|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02464 |
PLN02464 |
glycerol-3-phosphate dehydrogenase |
9-594 |
0e+00 |
|
glycerol-3-phosphate dehydrogenase
Pssm-ID: 215257 [Multi-domain] Cd Length: 627 Bit Score: 718.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 9 GVTAASACVGSVLAS--YTLDRWNTPhvvnnATVPPKRK-----RTLPPRADQIKSLM---SGEEFDVLIIGGGATGAGC 78
Cdd:PLN02464 12 GAAATAAGGAVYLSPqpASSDKGGGP-----ALDSLRDRiadpnASVPSRSAQESALIgatAAEPLDVLVVGGGATGAGV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 79 ALDSVTRGLKTALVELDDFASGTSSRSTKLIHGGVRYLQKAILGLDLEQYRMVKEALAERATMLESAPHLTHPLPIMLPV 158
Cdd:PLN02464 87 ALDAATRGLRVGLVEREDFSSGTSSRSTKLIHGGVRYLEKAVFQLDYGQLKLVFHALEERKQLIENAPHLCHALPIMTPC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 159 YTWWQVPYYWVGIKAYDLVAGDRNVKSSYYLSKKDALELFPMLKKDK----LCGAIVYYDGQQDDARMCLAVALTAARHG 234
Cdd:PLN02464 167 YDWFEVPYYWAGLKAYDLVAGPRLLHLSRYYSAKESLELFPTLAKKGkdgsLKGTVVYYDGQMNDSRLNVALACTAALAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 235 ATVCNHVEVKELLkKDDGTGKQVlcGAKVKDHISGKEFTVKAKCIVNAAGPFTDSIRKMDNPTVKSICCPSSGVHIVLPG 314
Cdd:PLN02464 247 AAVLNYAEVVSLI-KDESTGRIV--GARVRDNLTGKEFDVYAKVVVNAAGPFCDEVRKMADGKAKPMICPSSGVHIVLPD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 315 YYSPDQMGLLDPSTSDGRVIFFLPWQRQTIAGTTDLPCEITHNPTPTEDEIQFILNEIKNYLNadVEVRRGDVLSAWSGI 394
Cdd:PLN02464 324 YYSPEGMGLIVPKTKDGRVVFMLPWLGRTVAGTTDSKTPITMLPEPHEDEIQFILDAISDYLN--VKVRRSDVLSAWSGI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 395 RPLVSDPNKDDTQSLARNHIVHVSPSNLITIAGGKWTTYRAMAEHTIDAAIKACNLKPERAeAVTSYLKIEGGQGWTPTM 474
Cdd:PLN02464 402 RPLAVDPSAKSTESISRDHVVCEEPDGLVTITGGKWTTYRSMAEDAVDAAIKSGKLSPTNG-CVTTDLPLVGAEGYEPSL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 475 YIRLVQDF--------------GLECEVAQHLAKSYGDRAFAVSKMASLTGkrwpiIGNRIHPEFPYIDAEIRYGVR-EY 539
Cdd:PLN02464 481 FTQLAQQYvrmkrtyggkvvpgAMDTAAAKHLAHAYGGRADRVAEIAQNEG-----LGKRLAHGYPFLEAEVAYCARhEY 555
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 161077125 540 ACTAVDMIARRLRLAFLNVQAAQEALPVIVDIMGEELGWSKDEKERQIKHATEFL 594
Cdd:PLN02464 556 CESAVDFIARRTRLAFLDTDAAVRALPRVVEILAAEHGWDKSRKKQELQKAKEFL 610
|
|
| GlpA |
COG0578 |
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ... |
80-597 |
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: 577.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 80 LDSVTRGLKTALVELDDFASGTSSRSTKLIHGGVRYLqkailgldlEQY--RMVKEALAERATMLESAPHLTHPLPIMLP 157
Cdd:COG0578 1 RDAAGRGLSVALVEKGDFASGTSSRSSKLIHGGLRYL---------EQGefRLVREALREREVLLRNAPHLVRPLPFLLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 158 VYTWWQVP--YYWVGIKAYDLVAGDRNVKSSYYLSKKDALELFPMLKKDKLCGAIVYYDGQQDDARMCLAVALTAARHGA 235
Cdd:COG0578 72 LYKGGERPawLIRAGLFLYDLLAGRKGLPRHRRLSRAEALALAPLLRPDGLRGGFEYYDAQVDDARLVLELARTAAERGA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 236 TVCNHVEVKELLKKDDGtgkqvLCGAKVKDHISGKEFTVKAKCIVNAAGPFTDSIRKMDNPTVKSICCPSSGVHIVLPGY 315
Cdd:COG0578 152 VVLNYTRVTGLLRDGGR-----VWGVTVRDRLTGEEFTVRARVVVNATGPWVDELRALDGPKAPRRVRPSKGSHLVVPRL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 316 YSPDQMGLLDPSTSDGRVIFFLPWQRQTIAGTTDLPCE-ITHNPTPTEDEIQFILNEIKNYLnaDVEVRRGDVLSAWSGI 394
Cdd:COG0578 227 FLPLDDALYIFQNTDGRVVFAIPWEGRTLIGTTDTDYDgDPDEPAATEEEIDYLLEAANRYF--ARPLTRDDVVSTYAGV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 395 RPLVsDPNKDDTQSLARNHIVHVSPSNLITIAGGKWTTYRAMAEHTIDAAIKACNLkpERAEAVTSYLKIEGGQGWTPTM 474
Cdd:COG0578 305 RPLL-DDGGKDTSALSRDHVIEVGPAGLLSIAGGKLTTYRKMAEDAVDAAARLLGL--PRRPCWTADLPLPGGDAGFDAF 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 475 YIRLVQDFGLECEVAQHLAKSYGDRAFAVSKMAsltgKRWPIIGNRIHPEFPYIDAEIRYGVR-EYACTAVDMIARRLRL 553
Cdd:COG0578 382 VAALAAAPGLPEALARRLLRRYGTRAEEVLALA----AEDPDLGEPLGPGLPYLEAEVVYAVRhEMARTLEDVLLRRTRL 457
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 161077125 554 AFLNVQAAQEALPVIVDIMGEELGWSKDEKERQIKHATEFLANE 597
Cdd:COG0578 458 GLLDADAAAAAAPAVAELMAAELGWDDARRAAEVAAYRALLAAY 501
|
|
| glpD |
PRK12266 |
glycerol-3-phosphate dehydrogenase; Reviewed |
81-565 |
9.91e-70 |
|
glycerol-3-phosphate dehydrogenase; Reviewed
Pssm-ID: 237027 [Multi-domain] Cd Length: 508 Bit Score: 236.96 E-value: 9.91e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 81 DSVTRGLKTALVELDDFASGTSSRSTKLIHGGVRYLqkailgldlEQY--RMVKEALAERATMLESAPHLTHPLPIMLPv 158
Cdd:PRK12266 24 DAAGRGLSVLLCEQDDLASATSSASTKLIHGGLRYL---------EHYefRLVREALAEREVLLRMAPHIIWPMRFVLP- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 159 YTWWQVPYyWVgIKA----YDLVAGDRNVKSSYYLS-KKDALE--LFPMLKKdklcgAIVYYDGQQDDARMCLAVALTAA 231
Cdd:PRK12266 94 HRPHLRPA-WM-IRAglflYDHLGKRKSLPGSRGLDlGRDPAGspLKPEITR-----GFEYSDCWVDDARLVVLNARDAA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 232 RHGATVCNHVEVkELLKKDDGtgkqvLCGAKVKDHISGKEFTVKAKCIVNAAGP----FTDSIRKMDNPT----VKsicc 303
Cdd:PRK12266 167 ERGAEILTRTRV-VSARRENG-----LWHVTLEDTATGKRYTVRARALVNAAGPwvkqFLDDGLGLPSPYgirlVK---- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 304 pssGVHIVLPGYYSPDQMGLLdpSTSDGRVIFFLPWQRQ-TIAGTTDlpCEITHNPTP---TEDEIQFILNEIKNYLNad 379
Cdd:PRK12266 237 ---GSHIVVPRLFDHDQAYIL--QNPDGRIVFAIPYEDDfTLIGTTD--VEYKGDPAKvaiSEEEIDYLCKVVNRYFK-- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 380 VEVRRGDVLSAWSGIRPLVSDPNkDDTQSLARNHIVHVSPSN----LITIAGGKWTTYRAMAEHTIDaaiKACNLKPERA 455
Cdd:PRK12266 308 KQLTPADVVWTYSGVRPLCDDES-DSAQAITRDYTLELDDENggapLLSVFGGKITTYRKLAEHALE---KLAPYLPQMG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 456 EAVTSYLKIEGG--QGWTPTMYI-RLVQDF-GLECEVAQHLAKSYGDRAFAV----SKMASLtGKrwpIIGNRIHpefpy 527
Cdd:PRK12266 384 PAWTAGAPLPGGdfPGDRFDALAaALRRRYpWLPEALARRLARAYGTRAERLlggaTSLADL-GE---HFGHGLY----- 454
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 161077125 528 iDAEIRYGV-REYACTAVDMIARRLRLA-FLNvQAAQEAL 565
Cdd:PRK12266 455 -EAEVDYLVeHEWARTAEDILWRRTKLGlRLD-AEQQARL 492
|
|
| PRK13369 |
PRK13369 |
glycerol-3-phosphate dehydrogenase; Provisional |
81-564 |
3.67e-68 |
|
glycerol-3-phosphate dehydrogenase; Provisional
Pssm-ID: 237365 [Multi-domain] Cd Length: 502 Bit Score: 232.55 E-value: 3.67e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 81 DSVTRGLKTALVELDDFASGTSSRSTKLIHGGVRYlqkailgldLEQY--RMVKEALAERATMLESAPHLTHPLPIMLP- 157
Cdd:PRK13369 24 DAAGRGLKVLLCEKDDLAQGTSSRSGKLVHGGLRY---------LEYYefRLVREALIEREVLLAAAPHIIWPMRFVLPh 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 158 ---VYTWWQVPyywVGIKAYDLVAGDRNVKSSYYLSKKDALELFPMlkKDKLCGAIVYYDGQQDDARMCLAVALTAARHG 234
Cdd:PRK13369 95 speDRPAWLVR---LGLFLYDHLGGRKRLPGTRTLDLRRDPEGAPL--KPEYTKGFEYSDCWVDDARLVVLNALDAAERG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 235 ATVCNHVEVKELLKKDDgtgkqvLCGAKVKDHiSGKEFTVKAKCIVNAAGPFTDSI-----RKMDNPTVKSIccpsSGVH 309
Cdd:PRK13369 170 ATILTRTRCVSARREGG------LWRVETRDA-DGETRTVRARALVNAAGPWVTDVihrvaGSNSSRNVRLV----KGSH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 310 IVLPGYYSPDQMGLLdpSTSDGRVIFFLPWQRQ-TIAGTTDLPCE-ITHNPTPTEDEIQFILNEIKNYLNADveVRRGDV 387
Cdd:PRK13369 239 IVVPKFWDGAQAYLF--QNPDKRVIFANPYEGDfTLIGTTDIAYEgDPEDVAADEEEIDYLLDAANRYFKEK--LRREDV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 388 LSAWSGIRPLVSDpNKDDTQSLARNHIVHVSPSN----LITIAGGKWTTYRAMAEHTIDaaiKACNLKPERAEAVTSYLK 463
Cdd:PRK13369 315 VHSFSGVRPLFDD-GAGNPSAVTRDYVFDLDAETggapLLSVFGGKITTFRKLAEHALE---RLKPFFPQMGGDWTAGAP 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 464 IEGGQ-GWTPtmYIRLVQDFG-----LECEVAQHLAKSYGDRAFAVSKMA-SLTGkrwpiIGNRIHPEFpyIDAEIRYGV 536
Cdd:PRK13369 391 LPGGDiANAD--FDTFADDLRdrypwLPRPLAHRYARLYGTRAKDVLGGArSLED-----LGRHFGGGL--TEAEVRYLV 461
|
490 500
....*....|....*....|....*....
gi 161077125 537 -REYACTAVDMIARRLRLAfLNVQAAQEA 564
Cdd:PRK13369 462 aREWARTAEDILWRRTKLG-LHLSAAERA 489
|
|
| DAO_C |
pfam16901 |
C-terminal domain of alpha-glycerophosphate oxidase; DAO_C is the C-terminal region of ... |
458-583 |
1.01e-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: 186.20 E-value: 1.01e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 458 VTSYLKIEGGQGWTPTMYIRLVQDFGLECEVAQHLAKSYGDRAFAVSKMASLTGKrwPIIGNRIHPEFPYIDAEIRYGVR 537
Cdd:pfam16901 2 VTKKLPLLGADGYSANLAARLAQRYGLDEEVAEHLARRYGSRADEVLELALADGD--PELGERLSPAYPYIEAEVVYAVR 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 161077125 538 -EYACTAVDMIARRLRLAFLNVQAAQEALPVIVDIMGEELGWSKDEK 583
Cdd:pfam16901 80 hEMALTLVDVLARRTRLAFLDADAALEALPEVADLMAEELGWDEARR 126
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
65-434 |
3.74e-37 |
|
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: 142.15 E-value: 3.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 65 DVLIIGggatgagcaLDSVTRGLKTALVELD-DFASGTSSRSTKLIHGGVRYLQKailgldLEQYRMVKEALAERATML- 142
Cdd:pfam01266 1 DVVVIGggivglstaYELARRGLSVTLLERGdDPGSGASGRNAGLIHPGLRYLEP------SELARLALEALDLWEELEe 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 143 ESAPHLTHPLPIMLPVYTWWQVPYYWVGIKAYDLVAGDrnvksSYYLSKKDALELFPMLkkDKLCGAIVYYDGQQ-DDAR 221
Cdd:pfam01266 75 ELGIDCGFRRCGVLVLARDEEEEALEKLLAALRRLGVP-----AELLDAEELRELEPLL--PGLRGGLFYPDGGHvDPAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 222 MCLAVALTAARHGATVCNHVEVKELLKKDDGTGkqvlcgakVKDhisgkefTVKAKCIVNAAGPFTDSIRKmdnPTVKSI 301
Cdd:pfam01266 148 LLRALARAAEALGVRIIEGTEVTGIEEEGGVWG--------VVT-------TGEADAVVNAAGAWADLLAL---PGLRLP 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 302 CCPSSGVHIVLPGYYSPDQMGLLDPSTSDGRVIFFLP-WQRQTIAGTTDLPcEITHNPTPTEDEIQFILNEIKNYLNADV 380
Cdd:pfam01266 210 VRPVRGQVLVLEPLPEALLILPVPITVDPGRGVYLRPrADGRLLLGGTDEE-DGFDDPTPDPEEIEELLEAARRLFPALA 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 161077125 381 EVRRgdvlsAWSGIRPLvSDPNKDDTQSLARNHIV---HVSPSNLITIAGGKWTTYR 434
Cdd:pfam01266 289 DIER-----AWAGLRPL-PDGLPIIGRPGSPGLYLatgHGGHGLTLAPGIGKLLAEL 339
|
|
| glpA |
PRK11101 |
anaerobic glycerol-3-phosphate dehydrogenase subunit A; |
59-446 |
6.37e-26 |
|
anaerobic glycerol-3-phosphate dehydrogenase subunit A;
Pssm-ID: 236847 [Multi-domain] Cd Length: 546 Bit Score: 112.80 E-value: 6.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 59 MSGEEFDVLIIGGGATGAGCALDSVTRGLKTALVELDDFASGTSSRSTKLIHGGVRYLQKailglDLEQYRmvkEALAER 138
Cdd:PRK11101 2 RDSQETDVIIIGGGATGAGIARDCALRGLRCILVERHDIATGATGRNHGLLHSGARYAVT-----DAESAR---ECISEN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 139 ATMLESAPHLTHP---LPIMLPVYTW-WQVPYywvgIKAYDLvAGDRNVKssyyLSKKDALELFPMLKKDkLCGAIVYYD 214
Cdd:PRK11101 74 QILKRIARHCVEPtdgLFITLPEDDLaFQATF----IRACEE-AGIEAEA----IDPQQALILEPAVNPA-LIGAVKVPD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 215 GQQDDARMCLAVALTAARHGATVCNHVEVKELLKKDDgtgkqVLCGAKVKDHISGKEFTVKAKCIVNAAGPFTDSIRKMD 294
Cdd:PRK11101 144 GTVDPFRLTAANMLDAKEHGAQILTYHEVTGLIREGD-----TVCGVRVRDHLTGETQEIHAPVVVNAAGIWGQHIAEYA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 295 NPTVKSIccPSSGVHIVLPgyYSPDQMGL---LDPSTSDGRVifflPWQRQTIAGTTD--LPCEITHNPTPTEDEIQFIL 369
Cdd:PRK11101 219 DLRIRMF--PAKGSLLIMD--HRINNHVInrcRKPADADILV----PGDTISLIGTTStrIDYDQIDDNRVTAEEVDILL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 370 NEIKNYlnADVeVRRGDVLSAWSGIRPLVSDPNKDDTQSLARNhIV---HVSPSNL---ITIAGGKWTTYRAMAEHTIDA 443
Cdd:PRK11101 291 REGEKL--APV-MAKTRILRAYAGVRPLVASDDDPSGRNVSRG-IVlldHAERDGLdgfITITGGKLMTYRLMAEWATDA 366
|
...
gi 161077125 444 AIK 446
Cdd:PRK11101 367 VCR 369
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
62-400 |
1.17e-13 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 73.02 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 62 EEFDVLIIGggatgagcaldS-VT----------RGLKTALVELDDFASGTSSRSTklihGGVRYLQKAILGLDLeqYRM 130
Cdd:COG0665 1 ATADVVVIG-----------GgIAglstayhlarRGLDVTVLERGRPGSGASGRNA----GQLRPGLAALADRAL--VRL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 131 VKEALAERATMLEsaphlTHPLPIMlpvytWWQVPYYWVGIKAYDLVAGDRNVKS-------SYYLSKKDALELFPMLKK 203
Cdd:COG0665 64 AREALDLWRELAA-----ELGIDCD-----FRRTGVLYLARTEAELAALRAEAEAlralglpVELLDAAELREREPGLGS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 204 DKLCGAIVYYDGQQ-DDARMCLAVALTAARHGATVCNHVEVKELLKKDDGTgKQVLCGAKvkdhisgkefTVKAKCIVNA 282
Cdd:COG0665 134 PDYAGGLYDPDDGHvDPAKLVRALARAARAAGVRIREGTPVTGLEREGGRV-TGVRTERG----------TVRADAVVLA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 283 AGPFTDSIRKMDNPTVKSIccPSSGVHIVLPgyysPDQMGLLDPSTSDGRViFFLPW--QRQTIAGTTDLPCEithNPTP 360
Cdd:COG0665 203 AGAWSARLLPMLGLRLPLR--PVRGYVLVTE----PLPDLPLRPVLDDTGV-YLRPTadGRLLVGGTAEPAGF---DRAP 272
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 161077125 361 TEDEIQFILNEIKNYLNADVEVRrgdVLSAWSGIRPLVSD 400
Cdd:COG0665 273 TPERLEALLRRLRRLFPALADAE---IVRAWAGLRPMTPD 309
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
624-684 |
6.16e-13 |
|
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: 64.11 E-value: 6.16e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161077125 624 KRFQLIDKDKKGYVSINDIRRALKSFGDgDVSGEQLHEILREIDTNMNGQVELDEYLQMMS 684
Cdd:cd00051 4 EAFRLFDKDGDGTISADELKAALKSLGE-GLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
|
|
| EF-hand_7 |
pfam13499 |
EF-hand domain pair; |
616-684 |
2.08e-12 |
|
EF-hand domain pair;
Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 62.66 E-value: 2.08e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 616 KEEIQTyikRFQLIDKDKKGYVSINDIRRALKSFG-DGDVSGEQLHEILREIDTNMNGQVELDEYLQMMS 684
Cdd:pfam13499 1 EEKLKE---AFKLLDSDGDGYLDVEELKKLLRKLEeGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
613-690 |
6.90e-09 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 54.80 E-value: 6.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 613 KLSKEEIQTYIKR-------------FQLIDKDKKGYVSINDIRRALKSFGdgdVSGEQLHEILREIDTNMNGQVELDEY 679
Cdd:COG5126 49 RISREEFVAGMESlfeatvepfaraaFDLLDTDGDGKISADEFRRLLTALG---VSEEEADELFARLDTDGDGKISFEEF 125
|
90
....*....|.
gi 161077125 680 LQMMSAIKTGD 690
Cdd:COG5126 126 VAAVRDYYTPD 136
|
|
| PTZ00184 |
PTZ00184 |
calmodulin; Provisional |
610-724 |
3.06e-08 |
|
calmodulin; Provisional
Pssm-ID: 185504 [Multi-domain] Cd Length: 149 Bit Score: 53.23 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 610 IPIKLSKEEIQTYIKRFQLIDKDKKGYVSINDIRRALKSFGDGDVSGEqLHEILREIDTNMNGQVELDEYLQMMsaiktg 689
Cdd:PTZ00184 1 MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAE-LQDMINEVDADGNGTIDFPEFLTLM------ 73
|
90 100 110
....*....|....*....|....*....|....*
gi 161077125 690 dvaySRFARMAELEEQKHEAANLkqisVDRSGGGL 724
Cdd:PTZ00184 74 ----ARKMKDTDSEEEIKEAFKV----FDRDGNGF 100
|
|
| PTZ00184 |
PTZ00184 |
calmodulin; Provisional |
615-683 |
2.81e-07 |
|
calmodulin; Provisional
Pssm-ID: 185504 [Multi-domain] Cd Length: 149 Bit Score: 50.53 E-value: 2.81e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161077125 615 SKEEIqtyIKRFQLIDKDKKGYVSINDIRRALKSFGDgDVSGEQLHEILREIDTNMNGQVELDEYLQMM 683
Cdd:PTZ00184 82 SEEEI---KEAFKVFDRDGNGFISAAELRHVMTNLGE-KLTDEEVDEMIREADVDGDGQINYEEFVKMM 146
|
|
| PTZ00183 |
PTZ00183 |
centrin; Provisional |
603-685 |
1.77e-06 |
|
centrin; Provisional
Pssm-ID: 185503 [Multi-domain] Cd Length: 158 Bit Score: 48.53 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 603 NRTSKEripIKLSKEEIQTYIKRFQLIDKDKKGYVSINDIRRALKSFGdGDVSGEQLHEILREIDTNMNGQVELDEYLQM 682
Cdd:PTZ00183 3 KRRSER---PGLTEDQKKEIREAFDLFDTDGSGTIDPKELKVAMRSLG-FEPKKEEIKQMIADVDKDGSGKIDFEEFLDI 78
|
...
gi 161077125 683 MSA 685
Cdd:PTZ00183 79 MTK 81
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
624-699 |
1.10e-05 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 45.55 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 624 KRFQLIDKDKKGYVSINDIRRALKSF-----------GDGDVSGEQLH----------------EILREIDTNMNGQVEL 676
Cdd:COG5126 9 RRFDLLDADGDGVLERDDFEALFRRLwatlfseadtdGDGRISREEFVagmeslfeatvepfarAAFDLLDTDGDGKISA 88
|
90 100
....*....|....*....|....
gi 161077125 677 DEYLQMMSAIKTGD-VAYSRFARM 699
Cdd:COG5126 89 DEFRRLLTALGVSEeEADELFARL 112
|
|
| EF-hand_8 |
pfam13833 |
EF-hand domain pair; |
633-683 |
1.69e-05 |
|
EF-hand domain pair;
Pssm-ID: 404678 [Multi-domain] Cd Length: 54 Bit Score: 42.69 E-value: 1.69e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 161077125 633 KKGYVSINDIRRALKSFGDGDVSGEQLHEILREIDTNMNGQVELDEYLQMM 683
Cdd:pfam13833 1 EKGVITREELKRALALLGLKDLSEDEVDILFREFDTDGDGYISFDEFCVLL 51
|
|
| PTZ00183 |
PTZ00183 |
centrin; Provisional |
613-683 |
2.57e-05 |
|
centrin; Provisional
Pssm-ID: 185503 [Multi-domain] Cd Length: 158 Bit Score: 45.07 E-value: 2.57e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161077125 613 KLSKEEIQtyiKRFQLIDKDKKGYVSINDIRRALKSFGDgDVSGEQLHEILREIDTNMNGQVELDEYLQMM 683
Cdd:PTZ00183 86 RDPREEIL---KAFRLFDDDKTGKISLKNLKRVAKELGE-TITDEELQEMIDEADRNGDGEISEEEFYRIM 152
|
|
| EF-hand_6 |
pfam13405 |
EF-hand domain; |
624-650 |
2.42e-04 |
|
EF-hand domain;
Pssm-ID: 463869 [Multi-domain] Cd Length: 30 Bit Score: 38.70 E-value: 2.42e-04
10 20
....*....|....*....|....*..
gi 161077125 624 KRFQLIDKDKKGYVSINDIRRALKSFG 650
Cdd:pfam13405 4 EAFKLFDKDGDGKISLEELRKALRSLG 30
|
|
| LhgO |
COG0579 |
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism]; |
62-404 |
4.34e-04 |
|
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
Pssm-ID: 440344 [Multi-domain] Cd Length: 418 Bit Score: 43.21 E-value: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 62 EEFDVLIIgggatg-agcaldSVTRGLKTALVE-LDDFASGTSSRSTKLIHGGVRY------LQKAILGldleqYRMVKE 133
Cdd:COG0579 3 EMYDVVIIgagivglalarelSRYEDLKVLVLEkEDDVAQESSGNNSGVIHAGLYYtpgslkARLCVEG-----NELFYE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 134 ALAERATMLESAPHL---THPLpimlpvytwwQVPYywvgIKA-YDlvAGDRN-VKSSYYLSKKDALELFPMLKKDKLC- 207
Cdd:COG0579 78 LCRELGIPFKRCGKLvvaTGEE----------EVAF----LEKlYE--RGKANgVPGLEILDREELRELEPLLSDEGVAa 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 208 -----GAIVYYdgqqddARMCLAVALTAARHGATVCNHVEVKELLKKDDGTgkqvlcgaKVKdhISGKEFtvKAKCIVNA 282
Cdd:COG0579 142 lyspsTGIVDP------GALTRALAENAEANGVELLLNTEVTGIEREGDGW--------EVT--TNGGTI--RARFVINA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077125 283 AGPFTDSIRKMDNPTVKSICCPSSGVHIVLPGYYS---------PDQ----MG-LLDPsTSDGRVIF-----------FL 337
Cdd:COG0579 204 AGLYADRLAQMAGIGKDFGIFPVKGEYLVLDKPAElvnakvypvPDPgapfLGvHLTR-TIDGNLLFgpnavfvpkkeDS 282
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161077125 338 PWQRQTIAGTTDLPCEITHNPTPTEDEIQ------FILNEIKNYLNadvEVRRGDVLSAWSGIRPLVSDPNKD 404
Cdd:COG0579 283 LLDLFESLRFPNFWPMLAKNLLTKYLESVtslskeAFLEALRKYVP---ELPDEDLIPAFAGIRAQIIKPDGD 352
|
|
| EFh_parvalbumins |
cd16253 |
EF-hand, calcium binding motif, found in parvalbumins; Parvalbumins are small, acidic, ... |
614-685 |
5.16e-04 |
|
EF-hand, calcium binding motif, found in parvalbumins; Parvalbumins are small, acidic, cytosolic EF-hand-containing Ca2+-buffer and Ca2+ transporter/shuttle proteins belonging to EF-hand superfamily. They are expressed by vertebrates in fast-twitch muscle cells, specific neurons of the central and peripheral nervous system, sensory cells of the mammalian auditory organ (Corti's cell), and some other cells, and characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Thus, they may play an additional role in Mg2+ handling. Moreover, parvalbumins represent one of the major animal allergens. In metal-bound states, parvalbumins possess a rigid and stable tertiary structure and display strong allergenicity. In contrast, the metal-free parvalbumins are intrinsically disordered, and the loss of metal ions results in a conformational change that decreases their IgE binding capacity. Furthermore, parvalbumins have been widely used as a neuronal marker for a variety of functional brain systems. They also function as a Ca2+ shuttle transporting Ca2+ from troponin-C (TnC) to the sarcoplasmic reticulum (SR) Ca2+ pump during muscle relaxation. Thus they may facilitate myocardial relaxation and play important roles in cardiac diastolic dysfunction. Parvalbumins consists of alpha- and beta- sublineages, which can be distinguished on the basis of isoelectric point (pI > 5 for alpha; pI
Pssm-ID: 319996 [Multi-domain] Cd Length: 101 Bit Score: 39.85 E-value: 5.16e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161077125 614 LSKEEIQTYIKRFQLIDKDKKGYVSINDIRRALKSFGDG--DVSGEQLHEILREIDTNMNGQVELDEYLQMMSA 685
Cdd:cd16253 28 LSKKSPADIKKVFNILDQDKSGFIEEEELKLFLKNFSDGarVLSDKETKNFLAAGDSDGDGKIGVDEFKSMVKA 101
|
|
| EFh_parvalbumin_like |
cd16251 |
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ... |
612-685 |
1.61e-03 |
|
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes alpha- and beta-parvalbumins, and a group of uncharacterized calglandulin-like proteins. Parvalbumins are small, acidic, cytosolic EF-hand-containing Ca2+-buffer and Ca2+ transporter/shuttle proteins belonging to EF-hand superfamily. They are expressed by vertebrates in fast-twitch muscle cells, specific neurons of the central and peripheral nervous system, sensory cells of the mammalian auditory organ (Corti's cell), and some other cells, and characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Thus, they may play an additional role in Mg2+ handling. Moreover, parvalbumins represent one of the major animal allergens. In metal-bound states, parvalbumins possess a rigid and stable tertiary structure and display strong allergenicity. In contrast, the metal-free parvalbumins are intrinsically disordered, and the loss of metal ions results in a conformational change that decreases their IgE binding capacity. Furthermore, parvalbumins have been widely used as a neuronal marker for a variety of functional brain systems. They also function as a Ca2+ shuttle transporting Ca2+ from troponin-C (TnC) to the sarcoplasmic reticulum (SR) Ca2+ pump during muscle relaxation. Thus they may facilitate myocardial relaxation and play important roles in cardiac diastolic dysfunction. Parvalbumins consists of alpha- and beta- sublineages, which can be distinguished on the basis of isoelectric point (pI > 5 for alpha; pI
Pssm-ID: 319994 [Multi-domain] Cd Length: 101 Bit Score: 38.67 E-value: 1.61e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161077125 612 IKLSKEEIQTYIKRFQLIDKDKKGYVSINDIRRALKSFG-DG-DVSGEQLHEILREIDTNMNGQVELDEYLQMMSA 685
Cdd:cd16251 26 VGLKQKSEDQIKKVFQILDKDKSGFIEEEELKYILKGFSiAGrDLTDEETKALLAAGDTDGDGKIGVEEFATLVAG 101
|
|
| EFh_calglandulin_like |
cd16252 |
EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The ... |
617-682 |
3.27e-03 |
|
EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The family corresponds to a group of uncharacterized calglandulin-like proteins. Although their biological function remain unclear, they show high sequence similarity with human calglandulin-like protein GAGLP, which is an ortholog of calglandulin from the venom glands of Bothrops insularis snake. Both GAGLP and calglandulin are putative Ca2+-binding proteins with four EF-hand motifs. However, members in this family contain only three EF-hand motifs. In this point, they may belong to the parvalbumin-like EF-hand family, which is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix).
Pssm-ID: 319995 [Multi-domain] Cd Length: 106 Bit Score: 37.90 E-value: 3.27e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161077125 617 EEIQTYIKR-FQLIDKDKKGYVSINDIRRALKSFGDG----DVSGEQLHEILREIDTNMNGQVELDEYLQM 682
Cdd:cd16252 33 EQQEEAIRKaFQMLDKDKSGFIEWNEIKYILSTVPSSmpvaPLSDEEAEAMIQAADTDGDGRIDFQEFSDM 103
|
|
| EFh_PEF_Group_I |
cd16180 |
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ... |
626-681 |
4.96e-03 |
|
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds to Group I PEF proteins that have been found not only in higher animals but also in lower animals, plants, fungi and protists. Group I PEF proteins include apoptosis-linked gene 2 protein (ALG-2), peflin and similar proteins. ALG-2, also termed programmed cell death protein 6 (PDCD6), is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination. Peflin is a ubiquitously expressed 30-kD PEF protein containing five EF-hand motifs in its C-terminal domain and a longer N-terminal hydrophobic domain (NHB domain) than any other member of the PEF family. The NHB domain harbors nine repeats of a nonapeptide (A/PPGGPYGGP). Peflin may modulate the function of ALG-2 in Ca2+ signaling. It exists only as a heterodimer with ALG-2, and binds two Ca2+ ions through its EF1 and EF3 hands. Its additional EF5 hand is unpaired and does not bind Ca2+ ion but mediates the heterodimerization with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+.
Pssm-ID: 320055 [Multi-domain] Cd Length: 164 Bit Score: 38.28 E-value: 4.96e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 161077125 626 FQLIDKDKKGYVSINDIRRALKSFGDGDVSGEQLHEILREIDTNMNGQVELDEYLQ 681
Cdd:cd16180 6 FQAVDRDRSGRISAKELQRALSNGDWTPFSIETVRLMINMFDRDRSGTINFDEFVG 61
|
|
| EFh_PEF_ALG-2_like |
cd16185 |
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ... |
626-682 |
8.83e-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: 8.83e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161077125 626 FQLIDKDKKGYVSINDIRRALKS----FGDGDVsgEQLheiLREIDTNMNGQVELDEYLQM 682
Cdd:cd16185 6 FRAVDRDRSGSIDVNELQKALAGggllFSLATA--EKL---IRMFDRDGNGTIDFEEFAAL 61
|
|
|