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Conserved domains on  [gi|1370477336|ref|XP_024308566|]
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glycerol-3-phosphate dehydrogenase, mitochondrial isoform X1 [Homo sapiens]

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: ...
 1-599 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: 769.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336   1 MAFQKAVK-GTILVGGGALATVLGLSQFAHYRRKQMNlayvkAADCISEPVNR---EPPSREAQLLTLQNTS---EFDIL 73
Cdd:PLN02464    1 MSLARLRRlAAGAAATAAGGAVYLSPQPASSDKGGGP-----ALDSLRDRIADpnaSVPSRSAQESALIGATaaePLDVL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336  74 VIGGGATGSGCALDAVTRGLKTALVERDDFSSGTSSRSTKLIHGGVRYLQKAIMKLDIEQYRMVKEALHERANLLEIAPH 153
Cdd:PLN02464   76 VVGGGATGAGVALDAATRGLRVGLVEREDFSSGTSSRSTKLIHGGVRYLEKAVFQLDYGQLKLVFHALEERKQLIENAPH 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 154 LSAPLPIMLPVYKWWQLPYYWVGIKLYDLVAGSNCLKSSYVLSKSRALEHFPMLQKDK----LVGAIVYYDGQHNDARMN 229
Cdd:PLN02464  156 LCHALPIMTPCYDWFEVPYYWAGLKAYDLVAGPRLLHLSRYYSAKESLELFPTLAKKGkdgsLKGTVVYYDGQMNDSRLN 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 230 LAIALTAARYGAATANYMEVVSLLKktDPQTGkvRVSGARCKDVLTGQEFDVRAKCVINATGPFTDSVRKMDDKDAAAIC 309
Cdd:PLN02464  236 VALACTAALAGAAVLNYAEVVSLIK--DESTG--RIVGARVRDNLTGKEFDVYAKVVVNAAGPFCDEVRKMADGKAKPMI 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 310 QPSAGVHIVMPGYYSPESMGLLDPATSDGRVIFFLPWQKMTIAGTTDTPTDVTHHPIPSEEDINFILNEVRNYLscDVEV 389
Cdd:PLN02464  312 CPSSGVHIVLPDYYSPEGMGLIVPKTKDGRVVFMLPWLGRTVAGTTDSKTPITMLPEPHEDEIQFILDAISDYL--NVKV 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 390 RRGDVLAAWSGIRPLVTDPKSADTQSISRNHVVDISESGLITIAGGKWTTYRSMAEDTINAAVKTHNLK-AGPSRTVGLF 468
Cdd:PLN02464  390 RRSDVLSAWSGIRPLAVDPSAKSTESISRDHVVCEEPDGLVTITGGKWTTYRSMAEDAVDAAIKSGKLSpTNGCVTTDLP 469

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 469 LQGGKDWSPTLYIRLVQDY--------------GLESEVAQHLAATYGDKAFEVAKMASVTGkrwpiVGVRLVSEFPYIE 534
Cdd:PLN02464  470 LVGAEGYEPSLFTQLAQQYvrmkrtyggkvvpgAMDTAAAKHLAHAYGGRADRVAEIAQNEG-----LGKRLAHGYPFLE 544

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370477336 535 AEVKYGIK-EYACTAVDMISRRTRLAFLNVQAAEEALPRIVELMGRELNWDDYKKQEQLETARKFL 599
Cdd:PLN02464  545 AEVAYCARhEYCESAVDFIARRTRLAFLDTDAAVRALPRVVEILAAEHGWDKSRKKQELQKAKEFL 610
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 627-689 5.18e-15

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: 69.88  E-value: 5.18e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370477336 627 RYKKRFHKFDADQKGFITIVDVQRVLESINVQMDENTLHEILNEVDLNKNGQVELNEFLQLMS 689
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
 
Name Accession Description Interval E-value
PLN02464 PLN02464
glycerol-3-phosphate dehydrogenase
 1-599 0e+00

glycerol-3-phosphate dehydrogenase


Pssm-ID: 215257 [Multi-domain]  Cd Length: 627  Bit Score: 769.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336   1 MAFQKAVK-GTILVGGGALATVLGLSQFAHYRRKQMNlayvkAADCISEPVNR---EPPSREAQLLTLQNTS---EFDIL 73
Cdd:PLN02464    1 MSLARLRRlAAGAAATAAGGAVYLSPQPASSDKGGGP-----ALDSLRDRIADpnaSVPSRSAQESALIGATaaePLDVL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336  74 VIGGGATGSGCALDAVTRGLKTALVERDDFSSGTSSRSTKLIHGGVRYLQKAIMKLDIEQYRMVKEALHERANLLEIAPH 153
Cdd:PLN02464   76 VVGGGATGAGVALDAATRGLRVGLVEREDFSSGTSSRSTKLIHGGVRYLEKAVFQLDYGQLKLVFHALEERKQLIENAPH 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 154 LSAPLPIMLPVYKWWQLPYYWVGIKLYDLVAGSNCLKSSYVLSKSRALEHFPMLQKDK----LVGAIVYYDGQHNDARMN 229
Cdd:PLN02464  156 LCHALPIMTPCYDWFEVPYYWAGLKAYDLVAGPRLLHLSRYYSAKESLELFPTLAKKGkdgsLKGTVVYYDGQMNDSRLN 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 230 LAIALTAARYGAATANYMEVVSLLKktDPQTGkvRVSGARCKDVLTGQEFDVRAKCVINATGPFTDSVRKMDDKDAAAIC 309
Cdd:PLN02464  236 VALACTAALAGAAVLNYAEVVSLIK--DESTG--RIVGARVRDNLTGKEFDVYAKVVVNAAGPFCDEVRKMADGKAKPMI 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 310 QPSAGVHIVMPGYYSPESMGLLDPATSDGRVIFFLPWQKMTIAGTTDTPTDVTHHPIPSEEDINFILNEVRNYLscDVEV 389
Cdd:PLN02464  312 CPSSGVHIVLPDYYSPEGMGLIVPKTKDGRVVFMLPWLGRTVAGTTDSKTPITMLPEPHEDEIQFILDAISDYL--NVKV 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 390 RRGDVLAAWSGIRPLVTDPKSADTQSISRNHVVDISESGLITIAGGKWTTYRSMAEDTINAAVKTHNLK-AGPSRTVGLF 468
Cdd:PLN02464  390 RRSDVLSAWSGIRPLAVDPSAKSTESISRDHVVCEEPDGLVTITGGKWTTYRSMAEDAVDAAIKSGKLSpTNGCVTTDLP 469

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 469 LQGGKDWSPTLYIRLVQDY--------------GLESEVAQHLAATYGDKAFEVAKMASVTGkrwpiVGVRLVSEFPYIE 534
Cdd:PLN02464  470 LVGAEGYEPSLFTQLAQQYvrmkrtyggkvvpgAMDTAAAKHLAHAYGGRADRVAEIAQNEG-----LGKRLAHGYPFLE 544

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370477336 535 AEVKYGIK-EYACTAVDMISRRTRLAFLNVQAAEEALPRIVELMGRELNWDDYKKQEQLETARKFL 599
Cdd:PLN02464  545 AEVAYCARhEYCESAVDFIARRTRLAFLDTDAAVRALPRVVEILAAEHGWDKSRKKQELQKAKEFL 610
GlpA COG0578
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ...
 86-599 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: 587.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336  86 LDAVTRGLKTALVERDDFSSGTSSRSTKLIHGGVRYLqkaimkldiEQY--RMVKEALHERANLLEIAPHLSAPLPIMLP 163
Cdd:COG0578     1 RDAAGRGLSVALVEKGDFASGTSSRSSKLIHGGLRYL---------EQGefRLVREALREREVLLRNAPHLVRPLPFLLP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 164 VYKWWQLP--YYWVGIKLYDLVAGSNCLKSSYVLSKSRALEHFPMLQKDKLVGAIVYYDGQHNDARMNLAIALTAARYGA 241
Cdd:COG0578    72 LYKGGERPawLIRAGLFLYDLLAGRKGLPRHRRLSRAEALALAPLLRPDGLRGGFEYYDAQVDDARLVLELARTAAERGA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 242 ATANYMEVVSLLKKTDpqtgkvRVSGARCKDVLTGQEFDVRAKCVINATGPFTDSVRKMDDKDAAAICQPSAGVHIVMPG 321
Cdd:COG0578   152 VVLNYTRVTGLLRDGG------RVWGVTVRDRLTGEEFTVRARVVVNATGPWVDELRALDGPKAPRRVRPSKGSHLVVPR 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 322 YYSPESMGLLDPATSDGRVIFFLPWQKMTIAGTTDTP-TDVTHHPIPSEEDINFILNEVRNYLscDVEVRRGDVLAAWSG 400
Cdd:COG0578   226 LFLPLDDALYIFQNTDGRVVFAIPWEGRTLIGTTDTDyDGDPDEPAATEEEIDYLLEAANRYF--ARPLTRDDVVSTYAG 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 401 IRPLVtDPKSADTQSISRNHVVDISESGLITIAGGKWTTYRSMAEDTINAAVKTHNLKAGPSRTVGLFLQGGKDWSPTLY 480
Cdd:COG0578   304 VRPLL-DDGGKDTSALSRDHVIEVGPAGLLSIAGGKLTTYRKMAEDAVDAAARLLGLPRRPCWTADLPLPGGDAGFDAFV 382

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 481 IRLVQDYGLESEVAQHLAATYGDKAFEVAKMAsvtgKRWPIVGVRLVSEFPYIEAEVKYGIK-EYACTAVDMISRRTRLA 559
Cdd:COG0578   383 AALAAAPGLPEALARRLLRRYGTRAEEVLALA----AEDPDLGEPLGPGLPYLEAEVVYAVRhEMARTLEDVLLRRTRLG 458

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 1370477336 560 FLNVQAAEEALPRIVELMGRELNWDDYKKQEQLETARKFL 599
Cdd:COG0578   459 LLDADAAAAAAPAVAELMAAELGWDDARRAAEVAAYRALL 498
DAO_C pfam16901
C-terminal domain of alpha-glycerophosphate oxidase; DAO_C is the C-terminal region of ...
 462-588 2.31e-54

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: 182.74  E-value: 2.31e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 462 SRTVGLFLQGGKDWSPTLYIRLVQDYGLESEVAQHLAATYGDKAFEVAKMASVTGKrwPIVGVRLVSEFPYIEAEVKYGI 541
Cdd:pfam16901   1 CVTKKLPLLGADGYSANLAARLAQRYGLDEEVAEHLARRYGSRADEVLELALADGD--PELGERLSPAYPYIEAEVVYAV 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1370477336 542 K-EYACTAVDMISRRTRLAFLNVQAAEEALPRIVELMGRELNWDDYKK 588
Cdd:pfam16901  79 RhEMALTLVDVLARRTRLAFLDADAALEALPEVADLMAEELGWDEARR 126
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 627-689 5.18e-15

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: 69.88  E-value: 5.18e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370477336 627 RYKKRFHKFDADQKGFITIVDVQRVLESINVQMDENTLHEILNEVDLNKNGQVELNEFLQLMS 689
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EF-hand_7 pfam13499
EF-hand domain pair;
625-689 1.44e-11

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 60.34  E-value: 1.44e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370477336 625 IDRYKKRFHKFDADQKGFITIVDVQRVLESINVQ--MDENTLHEILNEVDLNKNGQVELNEFLQLMS 689
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGepLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
PTZ00184 PTZ00184
calmodulin; Provisional
 624-689 1.87e-08

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 54.00  E-value: 1.87e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370477336 624 DIDRYKKRFHKFDADQKGFITIVDVQRVLESINVQMDENTLHEILNEVDLNKNGQVELNEFLQLMS 689
Cdd:PTZ00184    9 QIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTLMA 74
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
614-691 7.47e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.94  E-value: 7.47e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370477336 614 DRSEISLLPSDIdrYKKRFHKFDADQKGFITIVDVQRVLESINVQMDENTLHEILNEVDLNKNGQVELNEFLQLMSAI 691
Cdd:COG5126    23 ERDDFEALFRRL--WATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTAL 98
glycerol3P_GlpB TIGR03378
glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are ...
 70-107 1.72e-04

glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are the B subunit, product of the glpB gene, of a three-subunit, membrane-anchored, FAD-dependent anaerobic glycerol-3-phosphate dehydrogenase. [Energy metabolism, Anaerobic]


Pssm-ID: 213807  Cd Length: 419  Bit Score: 44.62  E-value: 1.72e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1370477336  70 FDILVIGGGATGSGCALDAVTRGLKTALVERD----DFSSGT 107
Cdd:TIGR03378   1 FDVIIIGGGLAGLSCALRLAEAGKKCAIIAAGqsalHFSSGS 42
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 664-691 1.40e-03

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 36.59  E-value: 1.40e-03
                           10        20
                   ....*....|....*....|....*...
gi 1370477336  664 LHEILNEVDLNKNGQVELNEFLQLMSAI 691
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
 
Name Accession Description Interval E-value
PLN02464 PLN02464
glycerol-3-phosphate dehydrogenase
 1-599 0e+00

glycerol-3-phosphate dehydrogenase


Pssm-ID: 215257 [Multi-domain]  Cd Length: 627  Bit Score: 769.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336   1 MAFQKAVK-GTILVGGGALATVLGLSQFAHYRRKQMNlayvkAADCISEPVNR---EPPSREAQLLTLQNTS---EFDIL 73
Cdd:PLN02464    1 MSLARLRRlAAGAAATAAGGAVYLSPQPASSDKGGGP-----ALDSLRDRIADpnaSVPSRSAQESALIGATaaePLDVL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336  74 VIGGGATGSGCALDAVTRGLKTALVERDDFSSGTSSRSTKLIHGGVRYLQKAIMKLDIEQYRMVKEALHERANLLEIAPH 153
Cdd:PLN02464   76 VVGGGATGAGVALDAATRGLRVGLVEREDFSSGTSSRSTKLIHGGVRYLEKAVFQLDYGQLKLVFHALEERKQLIENAPH 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 154 LSAPLPIMLPVYKWWQLPYYWVGIKLYDLVAGSNCLKSSYVLSKSRALEHFPMLQKDK----LVGAIVYYDGQHNDARMN 229
Cdd:PLN02464  156 LCHALPIMTPCYDWFEVPYYWAGLKAYDLVAGPRLLHLSRYYSAKESLELFPTLAKKGkdgsLKGTVVYYDGQMNDSRLN 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 230 LAIALTAARYGAATANYMEVVSLLKktDPQTGkvRVSGARCKDVLTGQEFDVRAKCVINATGPFTDSVRKMDDKDAAAIC 309
Cdd:PLN02464  236 VALACTAALAGAAVLNYAEVVSLIK--DESTG--RIVGARVRDNLTGKEFDVYAKVVVNAAGPFCDEVRKMADGKAKPMI 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 310 QPSAGVHIVMPGYYSPESMGLLDPATSDGRVIFFLPWQKMTIAGTTDTPTDVTHHPIPSEEDINFILNEVRNYLscDVEV 389
Cdd:PLN02464  312 CPSSGVHIVLPDYYSPEGMGLIVPKTKDGRVVFMLPWLGRTVAGTTDSKTPITMLPEPHEDEIQFILDAISDYL--NVKV 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 390 RRGDVLAAWSGIRPLVTDPKSADTQSISRNHVVDISESGLITIAGGKWTTYRSMAEDTINAAVKTHNLK-AGPSRTVGLF 468
Cdd:PLN02464  390 RRSDVLSAWSGIRPLAVDPSAKSTESISRDHVVCEEPDGLVTITGGKWTTYRSMAEDAVDAAIKSGKLSpTNGCVTTDLP 469

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 469 LQGGKDWSPTLYIRLVQDY--------------GLESEVAQHLAATYGDKAFEVAKMASVTGkrwpiVGVRLVSEFPYIE 534
Cdd:PLN02464  470 LVGAEGYEPSLFTQLAQQYvrmkrtyggkvvpgAMDTAAAKHLAHAYGGRADRVAEIAQNEG-----LGKRLAHGYPFLE 544

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370477336 535 AEVKYGIK-EYACTAVDMISRRTRLAFLNVQAAEEALPRIVELMGRELNWDDYKKQEQLETARKFL 599
Cdd:PLN02464  545 AEVAYCARhEYCESAVDFIARRTRLAFLDTDAAVRALPRVVEILAAEHGWDKSRKKQELQKAKEFL 610
GlpA COG0578
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ...
 86-599 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: 587.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336  86 LDAVTRGLKTALVERDDFSSGTSSRSTKLIHGGVRYLqkaimkldiEQY--RMVKEALHERANLLEIAPHLSAPLPIMLP 163
Cdd:COG0578     1 RDAAGRGLSVALVEKGDFASGTSSRSSKLIHGGLRYL---------EQGefRLVREALREREVLLRNAPHLVRPLPFLLP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 164 VYKWWQLP--YYWVGIKLYDLVAGSNCLKSSYVLSKSRALEHFPMLQKDKLVGAIVYYDGQHNDARMNLAIALTAARYGA 241
Cdd:COG0578    72 LYKGGERPawLIRAGLFLYDLLAGRKGLPRHRRLSRAEALALAPLLRPDGLRGGFEYYDAQVDDARLVLELARTAAERGA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 242 ATANYMEVVSLLKKTDpqtgkvRVSGARCKDVLTGQEFDVRAKCVINATGPFTDSVRKMDDKDAAAICQPSAGVHIVMPG 321
Cdd:COG0578   152 VVLNYTRVTGLLRDGG------RVWGVTVRDRLTGEEFTVRARVVVNATGPWVDELRALDGPKAPRRVRPSKGSHLVVPR 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 322 YYSPESMGLLDPATSDGRVIFFLPWQKMTIAGTTDTP-TDVTHHPIPSEEDINFILNEVRNYLscDVEVRRGDVLAAWSG 400
Cdd:COG0578   226 LFLPLDDALYIFQNTDGRVVFAIPWEGRTLIGTTDTDyDGDPDEPAATEEEIDYLLEAANRYF--ARPLTRDDVVSTYAG 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 401 IRPLVtDPKSADTQSISRNHVVDISESGLITIAGGKWTTYRSMAEDTINAAVKTHNLKAGPSRTVGLFLQGGKDWSPTLY 480
Cdd:COG0578   304 VRPLL-DDGGKDTSALSRDHVIEVGPAGLLSIAGGKLTTYRKMAEDAVDAAARLLGLPRRPCWTADLPLPGGDAGFDAFV 382

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 481 IRLVQDYGLESEVAQHLAATYGDKAFEVAKMAsvtgKRWPIVGVRLVSEFPYIEAEVKYGIK-EYACTAVDMISRRTRLA 559
Cdd:COG0578   383 AALAAAPGLPEALARRLLRRYGTRAEEVLALA----AEDPDLGEPLGPGLPYLEAEVVYAVRhEMARTLEDVLLRRTRLG 458

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 1370477336 560 FLNVQAAEEALPRIVELMGRELNWDDYKKQEQLETARKFL 599
Cdd:COG0578   459 LLDADAAAAAAPAVAELMAAELGWDDARRAAEVAAYRALL 498
glpD PRK12266
glycerol-3-phosphate dehydrogenase; Reviewed
 66-569 5.68e-84

glycerol-3-phosphate dehydrogenase; Reviewed


Pssm-ID: 237027 [Multi-domain]  Cd Length: 508  Bit Score: 275.10  E-value: 5.68e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336  66 NTSEFDILVIGGGATGSGCALDAVTRGLKTALVERDDFSSGTSSRSTKLIHGGVRYLqkaimkldiEQY--RMVKEALHE 143
Cdd:PRK12266    3 MMETYDLLVIGGGINGAGIARDAAGRGLSVLLCEQDDLASATSSASTKLIHGGLRYL---------EHYefRLVREALAE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 144 RANLLEIAPHLSAPLPIMLPVYKW----WQLPyywVGIKLYDLVAGSNCLKSSYVLSKSRALEHFPMlqKDKLVGAIVYY 219
Cdd:PRK12266   74 REVLLRMAPHIIWPMRFVLPHRPHlrpaWMIR---AGLFLYDHLGKRKSLPGSRGLDLGRDPAGSPL--KPEITRGFEYS 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 220 DGQHNDARMNLAIALTAARYGAATANYMEVVSLlkktdpqtgkVRVSG---ARCKDVLTGQEFDVRAKCVINATGPFTDS 296
Cdd:PRK12266  149 DCWVDDARLVVLNARDAAERGAEILTRTRVVSA----------RRENGlwhVTLEDTATGKRYTVRARALVNAAGPWVKQ 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 297 V--RKMDDKDAAAI--CQpsaGVHIVMPGYYS-PESMGLLDPatsDGRVIFFLPWQ-KMTIAGTTDT-----PTDVThhp 365
Cdd:PRK12266  219 FldDGLGLPSPYGIrlVK---GSHIVVPRLFDhDQAYILQNP---DGRIVFAIPYEdDFTLIGTTDVeykgdPAKVA--- 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 366 IpSEEDINFILNEVRNYLscDVEVRRGDVLAAWSGIRPLVTDpKSADTQSISRNHVVDISESG----LITIAGGKWTTYR 441
Cdd:PRK12266  290 I-SEEEIDYLCKVVNRYF--KKQLTPADVVWTYSGVRPLCDD-ESDSAQAITRDYTLELDDENggapLLSVFGGKITTYR 365

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 442 SMAEDTINaAVKTHNLKAGPSRTVGLFLQGGkDWSPTLYIRLVQDY-----GLESEVAQHLAATYGDKAFEVAKMASVTG 516
Cdd:PRK12266  366 KLAEHALE-KLAPYLPQMGPAWTAGAPLPGG-DFPGDRFDALAAALrrrypWLPEALARRLARAYGTRAERLLGGATSLA 443

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370477336 517 KRWPIVGVRLvsefpYiEAEVKYGIK-EYACTAVDMISRRTRLAfLNVQAAEEA 569
Cdd:PRK12266  444 DLGEHFGHGL-----Y-EAEVDYLVEhEWARTAEDILWRRTKLG-LRLDAEQQA 490
PRK13369 PRK13369
glycerol-3-phosphate dehydrogenase; Provisional
 67-569 1.42e-79

glycerol-3-phosphate dehydrogenase; Provisional


Pssm-ID: 237365 [Multi-domain]  Cd Length: 502  Bit Score: 262.98  E-value: 1.42e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336  67 TSEFDILVIGGGATGSGCALDAVTRGLKTALVERDDFSSGTSSRSTKLIHGGVRYLqkaimkldiEQY--RMVKEALHER 144
Cdd:PRK13369    4 PETYDLFVIGGGINGAGIARDAAGRGLKVLLCEKDDLAQGTSSRSGKLVHGGLRYL---------EYYefRLVREALIER 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 145 ANLLEIAPHLSAPLPIMLPVYK----WWQLPyywVGIKLYDLVAGSNCLKSSYVLSKSRALEHFPMlqKDKLVGAIVYYD 220
Cdd:PRK13369   75 EVLLAAAPHIIWPMRFVLPHSPedrpAWLVR---LGLFLYDHLGGRKRLPGTRTLDLRRDPEGAPL--KPEYTKGFEYSD 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 221 GQHNDARMNLAIALTAARYGAATANYMEVVSLLKKTDpqTGKVRVSGARckdvltGQEFDVRAKCVINATGPFTDSVrkm 300
Cdd:PRK13369  150 CWVDDARLVVLNALDAAERGATILTRTRCVSARREGG--LWRVETRDAD------GETRTVRARALVNAAGPWVTDV--- 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 301 ddKDAAAICQPSAGV------HIVMPGYYSPESMGLLDpaTSDGRVIFFLPWQK-MTIAGTTDT-----PTDVThhpiPS 368
Cdd:PRK13369  219 --IHRVAGSNSSRNVrlvkgsHIVVPKFWDGAQAYLFQ--NPDKRVIFANPYEGdFTLIGTTDIayegdPEDVA----AD 290

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 369 EEDINFILNEVRNYLScdVEVRRGDVLAAWSGIRPLVTDpKSADTQSISRNHVVDISESG----LITIAGGKWTTYRSMA 444
Cdd:PRK13369  291 EEEIDYLLDAANRYFK--EKLRREDVVHSFSGVRPLFDD-GAGNPSAVTRDYVFDLDAETggapLLSVFGGKITTFRKLA 367

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 445 EDTINaAVKTHNLKAGPSRTVGLFLQGGkDWSPTLYIRLVQDYG-----LESEVAQHLAATYGDKAFEVAKMASVTGKRW 519
Cdd:PRK13369  368 EHALE-RLKPFFPQMGGDWTAGAPLPGG-DIANADFDTFADDLRdrypwLPRPLAHRYARLYGTRAKDVLGGARSLEDLG 445

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370477336 520 PIVGVRLVsefpyiEAEVKYGI-KEYACTAVDMISRRTRLAfLNVQAAEEA 569
Cdd:PRK13369  446 RHFGGGLT------EAEVRYLVaREWARTAEDILWRRTKLG-LHLSAAERA 489
DAO_C pfam16901
C-terminal domain of alpha-glycerophosphate oxidase; DAO_C is the C-terminal region of ...
 462-588 2.31e-54

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: 182.74  E-value: 2.31e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 462 SRTVGLFLQGGKDWSPTLYIRLVQDYGLESEVAQHLAATYGDKAFEVAKMASVTGKrwPIVGVRLVSEFPYIEAEVKYGI 541
Cdd:pfam16901   1 CVTKKLPLLGADGYSANLAARLAQRYGLDEEVAEHLARRYGSRADEVLELALADGD--PELGERLSPAYPYIEAEVVYAV 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1370477336 542 K-EYACTAVDMISRRTRLAFLNVQAAEEALPRIVELMGRELNWDDYKK 588
Cdd:pfam16901  79 RhEMALTLVDVLARRTRLAFLDADAALEALPEVADLMAEELGWDEARR 126
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 71-441 8.23e-46

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: 166.80  E-value: 8.23e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336  71 DILVIGGGATGSGCALDAVTRGLKTALVERD-DFSSGTSSRSTKLIHGGVRYLQKAimkldiEQYRMVKEALHERANLLE 149
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGdDPGSGASGRNAGLIHPGLRYLEPS------ELARLALEALDLWEELEE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 150 I-APHLSAPLPIMLPVYKWWQLPYYwvgIKLYDLVAGSNClkSSYVLSKSRALEHFPMLqkDKLVGAIVYYDGQH-NDAR 227
Cdd:pfam01266  75 ElGIDCGFRRCGVLVLARDEEEEAL---EKLLAALRRLGV--PAELLDAEELRELEPLL--PGLRGGLFYPDGGHvDPAR 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 228 MNLAIALTAARYGAATANYMEVVSLLKKTDPQTgkVRVSGarckdvltgqefdvRAKCVINATGPFTDSVRKMDDKdaaA 307
Cdd:pfam01266 148 LLRALARAAEALGVRIIEGTEVTGIEEEGGVWG--VVTTG--------------EADAVVNAAGAWADLLALPGLR---L 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 308 ICQPSAGVHIVMPGYYSPESMGLLDPATSDGRVIFFLPWQK-MTIAGTTDTPTDvTHHPIPSEEDINFILNEVRNYLScd 386
Cdd:pfam01266 209 PVRPVRGQVLVLEPLPEALLILPVPITVDPGRGVYLRPRADgRLLLGGTDEEDG-FDDPTPDPEEIEELLEAARRLFP-- 285

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370477336 387 vevRRGDVLAAWSGIRPLvTDPKSADTQSISRNHVVD--ISESGLITIAG-GKWTTYR 441
Cdd:pfam01266 286 ---ALADIERAWAGLRPL-PDGLPIIGRPGSPGLYLAtgHGGHGLTLAPGiGKLLAEL 339
glpA PRK11101
anaerobic glycerol-3-phosphate dehydrogenase subunit A;
69-558 2.88e-35

anaerobic glycerol-3-phosphate dehydrogenase subunit A;


Pssm-ID: 236847 [Multi-domain]  Cd Length: 546  Bit Score: 140.92  E-value: 2.88e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336  69 EFDILVIGGGATGSGCALDAVTRGLKTALVERDDFSSGTSSRSTKLIHGGVRYLQKaimklDIEQYRmvkEALHERANLL 148
Cdd:PRK11101    6 ETDVIIIGGGATGAGIARDCALRGLRCILVERHDIATGATGRNHGLLHSGARYAVT-----DAESAR---ECISENQILK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 149 EIAPHLSAP---LPIMLPVYkwwQLPYYWVGIKLYDLvAGSNCLKssyvLSKSRALEHFPMLQKDkLVGAIVYYDGQHND 225
Cdd:PRK11101   78 RIARHCVEPtdgLFITLPED---DLAFQATFIRACEE-AGIEAEA----IDPQQALILEPAVNPA-LIGAVKVPDGTVDP 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 226 ARMNLAIALTAARYGAATANYMEVVSLLKKTDpqtgkvRVSGARCKDVLTGQEFDVRAKCVINATGPFtdsvrkmddkdA 305
Cdd:PRK11101  149 FRLTAANMLDAKEHGAQILTYHEVTGLIREGD------TVCGVRVRDHLTGETQEIHAPVVVNAAGIW-----------G 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 306 AAICQpSAGVHIVMpgYYSPESMGLLD-------------PATSDGRVifflPWQKMTIAGTTDT--PTDVTHHPIPSEE 370
Cdd:PRK11101  212 QHIAE-YADLRIRM--FPAKGSLLIMDhrinnhvinrcrkPADADILV----PGDTISLIGTTSTriDYDQIDDNRVTAE 284

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 371 DINFILNEVRNYLSCdveVRRGDVLAAWSGIRPLVTDPKSADTQSISRNHV-VDISE----SGLITIAGGKWTTYRSMAE 445
Cdd:PRK11101  285 EVDILLREGEKLAPV---MAKTRILRAYAGVRPLVASDDDPSGRNVSRGIVlLDHAErdglDGFITITGGKLMTYRLMAE 361

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 446 DTINAAVKTHNlKAGPSRTVGLFLQGGKDWSPTLYIRLVqdyGLESEVAQHLAATYGDKAFEVakmasVTGKRwpiVGVR 525
Cdd:PRK11101  362 WATDAVCRKLG-NTRPCTTADTPLPGSQEPAEVTLRKVI---SLPAPLRGSAVYRHGDRAPAW-----LSEGR---LDRS 429

                         490       500       510
                  ....*....|....*....|....*....|....*
gi 1370477336 526 LVSEFPYIEA-EVKYGIKEYAC-TAVDMiSRRTRL 558
Cdd:PRK11101  430 LVCECEAVTAgEVRYAVENLNVnNLLDL-RRRTRV 463
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
69-407 1.64e-20

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 93.82  E-value: 1.64e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336  69 EFDILVIGGGATGSGCALDAVTRGLKTALVERDDFSSGTSSRSTklihGGVRYLQKAIMklDIEQYRMVKEALHEranLL 148
Cdd:COG0665     2 TADVVVIGGGIAGLSTAYHLARRGLDVTVLERGRPGSGASGRNA----GQLRPGLAALA--DRALVRLAREALDL---WR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 149 EIAPHLSAPLPimlpvykWWQLPYYWVGIK---LYDLVAGSNCLKS----SYVLSKSRALEHFPMLQKDKLVGAIVYydg 221
Cdd:COG0665    73 ELAAELGIDCD-------FRRTGVLYLARTeaeLAALRAEAEALRAlglpVELLDAAELREREPGLGSPDYAGGLYD--- 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 222 qHNDARMN-----LAIALTAARYGAATANYMEVVSLlkktdpqtgkvRVSGARCKDVLTGQEfDVRAKCVINATGPFTDS 296
Cdd:COG0665   143 -PDDGHVDpaklvRALARAARAAGVRIREGTPVTGL-----------EREGGRVTGVRTERG-TVRADAVVLAAGAWSAR 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 297 VRKMDDKDAAAicQPSAGVHIVMPgyysPESMGLLDPATSDGRVIFFLPWQKMTIAGTTDTPTDvtHHPIPSEEDINFIL 376
Cdd:COG0665   210 LLPMLGLRLPL--RPVRGYVLVTE----PLPDLPLRPVLDDTGVYLRPTADGRLLVGGTAEPAG--FDRAPTPERLEALL 281

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1370477336 377 NEVRNYL--SCDVEVRRgdvlaAWSGIRPLVTD 407
Cdd:COG0665   282 RRLRRLFpaLADAEIVR-----AWAGLRPMTPD 309
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 627-689 5.18e-15

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: 69.88  E-value: 5.18e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370477336 627 RYKKRFHKFDADQKGFITIVDVQRVLESINVQMDENTLHEILNEVDLNKNGQVELNEFLQLMS 689
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EF-hand_7 pfam13499
EF-hand domain pair;
625-689 1.44e-11

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 60.34  E-value: 1.44e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370477336 625 IDRYKKRFHKFDADQKGFITIVDVQRVLESINVQ--MDENTLHEILNEVDLNKNGQVELNEFLQLMS 689
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGepLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
PTZ00184 PTZ00184
calmodulin; Provisional
 624-689 1.87e-08

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 54.00  E-value: 1.87e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370477336 624 DIDRYKKRFHKFDADQKGFITIVDVQRVLESINVQMDENTLHEILNEVDLNKNGQVELNEFLQLMS 689
Cdd:PTZ00184    9 QIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTLMA 74
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
 69-291 2.09e-08

Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440673 [Multi-domain]  Cd Length: 443  Bit Score: 57.15  E-value: 2.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336  69 EFDILVIGGGATGSGCALDAVTRGLKTALVERDDFSSGTSSRSTklihGGVR----YLQKAIMKLDIEQYR--MVKEAlH 142
Cdd:COG1053     3 EYDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGGHTAAAQ----GGINaagtNVQKAAGEDSPEEHFydTVKGG-D 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 143 ERAN------LLEIAPhlsaplpimlPVYKW---WQLPYYWVGIKLYDLVAGSnclkssyvlSKSRAleHFPMLQKdklv 213
Cdd:COG1053    78 GLADqdlveaLAEEAP----------EAIDWleaQGVPFSRTPDGRLPQFGGH---------SVGRT--CYAGDGT---- 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 214 gaivyydGQHndarmnLAIAL--TAARYGAATANYMEVVSLLKKTDpqtgkvRVSGARCKDVlTGQEFDVRAKCVINATG 291
Cdd:COG1053   133 -------GHA------LLATLyqAALRLGVEIFTETEVLDLIVDDG------RVVGVVARDR-TGEIVRIRAKAVVLATG 192
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
 629-686 1.08e-07

EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta isozymes represent a class of metazoan PI-PLCs that are some of the most sensitive to calcium among all PLCs. Their activation is modulated by intracellular calcium ion concentration, phospholipids, polyamines, and other proteins, such as RhoAGAP. Like other PI-PLC isozymes, PI-PLC-delta isozymes contain a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C-terminal C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are three PI-PLC-delta isozymes (1, 3 and 4). PI-PLC-delta1 is relatively well characterized. It is activated by high calcium levels generated by other PI-PLC family members, and therefore functions as a calcium amplifier within the cell. Different PI-PLC-delta isozymes have different tissue distribution and different subcellular locations. PI-PLC-delta1 is mostly a cytoplasmic protein, PI-PLC-delta3 is located in the membrane, and PI-PLC-delta4 is predominantly detected in the cell nucleus. PI-PLC-delta isozymes is evolutionarily conserved even in non-mammalian species, such as yeast, slime molds and plants.


Pssm-ID: 320032 [Multi-domain]  Cd Length: 140  Bit Score: 51.46  E-value: 1.08e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370477336 629 KKRFHKFDADQKGFITIVDVQRVLESINVQMDENTLHEILNEVDLNKNGQVELNEFLQ 686
Cdd:cd16202     3 KDQFRKADKNGDGKLSFKECKKLLKKLNVKVDKDYAKKLFQEADTSGEDVLDEEEFVQ 60
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 627-692 2.67e-07

EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) isozymes; PI-PLC isozymes are signaling enzymes that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. This family corresponds to the four EF-hand motifs containing PI-PLC isozymes, including PI-PLC-beta (1-4), -gamma (1-2), -delta (1,3,4), -epsilon (1), -zeta (1), eta (1-2). Lower eukaryotes such as yeast and slime molds contain only delta-type isozymes. In contrast, other types of isoforms present in higher eukaryotes. This family also includes 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1 (PLC1) from fungi. Some homologs from plants contain only two atypical EF-hand motifs and they are not included. All PI-PLC isozymes except sperm-specific PI-PLC-zeta share a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. PI-PLC-zeta lacks the PH domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Most of EF-hand motifs found in PI-PLCs consist of a helix-loop-helix structure, but lack residues critical to metal binding. Moreover, the EF-hand region of most of PI-PLCs may have an important regulatory function, but it has yet to be identified. However, PI-PLC-zeta is a key exception. It is responsible for Ca2+ oscillations in fertilized oocytes and exhibits a high sensitivity to Ca2+ mediated through its EF-hand domain. In addition, PI-PLC-eta2 shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Also it appears that PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. PI-PLCs can be activated by a variety of extracellular ligands, such as growth factors, hormones, cytokines and lipids. Their activation has been implicated in tumorigenesis and/or metastasis linked to migration, proliferation, growth, inflammation, angiogenesis and actin cytoskeleton reorganization. PI-PLC-beta isozymes are activated by G-protein coupled receptor (GPCR) through different mechanisms. However, PI-PLC-gamma isozymes are activated by receptor tyrosine kinase (RTK), such as Rho and Ras GTPases. In contrast, PI-PLC-epsilon are activated by both GPCR and RTK. PI-PLC-delta1 and PLC-eta 1 are activated by GPCR-mediated calcium mobilization. The activation mechanism for PI-PLC-zeta remains unclear.


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 50.36  E-value: 2.67e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370477336 627 RYKKRFHKFDADQKGFITIVDVQRVLESINVQMDENTLHEILNEVDLNKNGQVELNEFLQLMSAIQ 692
Cdd:cd15898     1 WLRRQWIKADKDGDGKLSLKEIKKLLKRLNIRVSEKELKKLFKEVDTNGDGTLTFDEFEELYKSLT 66
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 69-102 1.84e-06

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 50.91  E-value: 1.84e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1370477336  69 EFDILVIGGGATGSGCALDAVTRGLKTALVERDD 102
Cdd:PRK06416    4 EYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEKEK 37
PTZ00184 PTZ00184
calmodulin; Provisional
 626-688 2.28e-06

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 47.83  E-value: 2.28e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370477336 626 DRYKKRFHKFDADQKGFITIVDVQRVLESINVQMDENTLHEILNEVDLNKNGQVELNEFLQLM 688
Cdd:PTZ00184   84 EEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKMM 146
PRK12843 PRK12843
FAD-dependent oxidoreductase;
59-111 2.43e-06

FAD-dependent oxidoreductase;


Pssm-ID: 237225 [Multi-domain]  Cd Length: 578  Bit Score: 50.89  E-value: 2.43e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370477336  59 AQLLTLQNTSEFDILVIGGGATGSGCALDAVTRGLKTALVERDDFSSGTSSRS 111
Cdd:PRK12843    6 SELSPERWDAEFDVIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGGTTATS 58
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
614-691 7.47e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.94  E-value: 7.47e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370477336 614 DRSEISLLPSDIdrYKKRFHKFDADQKGFITIVDVQRVLESINVQMDENTLHEILNEVDLNKNGQVELNEFLQLMSAI 691
Cdd:COG5126    23 ERDDFEALFRRL--WATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTAL 98
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
626-688 7.47e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.94  E-value: 7.47e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370477336 626 DRYKKRFHKFDADQKGFITIVDVQRVLESINVQMDEntLHEILNEVDLNKNGQVELNEFLQLM 688
Cdd:COG5126    69 PFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEE--ADELFARLDTDGDGKISFEEFVAAV 129
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
66-435 8.32e-06

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


Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 48.99  E-value: 8.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336  66 NTSEFDILVIGGGATGSGCALdAVTR--GLKTALVER-DDFSSGTSSRSTKLIHGGVRY----LqKAimKLDIEQYRMVK 138
Cdd:COG0579     1 MMEMYDVVIIGAGIVGLALAR-ELSRyeDLKVLVLEKeDDVAQESSGNNSGVIHAGLYYtpgsL-KA--RLCVEGNELFY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 139 EALHERANLLEIAPHLS-----APLPIMLpvykwwqlpyywvgiKLYDlvAGS-NCLKSSYVLSKSRALEHFPMLQKDKL 212
Cdd:COG0579    77 ELCRELGIPFKRCGKLVvatgeEEVAFLE---------------KLYE--RGKaNGVPGLEILDREELRELEPLLSDEGV 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 213 V------GAIVYYdgqhndARMNLAIALTAARYGAATANYMEVVSLLKKTDpqtgKVRVSgarckdvlTGQEfDVRAKCV 286
Cdd:COG0579   140 AalyspsTGIVDP------GALTRALAENAEANGVELLLNTEVTGIEREGD----GWEVT--------TNGG-TIRARFV 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 287 INATGPFTDSV-RKMDDKDAAAI---------CQPSAGV--HIV--MPGYYSPeSMG-LLDPaTSDGRVIF-----FLPW 346
Cdd:COG0579   201 INAAGLYADRLaQMAGIGKDFGIfpvkgeylvLDKPAELvnAKVypVPDPGAP-FLGvHLTR-TIDGNLLFgpnavFVPK 278

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336 347 QKMTIagtTDTPTDVTHHPIPS---------------EEDINFILNEVRNYLScdvEVRRGDVLAAWSGIRPlvtdpksa 411
Cdd:COG0579   279 KEDSL---LDLFESLRFPNFWPmlaknlltkylesvtSLSKEAFLEALRKYVP---ELPDEDLIPAFAGIRA-------- 344

                         410       420
                  ....*....|....*....|....*..
gi 1370477336 412 dtQSISRNH--VVDISES-GLITIAGG 435
Cdd:COG0579   345 --QIIKPDGdfVIEEADDpGSIHVLGI 369
FAD_oxidored pfam12831
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ...
 71-109 1.93e-05

FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.


Pssm-ID: 432816 [Multi-domain]  Cd Length: 420  Bit Score: 47.60  E-value: 1.93e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1370477336  71 DILVIGGGATGSGCALDAVTRGLKTALVERDDFSSGTSS 109
Cdd:pfam12831   1 DVVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGMLT 39
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 69-103 2.40e-05

Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation


Pssm-ID: 440861 [Multi-domain]  Cd Length: 456  Bit Score: 47.39  E-value: 2.40e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1370477336  69 EFDILVIGGGATGSGCALDAVTRGLKTALVERDDF 103
Cdd:COG1249     3 DYDLVVIGAGPGGYVAAIRAAQLGLKVALVEKGRL 37
GlpB COG3075
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];
69-107 3.28e-05

Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];


Pssm-ID: 442309  Cd Length: 415  Bit Score: 47.10  E-value: 3.28e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1370477336  69 EFDILVIGGGATGSGCALDAVTRGLKTALVERD----DFSSGT 107
Cdd:COG3075     2 KFDVVVIGGGLAGLTAAIRAAEAGLRVAIVSAGqsalHFSSGS 44
PRK06134 PRK06134
putative FAD-binding dehydrogenase; Reviewed
 54-156 1.02e-04

putative FAD-binding dehydrogenase; Reviewed


Pssm-ID: 180419 [Multi-domain]  Cd Length: 581  Bit Score: 45.48  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336  54 PPSREAQLLTLqntsEFDILVIGGGATGSGCALDAVTRGLKTALVERDDFSSGTSSRStklihGGVRYL------QKAIM 127
Cdd:PRK06134    1 TPSAAAYPPDL----ECDVLVIGSGAAGLSAAVTAAWHGLKVIVVEKDPVFGGTTAWS-----GGWMWIprnplaRRAGI 71

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1370477336 128 KLDIEQYRM-VKEALHERAN------LLEIAPHLSA 156
Cdd:PRK06134   72 VEDIEQPRTyLRHELGARYDaaridaFLEAGPHMVA 107
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
 71-111 1.55e-04

FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.


Pssm-ID: 395718 [Multi-domain]  Cd Length: 398  Bit Score: 44.59  E-value: 1.55e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1370477336  71 DILVIGGGATGSGCALDAVTRGLKTALVERDDFSSGTSSRS 111
Cdd:pfam00890   1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGATAWS 41
glycerol3P_GlpB TIGR03378
glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are ...
 70-107 1.72e-04

glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are the B subunit, product of the glpB gene, of a three-subunit, membrane-anchored, FAD-dependent anaerobic glycerol-3-phosphate dehydrogenase. [Energy metabolism, Anaerobic]


Pssm-ID: 213807  Cd Length: 419  Bit Score: 44.62  E-value: 1.72e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1370477336  70 FDILVIGGGATGSGCALDAVTRGLKTALVERD----DFSSGT 107
Cdd:TIGR03378   1 FDVIIIGGGLAGLSCALRLAEAGKKCAIIAAGqsalHFSSGS 42
PRK05329 PRK05329
glycerol-3-phosphate dehydrogenase subunit GlpB;
69-107 1.80e-04

glycerol-3-phosphate dehydrogenase subunit GlpB;


Pssm-ID: 235412  Cd Length: 422  Bit Score: 44.46  E-value: 1.80e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1370477336  69 EFDILVIGGGATGSGCALDAVTRGLKTALVERD----DFSSGT 107
Cdd:PRK05329    2 KFDVLVIGGGLAGLTAALAAAEAGKRVALVAKGqgalHFSSGS 44
PTZ00183 PTZ00183
centrin; Provisional
 630-688 2.15e-04

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 42.37  E-value: 2.15e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370477336 630 KRFHKFDADQKGFITIVDVQRVLESINVQMDENTLHEILNEVDLNKNGQVELNEFLQLM 688
Cdd:PTZ00183   94 KAFRLFDDDKTGKISLKNLKRVAKELGETITDEELQEMIDEADRNGDGEISEEEFYRIM 152
EFh_PI-PLCdelta4 cd16219
EF-hand motif found in phosphoinositide phospholipase C delta 4 (PI-PLC-delta4); PI-PLC-delta4, ...
 632-693 3.69e-04

EF-hand motif found in phosphoinositide phospholipase C delta 4 (PI-PLC-delta4); PI-PLC-delta4, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-4 (PLCD4), or phospholipase C-delta-4 (PLC-delta-4), is expressed in various tissues with the highest levels detected selectively in the brain, skeletal muscle, testis and kidney. It plays a significant role in cell growth, cell proliferation, tumorigenesis, and in an early stage of fertilization. PI-PLC-delta4 may function as a key enzyme in the regulation of PtdIns(4,5)P2 levels and Ca2+ metabolism in nuclei in response to growth factors, and its expression may be partially regulated by an increase in cytoplasmic Ca2+. Moreover, PI-PLC-delta4 binds glutamate receptor-interacting protein1 (GRIP1) in testis and is required for calcium mobilization essential for the zona pellucida-induced acrosome reaction in sperm. Overexpression or dysregulated expression of PLCdelta4 may initiate oncogenesis in certain tissues through upregulating erbB1/2 expression, extracellular signal-regulated kinase (ERK) signaling pathway, and proliferation in MCF-7 cells. PI-PLC-delta4 contains an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain, and a C-terminal C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Unlike PI-PLC-delta 1 and 3, a putative nuclear export sequence (NES) located in the EF-hand domain, which may be responsible transporting PI-PLC-delta1 and 3 from the cell nucleus, is not present in PI-PLC-delta4.


Pssm-ID: 320049 [Multi-domain]  Cd Length: 140  Bit Score: 41.37  E-value: 3.69e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370477336 632 FHKFDADQKGFITIVDVQRVLESINVQMDENTLHEILNEVDLNKNGQVELNEFLQLMSAIQK 693
Cdd:cd16219     6 FQKADKNKDGRMNFKEVRDLLKMMNVDMNEEHALRLFQMADKSESGTLEGEEFVLFYKALTQ 67
PRK07843 PRK07843
3-oxosteroid 1-dehydrogenase;
69-119 5.10e-04

3-oxosteroid 1-dehydrogenase;


Pssm-ID: 236111 [Multi-domain]  Cd Length: 557  Bit Score: 43.49  E-value: 5.10e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370477336  69 EFDILVIGGGATGSGCALDAVTRGLKTALVERDDFSSGTSSRSTklihGGV 119
Cdd:PRK07843    7 EYDVVVVGSGAAGMVAALTAAHRGLSTVVVEKAPHYGGSTARSG----GGV 53
PRK07494 PRK07494
UbiH/UbiF family hydroxylase;
63-161 5.86e-04

UbiH/UbiF family hydroxylase;


Pssm-ID: 181001 [Multi-domain]  Cd Length: 388  Bit Score: 42.97  E-value: 5.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336  63 TLQNTSEFDILVIGGGATGSGCALDAVTRGLKTALVERDdfSSGTSSRSTKLIHGGVRYLQKAimkldieqyrmvkeALH 142
Cdd:PRK07494    1 SLMEKEHTDIAVIGGGPAGLAAAIALARAGASVALVAPE--PPYADLRTTALLGPSIRFLERL--------------GLW 64

                          90
                  ....*....|....*....
gi 1370477336 143 ERanlleIAPHlSAPLPIM 161
Cdd:PRK07494   65 AR-----LAPH-AAPLQSM 77
PRK12842 PRK12842
putative succinate dehydrogenase; Reviewed
 62-119 7.90e-04

putative succinate dehydrogenase; Reviewed


Pssm-ID: 237224 [Multi-domain]  Cd Length: 574  Bit Score: 42.76  E-value: 7.90e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370477336  62 LTLQNTSEFDILVIGGGATGSGCALDAVTRGLKTALVERDDFSSGTSSRStklihGGV 119
Cdd:PRK12842    2 ECMTNELTCDVLVIGSGAGGLSAAITARKLGLDVVVLEKEPVFGGTTAFS-----GGV 54
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
 622-684 8.06e-04

EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also termed stromal cell-derived factor 4 (SDF-4), is a soluble, lumenal Golgi resident low-affinity Ca2+-binding protein that contains six copies of the EF-hand Ca2+-binding motif. It is required for secretory pathway calcium ATPase1 (SPCA1)-dependent Ca2+ import into the trans-Golgi network (TGN) and plays an essential role in Ca2+-dependent secretory cargo sorting at the TGN.


Pssm-ID: 320023 [Multi-domain]  Cd Length: 278  Bit Score: 41.90  E-value: 8.06e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370477336 622 PSDIDRYKKRFHKFDADQKGFITIVDVQR-----VLESINVQMDENTLHeiLNEVDLNKNGQVELNEF 684
Cdd:cd16225    30 PKKRKKLKEIFKKVDVNTDGFLSAEELEDwimekTQEHFQEAVEENEQI--FKAVDTDKDGNVSWEEY 95
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 664-691 1.40e-03

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 36.59  E-value: 1.40e-03
                           10        20
                   ....*....|....*....|....*...
gi 1370477336  664 LHEILNEVDLNKNGQVELNEFLQLMSAI 691
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 620-693 1.49e-03

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 38.41  E-value: 1.49e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370477336  620 LLPSDIDRYKKRFHKFDADQKGFITIVDVQRVLESINVqmDENTLHEILNEVDLNKNGQVELNEFLQLMSAIQK 693
Cdd:smart00027   4 ISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGL--PQTLLAKIWNLADIDNDGELDKDEFALAMHLIYR 75
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
 630-688 1.81e-03

EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand proteins family, also named the calbindin sub-family, contains a group of six EF-hand Ca2+-binding proteins, including calretinin (CR, also termed 29 kDa calbindin), calbindin D28K (CB, also termed vitamin D-dependent calcium-binding protein, avian-type), and secretagogin (SCGN). CR is a cytosolic hexa-EF-hand calcium-binding protein predominantly expressed in a variety of normal and tumorigenic t-specific neurons of the central and peripheral nervous system. It is a multifunctional protein implicated in many biological processes, including cell proliferation, differentiation, and cell death. CB is highly expressed in brain tissue. It is a strong calcium-binding and buffering protein responsible for preventing a neuronal death as well as maintaining and controlling calcium homeostasis. SCGN is a six EF-hand calcium-binding protein expressed in neuroendocrine, pancreatic endocrine and retinal cells. It plays a crucial role in cell apoptosis, receptor signaling and differentiation. It is also involved in vesicle secretion through binding to various proteins, including interacts with SNAP25, SNAP23, DOC2alpha, ARFGAP2, rootletin, KIF5B, beta-tubulin, DDAH-2, ATP-synthase and myeloid leukemia factor 2. SCGN functions as a Ca2+ sensor/coincidence detector modulating vesicular exocytosis of neurotransmitters, neuropeptides or hormones. Although the family members share a significant amount of secondary sequence homology, they display altered structural and biochemical characteristics, and operate in distinct fashions. CB contains six EF-hand motifs in a single globular domain, where EF-hands 1, 3, 4, 5 bind four calcium ions. CR contains six EF-hand motifs within two independent domains, CR I-II and CR III-VI. They harbor two and four EF-hand motifs, respectively. The first 5 EF-hand motifs are capable of binding calcium ions, while the EF-hand 6 is inactive. SCGN consists of the three globular domains each of which contains a pair of EF-hand motifs. Human SCGN simultaneously binds four calcium ions through its EF-hands 3, 4, 5 and 6 in one high affinity and three low affinity calcium-binding sites. In contrast, SCGNs in other lower eukaryotes, such as D. rerio, X. laevis, M. domestica, G. gallus, O. anatinus, are fully competent in terms of six calcium-binding.


Pssm-ID: 320075 [Multi-domain]  Cd Length: 254  Bit Score: 40.80  E-value: 1.81e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370477336 630 KRFHKFDADQKGFITIVDVQRVLESI----NVQMDENTLHE----ILNEVDLNKNGQVELNEFLQLM 688
Cdd:cd15902    94 KIWRKYDTDGSGFIEAKELKGFLKDLllknKKHVSPPKLDEytklILKEFDANKDGKLELDEMAKLL 160
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 628-693 1.96e-03

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 37.20  E-value: 1.96e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370477336 628 YKKRFHKFDADQKGFITIVDVQRVLESINVqmDENTLHEILNEVDLNKNGQVELNEFLQLMSAIQK 693
Cdd:cd00052     1 YDQIFRSLDPDGDGLISGDEARPFLGKSGL--PRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIAL 64
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 664-691 2.04e-03

EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 36.22  E-value: 2.04e-03
                          10        20
                  ....*....|....*....|....*...
gi 1370477336 664 LHEILNEVDLNKNGQVELNEFLQLMSAI 691
Cdd:pfam00036   2 LKEIFRLFDKDGDGKIDFEEFKELLKKL 29
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 632-687 2.34e-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: 39.51  E-value: 2.34e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370477336 632 FHKFDADQKGFITIVDVQRVLESINVQMDENTLHEILNEVDLNKNGQVELNEFLQL 687
Cdd:cd16185     6 FRAVDRDRSGSIDVNELQKALAGGGLLFSLATAEKLIRMFDRDGNGTIDFEEFAAL 61
PRK06370 PRK06370
FAD-containing oxidoreductase;
70-103 3.06e-03

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 40.57  E-value: 3.06e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1370477336  70 FDILVIGGGATGSGCALDAVTRGLKTALVERDDF 103
Cdd:PRK06370    6 YDAIVIGAGQAGPPLAARAAGLGMKVALIERGLL 39
EF-hand_8 pfam13833
EF-hand domain pair;
639-688 3.96e-03

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 36.14  E-value: 3.96e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370477336 639 QKGFITIVDVQRVLESINVQ-MDENTLHEILNEVDLNKNGQVELNEFLQLM 688
Cdd:pfam13833   1 EKGVITREELKRALALLGLKdLSEDEVDILFREFDTDGDGYISFDEFCVLL 51
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 632-692 4.02e-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: 38.66  E-value: 4.02e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370477336 632 FHKFDADQKGFITIVDVQRVLESINV-QMDENTLHEILNEVDLNKNGQVELNEFLQLMSAIQ 692
Cdd:cd16180     6 FQAVDRDRSGRISAKELQRALSNGDWtPFSIETVRLMINMFDRDRSGTINFDEFVGLWKYIQ 67
PTZ00183 PTZ00183
centrin; Provisional
 612-690 4.06e-03

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 38.52  E-value: 4.06e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370477336 612 LTDRSEISLLPSDIDRYKKRFHKFDADQKGFITIVDVQRVLESINVQMDENTLHEILNEVDLNKNGQVELNEFLQLMSA 690
Cdd:PTZ00183    3 KRRSERPGLTEDQKKEIREAFDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIADVDKDGSGKIDFEEFLDIMTK 81
EFh_PEF_peflin cd16184
EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed ...
 632-692 4.35e-03

EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed penta-EF hand (PEF) protein with a long N-terminal hydrophobic domain, or penta-EF hand domain-containing protein 1, 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+. In lower vertebrates, peflin may interact with transient receptor potential N (TRPN1), suggesting a potential role of peflin in fast transducer channel adaptation.


Pssm-ID: 320059 [Multi-domain]  Cd Length: 165  Bit Score: 38.78  E-value: 4.35e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370477336 632 FHKFDADQKGFITIVDVQRVLESIN-VQMDENTLHEILNEVDLNKNGQVELNEFLQLMSAIQ 692
Cdd:cd16184     6 FQAVDRDRSGKISAKELQQALVNGNwSHFNDETCRLMIGMFDKDKSGTIDIYEFQALWNYIQ 67
PRK07121 PRK07121
FAD-binding protein;
69-125 5.24e-03

FAD-binding protein;


Pssm-ID: 180854 [Multi-domain]  Cd Length: 492  Bit Score: 39.87  E-value: 5.24e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370477336  69 EFDILVIGGGATGSGCALDAVTRGLKTALVERDDFSSGTSSRStklihGGVRYL------QKA 125
Cdd:PRK07121   20 EADVVVVGFGAAGACAAIEAAAAGARVLVLERAAGAGGATALS-----GGVIYLgggtavQKA 77
EF-hand_6 pfam13405
EF-hand domain;
627-656 5.32e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 34.84  E-value: 5.32e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1370477336 627 RYKKRFHKFDADQKGFITIVDVQRVLESIN 656
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
soxA_mon TIGR01377
sarcosine oxidase, monomeric form; Sarcosine oxidase catalyzes the oxidative demethylation of ...
 70-140 5.54e-03

sarcosine oxidase, monomeric form; Sarcosine oxidase catalyzes the oxidative demethylation of sarcosine to glycine. The reaction converts tetrahydrofolate to 5,10-methylene-tetrahydrofolate. The enzyme is known in monomeric and heterotetrameric (alpha,beta,gamma,delta) forms [Energy metabolism, Amino acids and amines]


Pssm-ID: 130444 [Multi-domain]  Cd Length: 380  Bit Score: 39.81  E-value: 5.54e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370477336  70 FDILVIGGGATGSGCALDAVTRGLKTALVERDDF--SSGTSsrstkliHGGVRYLQKAImkLDIEQYRMVKEA 140
Cdd:TIGR01377   1 FDVIVVGAGIMGCFAAYHLAKHGKKTLLLEQFDLphSRGSS-------HGQSRIIRKAY--PEDFYTPMMLEC 64
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 69-107 5.82e-03

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 39.78  E-value: 5.82e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1370477336  69 EFDILVIGGGATGSGCALDAVTRGLKTALVERDDFsSGT 107
Cdd:PRK06292    3 KYDVIVIGAGPAGYVAARRAAKLGKKVALIEKGPL-GGT 40
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
38-103 8.21e-03

Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 39.46  E-value: 8.21e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370477336  38 AYVKAADCISEPVNReppsreAQLLTLQNTSEFD----ILVIGGGATGSGCALDAVTRGLKTALVERDDF 103
Cdd:COG1148   111 ATEKAKDLVRMAVAK------AKLLEPLEPIKVPvnkrALVIGGGIAGMTAALELAEQGYEVYLVEKEPE 174
 
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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