|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02464 |
PLN02464 |
glycerol-3-phosphate dehydrogenase |
1-599 |
0e+00 |
|
glycerol-3-phosphate dehydrogenase
Pssm-ID: 215257 [Multi-domain] Cd Length: 627 Bit Score: 733.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 1 MAFQKVVK-GTILMGGGALATVLGLSQFA-HYRRKQVSLAYVEAAtcFSEPvNREPPSREAQLMTLQNTS---EFDILVI 75
Cdd:PLN02464 1 MSLARLRRlAAGAAATAAGGAVYLSPQPAsSDKGGGPALDSLRDR--IADP-NASVPSRSAQESALIGATaaePLDVLVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 76 GGGATGCGCALDAVTRGLKTALVERNDFASGTSSRSTKLIHGGVRYLQKAITNLDVEQYRMVKEALHERANLLEIAPHLS 155
Cdd:PLN02464 78 GGGATGAGVALDAATRGLRVGLVEREDFSSGTSSRSTKLIHGGVRYLEKAVFQLDYGQLKLVFHALEERKQLIENAPHLC 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 156 APLPIMLPLYKWWQLPYYWVGIKMYDLVAGSHCLKSSYVLSKSRALEHFPMLQKDK----LVGAIVYYDGQHNDARMNLA 231
Cdd:PLN02464 158 HALPIMTPCYDWFEVPYYWAGLKAYDLVAGPRLLHLSRYYSAKESLELFPTLAKKGkdgsLKGTVVYYDGQMNDSRLNVA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 232 IALTAARYGAATANYMEVVSLLKktDPETGkeRVSGARCKDVLTGHEFNVRAKCVINATGPFTDSVRKMDDNDVVPICQP 311
Cdd:PLN02464 238 LACTAALAGAAVLNYAEVVSLIK--DESTG--RIVGARVRDNLTGKEFDVYAKVVVNAAGPFCDEVRKMADGKAKPMICP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 312 SAGVHIVMPGYYSPENMGLLDPATSDGRVIFFLPWEKMTIAGTTDSPTDVTHHPIPSEDDINFILNEVRNYLscDVEVRR 391
Cdd:PLN02464 314 SSGVHIVLPDYYSPEGMGLIVPKTKDGRVVFMLPWLGRTVAGTTDSKTPITMLPEPHEDEIQFILDAISDYL--NVKVRR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 392 GDVLAAWSGIRPLVTDPKSANTQSISRNHVVEVSDSGLITIAGGKWTTYRSMAEDTVNKAVKLHNL-NAGPSRTVGLFLQ 470
Cdd:PLN02464 392 SDVLSAWSGIRPLAVDPSAKSTESISRDHVVCEEPDGLVTITGGKWTTYRSMAEDAVDAAIKSGKLsPTNGCVTTDLPLV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 471 GGKDWSPTLYIRLVQDY--------------GLESEVAQHLAKTYGDKAFDVAKMASVTGkrwpvVGVRLVSEFPYIEAE 536
Cdd:PLN02464 472 GAEGYEPSLFTQLAQQYvrmkrtyggkvvpgAMDTAAAKHLAHAYGGRADRVAEIAQNEG-----LGKRLAHGYPFLEAE 546
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958760019 537 VKYGIK-EYACTAVDMISRRTRLAFLNVQAAEEALPKIVELMGRELNWSELRKQEELETATRFL 599
Cdd:PLN02464 547 VAYCARhEYCESAVDFIARRTRLAFLDTDAAVRALPRVVEILAAEHGWDKSRKKQELQKAKEFL 610
|
|
| GlpA |
COG0578 |
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ... |
86-599 |
0e+00 |
|
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate dehydrogenase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440343 [Multi-domain] Cd Length: 501 Bit Score: 585.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 86 LDAVTRGLKTALVERNDFASGTSSRSTKLIHGGVRYLqkaitnldvEQY--RMVKEALHERANLLEIAPHLSAPLPIMLP 163
Cdd:COG0578 1 RDAAGRGLSVALVEKGDFASGTSSRSSKLIHGGLRYL---------EQGefRLVREALREREVLLRNAPHLVRPLPFLLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 164 LYKWWQLP--YYWVGIKMYDLVAGSHCLKSSYVLSKSRALEHFPMLQKDKLVGAIVYYDGQHNDARMNLAIALTAARYGA 241
Cdd:COG0578 72 LYKGGERPawLIRAGLFLYDLLAGRKGLPRHRRLSRAEALALAPLLRPDGLRGGFEYYDAQVDDARLVLELARTAAERGA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 242 ATANYMEVVSLLKKTDpetgkeRVSGARCKDVLTGHEFNVRAKCVINATGPFTDSVRKMDDNDVVPICQPSAGVHIVMPG 321
Cdd:COG0578 152 VVLNYTRVTGLLRDGG------RVWGVTVRDRLTGEEFTVRARVVVNATGPWVDELRALDGPKAPRRVRPSKGSHLVVPR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 322 YYSPENMGLLDPATSDGRVIFFLPWEKMTIAGTTDspTDVTH---HPIPSEDDINFILNEVRNYLscDVEVRRGDVLAAW 398
Cdd:COG0578 226 LFLPLDDALYIFQNTDGRVVFAIPWEGRTLIGTTD--TDYDGdpdEPAATEEEIDYLLEAANRYF--ARPLTRDDVVSTY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 399 SGIRPLVtDPKSANTQSISRNHVVEVSDSGLITIAGGKWTTYRSMAEDTVNKAVKLHNLNAGPSRTVGLFLQGGKDWSPT 478
Cdd:COG0578 302 AGVRPLL-DDGGKDTSALSRDHVIEVGPAGLLSIAGGKLTTYRKMAEDAVDAAARLLGLPRRPCWTADLPLPGGDAGFDA 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 479 LYIRLVQDYGLESEVAQHLAKTYGDKAFDVAKMAsvtgKRWPVVGVRLVSEFPYIEAEVKYGIK-EYACTAVDMISRRTR 557
Cdd:COG0578 381 FVAALAAAPGLPEALARRLLRRYGTRAEEVLALA----AEDPDLGEPLGPGLPYLEAEVVYAVRhEMARTLEDVLLRRTR 456
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1958760019 558 LAFLNVQAAEEALPKIVELMGRELNWSELRKQEELETATRFL 599
Cdd:COG0578 457 LGLLDADAAAAAAPAVAELMAAELGWDDARRAAEVAAYRALL 498
|
|
| DAO_C |
pfam16901 |
C-terminal domain of alpha-glycerophosphate oxidase; DAO_C is the C-terminal region of ... |
462-588 |
3.04e-54 |
|
C-terminal domain of alpha-glycerophosphate oxidase; DAO_C is the C-terminal region of alpha-glycerophosphate oxidase.
Pssm-ID: 465305 [Multi-domain] Cd Length: 126 Bit Score: 182.35 E-value: 3.04e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 462 SRTVGLFLQGGKDWSPTLYIRLVQDYGLESEVAQHLAKTYGDKAFDVAKMASVTGKrwPVVGVRLVSEFPYIEAEVKYGI 541
Cdd:pfam16901 1 CVTKKLPLLGADGYSANLAARLAQRYGLDEEVAEHLARRYGSRADEVLELALADGD--PELGERLSPAYPYIEAEVVYAV 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1958760019 542 K-EYACTAVDMISRRTRLAFLNVQAAEEALPKIVELMGRELNWSELRK 588
Cdd:pfam16901 79 RhEMALTLVDVLARRTRLAFLDADAALEALPEVADLMAEELGWDEARR 126
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
627-689 |
3.18e-14 |
|
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.
Pssm-ID: 238008 [Multi-domain] Cd Length: 63 Bit Score: 67.57 E-value: 3.18e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958760019 627 RYKKRFHMFDEDEKGFITIVDVQRVLESINVQMDEDTLHEILCEVDLNKNGQVELHEFLQLMS 689
Cdd:cd00051 1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
|
|
| EF-hand_7 |
pfam13499 |
EF-hand domain pair; |
625-689 |
2.67e-09 |
|
EF-hand domain pair;
Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 53.80 E-value: 2.67e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958760019 625 IDRYKKRFHMFDEDEKGFITIVDVQRVLESI--NVQMDEDTLHEILCEVDLNKNGQVELHEFLQLMS 689
Cdd:pfam13499 1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLeeGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
|
|
| PTZ00184 |
PTZ00184 |
calmodulin; Provisional |
624-689 |
3.16e-07 |
|
calmodulin; Provisional
Pssm-ID: 185504 [Multi-domain] Cd Length: 149 Bit Score: 50.53 E-value: 3.16e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958760019 624 DIDRYKKRFHMFDEDEKGFITIVDVQRVLESINVQMDEDTLHEILCEVDLNKNGQVELHEFLQLMS 689
Cdd:PTZ00184 9 QIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTLMA 74
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
610-693 |
1.66e-05 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 45.17 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 610 EQLTDSTEISLLPPDIDRYKKRFHMFDEDEKGFITIVDVQRVLESINVqmDEDTLHEILCEVDLNKNGQVELHEFLQLMS 689
Cdd:COG5126 53 EEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGV--SEEEADELFARLDTDGDGKISFEEFVAAVR 130
|
....
gi 1958760019 690 AVHT 693
Cdd:COG5126 131 DYYT 134
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02464 |
PLN02464 |
glycerol-3-phosphate dehydrogenase |
1-599 |
0e+00 |
|
glycerol-3-phosphate dehydrogenase
Pssm-ID: 215257 [Multi-domain] Cd Length: 627 Bit Score: 733.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 1 MAFQKVVK-GTILMGGGALATVLGLSQFA-HYRRKQVSLAYVEAAtcFSEPvNREPPSREAQLMTLQNTS---EFDILVI 75
Cdd:PLN02464 1 MSLARLRRlAAGAAATAAGGAVYLSPQPAsSDKGGGPALDSLRDR--IADP-NASVPSRSAQESALIGATaaePLDVLVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 76 GGGATGCGCALDAVTRGLKTALVERNDFASGTSSRSTKLIHGGVRYLQKAITNLDVEQYRMVKEALHERANLLEIAPHLS 155
Cdd:PLN02464 78 GGGATGAGVALDAATRGLRVGLVEREDFSSGTSSRSTKLIHGGVRYLEKAVFQLDYGQLKLVFHALEERKQLIENAPHLC 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 156 APLPIMLPLYKWWQLPYYWVGIKMYDLVAGSHCLKSSYVLSKSRALEHFPMLQKDK----LVGAIVYYDGQHNDARMNLA 231
Cdd:PLN02464 158 HALPIMTPCYDWFEVPYYWAGLKAYDLVAGPRLLHLSRYYSAKESLELFPTLAKKGkdgsLKGTVVYYDGQMNDSRLNVA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 232 IALTAARYGAATANYMEVVSLLKktDPETGkeRVSGARCKDVLTGHEFNVRAKCVINATGPFTDSVRKMDDNDVVPICQP 311
Cdd:PLN02464 238 LACTAALAGAAVLNYAEVVSLIK--DESTG--RIVGARVRDNLTGKEFDVYAKVVVNAAGPFCDEVRKMADGKAKPMICP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 312 SAGVHIVMPGYYSPENMGLLDPATSDGRVIFFLPWEKMTIAGTTDSPTDVTHHPIPSEDDINFILNEVRNYLscDVEVRR 391
Cdd:PLN02464 314 SSGVHIVLPDYYSPEGMGLIVPKTKDGRVVFMLPWLGRTVAGTTDSKTPITMLPEPHEDEIQFILDAISDYL--NVKVRR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 392 GDVLAAWSGIRPLVTDPKSANTQSISRNHVVEVSDSGLITIAGGKWTTYRSMAEDTVNKAVKLHNL-NAGPSRTVGLFLQ 470
Cdd:PLN02464 392 SDVLSAWSGIRPLAVDPSAKSTESISRDHVVCEEPDGLVTITGGKWTTYRSMAEDAVDAAIKSGKLsPTNGCVTTDLPLV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 471 GGKDWSPTLYIRLVQDY--------------GLESEVAQHLAKTYGDKAFDVAKMASVTGkrwpvVGVRLVSEFPYIEAE 536
Cdd:PLN02464 472 GAEGYEPSLFTQLAQQYvrmkrtyggkvvpgAMDTAAAKHLAHAYGGRADRVAEIAQNEG-----LGKRLAHGYPFLEAE 546
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958760019 537 VKYGIK-EYACTAVDMISRRTRLAFLNVQAAEEALPKIVELMGRELNWSELRKQEELETATRFL 599
Cdd:PLN02464 547 VAYCARhEYCESAVDFIARRTRLAFLDTDAAVRALPRVVEILAAEHGWDKSRKKQELQKAKEFL 610
|
|
| GlpA |
COG0578 |
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ... |
86-599 |
0e+00 |
|
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate dehydrogenase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440343 [Multi-domain] Cd Length: 501 Bit Score: 585.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 86 LDAVTRGLKTALVERNDFASGTSSRSTKLIHGGVRYLqkaitnldvEQY--RMVKEALHERANLLEIAPHLSAPLPIMLP 163
Cdd:COG0578 1 RDAAGRGLSVALVEKGDFASGTSSRSSKLIHGGLRYL---------EQGefRLVREALREREVLLRNAPHLVRPLPFLLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 164 LYKWWQLP--YYWVGIKMYDLVAGSHCLKSSYVLSKSRALEHFPMLQKDKLVGAIVYYDGQHNDARMNLAIALTAARYGA 241
Cdd:COG0578 72 LYKGGERPawLIRAGLFLYDLLAGRKGLPRHRRLSRAEALALAPLLRPDGLRGGFEYYDAQVDDARLVLELARTAAERGA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 242 ATANYMEVVSLLKKTDpetgkeRVSGARCKDVLTGHEFNVRAKCVINATGPFTDSVRKMDDNDVVPICQPSAGVHIVMPG 321
Cdd:COG0578 152 VVLNYTRVTGLLRDGG------RVWGVTVRDRLTGEEFTVRARVVVNATGPWVDELRALDGPKAPRRVRPSKGSHLVVPR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 322 YYSPENMGLLDPATSDGRVIFFLPWEKMTIAGTTDspTDVTH---HPIPSEDDINFILNEVRNYLscDVEVRRGDVLAAW 398
Cdd:COG0578 226 LFLPLDDALYIFQNTDGRVVFAIPWEGRTLIGTTD--TDYDGdpdEPAATEEEIDYLLEAANRYF--ARPLTRDDVVSTY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 399 SGIRPLVtDPKSANTQSISRNHVVEVSDSGLITIAGGKWTTYRSMAEDTVNKAVKLHNLNAGPSRTVGLFLQGGKDWSPT 478
Cdd:COG0578 302 AGVRPLL-DDGGKDTSALSRDHVIEVGPAGLLSIAGGKLTTYRKMAEDAVDAAARLLGLPRRPCWTADLPLPGGDAGFDA 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 479 LYIRLVQDYGLESEVAQHLAKTYGDKAFDVAKMAsvtgKRWPVVGVRLVSEFPYIEAEVKYGIK-EYACTAVDMISRRTR 557
Cdd:COG0578 381 FVAALAAAPGLPEALARRLLRRYGTRAEEVLALA----AEDPDLGEPLGPGLPYLEAEVVYAVRhEMARTLEDVLLRRTR 456
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1958760019 558 LAFLNVQAAEEALPKIVELMGRELNWSELRKQEELETATRFL 599
Cdd:COG0578 457 LGLLDADAAAAAAPAVAELMAAELGWDDARRAAEVAAYRALL 498
|
|
| glpD |
PRK12266 |
glycerol-3-phosphate dehydrogenase; Reviewed |
87-569 |
6.71e-77 |
|
glycerol-3-phosphate dehydrogenase; Reviewed
Pssm-ID: 237027 [Multi-domain] Cd Length: 508 Bit Score: 256.22 E-value: 6.71e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 87 DAVTRGLKTALVERNDFASGTSSRSTKLIHGGVRYLqkaitnldvEQY--RMVKEALHERANLLEIAPHLSAPLPIMLPL 164
Cdd:PRK12266 24 DAAGRGLSVLLCEQDDLASATSSASTKLIHGGLRYL---------EHYefRLVREALAEREVLLRMAPHIIWPMRFVLPH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 165 YKW----WQLPyywVGIKMYDLVAGSHCLKSSYVLSKSRALEHFPMlqKDKLVGAIVYYDGQHNDARMNLAIALTAARYG 240
Cdd:PRK12266 95 RPHlrpaWMIR---AGLFLYDHLGKRKSLPGSRGLDLGRDPAGSPL--KPEITRGFEYSDCWVDDARLVVLNARDAAERG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 241 AATANYMEVVSLlkktdpetgkERVSG---ARCKDVLTGHEFNVRAKCVINATGP----FTDSVRKMDDNDVVPICQpsa 313
Cdd:PRK12266 170 AEILTRTRVVSA----------RRENGlwhVTLEDTATGKRYTVRARALVNAAGPwvkqFLDDGLGLPSPYGIRLVK--- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 314 GVHIVMPGYYSPE------NmglldpatSDGRVIFFLPWE-KMTIAGTTD-----SPTDVThhpIpSEDDINFILNEVRN 381
Cdd:PRK12266 237 GSHIVVPRLFDHDqayilqN--------PDGRIVFAIPYEdDFTLIGTTDveykgDPAKVA---I-SEEEIDYLCKVVNR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 382 YLscDVEVRRGDVLAAWSGIRPLVTDpKSANTQSISRNHVVEVSDSG----LITIAGGKWTTYRSMAEDTVNKaVKLHNL 457
Cdd:PRK12266 305 YF--KKQLTPADVVWTYSGVRPLCDD-ESDSAQAITRDYTLELDDENggapLLSVFGGKITTYRKLAEHALEK-LAPYLP 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 458 NAGPSRTVGLFLQGGkDWSPTLYIRLVQDY-----GLESEVAQHLAKTYGDKAFDVAKMASVTGKRWPVVGVRLvsefpY 532
Cdd:PRK12266 381 QMGPAWTAGAPLPGG-DFPGDRFDALAAALrrrypWLPEALARRLARAYGTRAERLLGGATSLADLGEHFGHGL-----Y 454
|
490 500 510
....*....|....*....|....*....|....*...
gi 1958760019 533 iEAEVKYGIK-EYACTAVDMISRRTRLAfLNVQAAEEA 569
Cdd:PRK12266 455 -EAEVDYLVEhEWARTAEDILWRRTKLG-LRLDAEQQA 490
|
|
| PRK13369 |
PRK13369 |
glycerol-3-phosphate dehydrogenase; Provisional |
87-569 |
9.14e-74 |
|
glycerol-3-phosphate dehydrogenase; Provisional
Pssm-ID: 237365 [Multi-domain] Cd Length: 502 Bit Score: 247.57 E-value: 9.14e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 87 DAVTRGLKTALVERNDFASGTSSRSTKLIHGGVRYLqkaitnldvEQY--RMVKEALHERANLLEIAPHLSAPLPIMLP- 163
Cdd:PRK13369 24 DAAGRGLKVLLCEKDDLAQGTSSRSGKLVHGGLRYL---------EYYefRLVREALIEREVLLAAAPHIIWPMRFVLPh 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 164 ---LYKWWQLPyywVGIKMYDLVAGSHCLKSSYVLSKSRALEHFPMlqKDKLVGAIVYYDGQHNDARMNLAIALTAARYG 240
Cdd:PRK13369 95 speDRPAWLVR---LGLFLYDHLGGRKRLPGTRTLDLRRDPEGAPL--KPEYTKGFEYSDCWVDDARLVVLNALDAAERG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 241 AATanymevvsllkktdpETGKERVSGARCKDVLT-------GHEFNVRAKCVINATGPFTDSVRKMddndvVPICQPSA 313
Cdd:PRK13369 170 ATI---------------LTRTRCVSARREGGLWRvetrdadGETRTVRARALVNAAGPWVTDVIHR-----VAGSNSSR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 314 GV------HIVMPGYYSPENMGLLDpaTSDGRVIFFLPWEK-MTIAGTTD-----SPTDVThhpiPSEDDINFILNEVRN 381
Cdd:PRK13369 230 NVrlvkgsHIVVPKFWDGAQAYLFQ--NPDKRVIFANPYEGdFTLIGTTDiayegDPEDVA----ADEEEIDYLLDAANR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 382 YLScdVEVRRGDVLAAWSGIRPLVTDpKSANTQSISRNHVVEVSDSG----LITIAGGKWTTYRSMAEDTVNKaVKLHNL 457
Cdd:PRK13369 304 YFK--EKLRREDVVHSFSGVRPLFDD-GAGNPSAVTRDYVFDLDAETggapLLSVFGGKITTFRKLAEHALER-LKPFFP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 458 NAGPSRTVGLFLQGGkDWSPTLYIRLVQDYG-----LESEVAQHLAKTYGDKAFDVAKMASVTGKRWPVVGVRLVsefpy 532
Cdd:PRK13369 380 QMGGDWTAGAPLPGG-DIANADFDTFADDLRdrypwLPRPLAHRYARLYGTRAKDVLGGARSLEDLGRHFGGGLT----- 453
|
490 500 510
....*....|....*....|....*....|....*...
gi 1958760019 533 iEAEVKYGI-KEYACTAVDMISRRTRLAfLNVQAAEEA 569
Cdd:PRK13369 454 -EAEVRYLVaREWARTAEDILWRRTKLG-LHLSAAERA 489
|
|
| DAO_C |
pfam16901 |
C-terminal domain of alpha-glycerophosphate oxidase; DAO_C is the C-terminal region of ... |
462-588 |
3.04e-54 |
|
C-terminal domain of alpha-glycerophosphate oxidase; DAO_C is the C-terminal region of alpha-glycerophosphate oxidase.
Pssm-ID: 465305 [Multi-domain] Cd Length: 126 Bit Score: 182.35 E-value: 3.04e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 462 SRTVGLFLQGGKDWSPTLYIRLVQDYGLESEVAQHLAKTYGDKAFDVAKMASVTGKrwPVVGVRLVSEFPYIEAEVKYGI 541
Cdd:pfam16901 1 CVTKKLPLLGADGYSANLAARLAQRYGLDEEVAEHLARRYGSRADEVLELALADGD--PELGERLSPAYPYIEAEVVYAV 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1958760019 542 K-EYACTAVDMISRRTRLAFLNVQAAEEALPKIVELMGRELNWSELRK 588
Cdd:pfam16901 79 RhEMALTLVDVLARRTRLAFLDADAALEALPEVADLMAEELGWDEARR 126
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
71-441 |
1.74e-33 |
|
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.
Pssm-ID: 426168 [Multi-domain] Cd Length: 339 Bit Score: 131.75 E-value: 1.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 71 DILVIGggatgcgcaLDAVTRGLKTALVERN-DFASGTSSRSTKLIHGGVRYLQKAitnldvEQYRMVKEALHERANLLE 149
Cdd:pfam01266 1 DVVVIGggivglstaYELARRGLSVTLLERGdDPGSGASGRNAGLIHPGLRYLEPS------ELARLALEALDLWEELEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 150 I-APHLSAPLPIMLPLYKWWQLPYYwvgIKMYDLVAGShcLKSSYVLSKSRALEHFPMLqkDKLVGAIVYYDGQH-NDAR 227
Cdd:pfam01266 75 ElGIDCGFRRCGVLVLARDEEEEAL---EKLLAALRRL--GVPAELLDAEELRELEPLL--PGLRGGLFYPDGGHvDPAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 228 MNLAIALTAARYGAATANYMEVVSLLKktdpetgKERVSGARckdvLTGHefnvrAKCVINATGPFTDSVRKMddnDVVP 307
Cdd:pfam01266 148 LLRALARAAEALGVRIIEGTEVTGIEE-------EGGVWGVV----TTGE-----ADAVVNAAGAWADLLALP---GLRL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 308 ICQPSAGVHIVMPGYYSPENMGLLDPATSDGRVIFFLPWEK-MTIAGTTDSPTDvTHHPIPSEDDINFILNEVRNYLScd 386
Cdd:pfam01266 209 PVRPVRGQVLVLEPLPEALLILPVPITVDPGRGVYLRPRADgRLLLGGTDEEDG-FDDPTPDPEEIEELLEAARRLFP-- 285
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958760019 387 vevRRGDVLAAWSGIRPLvTDPKSANTQSISRNHVVEV--SDSGLITIAG-GKWTTYR 441
Cdd:pfam01266 286 ---ALADIERAWAGLRPL-PDGLPIIGRPGSPGLYLATghGGHGLTLAPGiGKLLAEL 339
|
|
| glpA |
PRK11101 |
anaerobic glycerol-3-phosphate dehydrogenase subunit A; |
87-558 |
1.65e-28 |
|
anaerobic glycerol-3-phosphate dehydrogenase subunit A;
Pssm-ID: 236847 [Multi-domain] Cd Length: 546 Bit Score: 120.51 E-value: 1.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 87 DAVTRGLKTALVERNDFASGTSSRSTKLIHGGVRYlqkAITnlDVEQYRmvkEALHERANLLEIAPHLSAP---LPIMLP 163
Cdd:PRK11101 24 DCALRGLRCILVERHDIATGATGRNHGLLHSGARY---AVT--DAESAR---ECISENQILKRIARHCVEPtdgLFITLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 164 LYkwwQLPYYWVGIKMYDLvAGSHCLKssyvLSKSRALEHFPMLQKDkLVGAIVYYDGQHNDARMNLAIALTAARYGAAT 243
Cdd:PRK11101 96 ED---DLAFQATFIRACEE-AGIEAEA----IDPQQALILEPAVNPA-LIGAVKVPDGTVDPFRLTAANMLDAKEHGAQI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 244 ANYMEVVSLLKKTDpetgkeRVSGARCKDVLTGHEFNVRAKCVINATGPFTDSVRKMDDNDVVPIcqPSAGVHIVMPgyY 323
Cdd:PRK11101 167 LTYHEVTGLIREGD------TVCGVRVRDHLTGETQEIHAPVVVNAAGIWGQHIAEYADLRIRMF--PAKGSLLIMD--H 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 324 SPENMGL---LDPATSDGRVifflPWEKMTIAGTTDsptdvTHHPIPSEDDINFILNEVrnylscDVEVRRGDVLA---- 396
Cdd:PRK11101 237 RINNHVInrcRKPADADILV----PGDTISLIGTTS-----TRIDYDQIDDNRVTAEEV------DILLREGEKLApvma 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 397 ------AWSGIRPLVTDPKSANTQSISR-----NHVVEVSDSGLITIAGGKWTTYRSMAEDTVNKAVKLHNlNAGPSRTV 465
Cdd:PRK11101 302 ktrilrAYAGVRPLVASDDDPSGRNVSRgivllDHAERDGLDGFITITGGKLMTYRLMAEWATDAVCRKLG-NTRPCTTA 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 466 GLFLQGGKDWSPTLYIRLVqdyGLESEVAQHLAKTYGDKAFDVakmasVTGKRwpvVGVRLVSEFPYIEA-EVKYGIKEY 544
Cdd:PRK11101 381 DTPLPGSQEPAEVTLRKVI---SLPAPLRGSAVYRHGDRAPAW-----LSEGR---LDRSLVCECEAVTAgEVRYAVENL 449
|
490
....*....|....*
gi 1958760019 545 AC-TAVDMiSRRTRL 558
Cdd:PRK11101 450 NVnNLLDL-RRRTRV 463
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
91-407 |
8.55e-16 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 79.56 E-value: 8.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 91 RGLKTALVERNDFASGTSSRSTklihGGVRYLQKAITnlDVEQYRMVKEALHEranLLEIAPHLSAPLPimlplykWWQL 170
Cdd:COG0665 24 RGLDVTVLERGRPGSGASGRNA----GQLRPGLAALA--DRALVRLAREALDL---WRELAAELGIDCD-------FRRT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 171 PYYWVG--IKMYDLVAGSHCLKSSY-----VLSKSRALEHFPMLQKDKLVGAIVYydgqHNDARMN-----LAIALTAAR 238
Cdd:COG0665 88 GVLYLArtEAELAALRAEAEALRALglpveLLDAAELREREPGLGSPDYAGGLYD----PDDGHVDpaklvRALARAARA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 239 YGAATANYMEVVSLlkktdpetgkeRVSGARCKDVLTGHEfNVRAKCVINATGPFTDSVRKMDDNDvVPIcQPSAGVHIV 318
Cdd:COG0665 164 AGVRIREGTPVTGL-----------EREGGRVTGVRTERG-TVRADAVVLAAGAWSARLLPMLGLR-LPL-RPVRGYVLV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 319 MPgyysPENMGLLDPATSDGRVIFFLPWEKMTIAGTTDSPTDvtHHPIPSEDDINFILNEVRNYL--SCDVEVRRgdvla 396
Cdd:COG0665 230 TE----PLPDLPLRPVLDDTGVYLRPTADGRLLVGGTAEPAG--FDRAPTPERLEALLRRLRRLFpaLADAEIVR----- 298
|
330
....*....|.
gi 1958760019 397 AWSGIRPLVTD 407
Cdd:COG0665 299 AWAGLRPMTPD 309
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
627-689 |
3.18e-14 |
|
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.
Pssm-ID: 238008 [Multi-domain] Cd Length: 63 Bit Score: 67.57 E-value: 3.18e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958760019 627 RYKKRFHMFDEDEKGFITIVDVQRVLESINVQMDEDTLHEILCEVDLNKNGQVELHEFLQLMS 689
Cdd:cd00051 1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
|
|
| EF-hand_7 |
pfam13499 |
EF-hand domain pair; |
625-689 |
2.67e-09 |
|
EF-hand domain pair;
Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 53.80 E-value: 2.67e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958760019 625 IDRYKKRFHMFDEDEKGFITIVDVQRVLESI--NVQMDEDTLHEILCEVDLNKNGQVELHEFLQLMS 689
Cdd:pfam13499 1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLeeGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
|
|
| PTZ00184 |
PTZ00184 |
calmodulin; Provisional |
624-689 |
3.16e-07 |
|
calmodulin; Provisional
Pssm-ID: 185504 [Multi-domain] Cd Length: 149 Bit Score: 50.53 E-value: 3.16e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958760019 624 DIDRYKKRFHMFDEDEKGFITIVDVQRVLESINVQMDEDTLHEILCEVDLNKNGQVELHEFLQLMS 689
Cdd:PTZ00184 9 QIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTLMA 74
|
|
| EFh_PI-PLC |
cd15898 |
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ... |
627-688 |
5.70e-07 |
|
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) isozymes; PI-PLC isozymes are signaling enzymes that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. This family corresponds to the four EF-hand motifs containing PI-PLC isozymes, including PI-PLC-beta (1-4), -gamma (1-2), -delta (1,3,4), -epsilon (1), -zeta (1), eta (1-2). Lower eukaryotes such as yeast and slime molds contain only delta-type isozymes. In contrast, other types of isoforms present in higher eukaryotes. This family also includes 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1 (PLC1) from fungi. Some homologs from plants contain only two atypical EF-hand motifs and they are not included. All PI-PLC isozymes except sperm-specific PI-PLC-zeta share a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. PI-PLC-zeta lacks the PH domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Most of EF-hand motifs found in PI-PLCs consist of a helix-loop-helix structure, but lack residues critical to metal binding. Moreover, the EF-hand region of most of PI-PLCs may have an important regulatory function, but it has yet to be identified. However, PI-PLC-zeta is a key exception. It is responsible for Ca2+ oscillations in fertilized oocytes and exhibits a high sensitivity to Ca2+ mediated through its EF-hand domain. In addition, PI-PLC-eta2 shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Also it appears that PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. PI-PLCs can be activated by a variety of extracellular ligands, such as growth factors, hormones, cytokines and lipids. Their activation has been implicated in tumorigenesis and/or metastasis linked to migration, proliferation, growth, inflammation, angiogenesis and actin cytoskeleton reorganization. PI-PLC-beta isozymes are activated by G-protein coupled receptor (GPCR) through different mechanisms. However, PI-PLC-gamma isozymes are activated by receptor tyrosine kinase (RTK), such as Rho and Ras GTPases. In contrast, PI-PLC-epsilon are activated by both GPCR and RTK. PI-PLC-delta1 and PLC-eta 1 are activated by GPCR-mediated calcium mobilization. The activation mechanism for PI-PLC-zeta remains unclear.
Pssm-ID: 320029 [Multi-domain] Cd Length: 137 Bit Score: 49.20 E-value: 5.70e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958760019 627 RYKKRFHMFDEDEKGFITIVDVQRVLESINVQMDEDTLHEILCEVDLNKNGQVELHEFLQLM 688
Cdd:cd15898 1 WLRRQWIKADKDGDGKLSLKEIKKLLKRLNIRVSEKELKKLFKEVDTNGDGTLTFDEFEELY 62
|
|
| PTZ00184 |
PTZ00184 |
calmodulin; Provisional |
626-688 |
9.80e-07 |
|
calmodulin; Provisional
Pssm-ID: 185504 [Multi-domain] Cd Length: 149 Bit Score: 48.99 E-value: 9.80e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958760019 626 DRYKKRFHMFDEDEKGFITIVDVQRVLESINVQMDEDTLHEILCEVDLNKNGQVELHEFLQLM 688
Cdd:PTZ00184 84 EEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKMM 146
|
|
| PTZ00183 |
PTZ00183 |
centrin; Provisional |
630-688 |
1.04e-05 |
|
centrin; Provisional
Pssm-ID: 185503 [Multi-domain] Cd Length: 158 Bit Score: 46.22 E-value: 1.04e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958760019 630 KRFHMFDEDEKGFITIVDVQRVLESINVQMDEDTLHEILCEVDLNKNGQVELHEFLQLM 688
Cdd:PTZ00183 94 KAFRLFDDDKTGKISLKNLKRVAKELGETITDEELQEMIDEADRNGDGEISEEEFYRIM 152
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
610-693 |
1.66e-05 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 45.17 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760019 610 EQLTDSTEISLLPPDIDRYKKRFHMFDEDEKGFITIVDVQRVLESINVqmDEDTLHEILCEVDLNKNGQVELHEFLQLMS 689
Cdd:COG5126 53 EEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGV--SEEEADELFARLDTDGDGKISFEEFVAAVR 130
|
....
gi 1958760019 690 AVHT 693
Cdd:COG5126 131 DYYT 134
|
|
| EFh_PI-PLCdelta |
cd16202 |
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ... |
629-686 |
4.63e-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: 4.63e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958760019 629 KKRFHMFDEDEKGFITIVDVQRVLESINVQMDEDTLHEILCEVDLNKNGQVELHEFLQ 686
Cdd:cd16202 3 KDQFRKADKNGDGKLSFKECKKLLKKLNVKVDKDYAKKLFQEADTSGEDVLDEEEFVQ 60
|
|
| PTZ00183 |
PTZ00183 |
centrin; Provisional |
612-690 |
1.55e-03 |
|
centrin; Provisional
Pssm-ID: 185503 [Multi-domain] Cd Length: 158 Bit Score: 39.67 E-value: 1.55e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958760019 612 LTDSTEISLLPPDIDRYKKRFHMFDEDEKGFITIVDVQRVLESINVQMDEDTLHEILCEVDLNKNGQVELHEFLQLMSA 690
Cdd:PTZ00183 3 KRRSERPGLTEDQKKEIREAFDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIADVDKDGSGKIDFEEFLDIMTK 81
|
|
| EF-hand_6 |
pfam13405 |
EF-hand domain; |
627-656 |
5.93e-03 |
|
EF-hand domain;
Pssm-ID: 463869 [Multi-domain] Cd Length: 30 Bit Score: 34.84 E-value: 5.93e-03
10 20 30
....*....|....*....|....*....|
gi 1958760019 627 RYKKRFHMFDEDEKGFITIVDVQRVLESIN 656
Cdd:pfam13405 1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
|
|
| EFh_PEF_ALG-2_like |
cd16185 |
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ... |
632-691 |
8.54e-03 |
|
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein (ALG-2); The family includes some homologs of mammalian apoptosis-linked gene 2 protein (ALG-2) mainly found in lower eukaryotes, such as a parasitic protist Leishmarua major and a cellular slime mold Dictyostelium discoideum. These homologs contains five EF-hand motifs. Due to the presence of unfavorable residues at the Ca2+-coordinating positions, their non-canonical EF4 and EF5 hands may not bind Ca2+. Two Dictyostelium PEF proteins are the prototypes of this family. They may bind to cytoskeletal proteins and/or signal-transducing proteins localized to detergent-resistant membranes named lipid rafts, and occur as monomers or weak homo- or heterodimers like ALG-2. They can serve as a mediator for Ca2+ signaling-related Dictyostehum programmed cell death (PCD).
Pssm-ID: 320060 [Multi-domain] Cd Length: 163 Bit Score: 37.58 E-value: 8.54e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958760019 632 FHMFDEDEKGFITIVDVQRVLESINVQMDEDTLHEILCEVDLNKNGQV------ELHEFLQLMSAV 691
Cdd:cd16185 6 FRAVDRDRSGSIDVNELQKALAGGGLLFSLATAEKLIRMFDRDGNGTIdfeefaALHQFLSNMQNG 71
|
|
| |
