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Conserved domains on  [gi|966976445|ref|XP_014965626|]
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glycerol-3-phosphate dehydrogenase, mitochondrial isoform X2 [Macaca mulatta]

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: ...
 25-574 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: 752.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445  25 VNREPPSREAQLLTLQNTS---EFDILVIGGGATGSGCALDAVTRGLKTALVERDDFSSGTSSRSTKLIHGGVRYLQKAI 101
Cdd:PLN02464  49 PNASVPSRSAQESALIGATaaePLDVLVVGGGATGAGVALDAATRGLRVGLVEREDFSSGTSSRSTKLIHGGVRYLEKAV 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 102 MKLDIEQYRMVKEALHERANLLEIAPHLSAPLPIMLPVYKWWQLPYYWVGIKLYDLVAGSNCLKSSYVLSKSRALEHFPM 181
Cdd:PLN02464 129 FQLDYGQLKLVFHALEERKQLIENAPHLCHALPIMTPCYDWFEVPYYWAGLKAYDLVAGPRLLHLSRYYSAKESLELFPT 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 182 LQKDK----LVGAIVYYDGQHNDARMNLAIALTAARYGAATANYMEVVSLLKktDPQTGkvRVSGARCKDVLTGQEFDVR 257
Cdd:PLN02464 209 LAKKGkdgsLKGTVVYYDGQMNDSRLNVALACTAALAGAAVLNYAEVVSLIK--DESTG--RIVGARVRDNLTGKEFDVY 284

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 258 AKCVINATGPFTDSVRKMDDKDAAAICQPSAGVHIVMPGYYSPESMGLLDPATSDGRVIFFLPWQKMTIAGTTDTPTDVT 337
Cdd:PLN02464 285 AKVVVNAAGPFCDEVRKMADGKAKPMICPSSGVHIVLPDYYSPEGMGLIVPKTKDGRVVFMLPWLGRTVAGTTDSKTPIT 364

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 338 PHPIPSEEDINFILNEVRNYLscDVEVRRGDVLAAWSGIRPLVTDPKSADTQSISRNHVVDISESGLITIAGGKWTTYRS 417
Cdd:PLN02464 365 MLPEPHEDEIQFILDAISDYL--NVKVRRSDVLSAWSGIRPLAVDPSAKSTESISRDHVVCEEPDGLVTITGGKWTTYRS 442

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 418 MAEDTINAAIKTHNLK-AGPSRTVGLFLQGGKDWSPTLYIRLVQDY--------------GLESEVAQHLAATYGDKAFE 482
Cdd:PLN02464 443 MAEDAVDAAIKSGKLSpTNGCVTTDLPLVGAEGYEPSLFTQLAQQYvrmkrtyggkvvpgAMDTAAAKHLAHAYGGRADR 522

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 483 VAKMASVTGkrwpiVGVRLVSEFPYIEAEVKYGIK-EYACTAVDMISRRTRLAFLNVQAAEEALPRIVELMGRELNWDDH 561
Cdd:PLN02464 523 VAEIAQNEG-----LGKRLAHGYPFLEAEVAYCARhEYCESAVDFIARRTRLAFLDTDAAVRALPRVVEILAAEHGWDKS 597

                        570
                 ....*....|...
gi 966976445 562 KKQEQLETAKKFL 574
Cdd:PLN02464 598 RKKQELQKAKEFL 610
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 602-664 4.90e-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: 4.90e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966976445 602 RYKKRFHKFDADKKGFITIVDVQRVLESINVQMDENTLHEILNEVDLNKNGQVELNEFLQLMS 664
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
 
Name Accession Description Interval E-value
PLN02464 PLN02464
glycerol-3-phosphate dehydrogenase
 25-574 0e+00

glycerol-3-phosphate dehydrogenase


Pssm-ID: 215257 [Multi-domain]  Cd Length: 627  Bit Score: 752.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445  25 VNREPPSREAQLLTLQNTS---EFDILVIGGGATGSGCALDAVTRGLKTALVERDDFSSGTSSRSTKLIHGGVRYLQKAI 101
Cdd:PLN02464  49 PNASVPSRSAQESALIGATaaePLDVLVVGGGATGAGVALDAATRGLRVGLVEREDFSSGTSSRSTKLIHGGVRYLEKAV 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 102 MKLDIEQYRMVKEALHERANLLEIAPHLSAPLPIMLPVYKWWQLPYYWVGIKLYDLVAGSNCLKSSYVLSKSRALEHFPM 181
Cdd:PLN02464 129 FQLDYGQLKLVFHALEERKQLIENAPHLCHALPIMTPCYDWFEVPYYWAGLKAYDLVAGPRLLHLSRYYSAKESLELFPT 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 182 LQKDK----LVGAIVYYDGQHNDARMNLAIALTAARYGAATANYMEVVSLLKktDPQTGkvRVSGARCKDVLTGQEFDVR 257
Cdd:PLN02464 209 LAKKGkdgsLKGTVVYYDGQMNDSRLNVALACTAALAGAAVLNYAEVVSLIK--DESTG--RIVGARVRDNLTGKEFDVY 284

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 258 AKCVINATGPFTDSVRKMDDKDAAAICQPSAGVHIVMPGYYSPESMGLLDPATSDGRVIFFLPWQKMTIAGTTDTPTDVT 337
Cdd:PLN02464 285 AKVVVNAAGPFCDEVRKMADGKAKPMICPSSGVHIVLPDYYSPEGMGLIVPKTKDGRVVFMLPWLGRTVAGTTDSKTPIT 364

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 338 PHPIPSEEDINFILNEVRNYLscDVEVRRGDVLAAWSGIRPLVTDPKSADTQSISRNHVVDISESGLITIAGGKWTTYRS 417
Cdd:PLN02464 365 MLPEPHEDEIQFILDAISDYL--NVKVRRSDVLSAWSGIRPLAVDPSAKSTESISRDHVVCEEPDGLVTITGGKWTTYRS 442

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 418 MAEDTINAAIKTHNLK-AGPSRTVGLFLQGGKDWSPTLYIRLVQDY--------------GLESEVAQHLAATYGDKAFE 482
Cdd:PLN02464 443 MAEDAVDAAIKSGKLSpTNGCVTTDLPLVGAEGYEPSLFTQLAQQYvrmkrtyggkvvpgAMDTAAAKHLAHAYGGRADR 522

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 483 VAKMASVTGkrwpiVGVRLVSEFPYIEAEVKYGIK-EYACTAVDMISRRTRLAFLNVQAAEEALPRIVELMGRELNWDDH 561
Cdd:PLN02464 523 VAEIAQNEG-----LGKRLAHGYPFLEAEVAYCARhEYCESAVDFIARRTRLAFLDTDAAVRALPRVVEILAAEHGWDKS 597

                        570
                 ....*....|...
gi 966976445 562 KKQEQLETAKKFL 574
Cdd:PLN02464 598 RKKQELQKAKEFL 610
GlpA COG0578
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ...
 61-574 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: 569.38  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445  61 LDAVTRGLKTALVERDDFSSGTSSRSTKLIHGGVRYLqkaimkldiEQY--RMVKEALHERANLLEIAPHLSAPLPIMLP 138
Cdd:COG0578    1 RDAAGRGLSVALVEKGDFASGTSSRSSKLIHGGLRYL---------EQGefRLVREALREREVLLRNAPHLVRPLPFLLP 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 139 VYKWWQLP--YYWVGIKLYDLVAGSNCLKSSYVLSKSRALEHFPMLQKDKLVGAIVYYDGQHNDARMNLAIALTAARYGA 216
Cdd:COG0578   72 LYKGGERPawLIRAGLFLYDLLAGRKGLPRHRRLSRAEALALAPLLRPDGLRGGFEYYDAQVDDARLVLELARTAAERGA 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 217 ATANYMEVVSLLKKTDpqtgkvRVSGARCKDVLTGQEFDVRAKCVINATGPFTDSVRKMDDKDAAAICQPSAGVHIVMPG 296
Cdd:COG0578  152 VVLNYTRVTGLLRDGG------RVWGVTVRDRLTGEEFTVRARVVVNATGPWVDELRALDGPKAPRRVRPSKGSHLVVPR 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 297 YYSPESMGLLDPATSDGRVIFFLPWQKMTIAGTT-DTPTDVTPHPIPSEEDINFILNEVRNYLscDVEVRRGDVLAAWSG 375
Cdd:COG0578  226 LFLPLDDALYIFQNTDGRVVFAIPWEGRTLIGTTdTDYDGDPDEPAATEEEIDYLLEAANRYF--ARPLTRDDVVSTYAG 303

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 376 IRPLVtDPKSADTQSISRNHVVDISESGLITIAGGKWTTYRSMAEDTINAAIKTHNLKAGPSRTVGLFLQGGKDWSPTLY 455
Cdd:COG0578  304 VRPLL-DDGGKDTSALSRDHVIEVGPAGLLSIAGGKLTTYRKMAEDAVDAAARLLGLPRRPCWTADLPLPGGDAGFDAFV 382

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 456 IRLVQDYGLESEVAQHLAATYGDKAFEVAKMAsvtgKRWPIVGVRLVSEFPYIEAEVKYGIK-EYACTAVDMISRRTRLA 534
Cdd:COG0578  383 AALAAAPGLPEALARRLLRRYGTRAEEVLALA----AEDPDLGEPLGPGLPYLEAEVVYAVRhEMARTLEDVLLRRTRLG 458

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 966976445 535 FLNVQAAEEALPRIVELMGRELNWDDHKKQEQLETAKKFL 574
Cdd:COG0578  459 LLDADAAAAAAPAVAELMAAELGWDDARRAAEVAAYRALL 498
DAO_C pfam16901
C-terminal domain of alpha-glycerophosphate oxidase; DAO_C is the C-terminal region of ...
 437-563 3.11e-55

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


Pssm-ID: 465305 [Multi-domain]  Cd Length: 126  Bit Score: 184.66  E-value: 3.11e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445  437 SRTVGLFLQGGKDWSPTLYIRLVQDYGLESEVAQHLAATYGDKAFEVAKMASVTGKrwPIVGVRLVSEFPYIEAEVKYGI 516
Cdd:pfam16901   1 CVTKKLPLLGADGYSANLAARLAQRYGLDEEVAEHLARRYGSRADEVLELALADGD--PELGERLSPAYPYIEAEVVYAV 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 966976445  517 K-EYACTAVDMISRRTRLAFLNVQAAEEALPRIVELMGRELNWDDHKK 563
Cdd:pfam16901  79 RhEMALTLVDVLARRTRLAFLDADAALEALPEVADLMAEELGWDEARR 126
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 602-664 4.90e-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: 4.90e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966976445 602 RYKKRFHKFDADKKGFITIVDVQRVLESINVQMDENTLHEILNEVDLNKNGQVELNEFLQLMS 664
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EF-hand_7 pfam13499
EF-hand domain pair;
600-664 1.96e-11

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 59.96  E-value: 1.96e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966976445  600 IDRYKKRFHKFDADKKGFITIVDVQRVLESI--NVQMDENTLHEILNEVDLNKNGQVELNEFLQLMS 664
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLeeGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
PTZ00184 PTZ00184
calmodulin; Provisional
 599-664 1.85e-08

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 54.00  E-value: 1.85e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966976445 599 DIDRYKKRFHKFDADKKGFITIVDVQRVLESINVQMDENTLHEILNEVDLNKNGQVELNEFLQLMS 664
Cdd:PTZ00184   9 QIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTLMA 74
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
589-666 7.18e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.94  E-value: 7.18e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966976445 589 DRSEISLLPSDIdrYKKRFHKFDADKKGFITIVDVQRVLESINVQMDENTLHEILNEVDLNKNGQVELNEFLQLMSAI 666
Cdd:COG5126   23 ERDDFEALFRRL--WATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTAL 98
glycerol3P_GlpB TIGR03378
glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are ...
 45-82 1.64e-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: 1.64e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 966976445   45 FDILVIGGGATGSGCALDAVTRGLKTALVERD----DFSSGT 82
Cdd:TIGR03378   1 FDVIIIGGGLAGLSCALRLAEAGKKCAIIAAGqsalHFSSGS 42
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 639-666 1.48e-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: 1.48e-03
                           10        20
                   ....*....|....*....|....*...
gi 966976445   639 LHEILNEVDLNKNGQVELNEFLQLMSAI 666
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
 
Name Accession Description Interval E-value
PLN02464 PLN02464
glycerol-3-phosphate dehydrogenase
 25-574 0e+00

glycerol-3-phosphate dehydrogenase


Pssm-ID: 215257 [Multi-domain]  Cd Length: 627  Bit Score: 752.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445  25 VNREPPSREAQLLTLQNTS---EFDILVIGGGATGSGCALDAVTRGLKTALVERDDFSSGTSSRSTKLIHGGVRYLQKAI 101
Cdd:PLN02464  49 PNASVPSRSAQESALIGATaaePLDVLVVGGGATGAGVALDAATRGLRVGLVEREDFSSGTSSRSTKLIHGGVRYLEKAV 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 102 MKLDIEQYRMVKEALHERANLLEIAPHLSAPLPIMLPVYKWWQLPYYWVGIKLYDLVAGSNCLKSSYVLSKSRALEHFPM 181
Cdd:PLN02464 129 FQLDYGQLKLVFHALEERKQLIENAPHLCHALPIMTPCYDWFEVPYYWAGLKAYDLVAGPRLLHLSRYYSAKESLELFPT 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 182 LQKDK----LVGAIVYYDGQHNDARMNLAIALTAARYGAATANYMEVVSLLKktDPQTGkvRVSGARCKDVLTGQEFDVR 257
Cdd:PLN02464 209 LAKKGkdgsLKGTVVYYDGQMNDSRLNVALACTAALAGAAVLNYAEVVSLIK--DESTG--RIVGARVRDNLTGKEFDVY 284

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 258 AKCVINATGPFTDSVRKMDDKDAAAICQPSAGVHIVMPGYYSPESMGLLDPATSDGRVIFFLPWQKMTIAGTTDTPTDVT 337
Cdd:PLN02464 285 AKVVVNAAGPFCDEVRKMADGKAKPMICPSSGVHIVLPDYYSPEGMGLIVPKTKDGRVVFMLPWLGRTVAGTTDSKTPIT 364

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 338 PHPIPSEEDINFILNEVRNYLscDVEVRRGDVLAAWSGIRPLVTDPKSADTQSISRNHVVDISESGLITIAGGKWTTYRS 417
Cdd:PLN02464 365 MLPEPHEDEIQFILDAISDYL--NVKVRRSDVLSAWSGIRPLAVDPSAKSTESISRDHVVCEEPDGLVTITGGKWTTYRS 442

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 418 MAEDTINAAIKTHNLK-AGPSRTVGLFLQGGKDWSPTLYIRLVQDY--------------GLESEVAQHLAATYGDKAFE 482
Cdd:PLN02464 443 MAEDAVDAAIKSGKLSpTNGCVTTDLPLVGAEGYEPSLFTQLAQQYvrmkrtyggkvvpgAMDTAAAKHLAHAYGGRADR 522

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 483 VAKMASVTGkrwpiVGVRLVSEFPYIEAEVKYGIK-EYACTAVDMISRRTRLAFLNVQAAEEALPRIVELMGRELNWDDH 561
Cdd:PLN02464 523 VAEIAQNEG-----LGKRLAHGYPFLEAEVAYCARhEYCESAVDFIARRTRLAFLDTDAAVRALPRVVEILAAEHGWDKS 597

                        570
                 ....*....|...
gi 966976445 562 KKQEQLETAKKFL 574
Cdd:PLN02464 598 RKKQELQKAKEFL 610
GlpA COG0578
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ...
 61-574 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: 569.38  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445  61 LDAVTRGLKTALVERDDFSSGTSSRSTKLIHGGVRYLqkaimkldiEQY--RMVKEALHERANLLEIAPHLSAPLPIMLP 138
Cdd:COG0578    1 RDAAGRGLSVALVEKGDFASGTSSRSSKLIHGGLRYL---------EQGefRLVREALREREVLLRNAPHLVRPLPFLLP 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 139 VYKWWQLP--YYWVGIKLYDLVAGSNCLKSSYVLSKSRALEHFPMLQKDKLVGAIVYYDGQHNDARMNLAIALTAARYGA 216
Cdd:COG0578   72 LYKGGERPawLIRAGLFLYDLLAGRKGLPRHRRLSRAEALALAPLLRPDGLRGGFEYYDAQVDDARLVLELARTAAERGA 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 217 ATANYMEVVSLLKKTDpqtgkvRVSGARCKDVLTGQEFDVRAKCVINATGPFTDSVRKMDDKDAAAICQPSAGVHIVMPG 296
Cdd:COG0578  152 VVLNYTRVTGLLRDGG------RVWGVTVRDRLTGEEFTVRARVVVNATGPWVDELRALDGPKAPRRVRPSKGSHLVVPR 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 297 YYSPESMGLLDPATSDGRVIFFLPWQKMTIAGTT-DTPTDVTPHPIPSEEDINFILNEVRNYLscDVEVRRGDVLAAWSG 375
Cdd:COG0578  226 LFLPLDDALYIFQNTDGRVVFAIPWEGRTLIGTTdTDYDGDPDEPAATEEEIDYLLEAANRYF--ARPLTRDDVVSTYAG 303

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 376 IRPLVtDPKSADTQSISRNHVVDISESGLITIAGGKWTTYRSMAEDTINAAIKTHNLKAGPSRTVGLFLQGGKDWSPTLY 455
Cdd:COG0578  304 VRPLL-DDGGKDTSALSRDHVIEVGPAGLLSIAGGKLTTYRKMAEDAVDAAARLLGLPRRPCWTADLPLPGGDAGFDAFV 382

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 456 IRLVQDYGLESEVAQHLAATYGDKAFEVAKMAsvtgKRWPIVGVRLVSEFPYIEAEVKYGIK-EYACTAVDMISRRTRLA 534
Cdd:COG0578  383 AALAAAPGLPEALARRLLRRYGTRAEEVLALA----AEDPDLGEPLGPGLPYLEAEVVYAVRhEMARTLEDVLLRRTRLG 458

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 966976445 535 FLNVQAAEEALPRIVELMGRELNWDDHKKQEQLETAKKFL 574
Cdd:COG0578  459 LLDADAAAAAAPAVAELMAAELGWDDARRAAEVAAYRALL 498
glpD PRK12266
glycerol-3-phosphate dehydrogenase; Reviewed
 41-544 6.76e-78

glycerol-3-phosphate dehydrogenase; Reviewed


Pssm-ID: 237027 [Multi-domain]  Cd Length: 508  Bit Score: 258.15  E-value: 6.76e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445  41 NTSEFDILVIGGGATGSGCALDAVTRGLKTALVERDDFSSGTSSRSTKLIHGGVRYLqkaimkldiEQY--RMVKEALHE 118
Cdd:PRK12266   3 MMETYDLLVIGGGINGAGIARDAAGRGLSVLLCEQDDLASATSSASTKLIHGGLRYL---------EHYefRLVREALAE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 119 RANLLEIAPHLSAPLPIMLPVYKW----WQLPyywVGIKLYDLVAGSNCLKSSYVLSKSRALEHFPMlqKDKLVGAIVYY 194
Cdd:PRK12266  74 REVLLRMAPHIIWPMRFVLPHRPHlrpaWMIR---AGLFLYDHLGKRKSLPGSRGLDLGRDPAGSPL--KPEITRGFEYS 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 195 DGQHNDARMNLAIALTAARYGAATANYMEVVSLlkktdpqtgkVRVSG---ARCKDVLTGQEFDVRAKCVINATGPFTDS 271
Cdd:PRK12266 149 DCWVDDARLVVLNARDAAERGAEILTRTRVVSA----------RRENGlwhVTLEDTATGKRYTVRARALVNAAGPWVKQ 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 272 V--RKMDDKDAAAI--CQpsaGVHIVMPGYYS-PESMGLLDPatsDGRVIFFLPWQ-KMTIAGTT-DTPTDVTPHPIPSE 344
Cdd:PRK12266 219 FldDGLGLPSPYGIrlVK---GSHIVVPRLFDhDQAYILQNP---DGRIVFAIPYEdDFTLIGTTdVEYKGDPAKVAISE 292

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 345 EDINFILNEVRNYLscDVEVRRGDVLAAWSGIRPLVTDpKSADTQSISRNHVVDISESG----LITIAGGKWTTYRSMAE 420
Cdd:PRK12266 293 EEIDYLCKVVNRYF--KKQLTPADVVWTYSGVRPLCDD-ESDSAQAITRDYTLELDDENggapLLSVFGGKITTYRKLAE 369

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 421 DTINaAIKTHNLKAGPSRTVGLFLQGGkDWSPTLYIRLVQDY-----GLESEVAQHLAATYGDKAFEVAKMASVTGKRWP 495
Cdd:PRK12266 370 HALE-KLAPYLPQMGPAWTAGAPLPGG-DFPGDRFDALAAALrrrypWLPEALARRLARAYGTRAERLLGGATSLADLGE 447

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|
gi 966976445 496 IVGVRLvsefpYiEAEVKYGIK-EYACTAVDMISRRTRLAfLNVQAAEEA 544
Cdd:PRK12266 448 HFGHGL-----Y-EAEVDYLVEhEWARTAEDILWRRTKLG-LRLDAEQQA 490
PRK13369 PRK13369
glycerol-3-phosphate dehydrogenase; Provisional
 42-544 5.68e-75

glycerol-3-phosphate dehydrogenase; Provisional


Pssm-ID: 237365 [Multi-domain]  Cd Length: 502  Bit Score: 250.27  E-value: 5.68e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445  42 TSEFDILVIGGGATGSGCALDAVTRGLKTALVERDDFSSGTSSRSTKLIHGGVRYLqkaimkldiEQY--RMVKEALHER 119
Cdd:PRK13369   4 PETYDLFVIGGGINGAGIARDAAGRGLKVLLCEKDDLAQGTSSRSGKLVHGGLRYL---------EYYefRLVREALIER 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 120 ANLLEIAPHLSAPLPIMLPVYK----WWQLPyywVGIKLYDLVAGSNCLKSSYVLSKSRALEHFPMlqKDKLVGAIVYYD 195
Cdd:PRK13369  75 EVLLAAAPHIIWPMRFVLPHSPedrpAWLVR---LGLFLYDHLGGRKRLPGTRTLDLRRDPEGAPL--KPEYTKGFEYSD 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 196 GQHNDARMNLAIALTAARYGAATANYMEVVSLLKKTDpqTGKVRVSGARckdvltGQEFDVRAKCVINATGPFTDSVrkm 275
Cdd:PRK13369 150 CWVDDARLVVLNALDAAERGATILTRTRCVSARREGG--LWRVETRDAD------GETRTVRARALVNAAGPWVTDV--- 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 276 ddKDAAAICQPSAGV------HIVMPGYYSPESMGLLDpaTSDGRVIFFLPWQK-MTIAGTTDTPTDVTPHPI-PSEEDI 347
Cdd:PRK13369 219 --IHRVAGSNSSRNVrlvkgsHIVVPKFWDGAQAYLFQ--NPDKRVIFANPYEGdFTLIGTTDIAYEGDPEDVaADEEEI 294

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 348 NFILNEVRNYLScdVEVRRGDVLAAWSGIRPLVTDpKSADTQSISRNHVVDISESG----LITIAGGKWTTYRSMAEDTI 423
Cdd:PRK13369 295 DYLLDAANRYFK--EKLRREDVVHSFSGVRPLFDD-GAGNPSAVTRDYVFDLDAETggapLLSVFGGKITTFRKLAEHAL 371

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 424 NaAIKTHNLKAGPSRTVGLFLQGGkDWSPTLYIRLVQDYG-----LESEVAQHLAATYGDKAFEVAKMASVTGKRWPIVG 498
Cdd:PRK13369 372 E-RLKPFFPQMGGDWTAGAPLPGG-DIANADFDTFADDLRdrypwLPRPLAHRYARLYGTRAKDVLGGARSLEDLGRHFG 449

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*..
gi 966976445 499 VRLVsefpyiEAEVKYGI-KEYACTAVDMISRRTRLAfLNVQAAEEA 544
Cdd:PRK13369 450 GGLT------EAEVRYLVaREWARTAEDILWRRTKLG-LHLSAAERA 489
DAO_C pfam16901
C-terminal domain of alpha-glycerophosphate oxidase; DAO_C is the C-terminal region of ...
 437-563 3.11e-55

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


Pssm-ID: 465305 [Multi-domain]  Cd Length: 126  Bit Score: 184.66  E-value: 3.11e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445  437 SRTVGLFLQGGKDWSPTLYIRLVQDYGLESEVAQHLAATYGDKAFEVAKMASVTGKrwPIVGVRLVSEFPYIEAEVKYGI 516
Cdd:pfam16901   1 CVTKKLPLLGADGYSANLAARLAQRYGLDEEVAEHLARRYGSRADEVLELALADGD--PELGERLSPAYPYIEAEVVYAV 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 966976445  517 K-EYACTAVDMISRRTRLAFLNVQAAEEALPRIVELMGRELNWDDHKK 563
Cdd:pfam16901  79 RhEMALTLVDVLARRTRLAFLDADAALEALPEVADLMAEELGWDEARR 126
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 46-416 4.52e-44

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: 161.41  E-value: 4.52e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445   46 DILVIGGGATGSGCALDAVTRGLKTALVERD-DFSSGTSSRSTKLIHGGVRYLQKAimkldiEQYRMVKEALHERANLLE 124
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGdDPGSGASGRNAGLIHPGLRYLEPS------ELARLALEALDLWEELEE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445  125 I-APHLSAPLPIMLPVYKWWQLPYYwvgIKLYDLVAGSNClkSSYVLSKSRALEHFPMLqkDKLVGAIVYYDGQH-NDAR 202
Cdd:pfam01266  75 ElGIDCGFRRCGVLVLARDEEEEAL---EKLLAALRRLGV--PAELLDAEELRELEPLL--PGLRGGLFYPDGGHvDPAR 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445  203 MNLAIALTAARYGAATANYMEVVSLLKKTDPQTgkVRVSGarckdvltgqefdvRAKCVINATGPFTDSVRKMDDKdaaA 282
Cdd:pfam01266 148 LLRALARAAEALGVRIIEGTEVTGIEEEGGVWG--VVTTG--------------EADAVVNAAGAWADLLALPGLR---L 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445  283 ICQPSAGVHIVMPGYYSPESMGLLDPATSDGRVIFFLPWQ--KMTIAGttDTPTDVTPHPIPSEEDINFILNEVRNYLSc 360
Cdd:pfam01266 209 PVRPVRGQVLVLEPLPEALLILPVPITVDPGRGVYLRPRAdgRLLLGG--TDEEDGFDDPTPDPEEIEELLEAARRLFP- 285

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 966976445  361 dvevRRGDVLAAWSGIRPLvTDPKSADTQSISRNHVVD--ISESGLITIAG-GKWTTYR 416
Cdd:pfam01266 286 ----ALADIERAWAGLRPL-PDGLPIIGRPGSPGLYLAtgHGGHGLTLAPGiGKLLAEL 339
glpA PRK11101
anaerobic glycerol-3-phosphate dehydrogenase subunit A;
44-533 5.83e-33

anaerobic glycerol-3-phosphate dehydrogenase subunit A;


Pssm-ID: 236847 [Multi-domain]  Cd Length: 546  Bit Score: 133.99  E-value: 5.83e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445  44 EFDILVIGGGATGSGCALDAVTRGLKTALVERDDFSSGTSSRSTKLIHGGVRYLQKaimklDIEQYRmvkEALHERANLL 123
Cdd:PRK11101   6 ETDVIIIGGGATGAGIARDCALRGLRCILVERHDIATGATGRNHGLLHSGARYAVT-----DAESAR---ECISENQILK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 124 EIAPHLSAP---LPIMLPVYkwwQLPYYWVGIKLYDLvAGSNCLKssyvLSKSRALEHFPMLQKDkLVGAIVYYDGQHND 200
Cdd:PRK11101  78 RIARHCVEPtdgLFITLPED---DLAFQATFIRACEE-AGIEAEA----IDPQQALILEPAVNPA-LIGAVKVPDGTVDP 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 201 ARMNLAIALTAARYGAATANYMEVVSLLKKTDpqtgkvRVSGARCKDVLTGQEFDVRAKCVINATG-------PFTD-SV 272
Cdd:PRK11101 149 FRLTAANMLDAKEHGAQILTYHEVTGLIREGD------TVCGVRVRDHLTGETQEIHAPVVVNAAGiwgqhiaEYADlRI 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 273 RKMDDKDAAAI------------CQPSAGVHIVMPGyyspESMGLLdpATSDGRVifflPWQKMTiagttdtptdvTPHP 340
Cdd:PRK11101 223 RMFPAKGSLLImdhrinnhvinrCRKPADADILVPG----DTISLI--GTTSTRI----DYDQID-----------DNRV 281

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 341 IPSEEDINFilnevRNYLSCDVEVRRGDVLAAWSGIRPLVTDPKSADTQSISRNHV-VDISE----SGLITIAGGKWTTY 415
Cdd:PRK11101 282 TAEEVDILL-----REGEKLAPVMAKTRILRAYAGVRPLVASDDDPSGRNVSRGIVlLDHAErdglDGFITITGGKLMTY 356

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 416 RSMAEDTINAAIKTHNlKAGPSRTVGLFLQGGKDWSPTLYIRLVqdyGLESEVAQHLAATYGDKAFEVakmasVTGKRwp 495
Cdd:PRK11101 357 RLMAEWATDAVCRKLG-NTRPCTTADTPLPGSQEPAEVTLRKVI---SLPAPLRGSAVYRHGDRAPAW-----LSEGR-- 425

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 966976445 496 iVGVRLVSEFPYIEA-EVKYGIKEYAC-TAVDMiSRRTRL 533
Cdd:PRK11101 426 -LDRSLVCECEAVTAgEVRYAVENLNVnNLLDL-RRRTRV 463
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
44-382 6.59e-19

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 89.19  E-value: 6.59e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445  44 EFDILVIGGGATGSGCALDAVTRGLKTALVERDDFSSGTSSRSTklihGGVRYLQKAIMklDIEQYRMVKEALHEranLL 123
Cdd:COG0665    2 TADVVVIGGGIAGLSTAYHLARRGLDVTVLERGRPGSGASGRNA----GQLRPGLAALA--DRALVRLAREALDL---WR 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 124 EIAPHLSAPLPimlpvykWWQLPYYWVGIK---LYDLVAGSNCLKS----SYVLSKSRALEHFPMLQKDKLVGAIVYydg 196
Cdd:COG0665   73 ELAAELGIDCD-------FRRTGVLYLARTeaeLAALRAEAEALRAlglpVELLDAAELREREPGLGSPDYAGGLYD--- 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 197 qHNDARMN-----LAIALTAARYGAATANYMEVVSLlkktdpqtgkvRVSGARCKDVLTGQEfDVRAKCVINATGPFTDS 271
Cdd:COG0665  143 -PDDGHVDpaklvRALARAARAAGVRIREGTPVTGL-----------EREGGRVTGVRTERG-TVRADAVVLAAGAWSAR 209

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 272 VRKMDDKDAAAicQPSAGVHIVMPgyysPESMGLLDPATSDGRViFFLPWQK--MTIAGttdTPTDVTPHPIPSEEDINF 349
Cdd:COG0665  210 LLPMLGLRLPL--RPVRGYVLVTE----PLPDLPLRPVLDDTGV-YLRPTADgrLLVGG---TAEPAGFDRAPTPERLEA 279

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 966976445 350 ILNEVRNYL--SCDVEVRRgdvlaAWSGIRPLVTD 382
Cdd:COG0665  280 LLRRLRRLFpaLADAEIVR-----AWAGLRPMTPD 309
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 602-664 4.90e-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: 4.90e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966976445 602 RYKKRFHKFDADKKGFITIVDVQRVLESINVQMDENTLHEILNEVDLNKNGQVELNEFLQLMS 664
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EF-hand_7 pfam13499
EF-hand domain pair;
600-664 1.96e-11

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 59.96  E-value: 1.96e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966976445  600 IDRYKKRFHKFDADKKGFITIVDVQRVLESI--NVQMDENTLHEILNEVDLNKNGQVELNEFLQLMS 664
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLeeGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
 44-266 1.08e-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: 57.92  E-value: 1.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445  44 EFDILVIGGGATGSGCALDAVTRGLKTALVERDDFSSGTSSRSTklihGGVR----YLQKAIMKLDIEQYR--MVKEAlH 117
Cdd:COG1053    3 EYDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGGHTAAAQ----GGINaagtNVQKAAGEDSPEEHFydTVKGG-D 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 118 ERAN------LLEIAPhlsaplpimlPVYKW---WQLPYYWVGIKLYDLVAGSnclkssyvlSKSRAleHFPMLQKdklv 188
Cdd:COG1053   78 GLADqdlveaLAEEAP----------EAIDWleaQGVPFSRTPDGRLPQFGGH---------SVGRT--CYAGDGT---- 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 189 gaivyydGQHndarmnLAIAL--TAARYGAATANYMEVVSLLKKTDpqtgkvRVSGARCKDVlTGQEFDVRAKCVINATG 266
Cdd:COG1053  133 -------GHA------LLATLyqAALRLGVEIFTETEVLDLIVDDG------RVVGVVARDR-TGEIVRIRAKAVVLATG 192
PTZ00184 PTZ00184
calmodulin; Provisional
 599-664 1.85e-08

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 54.00  E-value: 1.85e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966976445 599 DIDRYKKRFHKFDADKKGFITIVDVQRVLESINVQMDENTLHEILNEVDLNKNGQVELNEFLQLMS 664
Cdd:PTZ00184   9 QIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTLMA 74
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
 604-661 1.39e-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: 51.07  E-value: 1.39e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 966976445 604 KKRFHKFDADKKGFITIVDVQRVLESINVQMDENTLHEILNEVDLNKNGQVELNEFLQ 661
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. ...
 602-667 1.63e-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: 50.74  E-value: 1.63e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966976445 602 RYKKRFHKFDADKKGFITIVDVQRVLESINVQMDENTLHEILNEVDLNKNGQVELNEFLQLMSAIQ 667
Cdd:cd15898    1 WLRRQWIKADKDGDGKLSLKEIKKLLKRLNIRVSEKELKKLFKEVDTNGDGTLTFDEFEELYKSLT 66
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 44-77 1.59e-06

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 51.30  E-value: 1.59e-06
                         10        20        30
                 ....*....|....*....|....*....|....
gi 966976445  44 EFDILVIGGGATGSGCALDAVTRGLKTALVERDD 77
Cdd:PRK06416   4 EYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEKEK 37
PTZ00184 PTZ00184
calmodulin; Provisional
 601-663 2.19e-06

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 47.83  E-value: 2.19e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966976445 601 DRYKKRFHKFDADKKGFITIVDVQRVLESINVQMDENTLHEILNEVDLNKNGQVELNEFLQLM 663
Cdd:PTZ00184  84 EEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKMM 146
PRK12843 PRK12843
FAD-dependent oxidoreductase;
34-86 2.31e-06

FAD-dependent oxidoreductase;


Pssm-ID: 237225 [Multi-domain]  Cd Length: 578  Bit Score: 50.89  E-value: 2.31e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 966976445  34 AQLLTLQNTSEFDILVIGGGATGSGCALDAVTRGLKTALVERDDFSSGTSSRS 86
Cdd:PRK12843   6 SELSPERWDAEFDVIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGGTTATS 58
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
589-666 7.18e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.94  E-value: 7.18e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966976445 589 DRSEISLLPSDIdrYKKRFHKFDADKKGFITIVDVQRVLESINVQMDENTLHEILNEVDLNKNGQVELNEFLQLMSAI 666
Cdd:COG5126   23 ERDDFEALFRRL--WATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTAL 98
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
601-663 9.96e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.55  E-value: 9.96e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966976445 601 DRYKKRFHKFDADKKGFITIVDVQRVLESINVQMDEntLHEILNEVDLNKNGQVELNEFLQLM 663
Cdd:COG5126   69 PFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEE--ADELFARLDTDGDGKISFEEFVAAV 129
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
41-410 1.11e-05

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


Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 48.22  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445  41 NTSEFDILVIGGGATGSGCALdAVTR--GLKTALVER-DDFSSGTSSRSTKLIHGGVRY----LqKAimKLDIEQYRMVK 113
Cdd:COG0579    1 MMEMYDVVIIGAGIVGLALAR-ELSRyeDLKVLVLEKeDDVAQESSGNNSGVIHAGLYYtpgsL-KA--RLCVEGNELFY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 114 EALHERANLLEIAPHLS-----APLPIMLpvykwwqlpyywvgiKLYDlvAGS-NCLKSSYVLSKSRALEHFPMLQKDKL 187
Cdd:COG0579   77 ELCRELGIPFKRCGKLVvatgeEEVAFLE---------------KLYE--RGKaNGVPGLEILDREELRELEPLLSDEGV 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 188 V------GAIVYYdgqhndARMNLAIALTAARYGAATANYMEVVSLLKKTDpqtgKVRVSgarckdvlTGQEfDVRAKCV 261
Cdd:COG0579  140 AalyspsTGIVDP------GALTRALAENAEANGVELLLNTEVTGIEREGD----GWEVT--------TNGG-TIRARFV 200

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 262 INATGPFTDSV-RKMDDKDAAAI---------CQPSAGV--HIV--MPGYYSPeSMG-LLDPaTSDGRVIF-----FLPW 321
Cdd:COG0579  201 INAAGLYADRLaQMAGIGKDFGIfpvkgeylvLDKPAELvnAKVypVPDPGAP-FLGvHLTR-TIDGNLLFgpnavFVPK 278

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445 322 QKMTIAGTTDTPTDVTPHPIPS------------EEDINFILNEVRNYLScdvEVRRGDVLAAWSGIRPlvtdpksadtQ 389
Cdd:COG0579  279 KEDSLLDLFESLRFPNFWPMLAknlltkylesvtSLSKEAFLEALRKYVP---ELPDEDLIPAFAGIRA----------Q 345

                        410       420
                 ....*....|....*....|....
gi 966976445 390 SISRNH--VVDISES-GLITIAGG 410
Cdd:COG0579  346 IIKPDGdfVIEEADDpGSIHVLGI 369
FAD_oxidored pfam12831
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ...
 46-84 1.58e-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: 47.99  E-value: 1.58e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 966976445   46 DILVIGGGATGSGCALDAVTRGLKTALVERDDFSSGTSS 84
Cdd:pfam12831   1 DVVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGMLT 39
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 44-78 2.01e-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: 47.77  E-value: 2.01e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 966976445  44 EFDILVIGGGATGSGCALDAVTRGLKTALVERDDF 78
Cdd:COG1249    3 DYDLVVIGAGPGGYVAAIRAAQLGLKVALVEKGRL 37
GlpB COG3075
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];
44-82 2.70e-05

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


Pssm-ID: 442309  Cd Length: 415  Bit Score: 47.10  E-value: 2.70e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 966976445  44 EFDILVIGGGATGSGCALDAVTRGLKTALVERD----DFSSGT 82
Cdd:COG3075    2 KFDVVVIGGGLAGLTAAIRAAEAGLRVAIVSAGqsalHFSSGS 44
PTZ00183 PTZ00183
centrin; Provisional
 605-663 6.49e-05

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 43.91  E-value: 6.49e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 966976445 605 KRFHKFDADKKGFITIVDVQRVLESINVQMDENTLHEILNEVDLNKNGQVELNEFLQLM 663
Cdd:PTZ00183  94 KAFRLFDDDKTGKISLKNLKRVAKELGETITDEELQEMIDEADRNGDGEISEEEFYRIM 152
PRK06134 PRK06134
putative FAD-binding dehydrogenase; Reviewed
 29-131 9.72e-05

putative FAD-binding dehydrogenase; Reviewed


Pssm-ID: 180419 [Multi-domain]  Cd Length: 581  Bit Score: 45.48  E-value: 9.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445  29 PPSREAQLLTLqntsEFDILVIGGGATGSGCALDAVTRGLKTALVERDDFSSGTSSRStklihGGVRYL------QKAIM 102
Cdd:PRK06134   1 TPSAAAYPPDL----ECDVLVIGSGAAGLSAAVTAAWHGLKVIVVEKDPVFGGTTAWS-----GGWMWIprnplaRRAGI 71

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 966976445 103 KLDIEQYRM-VKEALHERAN------LLEIAPHLSA 131
Cdd:PRK06134  72 VEDIEQPRTyLRHELGARYDaaridaFLEAGPHMVA 107
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
 46-86 1.39e-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: 44.97  E-value: 1.39e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 966976445   46 DILVIGGGATGSGCALDAVTRGLKTALVERDDFSSGTSSRS 86
Cdd:pfam00890   1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGATAWS 41
PRK05329 PRK05329
glycerol-3-phosphate dehydrogenase subunit GlpB;
44-82 1.63e-04

glycerol-3-phosphate dehydrogenase subunit GlpB;


Pssm-ID: 235412  Cd Length: 422  Bit Score: 44.46  E-value: 1.63e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 966976445  44 EFDILVIGGGATGSGCALDAVTRGLKTALVERD----DFSSGT 82
Cdd:PRK05329   2 KFDVLVIGGGLAGLTAALAAAEAGKRVALVAKGqgalHFSSGS 44
glycerol3P_GlpB TIGR03378
glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are ...
 45-82 1.64e-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: 1.64e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 966976445   45 FDILVIGGGATGSGCALDAVTRGLKTALVERD----DFSSGT 82
Cdd:TIGR03378   1 FDVIIIGGGLAGLSCALRLAEAGKKCAIIAAGqsalHFSSGS 42
EFh_PI-PLCdelta4 cd16219
EF-hand motif found in phosphoinositide phospholipase C delta 4 (PI-PLC-delta4); PI-PLC-delta4, ...
 607-668 1.77e-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: 42.14  E-value: 1.77e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966976445 607 FHKFDADKKGFITIVDVQRVLESINVQMDENTLHEILNEVDLNKNGQVELNEFLQLMSAIQK 668
Cdd:cd16219    6 FQKADKNKDGRMNFKEVRDLLKMMNVDMNEEHALRLFQMADKSESGTLEGEEFVLFYKALTQ 67
PRK07494 PRK07494
UbiH/UbiF family hydroxylase;
38-136 4.71e-04

UbiH/UbiF family hydroxylase;


Pssm-ID: 181001 [Multi-domain]  Cd Length: 388  Bit Score: 42.97  E-value: 4.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445  38 TLQNTSEFDILVIGGGATGSGCALDAVTRGLKTALVERDdfSSGTSSRSTKLIHGGVRYLQKAimkldieqyrmvkeALH 117
Cdd:PRK07494   1 SLMEKEHTDIAVIGGGPAGLAAAIALARAGASVALVAPE--PPYADLRTTALLGPSIRFLERL--------------GLW 64

                         90
                 ....*....|....*....
gi 966976445 118 ERanlleIAPHlSAPLPIM 136
Cdd:PRK07494  65 AR-----LAPH-AAPLQSM 77
PRK07843 PRK07843
3-oxosteroid 1-dehydrogenase;
44-94 4.88e-04

3-oxosteroid 1-dehydrogenase;


Pssm-ID: 236111 [Multi-domain]  Cd Length: 557  Bit Score: 43.49  E-value: 4.88e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 966976445  44 EFDILVIGGGATGSGCALDAVTRGLKTALVERDDFSSGTSSRSTklihGGV 94
Cdd:PRK07843   7 EYDVVVVGSGAAGMVAALTAAHRGLSTVVVEKAPHYGGSTARSG----GGV 53
PRK12842 PRK12842
putative succinate dehydrogenase; Reviewed
 37-94 6.31e-04

putative succinate dehydrogenase; Reviewed


Pssm-ID: 237224 [Multi-domain]  Cd Length: 574  Bit Score: 43.14  E-value: 6.31e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 966976445  37 LTLQNTSEFDILVIGGGATGSGCALDAVTRGLKTALVERDDFSSGTSSRStklihGGV 94
Cdd:PRK12842   2 ECMTNELTCDVLVIGSGAGGLSAAITARKLGLDVVVLEKEPVFGGTTAFS-----GGV 54
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
13-78 7.28e-04

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 42.92  E-value: 7.28e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976445  13 AYVKAADYISEPVNReppsreAQLLTLQNTSEFD----ILVIGGGATGSGCALDAVTRGLKTALVERDDF 78
Cdd:COG1148  111 ATEKAKDLVRMAVAK------AKLLEPLEPIKVPvnkrALVIGGGIAGMTAALELAEQGYEVYLVEKEPE 174
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
 597-659 8.75e-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: 8.75e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966976445 597 PSDIDRYKKRFHKFDADKKGFITIVDVQR-----VLESINVQMDENTLHeiLNEVDLNKNGQVELNEF 659
Cdd:cd16225   30 PKKRKKLKEIFKKVDVNTDGFLSAEELEDwimekTQEHFQEAVEENEQI--FKAVDTDKDGNVSWEEY 95
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 607-667 9.15e-04

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: 40.59  E-value: 9.15e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966976445 607 FHKFDADKKGFITIVDVQRVLESINV-QMDENTLHEILNEVDLNKNGQVELNEFLQLMSAIQ 667
Cdd:cd16180    6 FQAVDRDRSGRISAKELQRALSNGDWtPFSIETVRLMINMFDRDRSGTINFDEFVGLWKYIQ 67
PTZ00183 PTZ00183
centrin; Provisional
 587-665 9.38e-04

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 40.44  E-value: 9.38e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966976445 587 LTDRSEISLLPSDIDRYKKRFHKFDADKKGFITIVDVQRVLESINVQMDENTLHEILNEVDLNKNGQVELNEFLQLMSA 665
Cdd:PTZ00183   3 KRRSERPGLTEDQKKEIREAFDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIADVDKDGSGKIDFEEFLDIMTK 81
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
 605-663 1.06e-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: 41.57  E-value: 1.06e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966976445 605 KRFHKFDADKKGFITIVDVQRVLESI----NVQMDENTLHE----ILNEVDLNKNGQVELNEFLQLM 663
Cdd:cd15902   94 KIWRKYDTDGSGFIEAKELKGFLKDLllknKKHVSPPKLDEytklILKEFDANKDGKLELDEMAKLL 160
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 639-666 1.48e-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: 1.48e-03
                           10        20
                   ....*....|....*....|....*...
gi 966976445   639 LHEILNEVDLNKNGQVELNEFLQLMSAI 666
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 607-662 1.53e-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: 39.89  E-value: 1.53e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 966976445 607 FHKFDADKKGFITIVDVQRVLESINVQMDENTLHEILNEVDLNKNGQVELNEFLQL 662
Cdd:cd16185    6 FRAVDRDRSGSIDVNELQKALAGGGLLFSLATAEKLIRMFDRDGNGTIDFEEFAAL 61
EFh_PEF_peflin cd16184
EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed ...
 607-667 1.76e-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: 39.56  E-value: 1.76e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966976445 607 FHKFDADKKGFITIVDVQRVLESIN-VQMDENTLHEILNEVDLNKNGQVELNEFLQLMSAIQ 667
Cdd:cd16184    6 FQAVDRDRSGKISAKELQQALVNGNwSHFNDETCRLMIGMFDKDKSGTIDIYEFQALWNYIQ 67
EF-hand_6 pfam13405
EF-hand domain;
602-631 2.14e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 36.00  E-value: 2.14e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 966976445  602 RYKKRFHKFDADKKGFITIVDVQRVLESIN 631
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 639-666 2.38e-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: 35.84  E-value: 2.38e-03
                          10        20
                  ....*....|....*....|....*...
gi 966976445  639 LHEILNEVDLNKNGQVELNEFLQLMSAI 666
Cdd:pfam00036   2 LKEIFRLFDKDGDGKIDFEEFKELLKKL 29
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 603-668 2.49e-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: 36.81  E-value: 2.49e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966976445 603 YKKRFHKFDADKKGFITIVDVQRVLESINVqmDENTLHEILNEVDLNKNGQVELNEFLQLMSAIQK 668
Cdd:cd00052    1 YDQIFRSLDPDGDGLISGDEARPFLGKSGL--PRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIAL 64
PRK06370 PRK06370
FAD-containing oxidoreductase;
45-78 2.55e-03

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 40.96  E-value: 2.55e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 966976445  45 FDILVIGGGATGSGCALDAVTRGLKTALVERDDF 78
Cdd:PRK06370   6 YDAIVIGAGQAGPPLAARAAGLGMKVALIERGLL 39
PRK07121 PRK07121
FAD-binding protein;
44-100 4.19e-03

FAD-binding protein;


Pssm-ID: 180854 [Multi-domain]  Cd Length: 492  Bit Score: 40.26  E-value: 4.19e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966976445  44 EFDILVIGGGATGSGCALDAVTRGLKTALVERDDFSSGTSSRStklihGGVRYL------QKA 100
Cdd:PRK07121  20 EADVVVVGFGAAGACAAIEAAAAGARVLVLERAAGAGGATALS-----GGVIYLgggtavQKA 77
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 595-668 5.07e-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: 36.87  E-value: 5.07e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966976445   595 LLPSDIDRYKKRFHKFDADKKGFITIVDVQRVLESINVqmDENTLHEILNEVDLNKNGQVELNEFLQLMSAIQK 668
Cdd:smart00027   4 ISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGL--PQTLLAKIWNLADIDNDGELDKDEFALAMHLIYR 75
soxA_mon TIGR01377
sarcosine oxidase, monomeric form; Sarcosine oxidase catalyzes the oxidative demethylation of ...
 45-115 5.31e-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: 5.31e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966976445   45 FDILVIGGGATGSGCALDAVTRGLKTALVERDDF--SSGTSsrstkliHGGVRYLQKAImkLDIEQYRMVKEA 115
Cdd:TIGR01377   1 FDVIVVGAGIMGCFAAYHLAKHGKKTLLLEQFDLphSRGSS-------HGQSRIIRKAY--PEDFYTPMMLEC 64
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 44-82 5.34e-03

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 39.78  E-value: 5.34e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 966976445  44 EFDILVIGGGATGSGCALDAVTRGLKTALVERDDFsSGT 82
Cdd:PRK06292   3 KYDVIVIGAGPAGYVAARRAAKLGKKVALIEKGPL-GGT 40
EF-hand_8 pfam13833
EF-hand domain pair;
614-663 5.45e-03

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 35.75  E-value: 5.45e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 966976445  614 KKGFITIVDVQRVLESINVQ-MDENTLHEILNEVDLNKNGQVELNEFLQLM 663
Cdd:pfam13833   1 EKGVITREELKRALALLGLKdLSEDEVDILFREFDTDGDGYISFDEFCVLL 51
EFh_PI-PLCgamma cd16201
EF-hand motif found in phosphoinositide phospholipase C gamma isozymes (PI-PLC-gamma); ...
 604-662 9.13e-03

EF-hand motif found in phosphoinositide phospholipase C gamma isozymes (PI-PLC-gamma); PI-PLC-gamma isozymes represent a class of metazoan PI-PLCs that hydrolyze the membrane lipid phosphatidylinositol 4,5-bisphosphate (PIP2) to propagate diverse intracellular responses that underlie the physiological action of many hormones, neurotransmitters, and growth factors. They can form a complex with the phosphorylated cytoplasmic domains of the immunoglobulin Ig-alpha and Ig-beta subunits of the B cell receptor (BCR), the membrane-tethered Src family kinase Lyn, phosphorylated spleen tyrosine kinase (Syk), the phosphorylated adaptor protein B-cell linker (BLNK), and activated Bruton's tyrosine kinase (Btk). Like other PI-PLC isozymes, PI-PLC-gamma 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 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. Unique to PI-PLC-gamma, a second PH domain, which is split by two SH2 (Src homology 2) domains, and one SH3 (Src homology 3) domain, are present within this linker. The SH2 and SH3 domains are responsible for the binding of phosphotyrosine-containing sequences and proline-rich sequences, respectively. There are two PI-PLC-gamma isozymes (1-2), both of which are activated by receptor and non-receptor tyrosine kinases due to the presence of SH2 and SH3 domains.


Pssm-ID: 320031 [Multi-domain]  Cd Length: 145  Bit Score: 37.17  E-value: 9.13e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 966976445 604 KKRFHKFDADKKGFITIVDVQRVLESINVQMDENTLHEILNEVDLNKNGQVELNEFLQL 662
Cdd:cd16201    3 RKEFYSMDRTRRETVTLKDLKAFLPRVNCKISTNKLREKFQEVDTRRRGELGFDDFAQL 61
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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