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Conserved domains on  [gi|1958760013|ref|XP_038960258|]
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glycerol-3-phosphate dehydrogenase, mitochondrial isoform X1 [Rattus norvegicus]

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: 732.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013   1 MAFQKVVK-GTILMGGGALATVLGLSQFA-HYRRKQVSLAYVEAAtcFSEPvNREPPSREAQLMTLQNTS---EFDILVI 75
Cdd:PLN02464    1 MSLARLRRlAAGAAATAAGGAVYLSPQPAsSDKGGGPALDSLRDR--IADP-NASVPSRSAQESALIGATaaePLDVLVV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013  76 GGGATGCGCALDAVTRGLKTALVERNDFASGTSSRSTKLIHGGVRYLQKAITNLDVEQYRMVKEALHERANLLEIAPHLS 155
Cdd:PLN02464   78 GGGATGAGVALDAATRGLRVGLVEREDFSSGTSSRSTKLIHGGVRYLEKAVFQLDYGQLKLVFHALEERKQLIENAPHLC 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 156 APLPIMLPLYKWWQLPYYWVGIKMYDLVAGSHCLKSSYVLSKSRALEHFPMLQKDK----LVGAIVYYDGQHNDARMNLA 231
Cdd:PLN02464  158 HALPIMTPCYDWFEVPYYWAGLKAYDLVAGPRLLHLSRYYSAKESLELFPTLAKKGkdgsLKGTVVYYDGQMNDSRLNVA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 232 IALTAARYGAATANYMEVVSLLKktDPETGkeRVSGARCKDVLTGHEFNVRAKCVINATGPFTDSVRKMDDNDVVPICQP 311
Cdd:PLN02464  238 LACTAALAGAAVLNYAEVVSLIK--DESTG--RIVGARVRDNLTGKEFDVYAKVVVNAAGPFCDEVRKMADGKAKPMICP 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 312 SAGVHIVMPGYYSPENMGLLDPATSDGRVIFFLPWEKMTIAGTTDSPTDVTHHPIPSEDDINFILNEVRNYLscDVEVRR 391
Cdd:PLN02464  314 SSGVHIVLPDYYSPEGMGLIVPKTKDGRVVFMLPWLGRTVAGTTDSKTPITMLPEPHEDEIQFILDAISDYL--NVKVRR 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 392 GDVLAAWSGIRPLVTDPKSANTQSISRNHVVEVSDSGLITIAGGKWTTYRSMAEDTVNKAVKLHNL-NAGPSRTVGLFLQ 470
Cdd:PLN02464  392 SDVLSAWSGIRPLAVDPSAKSTESISRDHVVCEEPDGLVTITGGKWTTYRSMAEDAVDAAIKSGKLsPTNGCVTTDLPLV 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 471 GGKDWSPTLYIRLVQDY--------------GLESEVAQHLAKTYGDKAFDVAKMASVTGkrwpvVGVRLVSEFPYIEAE 536
Cdd:PLN02464  472 GAEGYEPSLFTQLAQQYvrmkrtyggkvvpgAMDTAAAKHLAHAYGGRADRVAEIAQNEG-----LGKRLAHGYPFLEAE 546
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958760013 537 VKYGIK-EYACTAVDMISRRTRLAFLNVQAAEEALPKIVELMGRELNWSELRKQEELETATRFL 599
Cdd:PLN02464  547 VAYCARhEYCESAVDFIARRTRLAFLDTDAAVRALPRVVEILAAEHGWDKSRKKQELQKAKEFL 610
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
627-689 3.18e-14

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: 67.57  E-value: 3.18e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958760013 627 RYKKRFHMFDEDEKGFITIVDVQRVLESINVQMDEDTLHEILCEVDLNKNGQVELHEFLQLMS 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: 732.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013   1 MAFQKVVK-GTILMGGGALATVLGLSQFA-HYRRKQVSLAYVEAAtcFSEPvNREPPSREAQLMTLQNTS---EFDILVI 75
Cdd:PLN02464    1 MSLARLRRlAAGAAATAAGGAVYLSPQPAsSDKGGGPALDSLRDR--IADP-NASVPSRSAQESALIGATaaePLDVLVV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013  76 GGGATGCGCALDAVTRGLKTALVERNDFASGTSSRSTKLIHGGVRYLQKAITNLDVEQYRMVKEALHERANLLEIAPHLS 155
Cdd:PLN02464   78 GGGATGAGVALDAATRGLRVGLVEREDFSSGTSSRSTKLIHGGVRYLEKAVFQLDYGQLKLVFHALEERKQLIENAPHLC 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 156 APLPIMLPLYKWWQLPYYWVGIKMYDLVAGSHCLKSSYVLSKSRALEHFPMLQKDK----LVGAIVYYDGQHNDARMNLA 231
Cdd:PLN02464  158 HALPIMTPCYDWFEVPYYWAGLKAYDLVAGPRLLHLSRYYSAKESLELFPTLAKKGkdgsLKGTVVYYDGQMNDSRLNVA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 232 IALTAARYGAATANYMEVVSLLKktDPETGkeRVSGARCKDVLTGHEFNVRAKCVINATGPFTDSVRKMDDNDVVPICQP 311
Cdd:PLN02464  238 LACTAALAGAAVLNYAEVVSLIK--DESTG--RIVGARVRDNLTGKEFDVYAKVVVNAAGPFCDEVRKMADGKAKPMICP 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 312 SAGVHIVMPGYYSPENMGLLDPATSDGRVIFFLPWEKMTIAGTTDSPTDVTHHPIPSEDDINFILNEVRNYLscDVEVRR 391
Cdd:PLN02464  314 SSGVHIVLPDYYSPEGMGLIVPKTKDGRVVFMLPWLGRTVAGTTDSKTPITMLPEPHEDEIQFILDAISDYL--NVKVRR 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 392 GDVLAAWSGIRPLVTDPKSANTQSISRNHVVEVSDSGLITIAGGKWTTYRSMAEDTVNKAVKLHNL-NAGPSRTVGLFLQ 470
Cdd:PLN02464  392 SDVLSAWSGIRPLAVDPSAKSTESISRDHVVCEEPDGLVTITGGKWTTYRSMAEDAVDAAIKSGKLsPTNGCVTTDLPLV 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 471 GGKDWSPTLYIRLVQDY--------------GLESEVAQHLAKTYGDKAFDVAKMASVTGkrwpvVGVRLVSEFPYIEAE 536
Cdd:PLN02464  472 GAEGYEPSLFTQLAQQYvrmkrtyggkvvpgAMDTAAAKHLAHAYGGRADRVAEIAQNEG-----LGKRLAHGYPFLEAE 546
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958760013 537 VKYGIK-EYACTAVDMISRRTRLAFLNVQAAEEALPKIVELMGRELNWSELRKQEELETATRFL 599
Cdd:PLN02464  547 VAYCARhEYCESAVDFIARRTRLAFLDTDAAVRALPRVVEILAAEHGWDKSRKKQELQKAKEFL 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: 585.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013  86 LDAVTRGLKTALVERNDFASGTSSRSTKLIHGGVRYLqkaitnldvEQY--RMVKEALHERANLLEIAPHLSAPLPIMLP 163
Cdd:COG0578     1 RDAAGRGLSVALVEKGDFASGTSSRSSKLIHGGLRYL---------EQGefRLVREALREREVLLRNAPHLVRPLPFLLP 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 164 LYKWWQLP--YYWVGIKMYDLVAGSHCLKSSYVLSKSRALEHFPMLQKDKLVGAIVYYDGQHNDARMNLAIALTAARYGA 241
Cdd:COG0578    72 LYKGGERPawLIRAGLFLYDLLAGRKGLPRHRRLSRAEALALAPLLRPDGLRGGFEYYDAQVDDARLVLELARTAAERGA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 242 ATANYMEVVSLLKKTDpetgkeRVSGARCKDVLTGHEFNVRAKCVINATGPFTDSVRKMDDNDVVPICQPSAGVHIVMPG 321
Cdd:COG0578   152 VVLNYTRVTGLLRDGG------RVWGVTVRDRLTGEEFTVRARVVVNATGPWVDELRALDGPKAPRRVRPSKGSHLVVPR 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 322 YYSPENMGLLDPATSDGRVIFFLPWEKMTIAGTTDspTDVTH---HPIPSEDDINFILNEVRNYLscDVEVRRGDVLAAW 398
Cdd:COG0578   226 LFLPLDDALYIFQNTDGRVVFAIPWEGRTLIGTTD--TDYDGdpdEPAATEEEIDYLLEAANRYF--ARPLTRDDVVSTY 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 399 SGIRPLVtDPKSANTQSISRNHVVEVSDSGLITIAGGKWTTYRSMAEDTVNKAVKLHNLNAGPSRTVGLFLQGGKDWSPT 478
Cdd:COG0578   302 AGVRPLL-DDGGKDTSALSRDHVIEVGPAGLLSIAGGKLTTYRKMAEDAVDAAARLLGLPRRPCWTADLPLPGGDAGFDA 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 479 LYIRLVQDYGLESEVAQHLAKTYGDKAFDVAKMAsvtgKRWPVVGVRLVSEFPYIEAEVKYGIK-EYACTAVDMISRRTR 557
Cdd:COG0578   381 FVAALAAAPGLPEALARRLLRRYGTRAEEVLALA----AEDPDLGEPLGPGLPYLEAEVVYAVRhEMARTLEDVLLRRTR 456
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 1958760013 558 LAFLNVQAAEEALPKIVELMGRELNWSELRKQEELETATRFL 599
Cdd:COG0578   457 LGLLDADAAAAAAPAVAELMAAELGWDDARRAAEVAAYRALL 498
DAO_C pfam16901
C-terminal domain of alpha-glycerophosphate oxidase; DAO_C is the C-terminal region of ...
462-588 3.66e-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: 181.96  E-value: 3.66e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 462 SRTVGLFLQGGKDWSPTLYIRLVQDYGLESEVAQHLAKTYGDKAFDVAKMASVTGKrwPVVGVRLVSEFPYIEAEVKYGI 541
Cdd:pfam16901   1 CVTKKLPLLGADGYSANLAARLAQRYGLDEEVAEHLARRYGSRADEVLELALADGD--PELGERLSPAYPYIEAEVVYAV 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958760013 542 K-EYACTAVDMISRRTRLAFLNVQAAEEALPKIVELMGRELNWSELRK 588
Cdd:pfam16901  79 RhEMALTLVDVLARRTRLAFLDADAALEALPEVADLMAEELGWDEARR 126
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
627-689 3.18e-14

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: 67.57  E-value: 3.18e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958760013 627 RYKKRFHMFDEDEKGFITIVDVQRVLESINVQMDEDTLHEILCEVDLNKNGQVELHEFLQLMS 689
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EF-hand_7 pfam13499
EF-hand domain pair;
625-689 2.49e-09

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 53.80  E-value: 2.49e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958760013 625 IDRYKKRFHMFDEDEKGFITIVDVQRVLESI--NVQMDEDTLHEILCEVDLNKNGQVELHEFLQLMS 689
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLeeGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
PTZ00184 PTZ00184
calmodulin; Provisional
624-689 3.16e-07

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 50.53  E-value: 3.16e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958760013 624 DIDRYKKRFHMFDEDEKGFITIVDVQRVLESINVQMDEDTLHEILCEVDLNKNGQVELHEFLQLMS 689
Cdd:PTZ00184    9 QIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTLMA 74
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
610-693 1.60e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.17  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 610 EQLTDSTEISLLPPDIDRYKKRFHMFDEDEKGFITIVDVQRVLESINVqmDEDTLHEILCEVDLNKNGQVELHEFLQLMS 689
Cdd:COG5126    53 EEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGV--SEEEADELFARLDTDGDGKISFEEFVAAVR 130

                  ....
gi 1958760013 690 AVHT 693
Cdd:COG5126   131 DYYT 134
 
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: 732.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013   1 MAFQKVVK-GTILMGGGALATVLGLSQFA-HYRRKQVSLAYVEAAtcFSEPvNREPPSREAQLMTLQNTS---EFDILVI 75
Cdd:PLN02464    1 MSLARLRRlAAGAAATAAGGAVYLSPQPAsSDKGGGPALDSLRDR--IADP-NASVPSRSAQESALIGATaaePLDVLVV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013  76 GGGATGCGCALDAVTRGLKTALVERNDFASGTSSRSTKLIHGGVRYLQKAITNLDVEQYRMVKEALHERANLLEIAPHLS 155
Cdd:PLN02464   78 GGGATGAGVALDAATRGLRVGLVEREDFSSGTSSRSTKLIHGGVRYLEKAVFQLDYGQLKLVFHALEERKQLIENAPHLC 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 156 APLPIMLPLYKWWQLPYYWVGIKMYDLVAGSHCLKSSYVLSKSRALEHFPMLQKDK----LVGAIVYYDGQHNDARMNLA 231
Cdd:PLN02464  158 HALPIMTPCYDWFEVPYYWAGLKAYDLVAGPRLLHLSRYYSAKESLELFPTLAKKGkdgsLKGTVVYYDGQMNDSRLNVA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 232 IALTAARYGAATANYMEVVSLLKktDPETGkeRVSGARCKDVLTGHEFNVRAKCVINATGPFTDSVRKMDDNDVVPICQP 311
Cdd:PLN02464  238 LACTAALAGAAVLNYAEVVSLIK--DESTG--RIVGARVRDNLTGKEFDVYAKVVVNAAGPFCDEVRKMADGKAKPMICP 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 312 SAGVHIVMPGYYSPENMGLLDPATSDGRVIFFLPWEKMTIAGTTDSPTDVTHHPIPSEDDINFILNEVRNYLscDVEVRR 391
Cdd:PLN02464  314 SSGVHIVLPDYYSPEGMGLIVPKTKDGRVVFMLPWLGRTVAGTTDSKTPITMLPEPHEDEIQFILDAISDYL--NVKVRR 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 392 GDVLAAWSGIRPLVTDPKSANTQSISRNHVVEVSDSGLITIAGGKWTTYRSMAEDTVNKAVKLHNL-NAGPSRTVGLFLQ 470
Cdd:PLN02464  392 SDVLSAWSGIRPLAVDPSAKSTESISRDHVVCEEPDGLVTITGGKWTTYRSMAEDAVDAAIKSGKLsPTNGCVTTDLPLV 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 471 GGKDWSPTLYIRLVQDY--------------GLESEVAQHLAKTYGDKAFDVAKMASVTGkrwpvVGVRLVSEFPYIEAE 536
Cdd:PLN02464  472 GAEGYEPSLFTQLAQQYvrmkrtyggkvvpgAMDTAAAKHLAHAYGGRADRVAEIAQNEG-----LGKRLAHGYPFLEAE 546
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958760013 537 VKYGIK-EYACTAVDMISRRTRLAFLNVQAAEEALPKIVELMGRELNWSELRKQEELETATRFL 599
Cdd:PLN02464  547 VAYCARhEYCESAVDFIARRTRLAFLDTDAAVRALPRVVEILAAEHGWDKSRKKQELQKAKEFL 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: 585.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013  86 LDAVTRGLKTALVERNDFASGTSSRSTKLIHGGVRYLqkaitnldvEQY--RMVKEALHERANLLEIAPHLSAPLPIMLP 163
Cdd:COG0578     1 RDAAGRGLSVALVEKGDFASGTSSRSSKLIHGGLRYL---------EQGefRLVREALREREVLLRNAPHLVRPLPFLLP 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 164 LYKWWQLP--YYWVGIKMYDLVAGSHCLKSSYVLSKSRALEHFPMLQKDKLVGAIVYYDGQHNDARMNLAIALTAARYGA 241
Cdd:COG0578    72 LYKGGERPawLIRAGLFLYDLLAGRKGLPRHRRLSRAEALALAPLLRPDGLRGGFEYYDAQVDDARLVLELARTAAERGA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 242 ATANYMEVVSLLKKTDpetgkeRVSGARCKDVLTGHEFNVRAKCVINATGPFTDSVRKMDDNDVVPICQPSAGVHIVMPG 321
Cdd:COG0578   152 VVLNYTRVTGLLRDGG------RVWGVTVRDRLTGEEFTVRARVVVNATGPWVDELRALDGPKAPRRVRPSKGSHLVVPR 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 322 YYSPENMGLLDPATSDGRVIFFLPWEKMTIAGTTDspTDVTH---HPIPSEDDINFILNEVRNYLscDVEVRRGDVLAAW 398
Cdd:COG0578   226 LFLPLDDALYIFQNTDGRVVFAIPWEGRTLIGTTD--TDYDGdpdEPAATEEEIDYLLEAANRYF--ARPLTRDDVVSTY 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 399 SGIRPLVtDPKSANTQSISRNHVVEVSDSGLITIAGGKWTTYRSMAEDTVNKAVKLHNLNAGPSRTVGLFLQGGKDWSPT 478
Cdd:COG0578   302 AGVRPLL-DDGGKDTSALSRDHVIEVGPAGLLSIAGGKLTTYRKMAEDAVDAAARLLGLPRRPCWTADLPLPGGDAGFDA 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 479 LYIRLVQDYGLESEVAQHLAKTYGDKAFDVAKMAsvtgKRWPVVGVRLVSEFPYIEAEVKYGIK-EYACTAVDMISRRTR 557
Cdd:COG0578   381 FVAALAAAPGLPEALARRLLRRYGTRAEEVLALA----AEDPDLGEPLGPGLPYLEAEVVYAVRhEMARTLEDVLLRRTR 456
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 1958760013 558 LAFLNVQAAEEALPKIVELMGRELNWSELRKQEELETATRFL 599
Cdd:COG0578   457 LGLLDADAAAAAAPAVAELMAAELGWDDARRAAEVAAYRALL 498
glpD PRK12266
glycerol-3-phosphate dehydrogenase; Reviewed
87-569 7.29e-77

glycerol-3-phosphate dehydrogenase; Reviewed


Pssm-ID: 237027 [Multi-domain]  Cd Length: 508  Bit Score: 256.22  E-value: 7.29e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013  87 DAVTRGLKTALVERNDFASGTSSRSTKLIHGGVRYLqkaitnldvEQY--RMVKEALHERANLLEIAPHLSAPLPIMLPL 164
Cdd:PRK12266   24 DAAGRGLSVLLCEQDDLASATSSASTKLIHGGLRYL---------EHYefRLVREALAEREVLLRMAPHIIWPMRFVLPH 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 165 YKW----WQLPyywVGIKMYDLVAGSHCLKSSYVLSKSRALEHFPMlqKDKLVGAIVYYDGQHNDARMNLAIALTAARYG 240
Cdd:PRK12266   95 RPHlrpaWMIR---AGLFLYDHLGKRKSLPGSRGLDLGRDPAGSPL--KPEITRGFEYSDCWVDDARLVVLNARDAAERG 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 241 AATANYMEVVSLlkktdpetgkERVSG---ARCKDVLTGHEFNVRAKCVINATGP----FTDSVRKMDDNDVVPICQpsa 313
Cdd:PRK12266  170 AEILTRTRVVSA----------RRENGlwhVTLEDTATGKRYTVRARALVNAAGPwvkqFLDDGLGLPSPYGIRLVK--- 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 314 GVHIVMPGYYSPE------NmglldpatSDGRVIFFLPWE-KMTIAGTTD-----SPTDVThhpIpSEDDINFILNEVRN 381
Cdd:PRK12266  237 GSHIVVPRLFDHDqayilqN--------PDGRIVFAIPYEdDFTLIGTTDveykgDPAKVA---I-SEEEIDYLCKVVNR 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 382 YLscDVEVRRGDVLAAWSGIRPLVTDpKSANTQSISRNHVVEVSDSG----LITIAGGKWTTYRSMAEDTVNKaVKLHNL 457
Cdd:PRK12266  305 YF--KKQLTPADVVWTYSGVRPLCDD-ESDSAQAITRDYTLELDDENggapLLSVFGGKITTYRKLAEHALEK-LAPYLP 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 458 NAGPSRTVGLFLQGGkDWSPTLYIRLVQDY-----GLESEVAQHLAKTYGDKAFDVAKMASVTGKRWPVVGVRLvsefpY 532
Cdd:PRK12266  381 QMGPAWTAGAPLPGG-DFPGDRFDALAAALrrrypWLPEALARRLARAYGTRAERLLGGATSLADLGEHFGHGL-----Y 454
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 1958760013 533 iEAEVKYGIK-EYACTAVDMISRRTRLAfLNVQAAEEA 569
Cdd:PRK12266  455 -EAEVDYLVEhEWARTAEDILWRRTKLG-LRLDAEQQA 490
PRK13369 PRK13369
glycerol-3-phosphate dehydrogenase; Provisional
87-569 9.34e-74

glycerol-3-phosphate dehydrogenase; Provisional


Pssm-ID: 237365 [Multi-domain]  Cd Length: 502  Bit Score: 247.57  E-value: 9.34e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013  87 DAVTRGLKTALVERNDFASGTSSRSTKLIHGGVRYLqkaitnldvEQY--RMVKEALHERANLLEIAPHLSAPLPIMLP- 163
Cdd:PRK13369   24 DAAGRGLKVLLCEKDDLAQGTSSRSGKLVHGGLRYL---------EYYefRLVREALIEREVLLAAAPHIIWPMRFVLPh 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 164 ---LYKWWQLPyywVGIKMYDLVAGSHCLKSSYVLSKSRALEHFPMlqKDKLVGAIVYYDGQHNDARMNLAIALTAARYG 240
Cdd:PRK13369   95 speDRPAWLVR---LGLFLYDHLGGRKRLPGTRTLDLRRDPEGAPL--KPEYTKGFEYSDCWVDDARLVVLNALDAAERG 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 241 AATanymevvsllkktdpETGKERVSGARCKDVLT-------GHEFNVRAKCVINATGPFTDSVRKMddndvVPICQPSA 313
Cdd:PRK13369  170 ATI---------------LTRTRCVSARREGGLWRvetrdadGETRTVRARALVNAAGPWVTDVIHR-----VAGSNSSR 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 314 GV------HIVMPGYYSPENMGLLDpaTSDGRVIFFLPWEK-MTIAGTTD-----SPTDVThhpiPSEDDINFILNEVRN 381
Cdd:PRK13369  230 NVrlvkgsHIVVPKFWDGAQAYLFQ--NPDKRVIFANPYEGdFTLIGTTDiayegDPEDVA----ADEEEIDYLLDAANR 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 382 YLScdVEVRRGDVLAAWSGIRPLVTDpKSANTQSISRNHVVEVSDSG----LITIAGGKWTTYRSMAEDTVNKaVKLHNL 457
Cdd:PRK13369  304 YFK--EKLRREDVVHSFSGVRPLFDD-GAGNPSAVTRDYVFDLDAETggapLLSVFGGKITTFRKLAEHALER-LKPFFP 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 458 NAGPSRTVGLFLQGGkDWSPTLYIRLVQDYG-----LESEVAQHLAKTYGDKAFDVAKMASVTGKRWPVVGVRLVsefpy 532
Cdd:PRK13369  380 QMGGDWTAGAPLPGG-DIANADFDTFADDLRdrypwLPRPLAHRYARLYGTRAKDVLGGARSLEDLGRHFGGGLT----- 453
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 1958760013 533 iEAEVKYGI-KEYACTAVDMISRRTRLAfLNVQAAEEA 569
Cdd:PRK13369  454 -EAEVRYLVaREWARTAEDILWRRTKLG-LHLSAAERA 489
DAO_C pfam16901
C-terminal domain of alpha-glycerophosphate oxidase; DAO_C is the C-terminal region of ...
462-588 3.66e-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: 181.96  E-value: 3.66e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 462 SRTVGLFLQGGKDWSPTLYIRLVQDYGLESEVAQHLAKTYGDKAFDVAKMASVTGKrwPVVGVRLVSEFPYIEAEVKYGI 541
Cdd:pfam16901   1 CVTKKLPLLGADGYSANLAARLAQRYGLDEEVAEHLARRYGSRADEVLELALADGD--PELGERLSPAYPYIEAEVVYAV 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958760013 542 K-EYACTAVDMISRRTRLAFLNVQAAEEALPKIVELMGRELNWSELRK 588
Cdd:pfam16901  79 RhEMALTLVDVLARRTRLAFLDADAALEALPEVADLMAEELGWDEARR 126
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
71-441 1.93e-33

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: 131.37  E-value: 1.93e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013  71 DILVIGggatgcgcaLDAVTRGLKTALVERN-DFASGTSSRSTKLIHGGVRYLQKAitnldvEQYRMVKEALHERANLLE 149
Cdd:pfam01266   1 DVVVIGggivglstaYELARRGLSVTLLERGdDPGSGASGRNAGLIHPGLRYLEPS------ELARLALEALDLWEELEE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 150 I-APHLSAPLPIMLPLYKWWQLPYYwvgIKMYDLVAGShcLKSSYVLSKSRALEHFPMLqkDKLVGAIVYYDGQH-NDAR 227
Cdd:pfam01266  75 ElGIDCGFRRCGVLVLARDEEEEAL---EKLLAALRRL--GVPAELLDAEELRELEPLL--PGLRGGLFYPDGGHvDPAR 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 228 MNLAIALTAARYGAATANYMEVVSLLKktdpetgKERVSGARckdvLTGHefnvrAKCVINATGPFTDSVRKMddnDVVP 307
Cdd:pfam01266 148 LLRALARAAEALGVRIIEGTEVTGIEE-------EGGVWGVV----TTGE-----ADAVVNAAGAWADLLALP---GLRL 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 308 ICQPSAGVHIVMPGYYSPENMGLLDPATSDGRVIFFLPWEK-MTIAGTTDSPTDvTHHPIPSEDDINFILNEVRNYLScd 386
Cdd:pfam01266 209 PVRPVRGQVLVLEPLPEALLILPVPITVDPGRGVYLRPRADgRLLLGGTDEEDG-FDDPTPDPEEIEELLEAARRLFP-- 285
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958760013 387 vevRRGDVLAAWSGIRPLvTDPKSANTQSISRNHVVEV--SDSGLITIAG-GKWTTYR 441
Cdd:pfam01266 286 ---ALADIERAWAGLRPL-PDGLPIIGRPGSPGLYLATghGGHGLTLAPGiGKLLAEL 339
glpA PRK11101
anaerobic glycerol-3-phosphate dehydrogenase subunit A;
87-558 1.65e-28

anaerobic glycerol-3-phosphate dehydrogenase subunit A;


Pssm-ID: 236847 [Multi-domain]  Cd Length: 546  Bit Score: 120.51  E-value: 1.65e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013  87 DAVTRGLKTALVERNDFASGTSSRSTKLIHGGVRYlqkAITnlDVEQYRmvkEALHERANLLEIAPHLSAP---LPIMLP 163
Cdd:PRK11101   24 DCALRGLRCILVERHDIATGATGRNHGLLHSGARY---AVT--DAESAR---ECISENQILKRIARHCVEPtdgLFITLP 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 164 LYkwwQLPYYWVGIKMYDLvAGSHCLKssyvLSKSRALEHFPMLQKDkLVGAIVYYDGQHNDARMNLAIALTAARYGAAT 243
Cdd:PRK11101   96 ED---DLAFQATFIRACEE-AGIEAEA----IDPQQALILEPAVNPA-LIGAVKVPDGTVDPFRLTAANMLDAKEHGAQI 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 244 ANYMEVVSLLKKTDpetgkeRVSGARCKDVLTGHEFNVRAKCVINATGPFTDSVRKMDDNDVVPIcqPSAGVHIVMPgyY 323
Cdd:PRK11101  167 LTYHEVTGLIREGD------TVCGVRVRDHLTGETQEIHAPVVVNAAGIWGQHIAEYADLRIRMF--PAKGSLLIMD--H 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 324 SPENMGL---LDPATSDGRVifflPWEKMTIAGTTDsptdvTHHPIPSEDDINFILNEVrnylscDVEVRRGDVLA---- 396
Cdd:PRK11101  237 RINNHVInrcRKPADADILV----PGDTISLIGTTS-----TRIDYDQIDDNRVTAEEV------DILLREGEKLApvma 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 397 ------AWSGIRPLVTDPKSANTQSISR-----NHVVEVSDSGLITIAGGKWTTYRSMAEDTVNKAVKLHNlNAGPSRTV 465
Cdd:PRK11101  302 ktrilrAYAGVRPLVASDDDPSGRNVSRgivllDHAERDGLDGFITITGGKLMTYRLMAEWATDAVCRKLG-NTRPCTTA 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 466 GLFLQGGKDWSPTLYIRLVqdyGLESEVAQHLAKTYGDKAFDVakmasVTGKRwpvVGVRLVSEFPYIEA-EVKYGIKEY 544
Cdd:PRK11101  381 DTPLPGSQEPAEVTLRKVI---SLPAPLRGSAVYRHGDRAPAW-----LSEGR---LDRSLVCECEAVTAgEVRYAVENL 449
                         490
                  ....*....|....*
gi 1958760013 545 AC-TAVDMiSRRTRL 558
Cdd:PRK11101  450 NVnNLLDL-RRRTRV 463
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
91-407 8.95e-16

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 79.56  E-value: 8.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013  91 RGLKTALVERNDFASGTSSRSTklihGGVRYLQKAITnlDVEQYRMVKEALHEranLLEIAPHLSAPLPimlplykWWQL 170
Cdd:COG0665    24 RGLDVTVLERGRPGSGASGRNA----GQLRPGLAALA--DRALVRLAREALDL---WRELAAELGIDCD-------FRRT 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 171 PYYWVG--IKMYDLVAGSHCLKSSY-----VLSKSRALEHFPMLQKDKLVGAIVYydgqHNDARMN-----LAIALTAAR 238
Cdd:COG0665    88 GVLYLArtEAELAALRAEAEALRALglpveLLDAAELREREPGLGSPDYAGGLYD----PDDGHVDpaklvRALARAARA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 239 YGAATANYMEVVSLlkktdpetgkeRVSGARCKDVLTGHEfNVRAKCVINATGPFTDSVRKMDDNDvVPIcQPSAGVHIV 318
Cdd:COG0665   164 AGVRIREGTPVTGL-----------EREGGRVTGVRTERG-TVRADAVVLAAGAWSARLLPMLGLR-LPL-RPVRGYVLV 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 319 MPgyysPENMGLLDPATSDGRVIFFLPWEKMTIAGTTDSPTDvtHHPIPSEDDINFILNEVRNYL--SCDVEVRRgdvla 396
Cdd:COG0665   230 TE----PLPDLPLRPVLDDTGVYLRPTADGRLLVGGTAEPAG--FDRAPTPERLEALLRRLRRLFpaLADAEIVR----- 298
                         330
                  ....*....|.
gi 1958760013 397 AWSGIRPLVTD 407
Cdd:COG0665   299 AWAGLRPMTPD 309
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
627-689 3.18e-14

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: 67.57  E-value: 3.18e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958760013 627 RYKKRFHMFDEDEKGFITIVDVQRVLESINVQMDEDTLHEILCEVDLNKNGQVELHEFLQLMS 689
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EF-hand_7 pfam13499
EF-hand domain pair;
625-689 2.49e-09

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 53.80  E-value: 2.49e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958760013 625 IDRYKKRFHMFDEDEKGFITIVDVQRVLESI--NVQMDEDTLHEILCEVDLNKNGQVELHEFLQLMS 689
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLeeGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
PTZ00184 PTZ00184
calmodulin; Provisional
624-689 3.16e-07

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 50.53  E-value: 3.16e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958760013 624 DIDRYKKRFHMFDEDEKGFITIVDVQRVLESINVQMDEDTLHEILCEVDLNKNGQVELHEFLQLMS 689
Cdd:PTZ00184    9 QIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTLMA 74
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
627-688 5.70e-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: 49.20  E-value: 5.70e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958760013 627 RYKKRFHMFDEDEKGFITIVDVQRVLESINVQMDEDTLHEILCEVDLNKNGQVELHEFLQLM 688
Cdd:cd15898     1 WLRRQWIKADKDGDGKLSLKEIKKLLKRLNIRVSEKELKKLFKEVDTNGDGTLTFDEFEELY 62
PTZ00184 PTZ00184
calmodulin; Provisional
626-688 9.80e-07

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 48.99  E-value: 9.80e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958760013 626 DRYKKRFHMFDEDEKGFITIVDVQRVLESINVQMDEDTLHEILCEVDLNKNGQVELHEFLQLM 688
Cdd:PTZ00184   84 EEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKMM 146
PTZ00183 PTZ00183
centrin; Provisional
630-688 1.04e-05

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 46.22  E-value: 1.04e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958760013 630 KRFHMFDEDEKGFITIVDVQRVLESINVQMDEDTLHEILCEVDLNKNGQVELHEFLQLM 688
Cdd:PTZ00183   94 KAFRLFDDDKTGKISLKNLKRVAKELGETITDEELQEMIDEADRNGDGEISEEEFYRIM 152
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
610-693 1.60e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.17  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760013 610 EQLTDSTEISLLPPDIDRYKKRFHMFDEDEKGFITIVDVQRVLESINVqmDEDTLHEILCEVDLNKNGQVELHEFLQLMS 689
Cdd:COG5126    53 EEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGV--SEEEADELFARLDTDGDGKISFEEFVAAVR 130

                  ....
gi 1958760013 690 AVHT 693
Cdd:COG5126   131 DYYT 134
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
629-686 4.49e-04

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: 41.06  E-value: 4.49e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958760013 629 KKRFHMFDEDEKGFITIVDVQRVLESINVQMDEDTLHEILCEVDLNKNGQVELHEFLQ 686
Cdd:cd16202     3 KDQFRKADKNGDGKLSFKECKKLLKKLNVKVDKDYAKKLFQEADTSGEDVLDEEEFVQ 60
PTZ00183 PTZ00183
centrin; Provisional
612-690 1.55e-03

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 39.67  E-value: 1.55e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958760013 612 LTDSTEISLLPPDIDRYKKRFHMFDEDEKGFITIVDVQRVLESINVQMDEDTLHEILCEVDLNKNGQVELHEFLQLMSA 690
Cdd:PTZ00183    3 KRRSERPGLTEDQKKEIREAFDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIADVDKDGSGKIDFEEFLDIMTK 81
EF-hand_6 pfam13405
EF-hand domain;
627-656 5.93e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 34.84  E-value: 5.93e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1958760013 627 RYKKRFHMFDEDEKGFITIVDVQRVLESIN 656
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
632-691 8.54e-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: 8.54e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958760013 632 FHMFDEDEKGFITIVDVQRVLESINVQMDEDTLHEILCEVDLNKNGQV------ELHEFLQLMSAV 691
Cdd:cd16185     6 FRAVDRDRSGSIDVNELQKALAGGGLLFSLATAEKLIRMFDRDGNGTIdfeefaALHQFLSNMQNG 71
 
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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