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Conserved domains on  [gi|1958760021|ref|XP_038960263|]
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glycerol-3-phosphate dehydrogenase, mitochondrial isoform X3 [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: ...
23-572 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: 732.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021  23 VNREPPSREAQLMTLQNTS---EFDILVIGGGATGCGCALDAVTRGLKTALVERNDFASGTSSRSTKLIHGGVRYLQKAI 99
Cdd:PLN02464   49 PNASVPSRSAQESALIGATaaePLDVLVVGGGATGAGVALDAATRGLRVGLVEREDFSSGTSSRSTKLIHGGVRYLEKAV 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 100 TNLDVEQYRMVKEALHERANLLEIAPHLSAPLPIMLPLYKWWQLPYYWVGIKMYDLVAGSHCLKSSYVLSKSRALEHFPM 179
Cdd:PLN02464  129 FQLDYGQLKLVFHALEERKQLIENAPHLCHALPIMTPCYDWFEVPYYWAGLKAYDLVAGPRLLHLSRYYSAKESLELFPT 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 180 LQKDK----LVGAIVYYDGQHNDARMNLAIALTAARYGAATANYMEVVSLLKktDPETGkeRVSGARCKDVLTGHEFNVR 255
Cdd:PLN02464  209 LAKKGkdgsLKGTVVYYDGQMNDSRLNVALACTAALAGAAVLNYAEVVSLIK--DESTG--RIVGARVRDNLTGKEFDVY 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 256 AKCVINATGPFTDSVRKMDDNDVVPICQPSAGVHIVMPGYYSPENMGLLDPATSDGRVIFFLPWEKMTIAGTTDSPTDVT 335
Cdd:PLN02464  285 AKVVVNAAGPFCDEVRKMADGKAKPMICPSSGVHIVLPDYYSPEGMGLIVPKTKDGRVVFMLPWLGRTVAGTTDSKTPIT 364
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 336 HHPIPSEDDINFILNEVRNYLscDVEVRRGDVLAAWSGIRPLVTDPKSANTQSISRNHVVEVSDSGLITIAGGKWTTYRS 415
Cdd:PLN02464  365 MLPEPHEDEIQFILDAISDYL--NVKVRRSDVLSAWSGIRPLAVDPSAKSTESISRDHVVCEEPDGLVTITGGKWTTYRS 442
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 416 MAEDTVNKAVKLHNL-NAGPSRTVGLFLQGGKDWSPTLYIRLVQDY--------------GLESEVAQHLAKTYGDKAFD 480
Cdd:PLN02464  443 MAEDAVDAAIKSGKLsPTNGCVTTDLPLVGAEGYEPSLFTQLAQQYvrmkrtyggkvvpgAMDTAAAKHLAHAYGGRADR 522
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 481 VAKMASVTGkrwpvVGVRLVSEFPYIEAEVKYGIK-EYACTAVDMISRRTRLAFLNVQAAEEALPKIVELMGRELNWSEL 559
Cdd:PLN02464  523 VAEIAQNEG-----LGKRLAHGYPFLEAEVAYCARhEYCESAVDFIARRTRLAFLDTDAAVRALPRVVEILAAEHGWDKS 597
                         570
                  ....*....|...
gi 1958760021 560 RKQEELETATRFL 572
Cdd:PLN02464  598 RKKQELQKAKEFL 610
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
600-662 3.06e-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: 3.06e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958760021 600 RYKKRFHMFDEDEKGFITIVDVQRVLESINVQMDEDTLHEILCEVDLNKNGQVELHEFLQLMS 662
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
 
Name Accession Description Interval E-value
PLN02464 PLN02464
glycerol-3-phosphate dehydrogenase
23-572 0e+00

glycerol-3-phosphate dehydrogenase


Pssm-ID: 215257 [Multi-domain]  Cd Length: 627  Bit Score: 732.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021  23 VNREPPSREAQLMTLQNTS---EFDILVIGGGATGCGCALDAVTRGLKTALVERNDFASGTSSRSTKLIHGGVRYLQKAI 99
Cdd:PLN02464   49 PNASVPSRSAQESALIGATaaePLDVLVVGGGATGAGVALDAATRGLRVGLVEREDFSSGTSSRSTKLIHGGVRYLEKAV 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 100 TNLDVEQYRMVKEALHERANLLEIAPHLSAPLPIMLPLYKWWQLPYYWVGIKMYDLVAGSHCLKSSYVLSKSRALEHFPM 179
Cdd:PLN02464  129 FQLDYGQLKLVFHALEERKQLIENAPHLCHALPIMTPCYDWFEVPYYWAGLKAYDLVAGPRLLHLSRYYSAKESLELFPT 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 180 LQKDK----LVGAIVYYDGQHNDARMNLAIALTAARYGAATANYMEVVSLLKktDPETGkeRVSGARCKDVLTGHEFNVR 255
Cdd:PLN02464  209 LAKKGkdgsLKGTVVYYDGQMNDSRLNVALACTAALAGAAVLNYAEVVSLIK--DESTG--RIVGARVRDNLTGKEFDVY 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 256 AKCVINATGPFTDSVRKMDDNDVVPICQPSAGVHIVMPGYYSPENMGLLDPATSDGRVIFFLPWEKMTIAGTTDSPTDVT 335
Cdd:PLN02464  285 AKVVVNAAGPFCDEVRKMADGKAKPMICPSSGVHIVLPDYYSPEGMGLIVPKTKDGRVVFMLPWLGRTVAGTTDSKTPIT 364
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 336 HHPIPSEDDINFILNEVRNYLscDVEVRRGDVLAAWSGIRPLVTDPKSANTQSISRNHVVEVSDSGLITIAGGKWTTYRS 415
Cdd:PLN02464  365 MLPEPHEDEIQFILDAISDYL--NVKVRRSDVLSAWSGIRPLAVDPSAKSTESISRDHVVCEEPDGLVTITGGKWTTYRS 442
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 416 MAEDTVNKAVKLHNL-NAGPSRTVGLFLQGGKDWSPTLYIRLVQDY--------------GLESEVAQHLAKTYGDKAFD 480
Cdd:PLN02464  443 MAEDAVDAAIKSGKLsPTNGCVTTDLPLVGAEGYEPSLFTQLAQQYvrmkrtyggkvvpgAMDTAAAKHLAHAYGGRADR 522
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 481 VAKMASVTGkrwpvVGVRLVSEFPYIEAEVKYGIK-EYACTAVDMISRRTRLAFLNVQAAEEALPKIVELMGRELNWSEL 559
Cdd:PLN02464  523 VAEIAQNEG-----LGKRLAHGYPFLEAEVAYCARhEYCESAVDFIARRTRLAFLDTDAAVRALPRVVEILAAEHGWDKS 597
                         570
                  ....*....|...
gi 1958760021 560 RKQEELETATRFL 572
Cdd:PLN02464  598 RKKQELQKAKEFL 610
GlpA COG0578
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ...
59-572 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: 585.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021  59 LDAVTRGLKTALVERNDFASGTSSRSTKLIHGGVRYLqkaitnldvEQY--RMVKEALHERANLLEIAPHLSAPLPIMLP 136
Cdd:COG0578     1 RDAAGRGLSVALVEKGDFASGTSSRSSKLIHGGLRYL---------EQGefRLVREALREREVLLRNAPHLVRPLPFLLP 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 137 LYKWWQLP--YYWVGIKMYDLVAGSHCLKSSYVLSKSRALEHFPMLQKDKLVGAIVYYDGQHNDARMNLAIALTAARYGA 214
Cdd:COG0578    72 LYKGGERPawLIRAGLFLYDLLAGRKGLPRHRRLSRAEALALAPLLRPDGLRGGFEYYDAQVDDARLVLELARTAAERGA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 215 ATANYMEVVSLLKKTDpetgkeRVSGARCKDVLTGHEFNVRAKCVINATGPFTDSVRKMDDNDVVPICQPSAGVHIVMPG 294
Cdd:COG0578   152 VVLNYTRVTGLLRDGG------RVWGVTVRDRLTGEEFTVRARVVVNATGPWVDELRALDGPKAPRRVRPSKGSHLVVPR 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 295 YYSPENMGLLDPATSDGRVIFFLPWEKMTIAGTTDspTDVTH---HPIPSEDDINFILNEVRNYLscDVEVRRGDVLAAW 371
Cdd:COG0578   226 LFLPLDDALYIFQNTDGRVVFAIPWEGRTLIGTTD--TDYDGdpdEPAATEEEIDYLLEAANRYF--ARPLTRDDVVSTY 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 372 SGIRPLVtDPKSANTQSISRNHVVEVSDSGLITIAGGKWTTYRSMAEDTVNKAVKLHNLNAGPSRTVGLFLQGGKDWSPT 451
Cdd:COG0578   302 AGVRPLL-DDGGKDTSALSRDHVIEVGPAGLLSIAGGKLTTYRKMAEDAVDAAARLLGLPRRPCWTADLPLPGGDAGFDA 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 452 LYIRLVQDYGLESEVAQHLAKTYGDKAFDVAKMAsvtgKRWPVVGVRLVSEFPYIEAEVKYGIK-EYACTAVDMISRRTR 530
Cdd:COG0578   381 FVAALAAAPGLPEALARRLLRRYGTRAEEVLALA----AEDPDLGEPLGPGLPYLEAEVVYAVRhEMARTLEDVLLRRTR 456
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 1958760021 531 LAFLNVQAAEEALPKIVELMGRELNWSELRKQEELETATRFL 572
Cdd:COG0578   457 LGLLDADAAAAAAPAVAELMAAELGWDDARRAAEVAAYRALL 498
DAO_C pfam16901
C-terminal domain of alpha-glycerophosphate oxidase; DAO_C is the C-terminal region of ...
435-561 2.66e-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: 2.66e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 435 SRTVGLFLQGGKDWSPTLYIRLVQDYGLESEVAQHLAKTYGDKAFDVAKMASVTGKrwPVVGVRLVSEFPYIEAEVKYGI 514
Cdd:pfam16901   1 CVTKKLPLLGADGYSANLAARLAQRYGLDEEVAEHLARRYGSRADEVLELALADGD--PELGERLSPAYPYIEAEVVYAV 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958760021 515 K-EYACTAVDMISRRTRLAFLNVQAAEEALPKIVELMGRELNWSELRK 561
Cdd:pfam16901  79 RhEMALTLVDVLARRTRLAFLDADAALEALPEVADLMAEELGWDEARR 126
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
600-662 3.06e-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: 3.06e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958760021 600 RYKKRFHMFDEDEKGFITIVDVQRVLESINVQMDEDTLHEILCEVDLNKNGQVELHEFLQLMS 662
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EF-hand_7 pfam13499
EF-hand domain pair;
598-662 2.78e-09

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 53.80  E-value: 2.78e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958760021 598 IDRYKKRFHMFDEDEKGFITIVDVQRVLESI--NVQMDEDTLHEILCEVDLNKNGQVELHEFLQLMS 662
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLeeGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
PTZ00184 PTZ00184
calmodulin; Provisional
597-662 3.18e-07

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 50.15  E-value: 3.18e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958760021 597 DIDRYKKRFHMFDEDEKGFITIVDVQRVLESINVQMDEDTLHEILCEVDLNKNGQVELHEFLQLMS 662
Cdd:PTZ00184    9 QIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTLMA 74
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
583-666 1.54e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.17  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 583 EQLTDSTEISLLPPDIDRYKKRFHMFDEDEKGFITIVDVQRVLESINVqmDEDTLHEILCEVDLNKNGQVELHEFLQLMS 662
Cdd:COG5126    53 EEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGV--SEEEADELFARLDTDGDGKISFEEFVAAVR 130

                  ....
gi 1958760021 663 AVHT 666
Cdd:COG5126   131 DYYT 134
 
Name Accession Description Interval E-value
PLN02464 PLN02464
glycerol-3-phosphate dehydrogenase
23-572 0e+00

glycerol-3-phosphate dehydrogenase


Pssm-ID: 215257 [Multi-domain]  Cd Length: 627  Bit Score: 732.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021  23 VNREPPSREAQLMTLQNTS---EFDILVIGGGATGCGCALDAVTRGLKTALVERNDFASGTSSRSTKLIHGGVRYLQKAI 99
Cdd:PLN02464   49 PNASVPSRSAQESALIGATaaePLDVLVVGGGATGAGVALDAATRGLRVGLVEREDFSSGTSSRSTKLIHGGVRYLEKAV 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 100 TNLDVEQYRMVKEALHERANLLEIAPHLSAPLPIMLPLYKWWQLPYYWVGIKMYDLVAGSHCLKSSYVLSKSRALEHFPM 179
Cdd:PLN02464  129 FQLDYGQLKLVFHALEERKQLIENAPHLCHALPIMTPCYDWFEVPYYWAGLKAYDLVAGPRLLHLSRYYSAKESLELFPT 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 180 LQKDK----LVGAIVYYDGQHNDARMNLAIALTAARYGAATANYMEVVSLLKktDPETGkeRVSGARCKDVLTGHEFNVR 255
Cdd:PLN02464  209 LAKKGkdgsLKGTVVYYDGQMNDSRLNVALACTAALAGAAVLNYAEVVSLIK--DESTG--RIVGARVRDNLTGKEFDVY 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 256 AKCVINATGPFTDSVRKMDDNDVVPICQPSAGVHIVMPGYYSPENMGLLDPATSDGRVIFFLPWEKMTIAGTTDSPTDVT 335
Cdd:PLN02464  285 AKVVVNAAGPFCDEVRKMADGKAKPMICPSSGVHIVLPDYYSPEGMGLIVPKTKDGRVVFMLPWLGRTVAGTTDSKTPIT 364
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 336 HHPIPSEDDINFILNEVRNYLscDVEVRRGDVLAAWSGIRPLVTDPKSANTQSISRNHVVEVSDSGLITIAGGKWTTYRS 415
Cdd:PLN02464  365 MLPEPHEDEIQFILDAISDYL--NVKVRRSDVLSAWSGIRPLAVDPSAKSTESISRDHVVCEEPDGLVTITGGKWTTYRS 442
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 416 MAEDTVNKAVKLHNL-NAGPSRTVGLFLQGGKDWSPTLYIRLVQDY--------------GLESEVAQHLAKTYGDKAFD 480
Cdd:PLN02464  443 MAEDAVDAAIKSGKLsPTNGCVTTDLPLVGAEGYEPSLFTQLAQQYvrmkrtyggkvvpgAMDTAAAKHLAHAYGGRADR 522
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 481 VAKMASVTGkrwpvVGVRLVSEFPYIEAEVKYGIK-EYACTAVDMISRRTRLAFLNVQAAEEALPKIVELMGRELNWSEL 559
Cdd:PLN02464  523 VAEIAQNEG-----LGKRLAHGYPFLEAEVAYCARhEYCESAVDFIARRTRLAFLDTDAAVRALPRVVEILAAEHGWDKS 597
                         570
                  ....*....|...
gi 1958760021 560 RKQEELETATRFL 572
Cdd:PLN02464  598 RKKQELQKAKEFL 610
GlpA COG0578
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ...
59-572 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: 585.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021  59 LDAVTRGLKTALVERNDFASGTSSRSTKLIHGGVRYLqkaitnldvEQY--RMVKEALHERANLLEIAPHLSAPLPIMLP 136
Cdd:COG0578     1 RDAAGRGLSVALVEKGDFASGTSSRSSKLIHGGLRYL---------EQGefRLVREALREREVLLRNAPHLVRPLPFLLP 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 137 LYKWWQLP--YYWVGIKMYDLVAGSHCLKSSYVLSKSRALEHFPMLQKDKLVGAIVYYDGQHNDARMNLAIALTAARYGA 214
Cdd:COG0578    72 LYKGGERPawLIRAGLFLYDLLAGRKGLPRHRRLSRAEALALAPLLRPDGLRGGFEYYDAQVDDARLVLELARTAAERGA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 215 ATANYMEVVSLLKKTDpetgkeRVSGARCKDVLTGHEFNVRAKCVINATGPFTDSVRKMDDNDVVPICQPSAGVHIVMPG 294
Cdd:COG0578   152 VVLNYTRVTGLLRDGG------RVWGVTVRDRLTGEEFTVRARVVVNATGPWVDELRALDGPKAPRRVRPSKGSHLVVPR 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 295 YYSPENMGLLDPATSDGRVIFFLPWEKMTIAGTTDspTDVTH---HPIPSEDDINFILNEVRNYLscDVEVRRGDVLAAW 371
Cdd:COG0578   226 LFLPLDDALYIFQNTDGRVVFAIPWEGRTLIGTTD--TDYDGdpdEPAATEEEIDYLLEAANRYF--ARPLTRDDVVSTY 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 372 SGIRPLVtDPKSANTQSISRNHVVEVSDSGLITIAGGKWTTYRSMAEDTVNKAVKLHNLNAGPSRTVGLFLQGGKDWSPT 451
Cdd:COG0578   302 AGVRPLL-DDGGKDTSALSRDHVIEVGPAGLLSIAGGKLTTYRKMAEDAVDAAARLLGLPRRPCWTADLPLPGGDAGFDA 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 452 LYIRLVQDYGLESEVAQHLAKTYGDKAFDVAKMAsvtgKRWPVVGVRLVSEFPYIEAEVKYGIK-EYACTAVDMISRRTR 530
Cdd:COG0578   381 FVAALAAAPGLPEALARRLLRRYGTRAEEVLALA----AEDPDLGEPLGPGLPYLEAEVVYAVRhEMARTLEDVLLRRTR 456
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 1958760021 531 LAFLNVQAAEEALPKIVELMGRELNWSELRKQEELETATRFL 572
Cdd:COG0578   457 LGLLDADAAAAAAPAVAELMAAELGWDDARRAAEVAAYRALL 498
glpD PRK12266
glycerol-3-phosphate dehydrogenase; Reviewed
60-542 3.70e-77

glycerol-3-phosphate dehydrogenase; Reviewed


Pssm-ID: 237027 [Multi-domain]  Cd Length: 508  Bit Score: 256.22  E-value: 3.70e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021  60 DAVTRGLKTALVERNDFASGTSSRSTKLIHGGVRYLqkaitnldvEQY--RMVKEALHERANLLEIAPHLSAPLPIMLPL 137
Cdd:PRK12266   24 DAAGRGLSVLLCEQDDLASATSSASTKLIHGGLRYL---------EHYefRLVREALAEREVLLRMAPHIIWPMRFVLPH 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 138 YKW----WQLPyywVGIKMYDLVAGSHCLKSSYVLSKSRALEHFPMlqKDKLVGAIVYYDGQHNDARMNLAIALTAARYG 213
Cdd:PRK12266   95 RPHlrpaWMIR---AGLFLYDHLGKRKSLPGSRGLDLGRDPAGSPL--KPEITRGFEYSDCWVDDARLVVLNARDAAERG 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 214 AATANYMEVVSLlkktdpetgkERVSG---ARCKDVLTGHEFNVRAKCVINATGP----FTDSVRKMDDNDVVPICQpsa 286
Cdd:PRK12266  170 AEILTRTRVVSA----------RRENGlwhVTLEDTATGKRYTVRARALVNAAGPwvkqFLDDGLGLPSPYGIRLVK--- 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 287 GVHIVMPGYYSPE------NmglldpatSDGRVIFFLPWE-KMTIAGTTD-----SPTDVThhpIpSEDDINFILNEVRN 354
Cdd:PRK12266  237 GSHIVVPRLFDHDqayilqN--------PDGRIVFAIPYEdDFTLIGTTDveykgDPAKVA---I-SEEEIDYLCKVVNR 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 355 YLscDVEVRRGDVLAAWSGIRPLVTDpKSANTQSISRNHVVEVSDSG----LITIAGGKWTTYRSMAEDTVNKaVKLHNL 430
Cdd:PRK12266  305 YF--KKQLTPADVVWTYSGVRPLCDD-ESDSAQAITRDYTLELDDENggapLLSVFGGKITTYRKLAEHALEK-LAPYLP 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 431 NAGPSRTVGLFLQGGkDWSPTLYIRLVQDY-----GLESEVAQHLAKTYGDKAFDVAKMASVTGKRWPVVGVRLvsefpY 505
Cdd:PRK12266  381 QMGPAWTAGAPLPGG-DFPGDRFDALAAALrrrypWLPEALARRLARAYGTRAERLLGGATSLADLGEHFGHGL-----Y 454
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 1958760021 506 iEAEVKYGIK-EYACTAVDMISRRTRLAfLNVQAAEEA 542
Cdd:PRK12266  455 -EAEVDYLVEhEWARTAEDILWRRTKLG-LRLDAEQQA 490
PRK13369 PRK13369
glycerol-3-phosphate dehydrogenase; Provisional
60-542 4.60e-74

glycerol-3-phosphate dehydrogenase; Provisional


Pssm-ID: 237365 [Multi-domain]  Cd Length: 502  Bit Score: 247.96  E-value: 4.60e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021  60 DAVTRGLKTALVERNDFASGTSSRSTKLIHGGVRYLqkaitnldvEQY--RMVKEALHERANLLEIAPHLSAPLPIMLP- 136
Cdd:PRK13369   24 DAAGRGLKVLLCEKDDLAQGTSSRSGKLVHGGLRYL---------EYYefRLVREALIEREVLLAAAPHIIWPMRFVLPh 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 137 ---LYKWWQLPyywVGIKMYDLVAGSHCLKSSYVLSKSRALEHFPMlqKDKLVGAIVYYDGQHNDARMNLAIALTAARYG 213
Cdd:PRK13369   95 speDRPAWLVR---LGLFLYDHLGGRKRLPGTRTLDLRRDPEGAPL--KPEYTKGFEYSDCWVDDARLVVLNALDAAERG 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 214 AATanymevvsllkktdpETGKERVSGARCKDVLT-------GHEFNVRAKCVINATGPFTDSVRKMddndvVPICQPSA 286
Cdd:PRK13369  170 ATI---------------LTRTRCVSARREGGLWRvetrdadGETRTVRARALVNAAGPWVTDVIHR-----VAGSNSSR 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 287 GV------HIVMPGYYSPENMGLLDpaTSDGRVIFFLPWEK-MTIAGTTD-----SPTDVThhpiPSEDDINFILNEVRN 354
Cdd:PRK13369  230 NVrlvkgsHIVVPKFWDGAQAYLFQ--NPDKRVIFANPYEGdFTLIGTTDiayegDPEDVA----ADEEEIDYLLDAANR 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 355 YLScdVEVRRGDVLAAWSGIRPLVTDpKSANTQSISRNHVVEVSDSG----LITIAGGKWTTYRSMAEDTVNKaVKLHNL 430
Cdd:PRK13369  304 YFK--EKLRREDVVHSFSGVRPLFDD-GAGNPSAVTRDYVFDLDAETggapLLSVFGGKITTFRKLAEHALER-LKPFFP 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 431 NAGPSRTVGLFLQGGkDWSPTLYIRLVQDYG-----LESEVAQHLAKTYGDKAFDVAKMASVTGKRWPVVGVRLVsefpy 505
Cdd:PRK13369  380 QMGGDWTAGAPLPGG-DIANADFDTFADDLRdrypwLPRPLAHRYARLYGTRAKDVLGGARSLEDLGRHFGGGLT----- 453
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 1958760021 506 iEAEVKYGI-KEYACTAVDMISRRTRLAfLNVQAAEEA 542
Cdd:PRK13369  454 -EAEVRYLVaREWARTAEDILWRRTKLG-LHLSAAERA 489
DAO_C pfam16901
C-terminal domain of alpha-glycerophosphate oxidase; DAO_C is the C-terminal region of ...
435-561 2.66e-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: 2.66e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 435 SRTVGLFLQGGKDWSPTLYIRLVQDYGLESEVAQHLAKTYGDKAFDVAKMASVTGKrwPVVGVRLVSEFPYIEAEVKYGI 514
Cdd:pfam16901   1 CVTKKLPLLGADGYSANLAARLAQRYGLDEEVAEHLARRYGSRADEVLELALADGD--PELGERLSPAYPYIEAEVVYAV 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958760021 515 K-EYACTAVDMISRRTRLAFLNVQAAEEALPKIVELMGRELNWSELRK 561
Cdd:pfam16901  79 RhEMALTLVDVLARRTRLAFLDADAALEALPEVADLMAEELGWDEARR 126
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
44-414 7.84e-34

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: 132.52  E-value: 7.84e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021  44 DILVIGggatgcgcaLDAVTRGLKTALVERN-DFASGTSSRSTKLIHGGVRYLQKAitnldvEQYRMVKEALHERANLLE 122
Cdd:pfam01266   1 DVVVIGggivglstaYELARRGLSVTLLERGdDPGSGASGRNAGLIHPGLRYLEPS------ELARLALEALDLWEELEE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 123 I-APHLSAPLPIMLPLYKWWQLPYYwvgIKMYDLVAGShcLKSSYVLSKSRALEHFPMLqkDKLVGAIVYYDGQH-NDAR 200
Cdd:pfam01266  75 ElGIDCGFRRCGVLVLARDEEEEAL---EKLLAALRRL--GVPAELLDAEELRELEPLL--PGLRGGLFYPDGGHvDPAR 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 201 MNLAIALTAARYGAATANYMEVVSLLKktdpetgKERVSGARckdvLTGHefnvrAKCVINATGPFTDSVRKMddnDVVP 280
Cdd:pfam01266 148 LLRALARAAEALGVRIIEGTEVTGIEE-------EGGVWGVV----TTGE-----ADAVVNAAGAWADLLALP---GLRL 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 281 ICQPSAGVHIVMPGYYSPENMGLLDPATSDGRVIFFLPWEK-MTIAGTTDSPTDvTHHPIPSEDDINFILNEVRNYLScd 359
Cdd:pfam01266 209 PVRPVRGQVLVLEPLPEALLILPVPITVDPGRGVYLRPRADgRLLLGGTDEEDG-FDDPTPDPEEIEELLEAARRLFP-- 285
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958760021 360 vevRRGDVLAAWSGIRPLvTDPKSANTQSISRNHVVEV--SDSGLITIAG-GKWTTYR 414
Cdd:pfam01266 286 ---ALADIERAWAGLRPL-PDGLPIIGRPGSPGLYLATghGGHGLTLAPGiGKLLAEL 339
glpA PRK11101
anaerobic glycerol-3-phosphate dehydrogenase subunit A;
60-531 1.49e-28

anaerobic glycerol-3-phosphate dehydrogenase subunit A;


Pssm-ID: 236847 [Multi-domain]  Cd Length: 546  Bit Score: 120.51  E-value: 1.49e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021  60 DAVTRGLKTALVERNDFASGTSSRSTKLIHGGVRYlqkAITnlDVEQYRmvkEALHERANLLEIAPHLSAP---LPIMLP 136
Cdd:PRK11101   24 DCALRGLRCILVERHDIATGATGRNHGLLHSGARY---AVT--DAESAR---ECISENQILKRIARHCVEPtdgLFITLP 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 137 LYkwwQLPYYWVGIKMYDLvAGSHCLKssyvLSKSRALEHFPMLQKDkLVGAIVYYDGQHNDARMNLAIALTAARYGAAT 216
Cdd:PRK11101   96 ED---DLAFQATFIRACEE-AGIEAEA----IDPQQALILEPAVNPA-LIGAVKVPDGTVDPFRLTAANMLDAKEHGAQI 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 217 ANYMEVVSLLKKTDpetgkeRVSGARCKDVLTGHEFNVRAKCVINATGPFTDSVRKMDDNDVVPIcqPSAGVHIVMPgyY 296
Cdd:PRK11101  167 LTYHEVTGLIREGD------TVCGVRVRDHLTGETQEIHAPVVVNAAGIWGQHIAEYADLRIRMF--PAKGSLLIMD--H 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 297 SPENMGL---LDPATSDGRVifflPWEKMTIAGTTDsptdvTHHPIPSEDDINFILNEVrnylscDVEVRRGDVLA---- 369
Cdd:PRK11101  237 RINNHVInrcRKPADADILV----PGDTISLIGTTS-----TRIDYDQIDDNRVTAEEV------DILLREGEKLApvma 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 370 ------AWSGIRPLVTDPKSANTQSISR-----NHVVEVSDSGLITIAGGKWTTYRSMAEDTVNKAVKLHNlNAGPSRTV 438
Cdd:PRK11101  302 ktrilrAYAGVRPLVASDDDPSGRNVSRgivllDHAERDGLDGFITITGGKLMTYRLMAEWATDAVCRKLG-NTRPCTTA 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 439 GLFLQGGKDWSPTLYIRLVqdyGLESEVAQHLAKTYGDKAFDVakmasVTGKRwpvVGVRLVSEFPYIEA-EVKYGIKEY 517
Cdd:PRK11101  381 DTPLPGSQEPAEVTLRKVI---SLPAPLRGSAVYRHGDRAPAW-----LSEGR---LDRSLVCECEAVTAgEVRYAVENL 449
                         490
                  ....*....|....*
gi 1958760021 518 AC-TAVDMiSRRTRL 531
Cdd:PRK11101  450 NVnNLLDL-RRRTRV 463
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
64-380 4.72e-16

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 80.33  E-value: 4.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021  64 RGLKTALVERNDFASGTSSRSTklihGGVRYLQKAITnlDVEQYRMVKEALHEranLLEIAPHLSAPLPimlplykWWQL 143
Cdd:COG0665    24 RGLDVTVLERGRPGSGASGRNA----GQLRPGLAALA--DRALVRLAREALDL---WRELAAELGIDCD-------FRRT 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 144 PYYWVG--IKMYDLVAGSHCLKSSY-----VLSKSRALEHFPMLQKDKLVGAIVYydgqHNDARMN-----LAIALTAAR 211
Cdd:COG0665    88 GVLYLArtEAELAALRAEAEALRALglpveLLDAAELREREPGLGSPDYAGGLYD----PDDGHVDpaklvRALARAARA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 212 YGAATANYMEVVSLlkktdpetgkeRVSGARCKDVLTGHEfNVRAKCVINATGPFTDSVRKMDDNDvVPIcQPSAGVHIV 291
Cdd:COG0665   164 AGVRIREGTPVTGL-----------EREGGRVTGVRTERG-TVRADAVVLAAGAWSARLLPMLGLR-LPL-RPVRGYVLV 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 292 MPgyysPENMGLLDPATSDGRVIFFLPWEKMTIAGTTDSPTDvtHHPIPSEDDINFILNEVRNYL--SCDVEVRRgdvla 369
Cdd:COG0665   230 TE----PLPDLPLRPVLDDTGVYLRPTADGRLLVGGTAEPAG--FDRAPTPERLEALLRRLRRLFpaLADAEIVR----- 298
                         330
                  ....*....|.
gi 1958760021 370 AWSGIRPLVTD 380
Cdd:COG0665   299 AWAGLRPMTPD 309
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
600-662 3.06e-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: 3.06e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958760021 600 RYKKRFHMFDEDEKGFITIVDVQRVLESINVQMDEDTLHEILCEVDLNKNGQVELHEFLQLMS 662
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EF-hand_7 pfam13499
EF-hand domain pair;
598-662 2.78e-09

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 53.80  E-value: 2.78e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958760021 598 IDRYKKRFHMFDEDEKGFITIVDVQRVLESI--NVQMDEDTLHEILCEVDLNKNGQVELHEFLQLMS 662
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLeeGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
PTZ00184 PTZ00184
calmodulin; Provisional
597-662 3.18e-07

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 50.15  E-value: 3.18e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958760021 597 DIDRYKKRFHMFDEDEKGFITIVDVQRVLESINVQMDEDTLHEILCEVDLNKNGQVELHEFLQLMS 662
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. ...
600-661 5.47e-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: 5.47e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958760021 600 RYKKRFHMFDEDEKGFITIVDVQRVLESINVQMDEDTLHEILCEVDLNKNGQVELHEFLQLM 661
Cdd:cd15898     1 WLRRQWIKADKDGDGKLSLKEIKKLLKRLNIRVSEKELKKLFKEVDTNGDGTLTFDEFEELY 62
PTZ00184 PTZ00184
calmodulin; Provisional
599-661 9.85e-07

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 48.99  E-value: 9.85e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958760021 599 DRYKKRFHMFDEDEKGFITIVDVQRVLESINVQMDEDTLHEILCEVDLNKNGQVELHEFLQLM 661
Cdd:PTZ00184   84 EEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKMM 146
PTZ00183 PTZ00183
centrin; Provisional
603-661 9.94e-06

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 46.22  E-value: 9.94e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958760021 603 KRFHMFDEDEKGFITIVDVQRVLESINVQMDEDTLHEILCEVDLNKNGQVELHEFLQLM 661
Cdd:PTZ00183   94 KAFRLFDDDKTGKISLKNLKRVAKELGETITDEELQEMIDEADRNGDGEISEEEFYRIM 152
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
583-666 1.54e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.17  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 583 EQLTDSTEISLLPPDIDRYKKRFHMFDEDEKGFITIVDVQRVLESINVqmDEDTLHEILCEVDLNKNGQVELHEFLQLMS 662
Cdd:COG5126    53 EEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGV--SEEEADELFARLDTDGDGKISFEEFVAAVR 130

                  ....
gi 1958760021 663 AVHT 666
Cdd:COG5126   131 DYYT 134
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
602-659 4.35e-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: 4.35e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958760021 602 KKRFHMFDEDEKGFITIVDVQRVLESINVQMDEDTLHEILCEVDLNKNGQVELHEFLQ 659
Cdd:cd16202     3 KDQFRKADKNGDGKLSFKECKKLLKKLNVKVDKDYAKKLFQEADTSGEDVLDEEEFVQ 60
PTZ00183 PTZ00183
centrin; Provisional
585-663 1.48e-03

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 39.67  E-value: 1.48e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958760021 585 LTDSTEISLLPPDIDRYKKRFHMFDEDEKGFITIVDVQRVLESINVQMDEDTLHEILCEVDLNKNGQVELHEFLQLMSA 663
Cdd:PTZ00183    3 KRRSERPGLTEDQKKEIREAFDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIADVDKDGSGKIDFEEFLDIMTK 81
EF-hand_6 pfam13405
EF-hand domain;
600-629 5.71e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 34.84  E-value: 5.71e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1958760021 600 RYKKRFHMFDEDEKGFITIVDVQRVLESIN 629
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 ...
605-664 8.18e-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: 8.18e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958760021 605 FHMFDEDEKGFITIVDVQRVLESINVQMDEDTLHEILCEVDLNKNGQV------ELHEFLQLMSAV 664
Cdd:cd16185     6 FRAVDRDRSGSIDVNELQKALAGGGLLFSLATAEKLIRMFDRDGNGTIdfeefaALHQFLSNMQNG 71
EFh_PEF_CalpA_B cd16196
Penta-EF hand, calcium binding motifs, found in Drosophila melanogaster calpain-A (CalpA), ...
597-666 9.88e-03

Penta-EF hand, calcium binding motifs, found in Drosophila melanogaster calpain-A (CalpA), calpain-B (CalpB), and similar proteins; The family contains two calpains that have been found in Drosophila, CalpA and CalpB. CalpA, also termed calcium-activated neutral proteinase A (CANP A), or calpain-A catalytic subunit, is a Drosophila calpain homolog specifically expressed in a few neurons in the central nervous system, in scattered endocrine cells in the midgut, and in blood cells. CalpB, also termed calcium-activated neutral proteinase B (CANP B), contains calpain-B catalytic subunit 1 and calpain-B catalytic subunit 2. Both CalpA and CalpB are closely related to that of vertebrate calpains, and they share similar domain architecture, which consists of four domains: the N-terminal domain I, the catalytic domain II carrying the three active site residues, Cys, His and Asn, the Ca2+-regulated phospholipid-binding domain III, and penta-EF-hand Ca2+-binding domain IV. Besides, CalpA and CalpB display some distinguishing structural features that are not found in mammalian typical calpains. CalpA harbors a 76 amino acid long hydrophobic stretch inserted in domain IV, which may be involved in membrane attachment of this enzyme. CalpB has an unusually long N-terminal tail of 224 amino acids, which belongs to the class of intrinsically unstructured proteins (IUP) and may become ordered upon binding to target protein(s). Moreover, they do not need small regulatory subunits for their catalytic activity, and their proteolytic function is not regulated by an intrinsic inhibitor as the Drosophila genome contains neither regulatory subunit nor calpastatin orthologs. As a result, they may exist as a monomer or perhaps as a homo- or heterodimer together with a second large subunit. Furthermore, both CalpA and CalpB are dispensable for viability and fertility and do not share vital functions during Drosophila development. Phosphatidylinositol 4,5-diphosphate, phosphatidylinositol 4-monophosphate, phosphatidylinositol, and phosphatidic acid can stimulate the activity and the rate of activation of CalpA, but not CalpB. Calpain A modulates Toll responses by limited Cactus/IkappaB proteolysis. CalpB directly interacts with talin, an important component of the focal adhesion complex, and functions as an important modulator in border cell migration within egg chambers, which may act via the digestion of talin. CalpB can be phosphorylated by cAMP-dependent protein kinase (protein kinase A, PKA; EC 2.7.11.11) at Ser240 and Ser845, as well as by mitogen-activated protein kinase (ERK1 and ERK2; EC 2.7.11.24) at Thr747. The activation of the ERK pathway by extracellular signals results in the phosphorylation and activation of calpain B. In Schneider cells (S2), calpain B was mainly in the cytoplasm and upon a rise in Ca2+ the enzyme adhered to intracellular membranes.


Pssm-ID: 320071 [Multi-domain]  Cd Length: 167  Bit Score: 37.57  E-value: 9.88e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760021 597 DIDRYKKRFHMFDEDEKGFITIVDVQRVLESINVQMDEDTLHEILCEVDlNKNGQVELHEFLQLMSAVHT 666
Cdd:cd16196    69 DLRSWKRVFKLFDTDGSGSFSSFELRNALNSAGFRLSNATLNALVLRYS-NKDGRISFDDFIMCAVKLKT 137
 
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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