|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02927 |
PLN02927 |
antheraxanthin epoxidase/zeaxanthin epoxidase |
73-659 |
0e+00 |
|
antheraxanthin epoxidase/zeaxanthin epoxidase
Pssm-ID: 178515 [Multi-domain] Cd Length: 668 Bit Score: 892.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 73 EGTRRPRVLVAGGGIGGLVLALAARRKGYEVTVFERDMSAVRGEGQYRGPIQIQSNALAALEAIDMSVAEEVMREGCVTG 152
Cdd:PLN02927 77 EKKKKSRVLVAGGGIGGLVFALAAKKKGFDVLVFEKDLSAIRGEGKYRGPIQIQSNALAALEAIDIDVAEQVMEAGCITG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 153 DRINGLVDGISGSWYIKFDTFTPAAERGLPVTRVISRMTLQQILARAVGDDAILNDSHVVDFIDDGNKVTAILEDGRKFE 232
Cdd:PLN02927 157 DRINGLVDGISGSWYVKFDTFTPAASRGLPVTRVISRMTLQQILARAVGEDVIRNESNVVDFEDSGDKVTVVLENGQRYE 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 233 GDLLVGADGIWSKVRKVLFGQSEATYSEYTCYTGIADFVPPDIDTVGYRVFLGHKQYFVSSDVGAGKMQWYAFHKEPAGG 312
Cdd:PLN02927 237 GDLLVGADGIWSKVRNNLFGRSEATYSGYTCYTGIADFIPADIESVGYRVFLGHKQYFVSSDVGGGKMQWYAFHEEPAGG 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 313 TDPENGKNKRLLEIFNGWCDNVVDLINATDEEAILRRDIYDRPPTFNWGKGRVTLLGDSVHAMQPNLGQGGCMAIEDGYQ 392
Cdd:PLN02927 317 ADAPNGMKKRLFEIFDGWCDNVLDLLHATEEDAILRRDIYDRSPGFTWGKGRVTLLGDSIHAMQPNMGQGGCMAIEDSFQ 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 393 LAVELEKSWQESAKSGTPMDIVSSLRRYEKERILRVSVIHGLARMAAIMATTYRPYLGVGLGPLSFLTKLRIPHPGRVGG 472
Cdd:PLN02927 397 LALELDEAWKQSVETNTPVDVVSSLKRYEESRRLRVAIIHAMARMAAIMASTYKAYLGVGLGPLSFLTKFRVPHPGRVGG 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 473 RFFIKYGMPLMLSWVLGGNSTKLEGRPLSCRLSDKANDQLRRWFEDDDALEQAMGGEWYLLPtsSGD----SQPIRLIRD 548
Cdd:PLN02927 477 RFFVDIAMPLMLDWVLGGNSEKLEGRPPSCRLTDKADDRLREWFEDDDALERTIKGEWYLIP--HGDdccvSETLCLTKD 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 549 EKKSLSIGSRSDPSNSTASLALPLPQISENHATITCKNKAFYVTDNGSEHGTWITDNEGRRYRVPPNFPVRFHPSDAIEF 628
Cdd:PLN02927 555 EDQPCIVGSEPDQDFPGMRIVIPSSQVSKMHARVIYKDGAFFLMDLRSEHGTYVTDNEGRRYRATPNFPARFRSSDIIEF 634
|
570 580 590
....*....|....*....|....*....|....
gi 122240921 629 GSDKKAVFRVKVLSTLPYESAR---GGPQILQAA 659
Cdd:PLN02927 635 GSDKKAAFRVKVIRKTPKSTRKnesNNDKLLQTA 668
|
|
| FHA_ZEP-like |
cd22702 |
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar ... |
522-642 |
1.04e-64 |
|
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar proteins; ZEP, also called protein ABA DEFICIENT 1, ABA1, protein IMPAIRED IN BABA-INDUCED STERILITY 3, protein LOW EXPRESSION OF OSMOTIC STRESS-RESPONSIVE GENES 6, or protein NON-PHOTOCHEMICAL QUENCHING 2, plays an important role in the xanthophyll cycle and abscisic acid (ABA) biosynthesis. It converts zeaxanthin into antheraxanthin and subsequently violaxanthin. ZEP is required for resistance to osmotic and drought stresses, ABA-dependent stomatal closure, seed development and dormancy, modulation of defense gene expression, and disease resistance and non-photochemical quencing (NPQ). The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438754 [Multi-domain] Cd Length: 123 Bit Score: 209.20 E-value: 1.04e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 522 LEQAMGGEWYLLPTSSGD--SQPIRLIRDEKKSLSIGSRSDPSNSTASLALPLPQISENHATITCKNKAFYVTDNGSEHG 599
Cdd:cd22702 1 LERATSAEWYLLPLGNDMdgGSPIRLTRDEKQPCIIGSDPHQAISGISVVIPSPQVSELHARITCKNGAFFLTDLGSEHG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 122240921 600 TWITDNEGRRYRVPPNFPVRFHPSDAIEFGSDKKAVFRVKVLS 642
Cdd:cd22702 81 TWINDNEGRRYRAPPNFPVRLHPSDVIEFGSDKKARFRVKVMK 123
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
75-447 |
1.13e-50 |
|
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 440419 [Multi-domain] Cd Length: 326 Bit Score: 178.59 E-value: 1.13e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 75 TRRPRVLVAGGGIGGLVLALAARRKGYEVTVFERDmSAVRGEGqyRGpIQIQSNALAALEAIDmsVAEEVMREGCVTGDR 154
Cdd:COG0654 1 MMRTDVLIVGGGPAGLALALALARAGIRVTVVERA-PPPRPDG--RG-IALSPRSLELLRRLG--LWDRLLARGAPIRGI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 155 IngLVDGISGSWYIKFDtftpAAERGLPVTRVISRMTLQQILARAVGDD--AILNDSHVVDFIDDGNKVTAILEDGRKFE 232
Cdd:COG0654 75 R--VRDGSDGRVLARFD----AAETGLPAGLVVPRADLERALLEAARALgvELRFGTEVTGLEQDADGVTVTLADGRTLR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 233 GDLLVGADGIWSKVRKVLFgqseatyseytcytgiadfvppdIDTVGYrvflGHKQYFVSSDVGAgkmqwyafhkepagg 312
Cdd:COG0654 149 ADLVVGADGARSAVRRLLG-----------------------IGFTGR----DYPQRALWAGVRT--------------- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 313 tdpengknkRLLEIFNGWCDNVVDLINATDEEA-ILRRDIYDRpptfnWGKGRVTLLGDSVHAMQPNLGQGGCMAIEDGY 391
Cdd:COG0654 187 ---------ELRARLAAAGPRLGELLELSPRSAfPLRRRRAER-----WRRGRVVLLGDAAHTMHPLGGQGANLALRDAA 252
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 122240921 392 QLAVELekswqesAKSGTPMDIVSSLRRYEKERILRVSVIHGLAR-MAAIMATTYRP 447
Cdd:COG0654 253 ALAWKL-------AAALRGRDDEAALARYERERRPRAARVQRAADaLGRLFHPDSPP 302
|
|
| PRK08163 |
PRK08163 |
3-hydroxybenzoate 6-monooxygenase; |
75-427 |
6.47e-47 |
|
3-hydroxybenzoate 6-monooxygenase;
Pssm-ID: 181262 [Multi-domain] Cd Length: 396 Bit Score: 170.60 E-value: 6.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 75 TRRPRVLVAGGGIGGLVLALAARRKGYEVTVFERdmSAVRGE---GqyrgpIQIQSNALAALEAIDMSvaeEVMREGCVT 151
Cdd:PRK08163 2 TKVTPVLIVGGGIGGLAAALALARQGIKVKLLEQ--AAEIGEigaG-----IQLGPNAFSALDALGVG---EAARQRAVF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 152 GDRInGLVDGISGSWYIKFDTFTPAAER-GLPVTrVISRMTLQQILARAVGDDA---ILNDSHVVDFIDDGNKVTAILED 227
Cdd:PRK08163 72 TDHL-TMMDAVDAEEVVRIPTGQAFRARfGNPYA-VIHRADIHLSLLEAVLDHPlveFRTSTHVVGIEQDGDGVTVFDQQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 228 GRKFEGDLLVGADGIWSKVRKVLFGqSEATYSEYTCYTGIADF--VPPDIDTVGYRVFLGHKQYFVSSDVGAGKMqwY-- 303
Cdd:PRK08163 150 GNRWTGDALIGCDGVKSVVRQSLVG-DAPRVTGHVVYRAVIDVddMPEDLRINAPVLWAGPHCHLVHYPLRGGEQ--Ynl 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 304 --AFH---KEPAGGTDpenGKNKRLLEIFNGWCDNVVDLInatDEEAILRR-DIYDRPPTFNWGKGRVTLLGDSVHAMQP 377
Cdd:PRK08163 227 vvTFHsreQEEWGVKD---GSKEEVLSYFEGIHPRPRQML---DKPTSWKRwATADREPVAKWSTGRVTLLGDAAHPMTQ 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 122240921 378 NLGQGGCMAIEDGYQLAVELEkswqesaksGTPMDIVSSLRRYEKERILR 427
Cdd:PRK08163 301 YMAQGACMALEDAVTLGKALE---------GCDGDAEAAFALYESVRIPR 341
|
|
| PRK06753 |
PRK06753 |
hypothetical protein; Provisional |
79-442 |
3.00e-44 |
|
hypothetical protein; Provisional
Pssm-ID: 168661 [Multi-domain] Cd Length: 373 Bit Score: 162.55 E-value: 3.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 79 RVLVAGGGIGGLVLALAARRKGYEVTVFERDMS-AVRGEGqyrgpIQIQSNALAALEAIDmsVAEEVMRegcvTGDRING 157
Cdd:PRK06753 2 KIAIIGAGIGGLTAAALLQEQGHEVKVFEKNESvKEVGAG-----IGIGDNVIKKLGNHD--LAKGIKN----AGQILST 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 158 --LVDGisgswyiKFDTFTPAAERGLPVTRVISRMTLQQILARAVGDDAILNDSHVVDFIDDGNKVTAILEDGRKFEGDL 235
Cdd:PRK06753 71 mnLLDD-------KGTLLNKVKLKSNTLNVTLHRQTLIDIIKSYVKEDAIFTGKEVTKIENETDKVTIHFADGESEAFDL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 236 LVGADGIWSKVRKVLFGQSEATYSEYTCYTGIadfvppdIDTVGYRVFLGHKQYF-VSSDVGA-----GKMQWYAFHKEP 309
Cdd:PRK06753 144 CIGADGIHSKVRQSVNADSKVRYQGYTCFRGL-------IDDIDLKLPDCAKEYWgTKGRFGIvpllnNQAYWFITINAK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 310 AGGTDPENGKNKRLLEIFNGWCDNVVDLINATDEEAILRRDIYDRPPTFNWGKGRVTLLGDSVHAMQPNLGQGGCMAIED 389
Cdd:PRK06753 217 ERDPKYSSFGKPHLQAYFNHYPNEVREILDKQSETGILHHDIYDLKPLKSFVYGRIVLLGDAAHATTPNMGQGAGQAMED 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 122240921 390 GYQLAVELEKSWQESAksgtpmdivssLRRYEKERILRVSVIHGLARMAAIMA 442
Cdd:PRK06753 297 AIVLANCLNAYDFEKA-----------LQRYDKIRVKHTAKVIKRSRKIGKIA 338
|
|
| PRK06847 |
PRK06847 |
hypothetical protein; Provisional |
79-428 |
1.88e-42 |
|
hypothetical protein; Provisional
Pssm-ID: 235874 [Multi-domain] Cd Length: 375 Bit Score: 157.73 E-value: 1.88e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 79 RVLVAGGGIGGLVLALAARRKGYEVTVFERDMS-AVRGEGqyrgpIQIQSNALAALEAIDmsVAEEVMREGCVTGDring 157
Cdd:PRK06847 6 KVLIVGGGIGGLSAAIALRRAGIAVDLVEIDPEwRVYGAG-----ITLQGNALRALRELG--VLDECLEAGFGFDG---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 158 lvdgisgswyikFDTFTPA------------AERGLPVTRVISRMTLQQIL---ARAVGDDAILNDShVVDFIDDGNKVT 222
Cdd:PRK06847 75 ------------VDLFDPDgtllaelptprlAGDDLPGGGGIMRPALARILadaARAAGADVRLGTT-VTAIEQDDDGVT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 223 AILEDGRKFEGDLLVGADGIWSKVRKVLFGqsEATYSEYTCyTGIADFV---PPDIDtvgyrvflgHKQYFVSSDVGAG- 298
Cdd:PRK06847 142 VTFSDGTTGRYDLVVGADGLYSKVRSLVFP--DEPEPEYTG-QGVWRAVlprPAEVD---------RSLMYLGPTTKAGv 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 299 ----KMQWYAFHKEPAGG--TDPENGKNKRLLEIFNGWCDNVVDLI--NATDEEAILRRDI----YDRPptfnWGKGRVT 366
Cdd:PRK06847 210 vplsEDLMYLFVTEPRPDnpRIEPDTLAALLRELLAPFGGPVLQELreQITDDAQVVYRPLetllVPAP----WHRGRVV 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 122240921 367 LLGDSVHAMQPNLGQGGCMAIEDGYQLAVELEKswqesaksgtPMDIVSSLRRYEKERILRV 428
Cdd:PRK06847 286 LIGDAAHATTPHLAQGAGMAIEDAIVLAEELAR----------HDSLEAALQAYYARRWERC 337
|
|
| PRK07538 |
PRK07538 |
hypothetical protein; Provisional |
78-425 |
6.02e-31 |
|
hypothetical protein; Provisional
Pssm-ID: 236046 [Multi-domain] Cd Length: 413 Bit Score: 125.39 E-value: 6.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 78 PRVLVAGGGIGGLVLALAARRKGYEVTVFErdmsAVR-----GEGqyrgpIQIQSNALAALeaIDMSVAEEVMREGCVTG 152
Cdd:PRK07538 1 MKVLIAGGGIGGLTLALTLHQRGIEVVVFE----AAPelrplGVG-----INLLPHAVREL--AELGLLDALDAIGIRTR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 153 DRInglvdgisgsWYIKFDTFTPAAERGL----PVTRV-ISRMTLQQILARAV----GDDAILNDSHVVDFIDDGNKVTA 223
Cdd:PRK07538 70 ELA----------YFNRHGQRIWSEPRGLaagyDWPQYsIHRGELQMLLLDAVrerlGPDAVRTGHRVVGFEQDADVTVV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 224 ILEDGR-----KFEGDLLVGADGIWSKVRKVLF-GQSEATYSEYTCYTGIADFVPpdIDTVGYRVFLGHKQ-----YFVS 292
Cdd:PRK07538 140 FLGDRAggdlvSVRGDVLIGADGIHSAVRAQLYpDEGPPRWNGVMMWRGVTEAPP--FLTGRSMVMAGHLDgklvvYPIS 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 293 SDVGAGKMQ---WYAFHKEPAGGTDPENGKNKR-----LLEIFNGWCDNVVD---LINATdeEAILRRDIYDRPPTFNWG 361
Cdd:PRK07538 218 EPVDADGRQlinWVAEVRVDDAGAPRREDWNRPgdledFLPHFADWRFDWLDvpaLIRAA--EAIYEYPMVDRDPLPRWT 295
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 122240921 362 KGRVTLLGDSVHAMQPNLGQGGCMAIEDGYQLAVELekswqesAKSGtpmDIVSSLRRYEKERI 425
Cdd:PRK07538 296 RGRVTLLGDAAHPMYPVGSNGASQAILDARALADAL-------AAHG---DPEAALAAYEAERR 349
|
|
| PRK07236 |
PRK07236 |
hypothetical protein; Provisional |
73-425 |
1.44e-23 |
|
hypothetical protein; Provisional
Pssm-ID: 235980 [Multi-domain] Cd Length: 386 Bit Score: 103.08 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 73 EGTRRPRVLVAGGGIGGLVLALAARRKGYEVTVFERDMSAVRGEGqyrGPIQIQSNALAALEAIdmsvaeevmreGCVTG 152
Cdd:PRK07236 2 THMSGPRAVVIGGSLGGLFAALLLRRAGWDVDVFERSPTELDGRG---AGIVLQPELLRALAEA-----------GVALP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 153 DRInglvdGISGSWYIKFD-TFTPAAERGLPVTrVISRMTLQQILARAVGDDAILNDSHVVDFIDDGNKVTAILEDGRKF 231
Cdd:PRK07236 68 ADI-----GVPSRERIYLDrDGRVVQRRPMPQT-QTSWNVLYRALRAAFPAERYHLGETLVGFEQDGDRVTARFADGRRE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 232 EGDLLVGADGIWSKVRKVLFGQSEATYSEYTCYTGIADfvPPDIDTVGYRVFLGHKQYFVSSDvgagkMQWYAFhkePAG 311
Cdd:PRK07236 142 TADLLVGADGGRSTVRAQLLPDVRPTYAGYVAWRGLVD--EAALPPEARAALRDRFTFQLGPG-----SHILGY---PVP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 312 GTDPENGKNKRLleiFNG-WCDNVVD-------LINAT---------------DEEAILRRDIYDR-PPTF--------- 358
Cdd:PRK07236 212 GEDGSTEPGKRR---YNWvWYRNAPAgeeldelLTDRDgtrrpfsvppgalrdDVLAELRDDAAELlAPVFaelveataq 288
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 122240921 359 ------------NWGKGRVTLLGDSVHAMQPNLGQGGCMAIEDGYQLAVELekswqesakSGTPMDIVSSLRRYEKERI 425
Cdd:PRK07236 289 pfvqaifdlevpRMAFGRVALLGDAAFVARPHTAAGVAKAAADAVALAEAL---------AAAAGDIDAALAAWEAERL 358
|
|
| PRK06475 |
PRK06475 |
FAD-binding protein; |
77-438 |
2.51e-22 |
|
FAD-binding protein;
Pssm-ID: 180582 [Multi-domain] Cd Length: 400 Bit Score: 99.90 E-value: 2.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 77 RPRVLVAGGGIGGLVLALAARRKGYEVTVFER--DMSAVrGEGqyrgpIQIQSNALAALEaiDMSVAEEVMREGcVTGDR 154
Cdd:PRK06475 2 RGSPLIAGAGVAGLSAALELAARGWAVTIIEKaqELSEV-GAG-----LQLAPNAMRHLE--RLGVADRLSGTG-VTPKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 155 INgLVDGISGSWYIKFDTFTPAAERGLPVTRVISRMTLQQILARAVGDDAILNDS---HVVDFIDDGNKVTA--ILEDGR 229
Cdd:PRK06475 73 LY-LMDGRKARPLLAMQLGDLARKRWHHPYIVCHRADLQSALLDACRNNPGIEIKlgaEMTSQRQTGNSITAtiIRTNSV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 230 KF-EGDLLVGADGIWSKVRKvLFGQSEATYSEYTCY--TGIADFVP-------PDIDTVgyRVFLGHKQYFVSSDVGAGK 299
Cdd:PRK06475 152 ETvSAAYLIACDGVWSMLRA-KAGFSKARFSGHIAWrtTLAADALPasflsamPEHKAV--SAWLGNKAHFIAYPVKGGK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 300 MqwYAF----HKEPAGGTDPENGKNKRLLEIFNGWCDNVVDLINATDEeailrrdiYDRPPTFNW------GKGRVTLLG 369
Cdd:PRK06475 229 F--FNFvaitGGENPGEVWSKTGDKAHLKSIYADWNKPVLQILAAIDE--------WTYWPLFEMadaqfvGPDRTIFLG 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 122240921 370 DSVHAMQPNLGQGGCMAIEDGYQLAVELEKSWQESAksgtpmdivssLRRYE---KERILRVSVIHGLARMA 438
Cdd:PRK06475 299 DASHAVTPFAAQGAAMAIEDAAALAEALDSDDQSAG-----------LKRFDsvrKERIAAVAKRGQLNRFA 359
|
|
| PRK07588 |
PRK07588 |
FAD-binding domain; |
79-400 |
5.51e-14 |
|
FAD-binding domain;
Pssm-ID: 169028 [Multi-domain] Cd Length: 391 Bit Score: 74.00 E-value: 5.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 79 RVLVAGGGIGGLVLALAARRKGYEVTVFERdMSAVRgegqyRGPIQIQSNALAALEAIDMSVAEEVMREG-------CV- 150
Cdd:PRK07588 2 KVAISGAGIAGPTLAYWLRRYGHEPTLIER-APELR-----TGGYMVDFWGVGYEVAKRMGITDQLREAGyqiehvrSVd 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 151 -TGDRINGL-VDGISGSWYIKFDTftpaaerglpvtrvISRMTLQQILARAVGD--DAILNDShvVDFIDDG-NKVTAIL 225
Cdd:PRK07588 76 pTGRRKADLnVDSFRRMVGDDFTS--------------LPRGDLAAAIYTAIDGqvETIFDDS--IATIDEHrDGVRVTF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 226 EDGRKFEGDLLVGADGIWSKVRKVLFGQSEatYSEYtcYTGI--ADFV-----PPDIDTVGYRVFLGHKQYFVSSDvGAG 298
Cdd:PRK07588 140 ERGTPRDFDLVIGADGLHSHVRRLVFGPER--DFEH--YLGCkvAACVvdgyrPRDERTYVLYNEVGRQVARVALR-GDR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 299 KMQWYAFHKEPAGGTDPENGKNKRLLEIFN--GW-CDNVVDLINATDEeaiLRRDIYDRPPTFNWGKGRVTLLGDSvhAM 375
Cdd:PRK07588 215 TLFLFIFRAEHDNPPLTPAEEKQLLRDQFGdvGWeTPDILAALDDVED---LYFDVVSQIRMDRWSRGRVALVGDA--AA 289
|
330 340
....*....|....*....|....*..
gi 122240921 376 QPNL--GQGGCMAIEDGYQLAVELEKS 400
Cdd:PRK07588 290 CPSLlgGEGSGLAITEAYVLAGELARA 316
|
|
| FAD_binding_3 |
pfam01494 |
FAD binding domain; This domain is involved in FAD binding in a number of enzymes. |
80-428 |
8.74e-13 |
|
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
Pssm-ID: 396193 [Multi-domain] Cd Length: 348 Bit Score: 70.05 E-value: 8.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 80 VLVAGGGIGGLVLALAARRKGYEVTVFERDMSAV---RGEGQYRGPIQIQSNALAALEAIDMSVAEEVMREgCVTGDRIN 156
Cdd:pfam01494 4 VLIVGGGPAGLMLALLLARAGVRVVLVERHATTSvlpRAHGLNQRTMELLRQAGLEDRILAEGVPHEGMGL-AFYNTRRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 157 GLVDGIsgswyikfdtFTPAAERGLPVTRVIsRMTLQQilARAVGDDaILNDSHVVDFIDDGNKVTAILEDGR-----KF 231
Cdd:pfam01494 83 ADLDFL----------TSPPRVTVYPQTELE-PILVEH--AEARGAQ-VRFGTEVLSLEQDGDGVTAVVRDRRdgeeyTV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 232 EGDLLVGADGIWSKVRKVLfGQSEATYSEYTCYTGIADFVPPDIDTVGYRVFLGHKQYFVSSDVGA------GKMQWYAF 305
Cdd:pfam01494 149 RAKYLVGCDGGRSPVRKTL-GIEFEGFEGVPFGSLDVLFDAPDLSDPVERAFVHYLIYAPHSRGFMvgpwrsAGRERYYV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 306 HKEPagGTDPENGKNK--------RLLEIFnGWCDNVVDLinatDEEAILR-RDIYDRPptfnWGKGRVTLLGDSVHAMQ 376
Cdd:pfam01494 228 QVPW--DEEVEERPEEftdeelkqRLRSIV-GIDLALVEI----LWKSIWGvASRVATR----YRKGRVFLAGDAAHIHP 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 122240921 377 PNLGQGGCMAIEDGYQLAVELEKSWQESAKSgtpmdivSSLRRYEKERILRV 428
Cdd:pfam01494 297 PTGGQGLNTAIQDAFNLAWKLAAVLRGQAGE-------SLLDTYSAERLPVA 341
|
|
| FixC |
COG0644 |
Dehydrogenase (flavoprotein) [Energy production and conversion]; |
85-250 |
1.49e-12 |
|
Dehydrogenase (flavoprotein) [Energy production and conversion];
Pssm-ID: 440409 [Multi-domain] Cd Length: 281 Bit Score: 68.46 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 85 GGIGGLVLALAARRKGYEVTVFERDmSAVR----GEGqyrgpiqIQSNALAALEAIDMSvaEEVMREgcVTGDRINgLVD 160
Cdd:COG0644 1 AGPAGSAAARRLARAGLSVLLLEKG-SFPGdkicGGG-------LLPRALEELEPLGLD--EPLERP--VRGARFY-SPG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 161 GISGSWyikfdtftpaaERGLPVTRVISRMTLQQILA-RAVGDDA-ILNDSHVVDFIDDGNKVTAILEDGRKFEGDLLVG 238
Cdd:COG0644 68 GKSVEL-----------PPGRGGGYVVDRARFDRWLAeQAEEAGAeVRTGTRVTDVLRDDGRVVVRTGDGEEIRADYVVD 136
|
170
....*....|..
gi 122240921 239 ADGIWSKVRKVL 250
Cdd:COG0644 137 ADGARSLLARKL 148
|
|
| PRK05868 |
PRK05868 |
FAD-binding protein; |
79-398 |
2.10e-11 |
|
FAD-binding protein;
Pssm-ID: 180297 [Multi-domain] Cd Length: 372 Bit Score: 66.16 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 79 RVLVAGGGIGGLVLALAARRKGYEVTVFERDmSAVRGEGQyrgPIQIQSNALAALEAIDMSVAEEVMRegcvTGDRINGL 158
Cdd:PRK05868 3 TVVVSGASVAGTAAAYWLGRHGYSVTMVERH-PGLRPGGQ---AIDVRGPALDVLERMGLLAAAQEHK----TRIRGASF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 159 VDGiSGSwyiKFDTFTPAAERGLPVTRV---ISRMTLQQILARAVGDDA-ILNDSHVVDFIDDGNKVTAILEDGRKFEGD 234
Cdd:PRK05868 75 VDR-DGN---ELFRDTESTPTGGPVNSPdieLLRDDLVELLYGATQPSVeYLFDDSISTLQDDGDSVRVTFERAAAREFD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 235 LLVGADGIWSKVRKVLFGQSEATYSEYTCYTGIadFVPPDidtvgyrvFLGHKQYfvssdvgagkMQWYAFHKEPAGGTD 314
Cdd:PRK05868 151 LVIGADGLHSNVRRLVFGPEEQFVKRLGTHAAI--FTVPN--------FLELDYW----------QTWHYGDSTMAGVYS 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 315 PENGKNKRLLEifnGWCDNVVDlINATDEEA----ILRRDIYD---RP---------PTF-----------NWGKGRVTL 367
Cdd:PRK05868 211 ARNNTEARAAL---AFMDTELR-IDYRDTEAqfaeLQRRMAEDgwvRAqllhymrsaPDFyfdemsqilmdRWSRGRVAL 286
|
330 340 350
....*....|....*....|....*....|.
gi 122240921 368 LGDSVHAMQPNLGQGGCMAIEDGYQLAVELE 398
Cdd:PRK05868 287 VGDAGYCCSPLSGQGTSVALLGAYILAGELK 317
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
531-638 |
1.73e-10 |
|
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.
Pssm-ID: 438714 [Multi-domain] Cd Length: 92 Bit Score: 58.06 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 531 YLLPTSSGDSQPIRLIRdeKKSLSIGSRSDpsnstASLALPLPQISENHATITCKNKAFYVTDNGSEHGTWItdnEGRRY 610
Cdd:cd00060 1 RLIVLDGDGGGREFPLT--KGVVTIGRSPD-----CDIVLDDPSVSRRHARIEVDGGGVYLEDLGSTNGTFV---NGKRI 70
|
90 100
....*....|....*....|....*...
gi 122240921 611 RVppnfPVRFHPSDAIEFGsdkKAVFRV 638
Cdd:cd00060 71 TP----PVPLQDGDVIRLG---DTTFRF 91
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
554-628 |
1.23e-07 |
|
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
Pssm-ID: 459831 [Multi-domain] Cd Length: 66 Bit Score: 49.11 E-value: 1.23e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 122240921 554 SIGSRSDpsnstASLALPLPQISENHATITCK-NKAFYVTDNGSEHGTWITDNegrryRVPPNfPVRFHPSDAIEF 628
Cdd:pfam00498 2 TIGRSPD-----CDIVLDDPSVSRRHAEIRYDgGGRFYLEDLGSTNGTFVNGQ-----RLGPE-PVRLKDGDVIRL 66
|
|
| PRK07045 |
PRK07045 |
putative monooxygenase; Reviewed |
80-424 |
1.38e-07 |
|
putative monooxygenase; Reviewed
Pssm-ID: 136171 [Multi-domain] Cd Length: 388 Bit Score: 54.14 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 80 VLVAGGGIGGLVLALAARRKGYEVTVFERdmsAVRGEGQyRGPIQIQSNALAALEAidMSVAEEVMREGCVTGDRINGLV 159
Cdd:PRK07045 8 VLINGSGIAGVALAHLLGARGHSVTVVER---AARNRAQ-NGADLLKPSGIGVVRA--MGLLDDVFAAGGLRRDAMRLYH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 160 DGIsgswYIKFDTFTPAAERG---LPVTRVISRMTLQQILARAVGDDAILNDSHVVDFIDDGNKVTAILEDGRKFEGDLL 236
Cdd:PRK07045 82 DKE----LIASLDYRSASALGyfiLIPCEQLRRLLLAKLDGLPNVRLRFETSIERIERDADGTVTSVTLSDGERVAPTVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 237 VGADGIWSKVRKVLFgQSEATYSEYTCYTGIADFVPPDIDTVGYRVFLGHKQ---YFVSSDVGAGKMQwYAFHKEPAGG- 312
Cdd:PRK07045 158 VGADGARSMIRDDVL-RMPAERVPYATPMAFGTIALTDSVRECNRLYVDSNQglaYFYPIGDQATRLV-VSFPADEMQGy 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 313 -TDPENGKNKRLLEIFNGwcDNVVDLINATDEEAILRRDIYDRPPTFNWGKGRVTLLGDSVHAMQPNLGQGGCMAIEDGY 391
Cdd:PRK07045 236 lADTTRTKLLARLNEFVG--DESADAMAAIGAGTAFPLIPLGRMNLDRYHKRNVVLLGDAAHSIHPITGQGMNLAIEDAG 313
|
330 340 350
....*....|....*....|....*....|...
gi 122240921 392 QLAVELEKSWQESaksgtpMDIVSSLRRYEKER 424
Cdd:PRK07045 314 ELGACLDLHLSGQ------IALADALERFERIR 340
|
|
| FHA_ArnA-like |
cd22680 |
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ... |
552-638 |
5.92e-07 |
|
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing protein ArnA and similar proteins; ArnA is an FHA domain-containing protein from Sulfolobus acidocaldarius that was shown to strongly interact with ArnB, a von Willebrand domain-containing protein. They act synergistically and negatively to modulate motility. ArnA is involved in regulating archaella expression in S. acidocaldarius. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438732 [Multi-domain] Cd Length: 96 Bit Score: 48.11 E-value: 5.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 552 SLSIGSrsDPSNStasLALPLPQISENHATITCKNKAFYVTDNGSEHGTWITDNEgrryRVPPnfPVRFHPSDAIEFGsd 631
Cdd:cd22680 22 SVSIGR--DPENV---IVIPDPFVSRNHARITVDSNEIYIEDLGSTNGTFVNDFK----RIKG--PAKLHPNDIIKLG-- 88
|
....*..
gi 122240921 632 KKAVFRV 638
Cdd:cd22680 89 RTTVLKV 95
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
539-640 |
6.55e-07 |
|
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
Pssm-ID: 441322 [Multi-domain] Cd Length: 96 Bit Score: 48.03 E-value: 6.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 539 DSQPIRLIRDEKKSLSIGSRSDpsnstASLALPLPQISENHATITCKNKAFYVTDNGSEHGTWItdnEGRRYRVppnfPV 618
Cdd:COG1716 9 GPLAGRRFPLDGGPLTIGRAPD-----NDIVLDDPTVSRRHARIRRDGGGWVLEDLGSTNGTFV---NGQRVTE----PA 76
|
90 100
....*....|....*....|..
gi 122240921 619 RFHPSDAIEFGsdkKAVFRVKV 640
Cdd:COG1716 77 PLRDGDVIRLG---KTELRFRL 95
|
|
| FHA |
smart00240 |
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ... |
562-605 |
1.40e-06 |
|
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.
Pssm-ID: 214578 [Multi-domain] Cd Length: 52 Bit Score: 45.63 E-value: 1.40e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 122240921 562 SNSTASLALPLPQISENHATITCK-NKAFYVTDNGSEHGTWITDN 605
Cdd:smart00240 6 SSEDCDIQLDGPSISRRHAVIVYDgGGRFYLIDLGSTNGTFVNGK 50
|
|
| PRK06185 |
PRK06185 |
FAD-dependent oxidoreductase; |
79-479 |
2.22e-06 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 235729 [Multi-domain] Cd Length: 407 Bit Score: 50.24 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 79 RVLVAGGGIGGLVLALAARRKGYEVTV------FERDMsavRGEGqyrgpiqIQSNALAALEaiDMSVAEEVMREGCVTG 152
Cdd:PRK06185 8 DCCIVGGGPAGMMLGLLLARAGVDVTVlekhadFLRDF---RGDT-------VHPSTLELMD--ELGLLERFLELPHQKV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 153 DRINGLVDGisgswyikfDTFTPAAERGLPVT-RVISRMT----LQQILARAVGDDA--ILNDSHVVDFIDDGNKVTAIL 225
Cdd:PRK06185 76 RTLRFEIGG---------RTVTLADFSRLPTPyPYIAMMPqwdfLDFLAEEASAYPNftLRMGAEVTGLIEEGGRVTGVR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 226 ---EDGR-KFEGDLLVGADGIWSKVRK------VLFGQSeatyseytcytgiADFV------PPDiDTVGYRVFLGHKQY 289
Cdd:PRK06185 147 artPDGPgEIRADLVVGADGRHSRVRAlaglevREFGAP-------------MDVLwfrlprEPD-DPESLMGRFGPGQG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 290 FVSSDVG----AG----KMQWYAFHkepAGGTDPengKNKRLLEIFnGWCDNVVDLINATDEEAILRRDIyDRPPTfnWG 361
Cdd:PRK06185 213 LIMIDRGdywqCGyvipKGGYAALR---AAGLEA---FRERVAELA-PELADRVAELKSWDDVKLLDVRV-DRLRR--WH 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 362 KGRVTLLGDSVHAMQPNLGQGGCMAIEDgyqlAVELEKSWQESAKSGTPMDivSSLRRYEKERILRVSVIHGLARMAAIM 441
Cdd:PRK06185 283 RPGLLCIGDAAHAMSPVGGVGINLAIQD----AVAAANILAEPLRRGRVSD--RDLAAVQRRREFPTRVTQALQRRIQRR 356
|
410 420 430
....*....|....*....|....*....|....*....
gi 122240921 442 ATTYRPYLGVGLGPLSFLTKL-RIPHPGRVGGRfFIKYG 479
Cdd:PRK06185 357 LLAPALAGRGPLGPPLLLRLLnRLPWLRRLPAR-LVGLG 394
|
|
| COQ6 |
TIGR01989 |
ubiquinone biosynthesis monooxygenase COQ6; This model represents the monooxygenase ... |
216-424 |
3.53e-06 |
|
ubiquinone biosynthesis monooxygenase COQ6; This model represents the monooxygenase responsible for the 4-hydroxylateion of the phenol ring in the aerobic biosynthesis of ubiquinone
Pssm-ID: 273914 [Multi-domain] Cd Length: 437 Bit Score: 49.76 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 216 DDGNKVTAILEDGRKFEGDLLVGADGIWSKVRKvlFGQSEATYSEYTCYTGIA--DFVPPDIDTVGYRVFL--GHKQYFV 291
Cdd:TIGR01989 155 DNSNWVHITLSDGQVLYTKLLIGADGSNSNVRK--AANIDTTGWNYNQHAVVAtlKLEEATENDVAWQRFLptGPIALLP 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 292 SSDVGAGkMQWYAFHKEPAggtdpengKNKRLLEifngwcDNVVDLINA--------------TDEE-AILRRDIYDR-- 354
Cdd:TIGR01989 233 LPDNNST-LVWSTSPEEAL--------RLLSLPP------EDFVDALNAafdlgysdhpysylLDYAmEKLNEDIGFRte 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 355 --------PP-----------TFNWG--------KGRVTLLGDSVHAMQPNLGQGGCMAIEDGYQLAVELEKSWQESAKS 407
Cdd:TIGR01989 298 gskscfqvPPrvigvvdksraAFPLGlghadeyvTKRVALVGDAAHRVHPLAGQGVNLGFGDVASLVKALAEAVSVGADI 377
|
250
....*....|....*..
gi 122240921 408 GTpmdiVSSLRRYEKER 424
Cdd:TIGR01989 378 GS----ISSLKPYERER 390
|
|
| FHA_PPP1R8 |
cd22674 |
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 ... |
544-637 |
4.13e-06 |
|
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 (PPP1R8) and similar proteins; PPP1R8, also called nuclear inhibitor of protein phosphatase 1 (NIPP-1), is an inhibitor subunit of the major nuclear protein phosphatase-1 (PP-1). It has RNA-binding activity but does not cleave RNA and may target PP-1 to RNA-associated substrates. It may also be involved in pre-mRNA splicing and binds DNA and might act as a transcriptional repressor. PPP1R8 seems to be required for cell proliferation. PPP1R8 contains an FHA domain that mediates interactions with threonine-phosphorylated maternal embryonic leucine zipper kinase (MELK). The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438726 [Multi-domain] Cd Length: 108 Bit Score: 46.10 E-value: 4.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 544 RLIRDEKKSLSIGSRSDpsnsTASLALPLPQISENHATITC--KNKAFYVTDNGSEHGTWITDNegrryRVPPNFPVRFH 621
Cdd:cd22674 20 KLMIDEKKYYLFGRNSD----VCDFVLDHPSCSRVHAALVYhkHLNRVFLIDLGSTHGTFVGGI-----RLEPHKPQQLP 90
|
90
....*....|....*..
gi 122240921 622 PSDAIEFG-SDKKAVFR 637
Cdd:cd22674 91 IDSTLRFGaSTRRYILR 107
|
|
| PRK07608 |
PRK07608 |
UbiH/UbiF family hydroxylase; |
80-248 |
4.97e-06 |
|
UbiH/UbiF family hydroxylase;
Pssm-ID: 181057 [Multi-domain] Cd Length: 388 Bit Score: 49.18 E-value: 4.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 80 VLVAGGGIGGLVLALAARRKGYEVTVFERDMSAVRGEGQYRGPIQIQSNALAAL-------EAIDMSvaeevmREGCVTG 152
Cdd:PRK07608 8 VVVVGGGLVGASLALALAQSGLRVALLAPRAPPRPADDAWDSRVYAISPSSQAFlerlgvwQALDAA------RLAPVYD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 153 DRINGLVDGisgswYIKFDtftpAAERGLPVTRVI--SRMtlqqiLARAVgdDAILNDSHVVDFID--------DGNKVT 222
Cdd:PRK07608 82 MRVFGDAHA-----RLHFS----AYQAGVPQLAWIveSSL-----IERAL--WAALRFQPNLTWFParaqglevDPDAAT 145
|
170 180
....*....|....*....|....*.
gi 122240921 223 AILEDGRKFEGDLLVGADGIWSKVRK 248
Cdd:PRK07608 146 LTLADGQVLRADLVVGADGAHSWVRS 171
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
75-108 |
9.38e-06 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 48.69 E-value: 9.38e-06
10 20 30
....*....|....*....|....*....|....
gi 122240921 75 TRRPRVLVAGGGIGGLVLALAARRKGYEVTVFER 108
Cdd:COG1233 1 MMMYDVVVIGAGIGGLAAAALLARAGYRVTVLEK 34
|
|
| FHA_PS1-like |
cd22691 |
forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) ... |
573-639 |
9.68e-06 |
|
forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) and similar proteins; PS1 is an FHA domain-containing protein required for normal spindle orientation at male meiosis II and normal formation of tetrad of microspores. It is not involved in female meiosis. Mutations in PS1 lead to the production of diploid pollen grains. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438743 [Multi-domain] Cd Length: 113 Bit Score: 45.10 E-value: 9.68e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 122240921 573 PQISENHATI--TCKNKAFYVTDNGSEHGTWITDNegrryRVPPNFPVRFHPSDAIEFGSDKKaVFRVK 639
Cdd:cd22691 46 PSISRFHLEIriIPSRRKITLTDLSSVHGTWVNGQ-----RIEPGVPVELEEGDTVRLGASTR-VYRLH 108
|
|
| FHA_Cep170 |
cd22704 |
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ... |
529-642 |
1.09e-05 |
|
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) family; The Cep170 family includes Cep170 and Cep170B. Cep170, also called Cep170A, KARP-1-binding protein, or KARP1-binding protein, is a protein that localizes to centrosomes as well as spindle microtubules and plays a role in microtubule organization and microtubule assembly. It is required for centriole subdistal appendage assembly. Cep170 is phosphorylated during M phase and interacts with Polo-like kinase 1 (Plk1). Cep170B, also called centrosomal protein 170B, plays a role in microtubule organization. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438756 [Multi-domain] Cd Length: 102 Bit Score: 44.62 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 529 EWYLLptsSGDSQPIRLIRD------EKKSLSIGSRSdpsnstaslalplpqISENHATIT--CKNKAFYVTDNGSEHGT 600
Cdd:cd22704 1 SWCLV---SSDGTRHRLPRSmlfvgrEDCDLILQSRS---------------VDKQHAVITydQIDNEFKIKDLGSLNGT 62
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 122240921 601 WITDNegrryRVPPNFPVRFHPSDAIEFGSDKKaVFRVKVLS 642
Cdd:cd22704 63 FVNDS-----RIPEQTYITLKLGDSIRFGYDTN-VYRFEQLS 98
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
77-109 |
1.43e-05 |
|
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440845 [Multi-domain] Cd Length: 443 Bit Score: 47.90 E-value: 1.43e-05
10 20 30
....*....|....*....|....*....|...
gi 122240921 77 RPRVLVAGGGIGGLVLALAARRKGYEVTVFERD 109
Cdd:COG1232 1 MKRVAVIGGGIAGLTAAYRLAKAGHEVTVLEAS 33
|
|
| FHA_RNF8 |
cd22663 |
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ... |
539-634 |
1.96e-05 |
|
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is a telomere-associated E3 ubiquitin-protein ligase that plays an important role in DNA double-strand break (DSB) repair via histone ubiquitination. It is localized in the nucleus and interacts with class III E2s (UBE2E2, UbcH6, and UBE2E3), but not with other E2s (UbcH5, UbcH7, UbcH10, hCdc34, and hBendless). It recruits UBC13 for lysine 63-based self polyubiquitylation. Its deficiency causes neuronal pathology and cognitive decline, and its loss results in neuron degeneration. RNF8, together with RNF168, catalyzes a series of ubiquitylation events on substrates such as H2A and H2AX, with the H2AK13/15 ubiquitylation being particularly important for recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of DSBs. Specially, RNF8 mediates the ubiquitination of gammaH2AX, and recruits 53BP1 and BRCA1 to DNA damage sites which promotes DNA damage response (DDR) and inhibits chromosomal instability. Moreover, RNF8 interacts with retinoid X receptor alpha (RXR alpha) and enhances its transcription-stimulating activity. It also regulates the rate of exit from mitosis and cytokinesis. RNF8 contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438715 [Multi-domain] Cd Length: 110 Bit Score: 43.89 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 539 DSQPIRLIRDEKKSLSIGsRSdPSNSTASLALPLPQISENHATITCKNK-AFYVTDNGSEHGTWITDNegrryRVPPNFP 617
Cdd:cd22663 9 GIDPLVLLLEDGKEVTVG-RG-LGVTYQLVSTCPLMISRNHCVLKKNDEgQWTIKDNKSLNGVWVNGE-----RIEPLKP 81
|
90
....*....|....*..
gi 122240921 618 VRFHPSDAIEFGSDKKA 634
Cdd:cd22663 82 YPLNEGDLIQLGVPPEN 98
|
|
| PRK07333 |
PRK07333 |
ubiquinone biosynthesis hydroxylase; |
80-248 |
1.97e-05 |
|
ubiquinone biosynthesis hydroxylase;
Pssm-ID: 180935 [Multi-domain] Cd Length: 403 Bit Score: 47.28 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 80 VLVAGGGIGGLVLALAARRKGYEVTVFERDMSAvrgEGQYRGPIQIQSNALAA---LEAIDmsVAEEV------MREGCV 150
Cdd:PRK07333 4 VVIAGGGYVGLALAVALKQAAPHLPVTVVDAAP---AGAWSRDPRASAIAAAArrmLEALG--VWDEIapeaqpITDMVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 151 TGDRINGLVDGIsgswyikFDTFTPAAERGLPVTRVISRMTLQQILARAVGDDAI--LNDSHVVDFIDDGNKVTAILEDG 228
Cdd:PRK07333 79 TDSRTSDPVRPV-------FLTFEGEVEPGEPFAHMVENRVLINALRKRAEALGIdlREATSVTDFETRDEGVTVTLSDG 151
|
170 180
....*....|....*....|
gi 122240921 229 RKFEGDLLVGADGIWSKVRK 248
Cdd:PRK07333 152 SVLEARLLVAADGARSKLRE 171
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
82-108 |
6.28e-05 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 41.36 E-value: 6.28e-05
10 20
....*....|....*....|....*..
gi 122240921 82 VAGGGIGGLVLALAARRKGYEVTVFER 108
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEK 27
|
|
| FHA_Kanadaptin |
cd22677 |
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ... |
573-629 |
1.24e-04 |
|
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also called human lung cancer oncogene 3 protein (HLC-3), kidney anion exchanger adapter protein, or solute carrier family 4 anion exchanger member 1 adapter protein (SLC4A1AP), is a nuclear protein widely expressed in mammalian tissues. It was originally isolated as a kidney Cl-/HCO3- anion exchanger 1 (kAE1)-binding protein. It is a highly mobile nucleocytoplasmic shuttling and multilocalizing protein. Its role in mammalian cells remains unclear. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438729 [Multi-domain] Cd Length: 106 Bit Score: 41.77 E-value: 1.24e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 122240921 573 PQISENHATI------TCKNKAFYVTDNGSEHGTWITDNegrryRVPPNFPVRFHPSDAIEFG 629
Cdd:cd22677 39 PSISRYHAVLqyrgdaDDHDGGFYLYDLGSTHGTFLNKQ-----RIPPKQYYRLRVGHVLKFG 96
|
|
| FHA_MDC1 |
cd22665 |
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ... |
555-632 |
1.98e-04 |
|
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; MDC1, also called nuclear factor with BRCT domains 1 (NFBD1), is a nuclear chromatin-associated protein that is required for checkpoint mediated cell cycle arrest in response to DNA damage within both the S and G2/M phases of the cell cycle. It directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. MDC1 contains a forkhead-associated (FHA) domain and two BRCT domains, as well as an internal 41-amino acid repeat sequence. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438717 [Multi-domain] Cd Length: 97 Bit Score: 40.68 E-value: 1.98e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 122240921 555 IGSrsDPSNStasLALPLPQISENHATITCKNKAFYVTDNGSEHGTWItdneGRRYRVPPNFPVRFHPSDAIEFGSDK 632
Cdd:cd22665 25 IGR--DPSCS---VVLPDKSVSKQHACIEVDGGTHLIEDLGSTNGTRI----GNKVRLKPNVRYELIDGDLLLFGDVK 93
|
|
| FHA_FhaB-like |
cd22693 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
549-638 |
2.31e-04 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaB and similar proteins; FhaB, also called FtsZ-interacting protein A (FipA), is a putative virulence factor involved in regulating cell shape. It can interact with polyketide-associated protein PapA5, a putative membrane protein involved in the biosynthesis of virulence enhancing lipids. FhaB regulates growth and cell division. It is probably required for divisomal protein assembly under oxidative stress. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438745 [Multi-domain] Cd Length: 91 Bit Score: 40.36 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 549 EKKSLSIGSRSDpsnstASLALPLPQISENHATITCKNKAFYVTDNGSEHGTWITDNegrryRVppNFPVRFHPSDAIEF 628
Cdd:cd22693 16 DKSGITIGRADD-----NDLVLSDDFVSSRHARIYLQGSSWYLEDLGSTNGTFVNGN-----RV--TQPVVVQPGDTIRI 83
|
90
....*....|
gi 122240921 629 GsdkKAVFRV 638
Cdd:cd22693 84 G---ATVFEV 90
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
76-109 |
2.49e-04 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 43.74 E-value: 2.49e-04
10 20 30
....*....|....*....|....*....|....
gi 122240921 76 RRPRVLVAGGGIGGLVLALAARRKGYEVTVFERD 109
Cdd:COG0665 1 ATADVVVIGGGIAGLSTAYHLARRGLDVTVLERG 34
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
79-109 |
3.37e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 43.72 E-value: 3.37e-04
10 20 30
....*....|....*....|....*....|.
gi 122240921 79 RVLVAGGGIGGLVLALAARRKGYEVTVFERD 109
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEAD 31
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
76-108 |
3.84e-04 |
|
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function prediction only];
Pssm-ID: 442577 [Multi-domain] Cd Length: 445 Bit Score: 43.30 E-value: 3.84e-04
10 20 30
....*....|....*....|....*....|...
gi 122240921 76 RRPRVLVAGGGIGGLVLALAARRKGYEVTVFER 108
Cdd:COG3349 2 MPPRVVVVGGGLAGLAAAVELAEAGFRVTLLEA 34
|
|
| mhpA |
PRK06183 |
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase; |
341-394 |
3.94e-04 |
|
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
Pssm-ID: 235727 [Multi-domain] Cd Length: 500 Bit Score: 43.36 E-value: 3.94e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 122240921 341 TDEEA-ILRRDIYdrppTFN------WGKGRVTLLGDSVHAMQPNLGQGGCMAIEDGYQLA 394
Cdd:PRK06183 261 TPDDAeLIRHAVY----TFHarvadrWRSGRVLLAGDAAHLMPPFAGQGMNSGIRDAANLA 317
|
|
| PRK08849 |
PRK08849 |
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional |
212-424 |
5.54e-04 |
|
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional
Pssm-ID: 181564 [Multi-domain] Cd Length: 384 Bit Score: 42.84 E-value: 5.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 212 VDFIDDGNKVTaiLEDGRKFEGDLLVGADGIWSKVR-KVLFGQSEATYSEYTCYTGIADFVPPDIDT------VGYRVFL 284
Cdd:PRK08849 137 LEFSAEGNRVT--LESGAEIEAKWVIGADGANSQVRqLAGIGITAWDYRQHCMLINVETEQPQQDITwqqftpSGPRSFL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 285 ---GHKqyfvssdvgaGKMQWYafhKEPaggtdpengknKRLLEifngwcdnvvdLINATDEEaiLRRDIYDRPP----- 356
Cdd:PRK08849 215 plcGNQ----------GSLVWY---DSP-----------KRIKQ-----------LSAMNPEQ--LRSEILRHFPaelge 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 357 --TFNWG-------------KGRVTLLGDSVHAMQPNLGQGGCMAIEDGYQLAVELEKSWQESaksgtpmdiVSSLRRYE 421
Cdd:PRK08849 258 ikVLQHGsfpltrrhaqqyvKNNCVLLGDAAHTINPLAGQGVNLGFKDVDVLLAETEKQGVLN---------DASFARYE 328
|
...
gi 122240921 422 KER 424
Cdd:PRK08849 329 RRR 331
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
80-115 |
5.55e-04 |
|
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440673 [Multi-domain] Cd Length: 443 Bit Score: 42.90 E-value: 5.55e-04
10 20 30
....*....|....*....|....*....|....*.
gi 122240921 80 VLVAGGGIGGLVLALAARRKGYEVTVFERdMSAVRG 115
Cdd:COG1053 6 VVVVGSGGAGLRAALEAAEAGLKVLVLEK-VPPRGG 40
|
|
| PRK08850 |
PRK08850 |
2-octaprenyl-6-methoxyphenol hydroxylase; Validated |
364-441 |
5.79e-04 |
|
2-octaprenyl-6-methoxyphenol hydroxylase; Validated
Pssm-ID: 236341 [Multi-domain] Cd Length: 405 Bit Score: 42.84 E-value: 5.79e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 122240921 364 RVTLLGDSVHAMQPNLGQGGCMAIEDGYQLAVELEKSWQESAKSGTpmdiVSSLRRYEKERILRVsvihglARMAAIM 441
Cdd:PRK08850 283 RVALVGDAAHTIHPLAGQGVNLGLLDAASLAQEILALWQQGRDIGL----KRNLRGYERWRKAEA------AKMIAAM 350
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
79-108 |
5.87e-04 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 39.11 E-value: 5.87e-04
10 20 30
....*....|....*....|....*....|
gi 122240921 79 RVLVAGGGIGGLVLALAARRKGYEVTVFER 108
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVER 30
|
|
| PRK08255 |
PRK08255 |
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase; |
234-436 |
7.31e-04 |
|
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase;
Pssm-ID: 236203 [Multi-domain] Cd Length: 765 Bit Score: 42.62 E-value: 7.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 234 DLLVGADGIWSKVRkvlfgqseatySEYtcytgiADFVPPDIDTVGYR-VFLG-HKQY----FVSSDVGAGKMQWYAFHK 307
Cdd:PRK08255 131 DLVIASDGLNSRIR-----------TRY------ADTFQPDIDTRRCRfVWLGtHKVFdaftFAFEETEHGWFQAHAYRF 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 308 EPAGGT------------------DPENGKnKRLLEIFNGWCDNVVDLINATDeeaiLRRDIYDRPPTF---NW----GK 362
Cdd:PRK08255 194 DDDTSTfivetpeevwraagldemSQEESI-AFCEKLFADYLDGHPLMSNASH----LRGSAWINFPRVvceRWvhwnRR 268
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 122240921 363 GRVTLLGDSVHAMQPNLGQGGCMAIEDGYQLAVELEKSwqesaksgtPMDIVSSLRRYEKERILRVSVIHGLAR 436
Cdd:PRK08255 269 VPVVLMGDAAHTAHFSIGSGTKLALEDAIELARCLHEH---------PGDLPAALAAYEEERRVEVLRIQNAAR 333
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
79-109 |
2.12e-03 |
|
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: 40.84 E-value: 2.12e-03
10 20 30
....*....|....*....|....*....|.
gi 122240921 79 RVLVAGGGIGGLVLALAARRKGYEVTVFERD 109
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLERG 31
|
|
| PRK06834 |
PRK06834 |
hypothetical protein; Provisional |
80-248 |
2.30e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235870 [Multi-domain] Cd Length: 488 Bit Score: 40.77 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 80 VLVAGGGIGGLVLALAARRKGYEVTVFER----DMSAVRGEGqyrgpiqiqsnaLAA--LEAIDM-SVAEEVMREGCVtg 152
Cdd:PRK06834 6 VVIAGGGPTGLMLAGELALAGVDVAIVERrpnqELVGSRAGG------------LHArtLEVLDQrGIADRFLAQGQV-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122240921 153 drinGLVDGISGswyIKFDTftpaaeRGLPvTRVISRMTLQQ-----ILARAVGDDA--ILNDSHVVDFIDDGNKVTAIL 225
Cdd:PRK06834 72 ----AQVTGFAA---TRLDI------SDFP-TRHNYGLALWQnhierILAEWVGELGvpIYRGREVTGFAQDDTGVDVEL 137
|
170 180
....*....|....*....|...
gi 122240921 226 EDGRKFEGDLLVGADGIWSKVRK 248
Cdd:PRK06834 138 SDGRTLRAQYLVGCDGGRSLVRK 160
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
75-109 |
2.41e-03 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 40.67 E-value: 2.41e-03
10 20 30
....*....|....*....|....*....|....*.
gi 122240921 75 TRRPRVLVAGGGIGGLVLALAARRKGYEVTVFE-RD 109
Cdd:COG1231 5 ARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEaRD 40
|
|
| mnmC |
PRK01747 |
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ... |
79-115 |
2.44e-03 |
|
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent 5-carboxymethylaminomethyl-2-thiouridine(34) oxidoreductase MnmC;
Pssm-ID: 234978 [Multi-domain] Cd Length: 662 Bit Score: 40.99 E-value: 2.44e-03
10 20 30
....*....|....*....|....*....|....*..
gi 122240921 79 RVLVAGGGIGGLVLALAARRKGYEVTVFERDMSAVRG 115
Cdd:PRK01747 262 DAAIIGGGIAGAALALALARRGWQVTLYEADEAPAQG 298
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
78-123 |
2.50e-03 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 400379 [Multi-domain] Cd Length: 301 Bit Score: 40.38 E-value: 2.50e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 122240921 78 PRVLVAGGGIGGLVLALAARRKGYEVTVFErdmsaVRGEGQYRGPI 123
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIE-----DEGTCPYGGCV 41
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
78-109 |
3.47e-03 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 40.61 E-value: 3.47e-03
10 20 30
....*....|....*....|....*....|..
gi 122240921 78 PRVLVAGGGIGGLVLALAARRKGYEVTVFERD 109
Cdd:COG1148 141 KRALVIGGGIAGMTAALELAEQGYEVYLVEKE 172
|
|
| FHA_Rv1747-like_rpt1 |
cd22694 |
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
544-612 |
4.37e-03 |
|
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ATP-binding/permease protein Rv1747 and similar proteins; Rv1747 is a putative ATP-binding cassette (ABC) transporter involved in the translocation of an unknown substrate across the membrane. It is required for normal virulent infection by M. tuberculosis. Rv1747 has a cytoplasmic regulatory module consisting of two pThr-interacting forkhead-associated (FHA) domains connected by a conformationally disordered linker with two phospho-acceptor threonines (pThr). Recruitment and phosphorylation of Rv1747 depend on the interaction between its two non-redundant FHA domains and the autophosphorylated form of serine/threonine protein kinase PknF. This model corresponds to the first FHA domain. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438746 [Multi-domain] Cd Length: 93 Bit Score: 36.92 E-value: 4.37e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 122240921 544 RLIRDEKKSLSIGSrsDPSNStasLALPLPQISENHATITCKNKAFYVTDNGSEHGTWItdnEGRRYRV 612
Cdd:cd22694 9 ELRFDPGSSVRIGR--DPDAD---VRLDDPRVSRRHALLEFDGDGWVYTDLGSRNGTYL---NGRRVQQ 69
|
|
| PRK07364 |
PRK07364 |
FAD-dependent hydroxylase; |
364-424 |
4.84e-03 |
|
FAD-dependent hydroxylase;
Pssm-ID: 236001 [Multi-domain] Cd Length: 415 Bit Score: 40.00 E-value: 4.84e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 122240921 364 RVTLLGDSVHAMQPNLGQGGCMAIEDGYQLAVELEKSWQESAKSGTpmdiVSSLRRYEKER 424
Cdd:PRK07364 295 RLALVGDAAHCCHPVGGQGLNLGIRDAAALAQVLQTAHQRGEDIGS----LAVLKRYERWR 351
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
75-108 |
5.11e-03 |
|
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];
Pssm-ID: 441675 [Multi-domain] Cd Length: 414 Bit Score: 39.85 E-value: 5.11e-03
10 20 30
....*....|....*....|....*....|....
gi 122240921 75 TRRPRVLVAGGGIGGLVLALAARRKGYEVTVFER 108
Cdd:COG2072 4 TEHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEK 37
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
79-109 |
5.62e-03 |
|
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 440259 [Multi-domain] Cd Length: 434 Bit Score: 39.73 E-value: 5.62e-03
10 20 30
....*....|....*....|....*....|.
gi 122240921 79 RVLVAGGGIGGLVLALAARRKGYEVTVFERD 109
Cdd:COG0493 123 KVAVVGSGPAGLAAAYQLARAGHEVTVFEAL 153
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
79-108 |
6.83e-03 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 39.47 E-value: 6.83e-03
10 20 30
....*....|....*....|....*....|
gi 122240921 79 RVLVAGGGIGGLVLALAARRKGYEVTVFER 108
Cdd:PRK12771 139 RVAVIGGGPAGLSAAYHLRRMGHAVTIFEA 168
|
|
| FHA_EspA-like |
cd22698 |
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ... |
534-602 |
7.54e-03 |
|
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA is a histidine protein kinase with a fork head-associated (FHA) domain at the N-terminus and a receiver domain at the C-terminus. It functions as an inhibitor of sporulation during early fruiting body development while cells are aggregating into raised mounds. EspA is part of a two-component signal transduction system that regulates the timing of sporulation initiation. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438750 [Multi-domain] Cd Length: 93 Bit Score: 36.24 E-value: 7.54e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 122240921 534 PTSSGDSQPIRLIRDEkksLSIGSRSDpsnstASLALPLPQISENHATITCKNKAFYVTDNGSEHGTWI 602
Cdd:cd22698 7 QKGSEEGKDYELDQDE---FTIGRSSN-----NDIRLNDHSVSRHHARIVRQGDKCNLTDLGSTNGTFL 67
|
|
| PRK12409 |
PRK12409 |
D-amino acid dehydrogenase small subunit; Provisional |
78-108 |
7.59e-03 |
|
D-amino acid dehydrogenase small subunit; Provisional
Pssm-ID: 237093 [Multi-domain] Cd Length: 410 Bit Score: 39.24 E-value: 7.59e-03
10 20 30
....*....|....*....|....*....|.
gi 122240921 78 PRVLVAGGGIGGLVLALAARRKGYEVTVFER 108
Cdd:PRK12409 2 SHIAVIGAGITGVTTAYALAQRGYQVTVFDR 32
|
|
| |
