFNYLEHYGG--------DWGERPVETTRSIRSpNWWLNLLTGNLNYHIEHHLFPGVPW 223
                         250       260
                  ....*....|....*....|....*
gi 22760516   451 HNYHKVAPLVQSLCAKHGIEYQSKP 475
Cdd:pfam00487 224 YRLPKLHRRLREALPEHGLPYRSLA 248
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
202-464 1.49e-16

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 225779 [Multi-domain]  Cd Length: 343  Bit Score: 80.60  E-value: 1.49e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516 202 AAWLTLWVFGTSFLPFLLCAVLLSAVQAQAGWLQHDFGHLSVFSTSKWNHLLHHFVIGhLKGAPASWWNHMHFQHHAKPN 281
Cdd:COG3239  49 ALLALSLAYWPSWWLLPLALLLAGLLLTGLFSVGHDCGHGSFFKNRWINDLIGHLAAA-LLLAPPVFWRISHNQHHAHTN 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516 282 CFRKDPDInmhpfffalgkilSVELGKQKKKympynhqhkyffligPPALLPLYFQWYIFYFVIQRKKWVDLAWMITFY- 360
Cdd:COG3239 128 ILDDDPET-------------YVSYPEQLRR---------------GPLRFQLIRLPWLAFGFGPRWALLHFELLEKLFk 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516 361 ----------VRFFLTYVPLLGLKAFLGLFFIVRFLESN-WFVWVTQMNH----IPMHIDHDrnMDWVSTQLQATCNVHK 425
Cdd:COG3239 180 rsgkapkaaaLATLLAAIGLAALLALAFFWGLIPLLLVGlWLVLVLFVHHtfdlLPHHGLED--WQWSDRALNARSNVDA 257
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 22760516 426 SAFNDWFSGHLNSQIEHHLFPTMPRHNYHKVAPLVQSLC 464
Cdd:COG3239 258 PPLLRFLTGNINYHVEHHLFPDVPWYRLPRAHRLIKEAL 296
Delta12-FADS-like cd03507
The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane ...
200-454 2.75e-14

The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane enzymes, delta-12 acyl-lipid desaturases, oleate 12-hydroxylases, omega3 and omega6 fatty acid desaturases, and other related proteins, found in a wide range of organisms including higher plants, green algae, diatoms, nematodes, fungi, and bacteria. The expression of these proteins appears to be temperature dependent: decreases in temperature result in increased levels of fatty acid desaturation within membrane lipids subsequently altering cell membrane fluidity. An important enzyme for the production of polyunsaturates in plants is the oleate delta-12 desaturase (Arabidopsis FAD2) of the endoplasmic reticulum. This enzyme accepts l-acyl-2-oleoyl-sn-glycero-3-phosphocholine as substrate and requires NADH:cytochrome b oxidoreductase, cytochrome b, and oxygen for activity. FAD2 converts oleate(18:1) to linoleate (18:2) and is closely related to oleate 12-hydroxylase which catalyzes the hydroxylation of oleate to ricinoleate. Plastid-bound desaturases (Arabidopsis delta-12 desaturase (FAD6), omega-3 desaturase (FAD8), omega-6 desaturase (FAD6)), as well as, the cyanobacterial thylakoid-bound FADSs require oxygen, ferredoxin, and ferredoxin oxidoreductase for activity. As in higher plants, the cyanobacteria delta-12 (DesA) and omega-3 (DesB) FADSs desaturate oleate (18:1) to linoleate (18:2) and linoleate (18:2) to linolenate (18:3), respectively. Omega-3 (DesB/FAD8) and omega-6 (DesD/FAD6) desaturases catalyze reactions that introduce a double bond between carbons three and four, and carbons six and seven, respectively, from the methyl end of fatty acids. As with other members of this superfamily, this domain family has extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of sequences also reveals the existence of three regions of conserved histidine cluster motifs that contain eight histidine residues: HXXXH, HXX(X)HH, and HXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within the homologue, stearoyl CoA desaturase. Mutation of any one of four of these histidines in the Synechocystis delta-12 acyl-lipid desaturase resulted in complete inactivity.


Pssm-ID: 239584  Cd Length: 222  Bit Score: 71.87  E-value: 2.75e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516 200 DGAAWLTLWVFGTSFLPFLLCAvLLSAVQAQAGW----LQHDFGHLSVFSTSKWNHLLHHfVIGHLKGAPASWWNHMHFQ 275
Cdd:cd03507  13 DILLLALLALAASLLLSWWLWP-LYWIVQGLFLTglfvLGHDCGHGSFSDNRRLNDIVGH-ILHSPLLVPYHSWRISHNR 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516 276 HHAKPNCFRKDpdINMHPfffalgkilsvelgKQKKKYMPYNHQHKYFFLIGPPALLPLyfqwyifyfviqrkkwvdlAW 355
Cdd:cd03507  91 HHAHTGNLEGD--EVWVP--------------VTEEEYAELPKRLPYRLYRNPFLMLSL-------------------GW 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516 356 MITFYVRFFLTY-VPLLGLKAflglffivrflesnWFVWVTQMNHIPMHIDHDRNMDWVSTQLQATCNVHKS--AFNDWF 432
Cdd:cd03507 136 PYYLLLNVLLYYlIPYLVVNA--------------WLVLITYLQHTFPDIPWYRADEWNFAQAGLLGTVDRDygGWLNWL 201
                       250       260
                ....*....|....*....|..
gi 22760516 433 SGHLNSQIEHHLFPTMPrhNYH 454
Cdd:cd03507 202 THIIGTHVAHHLFPRIP--HYN 221
PLN02252 PLN02252
nitrate reductase [NADPH]
54-177 2.34e-12

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 69.32  E-value: 2.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516   54 ARPAMAPdPVAAETAAQGPTPRYFTWDEVAQRSGCEERWLVIDRKVYNISEFTRRHPGGSRVISHYAGQDATDPFVAFHI 133
Cdd:PLN02252 498 AAPALKK-SVSTPFMNTNTGSKQYTMSEVRKHNSEDSCWIVVHGHVYDCTRFLKDHPGGADSILINAGTDCTEEFDAIHS 576
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 22760516  134 NKGlvKKYMNSLLIGELSPEQPSFEPTKNKELTDEFRELRATVE 177
Cdd:PLN02252 577 DKA--KKMLEDYRIGELVTTGAAASSSASSHPLSAISTASALAA 618
CYB5 COG5274
Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport ...
72-162 1.58e-11

Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport and metabolism];


Pssm-ID: 227599 [Multi-domain]  Cd Length: 164  Bit Score: 62.53  E-value: 1.58e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516  72 PTPRYFTWDEVAQRSGCEERWLVIDRKVYNISEFTRRHPGGSRVISHYAGQDATDPFVAFH----INKGLVKKYMNSLLI 147
Cdd:COG5274  47 ESPKPITAEEVAKHNKSEDCWIVINGKVYDVSQFLDEHPGGEDIIKDTAGKDATKAFNFLHhshqIGNLLKDVYVDQVHR 126
                        90
                ....*....|....*..
gi 22760516 148 --GELSPEQPSFEPTKN 162
Cdd:COG5274 127 peEELPLFKTAWYPLKV 143
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
217-289 7.16e-11

The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane hydroxylases, beta carotene ketolases (CrtW-like), hydroxylases (CrtR-like), and other related proteins. They are present in all groups of organisms with the exception of archaea. Membrane FADSs are non-heme, iron-containing, oxygen-dependent enzymes involved in regioselective introduction of double bonds in fatty acyl aliphatic chains. They play an important role in the maintenance of the proper structure and functioning of biological membranes. Alkane hydroxylases are bacterial, integral-membrane di-iron enzymes that share a requirement for iron and oxygen for activity similar to that of membrane FADSs, and are involved in the initial oxidation of inactivated alkanes. Beta-carotene ketolase and beta-carotene hydroxylase are carotenoid biosynthetic enzymes for astaxanthin and zeaxanthin, respectively. This superfamily domain has extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of these sequences also reveals three regions of conserved histidine cluster motifs that contain eight histidine residues: HXXX(X)H, HXX(X)HH, and HXXHH (an additional conserved histidine residue is seen between clusters 2 and 3). Spectroscopic and genetic evidence point to a nitrogen-rich coordination environment located in the cytoplasm with as many as eight histidines coordinating the two iron ions and a carboxylate residue bridging the two metals in the Pseudomonas oleovorans alkane hydroxylase (AlkB). In addition, the eight histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within the rat stearoyl CoA delta-9 desaturase.


Pssm-ID: 238511 [Multi-domain]  Cd Length: 122  Bit Score: 59.41  E-value: 7.16e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22760516 217 FLLCAVLLSAVQAQAGWLQHDFGHLSVFSTSKWNHLLHHFVIGHLkGAPASWWNHMHFQHHAKPNCFRKDPDI 289
Cdd:cd01060   1 LLLALLLGLLGGLGLTVLAHELGHRSFFRSRWLNRLLGALLGLAL-GGSYGWWRRSHRRHHRYTNTPGKDPDS 72
PRK07003 PRK07003
DNA polymerase III subunits gamma and tau; Validated
3-75 5.79e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 42.53  E-value: 5.79e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22760516    3 TRAARPAglPCGAENPARRRLALGARQQIHSWSPRTPSTRLTAPAGPARGVARPAMAPDPVAAETAAQGPTPR 75
Cdd:PRK07003 530 PEARPPT--PAAAAPAARAGGAAAALDVLRNAGMRVSSDRGARAAAAAKPAAAPAAAPKPAAPRVAVQVPTPR 600
CrtR_beta-carotene-hydroxylase cd03514
Beta-carotene hydroxylase (CrtR), the carotenoid zeaxanthin biosynthetic enzyme catalyzes the ...
202-289 2.76e-03

Beta-carotene hydroxylase (CrtR), the carotenoid zeaxanthin biosynthetic enzyme catalyzes the addition of hydroxyl groups to the beta-ionone rings of beta-carotene to form zeaxanthin and is found in bacteria and red algae. Carotenoids are important natural pigments; zeaxanthin and lutein are the only dietary carotenoids that accumulate in the macular region of the retina and lens. It is proposed that these carotenoids protect ocular tissues against photooxidative damage. CrtR does not show overall amino acid sequence similarity to the beta-carotene hydroxylases similar to CrtZ, an astaxanthin biosynthetic beta-carotene hydroxylase. However, CrtR does show sequence similarity to the green alga, Haematococcus pluvialis, beta-carotene ketolase (CrtW), which converts beta-carotene to canthaxanthin. Sequences of the CrtR_beta-carotene-hydroxylase domain family, as well as, the CrtW_beta-carotene-ketolase domain family appear to be structurally related to membrane fatty acid desaturases and alkane hydroxylases. They all share in common extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of these sequences also reveals three regions of conserved histidine cluster motifs that contain eight histidine residues: HXXXH, HXXHH, and HXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within homologs, stearoyl CoA desaturase and alkane hydroxylase.


Pssm-ID: 239591  Cd Length: 207  Bit Score: 38.89  E-value: 2.76e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760516 202 AAWLTLWVFGTSFLPFLLCAVLLSAVQAQAGWLQHDFGHLSVFSTSKWNHLLHHfVIGHLKGAPASWWNHMHFQHHAKPN 281
Cdd:cd03514   9 LVWLSTWGYVISYLPLWVCFILNTLSLHLAGTVIHDASHKAASRNRWINELIGH-VSAFFLGFPFPVFRRVHMQHHAHTN 87

                ....*...
gi 22760516 282 CFRKDPDI 289
Cdd:cd03514  88 DPEKDPDH 95
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
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