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Conserved domains on  [gi|161077125|ref|NP_001097332|]
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glycerophosphate oxidase 1, isoform D [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DAO super family cl40741
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
9-594 0e+00

FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.


The actual alignment was detected with superfamily member PLN02464:

Pssm-ID: 477422 [Multi-domain]  Cd Length: 627  Bit Score: 718.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125   9 GVTAASACVGSVLAS--YTLDRWNTPhvvnnATVPPKRK-----RTLPPRADQIKSLM---SGEEFDVLIIGGGATGAGC 78
Cdd:PLN02464  12 GAAATAAGGAVYLSPqpASSDKGGGP-----ALDSLRDRiadpnASVPSRSAQESALIgatAAEPLDVLVVGGGATGAGV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125  79 ALDSVTRGLKTALVELDDFASGTSSRSTKLIHGGVRYLQKAILGLDLEQYRMVKEALAERATMLESAPHLTHPLPIMLPV 158
Cdd:PLN02464  87 ALDAATRGLRVGLVEREDFSSGTSSRSTKLIHGGVRYLEKAVFQLDYGQLKLVFHALEERKQLIENAPHLCHALPIMTPC 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 159 YTWWQVPYYWVGIKAYDLVAGDRNVKSSYYLSKKDALELFPMLKKDK----LCGAIVYYDGQQDDARMCLAVALTAARHG 234
Cdd:PLN02464 167 YDWFEVPYYWAGLKAYDLVAGPRLLHLSRYYSAKESLELFPTLAKKGkdgsLKGTVVYYDGQMNDSRLNVALACTAALAG 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 235 ATVCNHVEVKELLkKDDGTGKQVlcGAKVKDHISGKEFTVKAKCIVNAAGPFTDSIRKMDNPTVKSICCPSSGVHIVLPG 314
Cdd:PLN02464 247 AAVLNYAEVVSLI-KDESTGRIV--GARVRDNLTGKEFDVYAKVVVNAAGPFCDEVRKMADGKAKPMICPSSGVHIVLPD 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 315 YYSPDQMGLLDPSTSDGRVIFFLPWQRQTIAGTTDLPCEITHNPTPTEDEIQFILNEIKNYLNadVEVRRGDVLSAWSGI 394
Cdd:PLN02464 324 YYSPEGMGLIVPKTKDGRVVFMLPWLGRTVAGTTDSKTPITMLPEPHEDEIQFILDAISDYLN--VKVRRSDVLSAWSGI 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 395 RPLVSDPNKDDTQSLARNHIVHVSPSNLITIAGGKWTTYRAMAEHTIDAAIKACNLKPERAeAVTSYLKIEGGQGWTPTM 474
Cdd:PLN02464 402 RPLAVDPSAKSTESISRDHVVCEEPDGLVTITGGKWTTYRSMAEDAVDAAIKSGKLSPTNG-CVTTDLPLVGAEGYEPSL 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 475 YIRLVQDF--------------GLECEVAQHLAKSYGDRAFAVSKMASLTGkrwpiIGNRIHPEFPYIDAEIRYGVR-EY 539
Cdd:PLN02464 481 FTQLAQQYvrmkrtyggkvvpgAMDTAAAKHLAHAYGGRADRVAEIAQNEG-----LGKRLAHGYPFLEAEVAYCARhEY 555
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 161077125 540 ACTAVDMIARRLRLAFLNVQAAQEALPVIVDIMGEELGWSKDEKERQIKHATEFL 594
Cdd:PLN02464 556 CESAVDFIARRTRLAFLDTDAAVRALPRVVEILAAEHGWDKSRKKQELQKAKEFL 610
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
624-684 6.16e-13

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


:

Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 64.11  E-value: 6.16e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161077125 624 KRFQLIDKDKKGYVSINDIRRALKSFGDgDVSGEQLHEILREIDTNMNGQVELDEYLQMMS 684
Cdd:cd00051    4 EAFRLFDKDGDGTISADELKAALKSLGE-GLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
 
Name Accession Description Interval E-value
PLN02464 PLN02464
glycerol-3-phosphate dehydrogenase
9-594 0e+00

glycerol-3-phosphate dehydrogenase


Pssm-ID: 215257 [Multi-domain]  Cd Length: 627  Bit Score: 718.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125   9 GVTAASACVGSVLAS--YTLDRWNTPhvvnnATVPPKRK-----RTLPPRADQIKSLM---SGEEFDVLIIGGGATGAGC 78
Cdd:PLN02464  12 GAAATAAGGAVYLSPqpASSDKGGGP-----ALDSLRDRiadpnASVPSRSAQESALIgatAAEPLDVLVVGGGATGAGV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125  79 ALDSVTRGLKTALVELDDFASGTSSRSTKLIHGGVRYLQKAILGLDLEQYRMVKEALAERATMLESAPHLTHPLPIMLPV 158
Cdd:PLN02464  87 ALDAATRGLRVGLVEREDFSSGTSSRSTKLIHGGVRYLEKAVFQLDYGQLKLVFHALEERKQLIENAPHLCHALPIMTPC 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 159 YTWWQVPYYWVGIKAYDLVAGDRNVKSSYYLSKKDALELFPMLKKDK----LCGAIVYYDGQQDDARMCLAVALTAARHG 234
Cdd:PLN02464 167 YDWFEVPYYWAGLKAYDLVAGPRLLHLSRYYSAKESLELFPTLAKKGkdgsLKGTVVYYDGQMNDSRLNVALACTAALAG 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 235 ATVCNHVEVKELLkKDDGTGKQVlcGAKVKDHISGKEFTVKAKCIVNAAGPFTDSIRKMDNPTVKSICCPSSGVHIVLPG 314
Cdd:PLN02464 247 AAVLNYAEVVSLI-KDESTGRIV--GARVRDNLTGKEFDVYAKVVVNAAGPFCDEVRKMADGKAKPMICPSSGVHIVLPD 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 315 YYSPDQMGLLDPSTSDGRVIFFLPWQRQTIAGTTDLPCEITHNPTPTEDEIQFILNEIKNYLNadVEVRRGDVLSAWSGI 394
Cdd:PLN02464 324 YYSPEGMGLIVPKTKDGRVVFMLPWLGRTVAGTTDSKTPITMLPEPHEDEIQFILDAISDYLN--VKVRRSDVLSAWSGI 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 395 RPLVSDPNKDDTQSLARNHIVHVSPSNLITIAGGKWTTYRAMAEHTIDAAIKACNLKPERAeAVTSYLKIEGGQGWTPTM 474
Cdd:PLN02464 402 RPLAVDPSAKSTESISRDHVVCEEPDGLVTITGGKWTTYRSMAEDAVDAAIKSGKLSPTNG-CVTTDLPLVGAEGYEPSL 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 475 YIRLVQDF--------------GLECEVAQHLAKSYGDRAFAVSKMASLTGkrwpiIGNRIHPEFPYIDAEIRYGVR-EY 539
Cdd:PLN02464 481 FTQLAQQYvrmkrtyggkvvpgAMDTAAAKHLAHAYGGRADRVAEIAQNEG-----LGKRLAHGYPFLEAEVAYCARhEY 555
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 161077125 540 ACTAVDMIARRLRLAFLNVQAAQEALPVIVDIMGEELGWSKDEKERQIKHATEFL 594
Cdd:PLN02464 556 CESAVDFIARRTRLAFLDTDAAVRALPRVVEILAAEHGWDKSRKKQELQKAKEFL 610
GlpA COG0578
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ...
80-597 0e+00

Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate dehydrogenase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440343 [Multi-domain]  Cd Length: 501  Bit Score: 577.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125  80 LDSVTRGLKTALVELDDFASGTSSRSTKLIHGGVRYLqkailgldlEQY--RMVKEALAERATMLESAPHLTHPLPIMLP 157
Cdd:COG0578    1 RDAAGRGLSVALVEKGDFASGTSSRSSKLIHGGLRYL---------EQGefRLVREALREREVLLRNAPHLVRPLPFLLP 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 158 VYTWWQVP--YYWVGIKAYDLVAGDRNVKSSYYLSKKDALELFPMLKKDKLCGAIVYYDGQQDDARMCLAVALTAARHGA 235
Cdd:COG0578   72 LYKGGERPawLIRAGLFLYDLLAGRKGLPRHRRLSRAEALALAPLLRPDGLRGGFEYYDAQVDDARLVLELARTAAERGA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 236 TVCNHVEVKELLKKDDGtgkqvLCGAKVKDHISGKEFTVKAKCIVNAAGPFTDSIRKMDNPTVKSICCPSSGVHIVLPGY 315
Cdd:COG0578  152 VVLNYTRVTGLLRDGGR-----VWGVTVRDRLTGEEFTVRARVVVNATGPWVDELRALDGPKAPRRVRPSKGSHLVVPRL 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 316 YSPDQMGLLDPSTSDGRVIFFLPWQRQTIAGTTDLPCE-ITHNPTPTEDEIQFILNEIKNYLnaDVEVRRGDVLSAWSGI 394
Cdd:COG0578  227 FLPLDDALYIFQNTDGRVVFAIPWEGRTLIGTTDTDYDgDPDEPAATEEEIDYLLEAANRYF--ARPLTRDDVVSTYAGV 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 395 RPLVsDPNKDDTQSLARNHIVHVSPSNLITIAGGKWTTYRAMAEHTIDAAIKACNLkpERAEAVTSYLKIEGGQGWTPTM 474
Cdd:COG0578  305 RPLL-DDGGKDTSALSRDHVIEVGPAGLLSIAGGKLTTYRKMAEDAVDAAARLLGL--PRRPCWTADLPLPGGDAGFDAF 381
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 475 YIRLVQDFGLECEVAQHLAKSYGDRAFAVSKMAsltgKRWPIIGNRIHPEFPYIDAEIRYGVR-EYACTAVDMIARRLRL 553
Cdd:COG0578  382 VAALAAAPGLPEALARRLLRRYGTRAEEVLALA----AEDPDLGEPLGPGLPYLEAEVVYAVRhEMARTLEDVLLRRTRL 457
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....
gi 161077125 554 AFLNVQAAQEALPVIVDIMGEELGWSKDEKERQIKHATEFLANE 597
Cdd:COG0578  458 GLLDADAAAAAAPAVAELMAAELGWDDARRAAEVAAYRALLAAY 501
DAO_C pfam16901
C-terminal domain of alpha-glycerophosphate oxidase; DAO_C is the C-terminal region of ...
458-583 1.01e-55

C-terminal domain of alpha-glycerophosphate oxidase; DAO_C is the C-terminal region of alpha-glycerophosphate oxidase.


Pssm-ID: 465305 [Multi-domain]  Cd Length: 126  Bit Score: 186.20  E-value: 1.01e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125  458 VTSYLKIEGGQGWTPTMYIRLVQDFGLECEVAQHLAKSYGDRAFAVSKMASLTGKrwPIIGNRIHPEFPYIDAEIRYGVR 537
Cdd:pfam16901   2 VTKKLPLLGADGYSANLAARLAQRYGLDEEVAEHLARRYGSRADEVLELALADGD--PELGERLSPAYPYIEAEVVYAVR 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 161077125  538 -EYACTAVDMIARRLRLAFLNVQAAQEALPVIVDIMGEELGWSKDEK 583
Cdd:pfam16901  80 hEMALTLVDVLARRTRLAFLDADAALEALPEVADLMAEELGWDEARR 126
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
624-684 6.16e-13

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 64.11  E-value: 6.16e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161077125 624 KRFQLIDKDKKGYVSINDIRRALKSFGDgDVSGEQLHEILREIDTNMNGQVELDEYLQMMS 684
Cdd:cd00051    4 EAFRLFDKDGDGTISADELKAALKSLGE-GLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EF-hand_7 pfam13499
EF-hand domain pair;
616-684 2.08e-12

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 62.66  E-value: 2.08e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125  616 KEEIQTyikRFQLIDKDKKGYVSINDIRRALKSFG-DGDVSGEQLHEILREIDTNMNGQVELDEYLQMMS 684
Cdd:pfam13499   1 EEKLKE---AFKLLDSDGDGYLDVEELKKLLRKLEeGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
613-690 6.90e-09

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 54.80  E-value: 6.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 613 KLSKEEIQTYIKR-------------FQLIDKDKKGYVSINDIRRALKSFGdgdVSGEQLHEILREIDTNMNGQVELDEY 679
Cdd:COG5126   49 RISREEFVAGMESlfeatvepfaraaFDLLDTDGDGKISADEFRRLLTALG---VSEEEADELFARLDTDGDGKISFEEF 125
                         90
                 ....*....|.
gi 161077125 680 LQMMSAIKTGD 690
Cdd:COG5126  126 VAAVRDYYTPD 136
PTZ00184 PTZ00184
calmodulin; Provisional
610-724 3.06e-08

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 53.23  E-value: 3.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 610 IPIKLSKEEIQTYIKRFQLIDKDKKGYVSINDIRRALKSFGDGDVSGEqLHEILREIDTNMNGQVELDEYLQMMsaiktg 689
Cdd:PTZ00184   1 MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAE-LQDMINEVDADGNGTIDFPEFLTLM------ 73
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 161077125 690 dvaySRFARMAELEEQKHEAANLkqisVDRSGGGL 724
Cdd:PTZ00184  74 ----ARKMKDTDSEEEIKEAFKV----FDRDGNGF 100
 
Name Accession Description Interval E-value
PLN02464 PLN02464
glycerol-3-phosphate dehydrogenase
9-594 0e+00

glycerol-3-phosphate dehydrogenase


Pssm-ID: 215257 [Multi-domain]  Cd Length: 627  Bit Score: 718.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125   9 GVTAASACVGSVLAS--YTLDRWNTPhvvnnATVPPKRK-----RTLPPRADQIKSLM---SGEEFDVLIIGGGATGAGC 78
Cdd:PLN02464  12 GAAATAAGGAVYLSPqpASSDKGGGP-----ALDSLRDRiadpnASVPSRSAQESALIgatAAEPLDVLVVGGGATGAGV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125  79 ALDSVTRGLKTALVELDDFASGTSSRSTKLIHGGVRYLQKAILGLDLEQYRMVKEALAERATMLESAPHLTHPLPIMLPV 158
Cdd:PLN02464  87 ALDAATRGLRVGLVEREDFSSGTSSRSTKLIHGGVRYLEKAVFQLDYGQLKLVFHALEERKQLIENAPHLCHALPIMTPC 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 159 YTWWQVPYYWVGIKAYDLVAGDRNVKSSYYLSKKDALELFPMLKKDK----LCGAIVYYDGQQDDARMCLAVALTAARHG 234
Cdd:PLN02464 167 YDWFEVPYYWAGLKAYDLVAGPRLLHLSRYYSAKESLELFPTLAKKGkdgsLKGTVVYYDGQMNDSRLNVALACTAALAG 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 235 ATVCNHVEVKELLkKDDGTGKQVlcGAKVKDHISGKEFTVKAKCIVNAAGPFTDSIRKMDNPTVKSICCPSSGVHIVLPG 314
Cdd:PLN02464 247 AAVLNYAEVVSLI-KDESTGRIV--GARVRDNLTGKEFDVYAKVVVNAAGPFCDEVRKMADGKAKPMICPSSGVHIVLPD 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 315 YYSPDQMGLLDPSTSDGRVIFFLPWQRQTIAGTTDLPCEITHNPTPTEDEIQFILNEIKNYLNadVEVRRGDVLSAWSGI 394
Cdd:PLN02464 324 YYSPEGMGLIVPKTKDGRVVFMLPWLGRTVAGTTDSKTPITMLPEPHEDEIQFILDAISDYLN--VKVRRSDVLSAWSGI 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 395 RPLVSDPNKDDTQSLARNHIVHVSPSNLITIAGGKWTTYRAMAEHTIDAAIKACNLKPERAeAVTSYLKIEGGQGWTPTM 474
Cdd:PLN02464 402 RPLAVDPSAKSTESISRDHVVCEEPDGLVTITGGKWTTYRSMAEDAVDAAIKSGKLSPTNG-CVTTDLPLVGAEGYEPSL 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 475 YIRLVQDF--------------GLECEVAQHLAKSYGDRAFAVSKMASLTGkrwpiIGNRIHPEFPYIDAEIRYGVR-EY 539
Cdd:PLN02464 481 FTQLAQQYvrmkrtyggkvvpgAMDTAAAKHLAHAYGGRADRVAEIAQNEG-----LGKRLAHGYPFLEAEVAYCARhEY 555
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 161077125 540 ACTAVDMIARRLRLAFLNVQAAQEALPVIVDIMGEELGWSKDEKERQIKHATEFL 594
Cdd:PLN02464 556 CESAVDFIARRTRLAFLDTDAAVRALPRVVEILAAEHGWDKSRKKQELQKAKEFL 610
GlpA COG0578
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ...
80-597 0e+00

Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate dehydrogenase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440343 [Multi-domain]  Cd Length: 501  Bit Score: 577.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125  80 LDSVTRGLKTALVELDDFASGTSSRSTKLIHGGVRYLqkailgldlEQY--RMVKEALAERATMLESAPHLTHPLPIMLP 157
Cdd:COG0578    1 RDAAGRGLSVALVEKGDFASGTSSRSSKLIHGGLRYL---------EQGefRLVREALREREVLLRNAPHLVRPLPFLLP 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 158 VYTWWQVP--YYWVGIKAYDLVAGDRNVKSSYYLSKKDALELFPMLKKDKLCGAIVYYDGQQDDARMCLAVALTAARHGA 235
Cdd:COG0578   72 LYKGGERPawLIRAGLFLYDLLAGRKGLPRHRRLSRAEALALAPLLRPDGLRGGFEYYDAQVDDARLVLELARTAAERGA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 236 TVCNHVEVKELLKKDDGtgkqvLCGAKVKDHISGKEFTVKAKCIVNAAGPFTDSIRKMDNPTVKSICCPSSGVHIVLPGY 315
Cdd:COG0578  152 VVLNYTRVTGLLRDGGR-----VWGVTVRDRLTGEEFTVRARVVVNATGPWVDELRALDGPKAPRRVRPSKGSHLVVPRL 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 316 YSPDQMGLLDPSTSDGRVIFFLPWQRQTIAGTTDLPCE-ITHNPTPTEDEIQFILNEIKNYLnaDVEVRRGDVLSAWSGI 394
Cdd:COG0578  227 FLPLDDALYIFQNTDGRVVFAIPWEGRTLIGTTDTDYDgDPDEPAATEEEIDYLLEAANRYF--ARPLTRDDVVSTYAGV 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 395 RPLVsDPNKDDTQSLARNHIVHVSPSNLITIAGGKWTTYRAMAEHTIDAAIKACNLkpERAEAVTSYLKIEGGQGWTPTM 474
Cdd:COG0578  305 RPLL-DDGGKDTSALSRDHVIEVGPAGLLSIAGGKLTTYRKMAEDAVDAAARLLGL--PRRPCWTADLPLPGGDAGFDAF 381
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 475 YIRLVQDFGLECEVAQHLAKSYGDRAFAVSKMAsltgKRWPIIGNRIHPEFPYIDAEIRYGVR-EYACTAVDMIARRLRL 553
Cdd:COG0578  382 VAALAAAPGLPEALARRLLRRYGTRAEEVLALA----AEDPDLGEPLGPGLPYLEAEVVYAVRhEMARTLEDVLLRRTRL 457
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....
gi 161077125 554 AFLNVQAAQEALPVIVDIMGEELGWSKDEKERQIKHATEFLANE 597
Cdd:COG0578  458 GLLDADAAAAAAPAVAELMAAELGWDDARRAAEVAAYRALLAAY 501
glpD PRK12266
glycerol-3-phosphate dehydrogenase; Reviewed
81-565 9.91e-70

glycerol-3-phosphate dehydrogenase; Reviewed


Pssm-ID: 237027 [Multi-domain]  Cd Length: 508  Bit Score: 236.96  E-value: 9.91e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125  81 DSVTRGLKTALVELDDFASGTSSRSTKLIHGGVRYLqkailgldlEQY--RMVKEALAERATMLESAPHLTHPLPIMLPv 158
Cdd:PRK12266  24 DAAGRGLSVLLCEQDDLASATSSASTKLIHGGLRYL---------EHYefRLVREALAEREVLLRMAPHIIWPMRFVLP- 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 159 YTWWQVPYyWVgIKA----YDLVAGDRNVKSSYYLS-KKDALE--LFPMLKKdklcgAIVYYDGQQDDARMCLAVALTAA 231
Cdd:PRK12266  94 HRPHLRPA-WM-IRAglflYDHLGKRKSLPGSRGLDlGRDPAGspLKPEITR-----GFEYSDCWVDDARLVVLNARDAA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 232 RHGATVCNHVEVkELLKKDDGtgkqvLCGAKVKDHISGKEFTVKAKCIVNAAGP----FTDSIRKMDNPT----VKsicc 303
Cdd:PRK12266 167 ERGAEILTRTRV-VSARRENG-----LWHVTLEDTATGKRYTVRARALVNAAGPwvkqFLDDGLGLPSPYgirlVK---- 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 304 pssGVHIVLPGYYSPDQMGLLdpSTSDGRVIFFLPWQRQ-TIAGTTDlpCEITHNPTP---TEDEIQFILNEIKNYLNad 379
Cdd:PRK12266 237 ---GSHIVVPRLFDHDQAYIL--QNPDGRIVFAIPYEDDfTLIGTTD--VEYKGDPAKvaiSEEEIDYLCKVVNRYFK-- 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 380 VEVRRGDVLSAWSGIRPLVSDPNkDDTQSLARNHIVHVSPSN----LITIAGGKWTTYRAMAEHTIDaaiKACNLKPERA 455
Cdd:PRK12266 308 KQLTPADVVWTYSGVRPLCDDES-DSAQAITRDYTLELDDENggapLLSVFGGKITTYRKLAEHALE---KLAPYLPQMG 383
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 456 EAVTSYLKIEGG--QGWTPTMYI-RLVQDF-GLECEVAQHLAKSYGDRAFAV----SKMASLtGKrwpIIGNRIHpefpy 527
Cdd:PRK12266 384 PAWTAGAPLPGGdfPGDRFDALAaALRRRYpWLPEALARRLARAYGTRAERLlggaTSLADL-GE---HFGHGLY----- 454
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 161077125 528 iDAEIRYGV-REYACTAVDMIARRLRLA-FLNvQAAQEAL 565
Cdd:PRK12266 455 -EAEVDYLVeHEWARTAEDILWRRTKLGlRLD-AEQQARL 492
PRK13369 PRK13369
glycerol-3-phosphate dehydrogenase; Provisional
81-564 3.67e-68

glycerol-3-phosphate dehydrogenase; Provisional


Pssm-ID: 237365 [Multi-domain]  Cd Length: 502  Bit Score: 232.55  E-value: 3.67e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125  81 DSVTRGLKTALVELDDFASGTSSRSTKLIHGGVRYlqkailgldLEQY--RMVKEALAERATMLESAPHLTHPLPIMLP- 157
Cdd:PRK13369  24 DAAGRGLKVLLCEKDDLAQGTSSRSGKLVHGGLRY---------LEYYefRLVREALIEREVLLAAAPHIIWPMRFVLPh 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 158 ---VYTWWQVPyywVGIKAYDLVAGDRNVKSSYYLSKKDALELFPMlkKDKLCGAIVYYDGQQDDARMCLAVALTAARHG 234
Cdd:PRK13369  95 speDRPAWLVR---LGLFLYDHLGGRKRLPGTRTLDLRRDPEGAPL--KPEYTKGFEYSDCWVDDARLVVLNALDAAERG 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 235 ATVCNHVEVKELLKKDDgtgkqvLCGAKVKDHiSGKEFTVKAKCIVNAAGPFTDSI-----RKMDNPTVKSIccpsSGVH 309
Cdd:PRK13369 170 ATILTRTRCVSARREGG------LWRVETRDA-DGETRTVRARALVNAAGPWVTDVihrvaGSNSSRNVRLV----KGSH 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 310 IVLPGYYSPDQMGLLdpSTSDGRVIFFLPWQRQ-TIAGTTDLPCE-ITHNPTPTEDEIQFILNEIKNYLNADveVRRGDV 387
Cdd:PRK13369 239 IVVPKFWDGAQAYLF--QNPDKRVIFANPYEGDfTLIGTTDIAYEgDPEDVAADEEEIDYLLDAANRYFKEK--LRREDV 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 388 LSAWSGIRPLVSDpNKDDTQSLARNHIVHVSPSN----LITIAGGKWTTYRAMAEHTIDaaiKACNLKPERAEAVTSYLK 463
Cdd:PRK13369 315 VHSFSGVRPLFDD-GAGNPSAVTRDYVFDLDAETggapLLSVFGGKITTFRKLAEHALE---RLKPFFPQMGGDWTAGAP 390
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 464 IEGGQ-GWTPtmYIRLVQDFG-----LECEVAQHLAKSYGDRAFAVSKMA-SLTGkrwpiIGNRIHPEFpyIDAEIRYGV 536
Cdd:PRK13369 391 LPGGDiANAD--FDTFADDLRdrypwLPRPLAHRYARLYGTRAKDVLGGArSLED-----LGRHFGGGL--TEAEVRYLV 461
                        490       500
                 ....*....|....*....|....*....
gi 161077125 537 -REYACTAVDMIARRLRLAfLNVQAAQEA 564
Cdd:PRK13369 462 aREWARTAEDILWRRTKLG-LHLSAAERA 489
DAO_C pfam16901
C-terminal domain of alpha-glycerophosphate oxidase; DAO_C is the C-terminal region of ...
458-583 1.01e-55

C-terminal domain of alpha-glycerophosphate oxidase; DAO_C is the C-terminal region of alpha-glycerophosphate oxidase.


Pssm-ID: 465305 [Multi-domain]  Cd Length: 126  Bit Score: 186.20  E-value: 1.01e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125  458 VTSYLKIEGGQGWTPTMYIRLVQDFGLECEVAQHLAKSYGDRAFAVSKMASLTGKrwPIIGNRIHPEFPYIDAEIRYGVR 537
Cdd:pfam16901   2 VTKKLPLLGADGYSANLAARLAQRYGLDEEVAEHLARRYGSRADEVLELALADGD--PELGERLSPAYPYIEAEVVYAVR 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 161077125  538 -EYACTAVDMIARRLRLAFLNVQAAQEALPVIVDIMGEELGWSKDEK 583
Cdd:pfam16901  80 hEMALTLVDVLARRTRLAFLDADAALEALPEVADLMAEELGWDEARR 126
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
65-434 3.74e-37

FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 142.15  E-value: 3.74e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125   65 DVLIIGggatgagcaLDSVTRGLKTALVELD-DFASGTSSRSTKLIHGGVRYLQKailgldLEQYRMVKEALAERATML- 142
Cdd:pfam01266   1 DVVVIGggivglstaYELARRGLSVTLLERGdDPGSGASGRNAGLIHPGLRYLEP------SELARLALEALDLWEELEe 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125  143 ESAPHLTHPLPIMLPVYTWWQVPYYWVGIKAYDLVAGDrnvksSYYLSKKDALELFPMLkkDKLCGAIVYYDGQQ-DDAR 221
Cdd:pfam01266  75 ELGIDCGFRRCGVLVLARDEEEEALEKLLAALRRLGVP-----AELLDAEELRELEPLL--PGLRGGLFYPDGGHvDPAR 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125  222 MCLAVALTAARHGATVCNHVEVKELLKKDDGTGkqvlcgakVKDhisgkefTVKAKCIVNAAGPFTDSIRKmdnPTVKSI 301
Cdd:pfam01266 148 LLRALARAAEALGVRIIEGTEVTGIEEEGGVWG--------VVT-------TGEADAVVNAAGAWADLLAL---PGLRLP 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125  302 CCPSSGVHIVLPGYYSPDQMGLLDPSTSDGRVIFFLP-WQRQTIAGTTDLPcEITHNPTPTEDEIQFILNEIKNYLNADV 380
Cdd:pfam01266 210 VRPVRGQVLVLEPLPEALLILPVPITVDPGRGVYLRPrADGRLLLGGTDEE-DGFDDPTPDPEEIEELLEAARRLFPALA 288
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 161077125  381 EVRRgdvlsAWSGIRPLvSDPNKDDTQSLARNHIV---HVSPSNLITIAGGKWTTYR 434
Cdd:pfam01266 289 DIER-----AWAGLRPL-PDGLPIIGRPGSPGLYLatgHGGHGLTLAPGIGKLLAEL 339
glpA PRK11101
anaerobic glycerol-3-phosphate dehydrogenase subunit A;
59-446 6.37e-26

anaerobic glycerol-3-phosphate dehydrogenase subunit A;


Pssm-ID: 236847 [Multi-domain]  Cd Length: 546  Bit Score: 112.80  E-value: 6.37e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125  59 MSGEEFDVLIIGGGATGAGCALDSVTRGLKTALVELDDFASGTSSRSTKLIHGGVRYLQKailglDLEQYRmvkEALAER 138
Cdd:PRK11101   2 RDSQETDVIIIGGGATGAGIARDCALRGLRCILVERHDIATGATGRNHGLLHSGARYAVT-----DAESAR---ECISEN 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 139 ATMLESAPHLTHP---LPIMLPVYTW-WQVPYywvgIKAYDLvAGDRNVKssyyLSKKDALELFPMLKKDkLCGAIVYYD 214
Cdd:PRK11101  74 QILKRIARHCVEPtdgLFITLPEDDLaFQATF----IRACEE-AGIEAEA----IDPQQALILEPAVNPA-LIGAVKVPD 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 215 GQQDDARMCLAVALTAARHGATVCNHVEVKELLKKDDgtgkqVLCGAKVKDHISGKEFTVKAKCIVNAAGPFTDSIRKMD 294
Cdd:PRK11101 144 GTVDPFRLTAANMLDAKEHGAQILTYHEVTGLIREGD-----TVCGVRVRDHLTGETQEIHAPVVVNAAGIWGQHIAEYA 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 295 NPTVKSIccPSSGVHIVLPgyYSPDQMGL---LDPSTSDGRVifflPWQRQTIAGTTD--LPCEITHNPTPTEDEIQFIL 369
Cdd:PRK11101 219 DLRIRMF--PAKGSLLIMD--HRINNHVInrcRKPADADILV----PGDTISLIGTTStrIDYDQIDDNRVTAEEVDILL 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 370 NEIKNYlnADVeVRRGDVLSAWSGIRPLVSDPNKDDTQSLARNhIV---HVSPSNL---ITIAGGKWTTYRAMAEHTIDA 443
Cdd:PRK11101 291 REGEKL--APV-MAKTRILRAYAGVRPLVASDDDPSGRNVSRG-IVlldHAERDGLdgfITITGGKLMTYRLMAEWATDA 366

                 ...
gi 161077125 444 AIK 446
Cdd:PRK11101 367 VCR 369
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
62-400 1.17e-13

Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 73.02  E-value: 1.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125  62 EEFDVLIIGggatgagcaldS-VT----------RGLKTALVELDDFASGTSSRSTklihGGVRYLQKAILGLDLeqYRM 130
Cdd:COG0665    1 ATADVVVIG-----------GgIAglstayhlarRGLDVTVLERGRPGSGASGRNA----GQLRPGLAALADRAL--VRL 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 131 VKEALAERATMLEsaphlTHPLPIMlpvytWWQVPYYWVGIKAYDLVAGDRNVKS-------SYYLSKKDALELFPMLKK 203
Cdd:COG0665   64 AREALDLWRELAA-----ELGIDCD-----FRRTGVLYLARTEAELAALRAEAEAlralglpVELLDAAELREREPGLGS 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 204 DKLCGAIVYYDGQQ-DDARMCLAVALTAARHGATVCNHVEVKELLKKDDGTgKQVLCGAKvkdhisgkefTVKAKCIVNA 282
Cdd:COG0665  134 PDYAGGLYDPDDGHvDPAKLVRALARAARAAGVRIREGTPVTGLEREGGRV-TGVRTERG----------TVRADAVVLA 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 283 AGPFTDSIRKMDNPTVKSIccPSSGVHIVLPgyysPDQMGLLDPSTSDGRViFFLPW--QRQTIAGTTDLPCEithNPTP 360
Cdd:COG0665  203 AGAWSARLLPMLGLRLPLR--PVRGYVLVTE----PLPDLPLRPVLDDTGV-YLRPTadGRLLVGGTAEPAGF---DRAP 272
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 161077125 361 TEDEIQFILNEIKNYLNADVEVRrgdVLSAWSGIRPLVSD 400
Cdd:COG0665  273 TPERLEALLRRLRRLFPALADAE---IVRAWAGLRPMTPD 309
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
624-684 6.16e-13

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 64.11  E-value: 6.16e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161077125 624 KRFQLIDKDKKGYVSINDIRRALKSFGDgDVSGEQLHEILREIDTNMNGQVELDEYLQMMS 684
Cdd:cd00051    4 EAFRLFDKDGDGTISADELKAALKSLGE-GLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EF-hand_7 pfam13499
EF-hand domain pair;
616-684 2.08e-12

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 62.66  E-value: 2.08e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125  616 KEEIQTyikRFQLIDKDKKGYVSINDIRRALKSFG-DGDVSGEQLHEILREIDTNMNGQVELDEYLQMMS 684
Cdd:pfam13499   1 EEKLKE---AFKLLDSDGDGYLDVEELKKLLRKLEeGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
613-690 6.90e-09

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 54.80  E-value: 6.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 613 KLSKEEIQTYIKR-------------FQLIDKDKKGYVSINDIRRALKSFGdgdVSGEQLHEILREIDTNMNGQVELDEY 679
Cdd:COG5126   49 RISREEFVAGMESlfeatvepfaraaFDLLDTDGDGKISADEFRRLLTALG---VSEEEADELFARLDTDGDGKISFEEF 125
                         90
                 ....*....|.
gi 161077125 680 LQMMSAIKTGD 690
Cdd:COG5126  126 VAAVRDYYTPD 136
PTZ00184 PTZ00184
calmodulin; Provisional
610-724 3.06e-08

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 53.23  E-value: 3.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 610 IPIKLSKEEIQTYIKRFQLIDKDKKGYVSINDIRRALKSFGDGDVSGEqLHEILREIDTNMNGQVELDEYLQMMsaiktg 689
Cdd:PTZ00184   1 MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAE-LQDMINEVDADGNGTIDFPEFLTLM------ 73
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 161077125 690 dvaySRFARMAELEEQKHEAANLkqisVDRSGGGL 724
Cdd:PTZ00184  74 ----ARKMKDTDSEEEIKEAFKV----FDRDGNGF 100
PTZ00184 PTZ00184
calmodulin; Provisional
615-683 2.81e-07

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 50.53  E-value: 2.81e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161077125 615 SKEEIqtyIKRFQLIDKDKKGYVSINDIRRALKSFGDgDVSGEQLHEILREIDTNMNGQVELDEYLQMM 683
Cdd:PTZ00184  82 SEEEI---KEAFKVFDRDGNGFISAAELRHVMTNLGE-KLTDEEVDEMIREADVDGDGQINYEEFVKMM 146
PTZ00183 PTZ00183
centrin; Provisional
603-685 1.77e-06

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 48.53  E-value: 1.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 603 NRTSKEripIKLSKEEIQTYIKRFQLIDKDKKGYVSINDIRRALKSFGdGDVSGEQLHEILREIDTNMNGQVELDEYLQM 682
Cdd:PTZ00183   3 KRRSER---PGLTEDQKKEIREAFDLFDTDGSGTIDPKELKVAMRSLG-FEPKKEEIKQMIADVDKDGSGKIDFEEFLDI 78

                 ...
gi 161077125 683 MSA 685
Cdd:PTZ00183  79 MTK 81
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
624-699 1.10e-05

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.55  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 624 KRFQLIDKDKKGYVSINDIRRALKSF-----------GDGDVSGEQLH----------------EILREIDTNMNGQVEL 676
Cdd:COG5126    9 RRFDLLDADGDGVLERDDFEALFRRLwatlfseadtdGDGRISREEFVagmeslfeatvepfarAAFDLLDTDGDGKISA 88
                         90       100
                 ....*....|....*....|....
gi 161077125 677 DEYLQMMSAIKTGD-VAYSRFARM 699
Cdd:COG5126   89 DEFRRLLTALGVSEeEADELFARL 112
EF-hand_8 pfam13833
EF-hand domain pair;
633-683 1.69e-05

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 42.69  E-value: 1.69e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 161077125  633 KKGYVSINDIRRALKSFGDGDVSGEQLHEILREIDTNMNGQVELDEYLQMM 683
Cdd:pfam13833   1 EKGVITREELKRALALLGLKDLSEDEVDILFREFDTDGDGYISFDEFCVLL 51
PTZ00183 PTZ00183
centrin; Provisional
613-683 2.57e-05

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 45.07  E-value: 2.57e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161077125 613 KLSKEEIQtyiKRFQLIDKDKKGYVSINDIRRALKSFGDgDVSGEQLHEILREIDTNMNGQVELDEYLQMM 683
Cdd:PTZ00183  86 RDPREEIL---KAFRLFDDDKTGKISLKNLKRVAKELGE-TITDEELQEMIDEADRNGDGEISEEEFYRIM 152
EF-hand_6 pfam13405
EF-hand domain;
624-650 2.42e-04

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 38.70  E-value: 2.42e-04
                          10        20
                  ....*....|....*....|....*..
gi 161077125  624 KRFQLIDKDKKGYVSINDIRRALKSFG 650
Cdd:pfam13405   4 EAFKLFDKDGDGKISLEELRKALRSLG 30
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
62-404 4.34e-04

L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];


Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 43.21  E-value: 4.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125  62 EEFDVLIIgggatg-agcaldSVTRGLKTALVE-LDDFASGTSSRSTKLIHGGVRY------LQKAILGldleqYRMVKE 133
Cdd:COG0579    3 EMYDVVIIgagivglalarelSRYEDLKVLVLEkEDDVAQESSGNNSGVIHAGLYYtpgslkARLCVEG-----NELFYE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 134 ALAERATMLESAPHL---THPLpimlpvytwwQVPYywvgIKA-YDlvAGDRN-VKSSYYLSKKDALELFPMLKKDKLC- 207
Cdd:COG0579   78 LCRELGIPFKRCGKLvvaTGEE----------EVAF----LEKlYE--RGKANgVPGLEILDREELRELEPLLSDEGVAa 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 208 -----GAIVYYdgqqddARMCLAVALTAARHGATVCNHVEVKELLKKDDGTgkqvlcgaKVKdhISGKEFtvKAKCIVNA 282
Cdd:COG0579  142 lyspsTGIVDP------GALTRALAENAEANGVELLLNTEVTGIEREGDGW--------EVT--TNGGTI--RARFVINA 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 283 AGPFTDSIRKMDNPTVKSICCPSSGVHIVLPGYYS---------PDQ----MG-LLDPsTSDGRVIF-----------FL 337
Cdd:COG0579  204 AGLYADRLAQMAGIGKDFGIFPVKGEYLVLDKPAElvnakvypvPDPgapfLGvHLTR-TIDGNLLFgpnavfvpkkeDS 282
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161077125 338 PWQRQTIAGTTDLPCEITHNPTPTEDEIQ------FILNEIKNYLNadvEVRRGDVLSAWSGIRPLVSDPNKD 404
Cdd:COG0579  283 LLDLFESLRFPNFWPMLAKNLLTKYLESVtslskeAFLEALRKYVP---ELPDEDLIPAFAGIRAQIIKPDGD 352
EFh_parvalbumins cd16253
EF-hand, calcium binding motif, found in parvalbumins; Parvalbumins are small, acidic, ...
614-685 5.16e-04

EF-hand, calcium binding motif, found in parvalbumins; Parvalbumins are small, acidic, cytosolic EF-hand-containing Ca2+-buffer and Ca2+ transporter/shuttle proteins belonging to EF-hand superfamily. They are expressed by vertebrates in fast-twitch muscle cells, specific neurons of the central and peripheral nervous system, sensory cells of the mammalian auditory organ (Corti's cell), and some other cells, and characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Thus, they may play an additional role in Mg2+ handling. Moreover, parvalbumins represent one of the major animal allergens. In metal-bound states, parvalbumins possess a rigid and stable tertiary structure and display strong allergenicity. In contrast, the metal-free parvalbumins are intrinsically disordered, and the loss of metal ions results in a conformational change that decreases their IgE binding capacity. Furthermore, parvalbumins have been widely used as a neuronal marker for a variety of functional brain systems. They also function as a Ca2+ shuttle transporting Ca2+ from troponin-C (TnC) to the sarcoplasmic reticulum (SR) Ca2+ pump during muscle relaxation. Thus they may facilitate myocardial relaxation and play important roles in cardiac diastolic dysfunction. Parvalbumins consists of alpha- and beta- sublineages, which can be distinguished on the basis of isoelectric point (pI > 5 for alpha; pI


Pssm-ID: 319996 [Multi-domain]  Cd Length: 101  Bit Score: 39.85  E-value: 5.16e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161077125 614 LSKEEIQTYIKRFQLIDKDKKGYVSINDIRRALKSFGDG--DVSGEQLHEILREIDTNMNGQVELDEYLQMMSA 685
Cdd:cd16253   28 LSKKSPADIKKVFNILDQDKSGFIEEEELKLFLKNFSDGarVLSDKETKNFLAAGDSDGDGKIGVDEFKSMVKA 101
EFh_parvalbumin_like cd16251
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ...
612-685 1.61e-03

EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes alpha- and beta-parvalbumins, and a group of uncharacterized calglandulin-like proteins. Parvalbumins are small, acidic, cytosolic EF-hand-containing Ca2+-buffer and Ca2+ transporter/shuttle proteins belonging to EF-hand superfamily. They are expressed by vertebrates in fast-twitch muscle cells, specific neurons of the central and peripheral nervous system, sensory cells of the mammalian auditory organ (Corti's cell), and some other cells, and characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Thus, they may play an additional role in Mg2+ handling. Moreover, parvalbumins represent one of the major animal allergens. In metal-bound states, parvalbumins possess a rigid and stable tertiary structure and display strong allergenicity. In contrast, the metal-free parvalbumins are intrinsically disordered, and the loss of metal ions results in a conformational change that decreases their IgE binding capacity. Furthermore, parvalbumins have been widely used as a neuronal marker for a variety of functional brain systems. They also function as a Ca2+ shuttle transporting Ca2+ from troponin-C (TnC) to the sarcoplasmic reticulum (SR) Ca2+ pump during muscle relaxation. Thus they may facilitate myocardial relaxation and play important roles in cardiac diastolic dysfunction. Parvalbumins consists of alpha- and beta- sublineages, which can be distinguished on the basis of isoelectric point (pI > 5 for alpha; pI


Pssm-ID: 319994 [Multi-domain]  Cd Length: 101  Bit Score: 38.67  E-value: 1.61e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161077125 612 IKLSKEEIQTYIKRFQLIDKDKKGYVSINDIRRALKSFG-DG-DVSGEQLHEILREIDTNMNGQVELDEYLQMMSA 685
Cdd:cd16251   26 VGLKQKSEDQIKKVFQILDKDKSGFIEEEELKYILKGFSiAGrDLTDEETKALLAAGDTDGDGKIGVEEFATLVAG 101
EFh_calglandulin_like cd16252
EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The ...
617-682 3.27e-03

EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The family corresponds to a group of uncharacterized calglandulin-like proteins. Although their biological function remain unclear, they show high sequence similarity with human calglandulin-like protein GAGLP, which is an ortholog of calglandulin from the venom glands of Bothrops insularis snake. Both GAGLP and calglandulin are putative Ca2+-binding proteins with four EF-hand motifs. However, members in this family contain only three EF-hand motifs. In this point, they may belong to the parvalbumin-like EF-hand family, which is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix).


Pssm-ID: 319995 [Multi-domain]  Cd Length: 106  Bit Score: 37.90  E-value: 3.27e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161077125 617 EEIQTYIKR-FQLIDKDKKGYVSINDIRRALKSFGDG----DVSGEQLHEILREIDTNMNGQVELDEYLQM 682
Cdd:cd16252   33 EQQEEAIRKaFQMLDKDKSGFIEWNEIKYILSTVPSSmpvaPLSDEEAEAMIQAADTDGDGRIDFQEFSDM 103
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
626-681 4.96e-03

Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds to Group I PEF proteins that have been found not only in higher animals but also in lower animals, plants, fungi and protists. Group I PEF proteins include apoptosis-linked gene 2 protein (ALG-2), peflin and similar proteins. ALG-2, also termed programmed cell death protein 6 (PDCD6), is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination. Peflin is a ubiquitously expressed 30-kD PEF protein containing five EF-hand motifs in its C-terminal domain and a longer N-terminal hydrophobic domain (NHB domain) than any other member of the PEF family. The NHB domain harbors nine repeats of a nonapeptide (A/PPGGPYGGP). Peflin may modulate the function of ALG-2 in Ca2+ signaling. It exists only as a heterodimer with ALG-2, and binds two Ca2+ ions through its EF1 and EF3 hands. Its additional EF5 hand is unpaired and does not bind Ca2+ ion but mediates the heterodimerization with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+.


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 38.28  E-value: 4.96e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 161077125 626 FQLIDKDKKGYVSINDIRRALKSFGDGDVSGEQLHEILREIDTNMNGQVELDEYLQ 681
Cdd:cd16180    6 FQAVDRDRSGRISAKELQRALSNGDWTPFSIETVRLMINMFDRDRSGTINFDEFVG 61
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
626-682 8.83e-03

EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein (ALG-2); The family includes some homologs of mammalian apoptosis-linked gene 2 protein (ALG-2) mainly found in lower eukaryotes, such as a parasitic protist Leishmarua major and a cellular slime mold Dictyostelium discoideum. These homologs contains five EF-hand motifs. Due to the presence of unfavorable residues at the Ca2+-coordinating positions, their non-canonical EF4 and EF5 hands may not bind Ca2+. Two Dictyostelium PEF proteins are the prototypes of this family. They may bind to cytoskeletal proteins and/or signal-transducing proteins localized to detergent-resistant membranes named lipid rafts, and occur as monomers or weak homo- or heterodimers like ALG-2. They can serve as a mediator for Ca2+ signaling-related Dictyostehum programmed cell death (PCD).


Pssm-ID: 320060 [Multi-domain]  Cd Length: 163  Bit Score: 37.58  E-value: 8.83e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161077125 626 FQLIDKDKKGYVSINDIRRALKS----FGDGDVsgEQLheiLREIDTNMNGQVELDEYLQM 682
Cdd:cd16185    6 FRAVDRDRSGSIDVNELQKALAGggllFSLATA--EKL---IRMFDRDGNGTIDFEEFAAL 61
 
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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