|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02927 |
PLN02927 |
antheraxanthin epoxidase/zeaxanthin epoxidase |
73-652 |
0e+00 |
|
antheraxanthin epoxidase/zeaxanthin epoxidase
Pssm-ID: 178515 [Multi-domain] Cd Length: 668 Bit Score: 884.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 73 VLVAGGGIGGLVFALAAKRKGFEVVVLERDMSAVRGEGKYRGPIQLQSNALAVLEAVDAGAADQVMDAGCITGNRVNGIV 152
Cdd:PLN02927 84 VLVAGGGIGGLVFALAAKKKGFDVLVFEKDLSAIRGEGKYRGPIQIQSNALAALEAIDIDVAEQVMEAGCITGDRINGLV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 153 DGVSGSWYIKFDTFTPAAERGLPVTRVISRMTLQQILARAVGDDAILNDSHVVDFIDDGNKVTAILEDGRKFEGDLLVGA 232
Cdd:PLN02927 164 DGISGSWYVKFDTFTPAASRGLPVTRVISRMTLQQILARAVGEDVIRNESNVVDFEDSGDKVTVVLENGQRYEGDLLVGA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 233 DGIWSKVRKVLFGQSEATYSEYTCYTGIADFVPPDIDTVGYRVFLGHKQYFVSSDVGAGKMQWYAFHKEPAGGTDPENGK 312
Cdd:PLN02927 244 DGIWSKVRNNLFGRSEATYSGYTCYTGIADFIPADIESVGYRVFLGHKQYFVSSDVGGGKMQWYAFHEEPAGGADAPNGM 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 313 NKRLLEIFNGWCDNVVDLINATDEEAILRRDIYDRPPTFNWGKGRVTLLGDSVHAMQPNLGQGGCMAIEDGYQLAVELEK 392
Cdd:PLN02927 324 KKRLFEIFDGWCDNVLDLLHATEEDAILRRDIYDRSPGFTWGKGRVTLLGDSIHAMQPNMGQGGCMAIEDSFQLALELDE 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 393 SWQESAKSGTPMDIVSSLRRYEKERILRVSVIHGLARMAAIMATTYRPYLGVGLGPLSFLTKLRIPHPGRVGGRFFIKYG 472
Cdd:PLN02927 404 AWKQSVETNTPVDVVSSLKRYEESRRLRVAIIHAMARMAAIMASTYKAYLGVGLGPLSFLTKFRVPHPGRVGGRFFVDIA 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 473 MPLMLSWVLGGNSTKLEGRPLSCRLSDKANDQLRRWFEDDDALEQAMGGEWYLLPtsSGD----SQPIRLIRDEKKSLSI 548
Cdd:PLN02927 484 MPLMLDWVLGGNSEKLEGRPPSCRLTDKADDRLREWFEDDDALERTIKGEWYLIP--HGDdccvSETLCLTKDEDQPCIV 561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 549 GSRSDPSNSTASLALPLPQISENHATITCKNKAFYVTDNGSEHGTWITDNEGRRYRVPPNFPVRFHPSDAIEFGSDKKAV 628
Cdd:PLN02927 562 GSEPDQDFPGMRIVIPSSQVSKMHARVIYKDGAFFLMDLRSEHGTYVTDNEGRRYRATPNFPARFRSSDIIEFGSDKKAA 641
|
570 580
....*....|....*....|....*..
gi 1002264030 629 FRVKVLSTLPYESAR---GGPQILQAA 652
Cdd:PLN02927 642 FRVKVIRKTPKSTRKnesNNDKLLQTA 668
|
|
| FHA_ZEP-like |
cd22702 |
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar ... |
515-635 |
9.58e-65 |
|
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: 9.58e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 515 LEQAMGGEWYLLPTSSGD--SQPIRLIRDEKKSLSIGSRSDPSNSTASLALPLPQISENHATITCKNKAFYVTDNGSEHG 592
Cdd:cd22702 1 LERATSAEWYLLPLGNDMdgGSPIRLTRDEKQPCIIGSDPHQAISGISVVIPSPQVSELHARITCKNGAFFLTDLGSEHG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1002264030 593 TWITDNEGRRYRVPPNFPVRFHPSDAIEFGSDKKAVFRVKVLS 635
Cdd:cd22702 81 TWINDNEGRRYRAPPNFPVRLHPSDVIEFGSDKKARFRVKVMK 123
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
73-440 |
3.95e-48 |
|
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: 171.66 E-value: 3.95e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 73 VLVAGGGIGGLVFALAAKRKGFEVVVLERDmSAVRGEGkyRGpIQLQSNALAVLEAvdAGAADQVMDAGC-ITGNRVngi 151
Cdd:COG0654 6 VLIVGGGPAGLALALALARAGIRVTVVERA-PPPRPDG--RG-IALSPRSLELLRR--LGLWDRLLARGApIRGIRV--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 152 VDGVSGSWYIKFDtftpAAERGLPVTRVISRMTLQQILARAVGDD--AILNDSHVVDFIDDGNKVTAILEDGRKFEGDLL 229
Cdd:COG0654 77 RDGSDGRVLARFD----AAETGLPAGLVVPRADLERALLEAARALgvELRFGTEVTGLEQDADGVTVTLADGRTLRADLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 230 VGADGIWSKVRKVLFgqseatyseytcytgiadfvppdIDTVGYrvflGHKQYFVSSDVGAgkmqwyafhkepaggtdpe 309
Cdd:COG0654 153 VGADGARSAVRRLLG-----------------------IGFTGR----DYPQRALWAGVRT------------------- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 310 ngknkRLLEIFNGWCDNVVDLINATDEEA-ILRRDIYDRpptfnWGKGRVTLLGDSVHAMQPNLGQGGCMAIEDGYQLAV 388
Cdd:COG0654 187 -----ELRARLAAAGPRLGELLELSPRSAfPLRRRRAER-----WRRGRVVLLGDAAHTMHPLGGQGANLALRDAAALAW 256
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1002264030 389 ELekswqesAKSGTPMDIVSSLRRYEKERILRVSVIHGLAR-MAAIMATTYRP 440
Cdd:COG0654 257 KL-------AAALRGRDDEAALARYERERRPRAARVQRAADaLGRLFHPDSPP 302
|
|
| PRK08163 |
PRK08163 |
3-hydroxybenzoate 6-monooxygenase; |
73-420 |
1.08e-43 |
|
3-hydroxybenzoate 6-monooxygenase;
Pssm-ID: 181262 [Multi-domain] Cd Length: 396 Bit Score: 161.36 E-value: 1.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 73 VLVAGGGIGGLVFALAAKRKGFEVVVLERdmSAVRGE---GkyrgpIQLQSNALAVLEAVdaGAADQVMDAGCITGNRVn 149
Cdd:PRK08163 7 VLIVGGGIGGLAAALALARQGIKVKLLEQ--AAEIGEigaG-----IQLGPNAFSALDAL--GVGEAARQRAVFTDHLT- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 150 gIVDGVSGSWYIKFDTFTPAAER-GLPVTrVISRMTLQQILARAVGDDA---ILNDSHVVDFIDDGNKVTAILEDGRKFE 225
Cdd:PRK08163 77 -MMDAVDAEEVVRIPTGQAFRARfGNPYA-VIHRADIHLSLLEAVLDHPlveFRTSTHVVGIEQDGDGVTVFDQQGNRWT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 226 GDLLVGADGIWSKVRKVLFGqSEATYSEYTCYTGIADF--VPPDIDTVGYRVFLGHKQYFVSSDVGAGKMqwY----AFH 299
Cdd:PRK08163 155 GDALIGCDGVKSVVRQSLVG-DAPRVTGHVVYRAVIDVddMPEDLRINAPVLWAGPHCHLVHYPLRGGEQ--YnlvvTFH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 300 ---KEPAGGTDpenGKNKRLLEIFNGWCDNVVDLInatDEEAILRR-DIYDRPPTFNWGKGRVTLLGDSVHAMQPNLGQG 375
Cdd:PRK08163 232 sreQEEWGVKD---GSKEEVLSYFEGIHPRPRQML---DKPTSWKRwATADREPVAKWSTGRVTLLGDAAHPMTQYMAQG 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1002264030 376 GCMAIEDGYQLAVELEkswqesaksGTPMDIVSSLRRYEKERILR 420
Cdd:PRK08163 306 ACMALEDAVTLGKALE---------GCDGDAEAAFALYESVRIPR 341
|
|
| PRK06753 |
PRK06753 |
hypothetical protein; Provisional |
73-435 |
1.05e-40 |
|
hypothetical protein; Provisional
Pssm-ID: 168661 [Multi-domain] Cd Length: 373 Bit Score: 152.54 E-value: 1.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 73 VLVAGGGIGGLVFALAAKRKGFEVVVLERDMS-AVRGEGkyrgpIQLQSNALAVLEAVDAgaADQVMDAGcitgNRVNG- 150
Cdd:PRK06753 3 IAIIGAGIGGLTAAALLQEQGHEVKVFEKNESvKEVGAG-----IGIGDNVIKKLGNHDL--AKGIKNAG----QILSTm 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 151 -IVDGvsgswyiKFDTFTPAAERGLPVTRVISRMTLQQILARAVGDDAILNDSHVVDFIDDGNKVTAILEDGRKFEGDLL 229
Cdd:PRK06753 72 nLLDD-------KGTLLNKVKLKSNTLNVTLHRQTLIDIIKSYVKEDAIFTGKEVTKIENETDKVTIHFADGESEAFDLC 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 230 VGADGIWSKVRKVLFGQSEATYSEYTCYTGIadfvppdIDTVGYRVFLGHKQYF-VSSDVGA-----GKMQWYAFHKEPA 303
Cdd:PRK06753 145 IGADGIHSKVRQSVNADSKVRYQGYTCFRGL-------IDDIDLKLPDCAKEYWgTKGRFGIvpllnNQAYWFITINAKE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 304 GGTDPENGKNKRLLEIFNGWCDNVVDLINATDEEAILRRDIYDRPPTFNWGKGRVTLLGDSVHAMQPNLGQGGCMAIEDG 383
Cdd:PRK06753 218 RDPKYSSFGKPHLQAYFNHYPNEVREILDKQSETGILHHDIYDLKPLKSFVYGRIVLLGDAAHATTPNMGQGAGQAMEDA 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1002264030 384 YQLAVELEKSWQESAksgtpmdivssLRRYEKERILRVSVIHGLARMAAIMA 435
Cdd:PRK06753 298 IVLANCLNAYDFEKA-----------LQRYDKIRVKHTAKVIKRSRKIGKIA 338
|
|
| PRK06847 |
PRK06847 |
hypothetical protein; Provisional |
73-421 |
1.90e-40 |
|
hypothetical protein; Provisional
Pssm-ID: 235874 [Multi-domain] Cd Length: 375 Bit Score: 151.95 E-value: 1.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 73 VLVAGGGIGGLVFALAAKRKGFEVVVLERDMS-AVRGEGkyrgpIQLQSNALAVLEAVdaGAADQVMDAGCITgnrvngi 151
Cdd:PRK06847 7 VLIVGGGIGGLSAAIALRRAGIAVDLVEIDPEwRVYGAG-----ITLQGNALRALREL--GVLDECLEAGFGF------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 152 vDGVsgswyikfDTFTPA------------AERGLPVTRVISRMTLQQIL---ARAVGDDAILNDShVVDFIDDGNKVTA 216
Cdd:PRK06847 73 -DGV--------DLFDPDgtllaelptprlAGDDLPGGGGIMRPALARILadaARAAGADVRLGTT-VTAIEQDDDGVTV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 217 ILEDGRKFEGDLLVGADGIWSKVRKVLFGqsEATYSEYTCyTGIADFV---PPDIDtvgyrvflgHKQYFVSSDVGAG-- 291
Cdd:PRK06847 143 TFSDGTTGRYDLVVGADGLYSKVRSLVFP--DEPEPEYTG-QGVWRAVlprPAEVD---------RSLMYLGPTTKAGvv 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 292 ---KMQWYAFHKEPAGG--TDPENGKNKRLLEIFNGWCDNVVDLI--NATDEEAILRRDI----YDRPptfnWGKGRVTL 360
Cdd:PRK06847 211 plsEDLMYLFVTEPRPDnpRIEPDTLAALLRELLAPFGGPVLQELreQITDDAQVVYRPLetllVPAP----WHRGRVVL 286
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002264030 361 LGDSVHAMQPNLGQGGCMAIEDGYQLAVELEKswqesaksgtPMDIVSSLRRYEKERILRV 421
Cdd:PRK06847 287 IGDAAHATTPHLAQGAGMAIEDAIVLAEELAR----------HDSLEAALQAYYARRWERC 337
|
|
| PRK07538 |
PRK07538 |
hypothetical protein; Provisional |
73-418 |
6.09e-31 |
|
hypothetical protein; Provisional
Pssm-ID: 236046 [Multi-domain] Cd Length: 413 Bit Score: 125.39 E-value: 6.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 73 VLVAGGGIGGLVFALAAKRKGFEVVVLErdmsAVR-----GEGkyrgpIQLQSNALAVLEavDAGAADQVMDAGCITGNR 147
Cdd:PRK07538 3 VLIAGGGIGGLTLALTLHQRGIEVVVFE----AAPelrplGVG-----INLLPHAVRELA--ELGLLDALDAIGIRTREL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 148 VngivdgvsgsWYIKFDTFTPAAERGL----PVTRV-ISRMTLQQILARAV----GDDAILNDSHVVDFIDDGNKVTAIL 218
Cdd:PRK07538 72 A----------YFNRHGQRIWSEPRGLaagyDWPQYsIHRGELQMLLLDAVrerlGPDAVRTGHRVVGFEQDADVTVVFL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 219 EDGR-----KFEGDLLVGADGIWSKVRKVLF-GQSEATYSEYTCYTGIADFVPpdIDTVGYRVFLGHKQ-----YFVSSD 287
Cdd:PRK07538 142 GDRAggdlvSVRGDVLIGADGIHSAVRAQLYpDEGPPRWNGVMMWRGVTEAPP--FLTGRSMVMAGHLDgklvvYPISEP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 288 VGAGKMQ---WYAFHKEPAGGTDPENGKNKR-----LLEIFNGWCDNVVD---LINATdeEAILRRDIYDRPPTFNWGKG 356
Cdd:PRK07538 220 VDADGRQlinWVAEVRVDDAGAPRREDWNRPgdledFLPHFADWRFDWLDvpaLIRAA--EAIYEYPMVDRDPLPRWTRG 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002264030 357 RVTLLGDSVHAMQPNLGQGGCMAIEDGYQLAVELekswqesAKSGtpmDIVSSLRRYEKERI 418
Cdd:PRK07538 298 RVTLLGDAAHPMYPVGSNGASQAILDARALADAL-------AAHG---DPEAALAAYEAERR 349
|
|
| PRK06475 |
PRK06475 |
FAD-binding protein; |
74-431 |
2.55e-22 |
|
FAD-binding protein;
Pssm-ID: 180582 [Multi-domain] Cd Length: 400 Bit Score: 99.51 E-value: 2.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 74 LVAGGGIGGLVFALAAKRKGFEVVVLER--DMSAVrGEGkyrgpIQLQSNALAVLEAVdaGAADQVMDAGCITgnRVNGI 151
Cdd:PRK06475 6 LIAGAGVAGLSAALELAARGWAVTIIEKaqELSEV-GAG-----LQLAPNAMRHLERL--GVADRLSGTGVTP--KALYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 152 VDGVSGSWYIKFDTFTPAAERGLPVTRVISRMTLQQILARAVGDDAILNDS---HVVDFIDDGNKVTA--ILEDGRKF-E 225
Cdd:PRK06475 76 MDGRKARPLLAMQLGDLARKRWHHPYIVCHRADLQSALLDACRNNPGIEIKlgaEMTSQRQTGNSITAtiIRTNSVETvS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 226 GDLLVGADGIWSKVRKvLFGQSEATYSEYTCY--TGIADFVP-------PDIDTVgyRVFLGHKQYFVSSDVGAGKMqwY 296
Cdd:PRK06475 156 AAYLIACDGVWSMLRA-KAGFSKARFSGHIAWrtTLAADALPasflsamPEHKAV--SAWLGNKAHFIAYPVKGGKF--F 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 297 AF----HKEPAGGTDPENGKNKRLLEIFNGWCDNVVDLINATDEeailrrdiYDRPPTFNW------GKGRVTLLGDSVH 366
Cdd:PRK06475 231 NFvaitGGENPGEVWSKTGDKAHLKSIYADWNKPVLQILAAIDE--------WTYWPLFEMadaqfvGPDRTIFLGDASH 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002264030 367 AMQPNLGQGGCMAIEDGYQLAVELEKSWQESAksgtpmdivssLRRYE---KERILRVSVIHGLARMA 431
Cdd:PRK06475 303 AVTPFAAQGAAMAIEDAAALAEALDSDDQSAG-----------LKRFDsvrKERIAAVAKRGQLNRFA 359
|
|
| PRK07236 |
PRK07236 |
hypothetical protein; Provisional |
73-418 |
3.45e-19 |
|
hypothetical protein; Provisional
Pssm-ID: 235980 [Multi-domain] Cd Length: 386 Bit Score: 89.98 E-value: 3.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 73 VLVAGGGIGGLVFALAAKRKGFEVVVLERDMSAVRGEGkyrGPIQLQSNALAVLEAVDAGAADQVmdagcitgnrvngiv 152
Cdd:PRK07236 9 AVVIGGSLGGLFAALLLRRAGWDVDVFERSPTELDGRG---AGIVLQPELLRALAEAGVALPADI--------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 153 dGVSGSWYIKFD-TFTPAAERGLPVTrVISRMTLQQILARAVGDDAILNDSHVVDFIDDGNKVTAILEDGRKFEGDLLVG 231
Cdd:PRK07236 71 -GVPSRERIYLDrDGRVVQRRPMPQT-QTSWNVLYRALRAAFPAERYHLGETLVGFEQDGDRVTARFADGRRETADLLVG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 232 ADGIWSKVRKVLFGQSEATYSEYTCYTGIADfvPPDIDTVGYRVFLGHKQYFVSSDvgagkMQWYAFhkePAGGTDPENG 311
Cdd:PRK07236 149 ADGGRSTVRAQLLPDVRPTYAGYVAWRGLVD--EAALPPEARAALRDRFTFQLGPG-----SHILGY---PVPGEDGSTE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 312 KNKRLleiFNG-WCDNVVD-------LINAT---------------DEEAILRRDIYDR-PPTF---------------- 351
Cdd:PRK07236 219 PGKRR---YNWvWYRNAPAgeeldelLTDRDgtrrpfsvppgalrdDVLAELRDDAAELlAPVFaelveataqpfvqaif 295
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002264030 352 -----NWGKGRVTLLGDSVHAMQPNLGQGGCMAIEDGYQLAVELekswqesakSGTPMDIVSSLRRYEKERI 418
Cdd:PRK07236 296 dlevpRMAFGRVALLGDAAFVARPHTAAGVAKAAADAVALAEAL---------AAAAGDIDAALAAWEAERL 358
|
|
| FAD_binding_3 |
pfam01494 |
FAD binding domain; This domain is involved in FAD binding in a number of enzymes. |
73-421 |
7.38e-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: 70.43 E-value: 7.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 73 VLVAGGGIGGLVFALAAKRKGFEVVVLERDMSAVRgEGKYRGpiqLQSNALAVLEavDAGAADQVMDAGciTGNRVNGI- 151
Cdd:pfam01494 4 VLIVGGGPAGLMLALLLARAGVRVVLVERHATTSV-LPRAHG---LNQRTMELLR--QAGLEDRILAEG--VPHEGMGLa 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 152 VDGVSGSWYIKFDTfTPAAERGLPVTRVIsRMTLQQilARAVGDDaILNDSHVVDFIDDGNKVTAILEDGR-----KFEG 226
Cdd:pfam01494 76 FYNTRRRADLDFLT-SPPRVTVYPQTELE-PILVEH--AEARGAQ-VRFGTEVLSLEQDGDGVTAVVRDRRdgeeyTVRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 227 DLLVGADGIWSKVRKVLfGQSEATYSEYTCYTGIADFVPPDIDTVGYRVFLGHKQYFVSSDVGA------GKMQWYAFHK 300
Cdd:pfam01494 151 KYLVGCDGGRSPVRKTL-GIEFEGFEGVPFGSLDVLFDAPDLSDPVERAFVHYLIYAPHSRGFMvgpwrsAGRERYYVQV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 301 EPagGTDPENGKNK--------RLLEIFnGWCDNVVDLinatDEEAILR-RDIYDRPptfnWGKGRVTLLGDSVHAMQPN 371
Cdd:pfam01494 230 PW--DEEVEERPEEftdeelkqRLRSIV-GIDLALVEI----LWKSIWGvASRVATR----YRKGRVFLAGDAAHIHPPT 298
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1002264030 372 LGQGGCMAIEDGYQLAVELEKSWQESAKSgtpmdivSSLRRYEKERILRV 421
Cdd:pfam01494 299 GGQGLNTAIQDAFNLAWKLAAVLRGQAGE-------SLLDTYSAERLPVA 341
|
|
| PRK07588 |
PRK07588 |
FAD-binding domain; |
73-393 |
8.46e-12 |
|
FAD-binding domain;
Pssm-ID: 169028 [Multi-domain] Cd Length: 391 Bit Score: 67.45 E-value: 8.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 73 VLVAGGGIGGLVFALAAKRKGFEVVVLERdMSAVRgEGKYrgpiqlqsnalavleAVDA-GAADQVMDagcitgnRVnGI 151
Cdd:PRK07588 3 VAISGAGIAGPTLAYWLRRYGHEPTLIER-APELR-TGGY---------------MVDFwGVGYEVAK-------RM-GI 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 152 VDGVSGSWY-IK-FDTFTPAAERGLPV-TRVISRMTLQQILARAVGD-------------DAILNDShvVDFIDDG-NKV 214
Cdd:PRK07588 58 TDQLREAGYqIEhVRSVDPTGRRKADLnVDSFRRMVGDDFTSLPRGDlaaaiytaidgqvETIFDDS--IATIDEHrDGV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 215 TAILEDGRKFEGDLLVGADGIWSKVRKVLFGQSEatYSEYtcYTGI--ADFV-----PPDIDTVGYRVFLGHKQYFVSSD 287
Cdd:PRK07588 136 RVTFERGTPRDFDLVIGADGLHSHVRRLVFGPER--DFEH--YLGCkvAACVvdgyrPRDERTYVLYNEVGRQVARVALR 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 288 vGAGKMQWYAFHKEPAGGTDPENGKNKRLLEIFN--GW-CDNVVDLINATDEeaiLRRDIYDRPPTFNWGKGRVTLLGDS 364
Cdd:PRK07588 212 -GDRTLFLFIFRAEHDNPPLTPAEEKQLLRDQFGdvGWeTPDILAALDDVED---LYFDVVSQIRMDRWSRGRVALVGDA 287
|
330 340 350
....*....|....*....|....*....|.
gi 1002264030 365 vhAMQPNL--GQGGCMAIEDGYQLAVELEKS 393
Cdd:PRK07588 288 --AACPSLlgGEGSGLAITEAYVLAGELARA 316
|
|
| FixC |
COG0644 |
Dehydrogenase (flavoprotein) [Energy production and conversion]; |
78-243 |
6.28e-11 |
|
Dehydrogenase (flavoprotein) [Energy production and conversion];
Pssm-ID: 440409 [Multi-domain] Cd Length: 281 Bit Score: 63.45 E-value: 6.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 78 GGIGGLVFALAAKRKGFEVVVLERDmSAVR----GEGkyrgpiqLQSNALAVLEavDAGAADQVMDAgcITGNRVNgIVD 153
Cdd:COG0644 1 AGPAGSAAARRLARAGLSVLLLEKG-SFPGdkicGGG-------LLPRALEELE--PLGLDEPLERP--VRGARFY-SPG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 154 GVSGSWyikfdtftpaaERGLPVTRVISRMTLQQILA-RAVGDDA-ILNDSHVVDFIDDGNKVTAILEDGRKFEGDLLVG 231
Cdd:COG0644 68 GKSVEL-----------PPGRGGGYVVDRARFDRWLAeQAEEAGAeVRTGTRVTDVLRDDGRVVVRTGDGEEIRADYVVD 136
|
170
....*....|..
gi 1002264030 232 ADGIWSKVRKVL 243
Cdd:COG0644 137 ADGARSLLARKL 148
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
524-631 |
2.18e-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: 57.67 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 524 YLLPTSSGDSQPIRLIRdeKKSLSIGSRSDpsnstASLALPLPQISENHATITCKNKAFYVTDNGSEHGTWItdnEGRRY 603
Cdd:cd00060 1 RLIVLDGDGGGREFPLT--KGVVTIGRSPD-----CDIVLDDPSVSRRHARIEVDGGGVYLEDLGSTNGTFV---NGKRI 70
|
90 100
....*....|....*....|....*...
gi 1002264030 604 RVppnfPVRFHPSDAIEFGsdkKAVFRV 631
Cdd:cd00060 71 TP----PVPLQDGDVIRLG---DTTFRF 91
|
|
| PRK05868 |
PRK05868 |
FAD-binding protein; |
73-391 |
6.27e-10 |
|
FAD-binding protein;
Pssm-ID: 180297 [Multi-domain] Cd Length: 372 Bit Score: 61.54 E-value: 6.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 73 VLVAGGGIGGLVFALAAKRKGFEVVVLERDmSAVRGEGK---YRGPiqlqsnALAVLEAVDAGAADQVMDagciTGNRVN 149
Cdd:PRK05868 4 VVVSGASVAGTAAAYWLGRHGYSVTMVERH-PGLRPGGQaidVRGP------ALDVLERMGLLAAAQEHK----TRIRGA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 150 GIVDGvSGSwyiKFDTFTPAAERGLPVTRV---ISRMTLQQILARAVGDDA-ILNDSHVVDFIDDGNKVTAILEDGRKFE 225
Cdd:PRK05868 73 SFVDR-DGN---ELFRDTESTPTGGPVNSPdieLLRDDLVELLYGATQPSVeYLFDDSISTLQDDGDSVRVTFERAAARE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 226 GDLLVGADGIWSKVRKVLFGQSEATYSEYTCYTGIadFVPPDidtvgyrvFLGHKQYfvssdvgagkMQWYAFHKEPAGG 305
Cdd:PRK05868 149 FDLVIGADGLHSNVRRLVFGPEEQFVKRLGTHAAI--FTVPN--------FLELDYW----------QTWHYGDSTMAGV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 306 TDPENGKNKRLLEifnGWCDNVVDlINATDEEA----ILRRDIYD---RP---------PTF-----------NWGKGRV 358
Cdd:PRK05868 209 YSARNNTEARAAL---AFMDTELR-IDYRDTEAqfaeLQRRMAEDgwvRAqllhymrsaPDFyfdemsqilmdRWSRGRV 284
|
330 340 350
....*....|....*....|....*....|...
gi 1002264030 359 TLLGDSVHAMQPNLGQGGCMAIEDGYQLAVELE 391
Cdd:PRK05868 285 ALVGDAGYCCSPLSGQGTSVALLGAYILAGELK 317
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
547-621 |
1.50e-07 |
|
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
Pssm-ID: 459831 [Multi-domain] Cd Length: 66 Bit Score: 48.73 E-value: 1.50e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002264030 547 SIGSRSDpsnstASLALPLPQISENHATITCK-NKAFYVTDNGSEHGTWITDNegrryRVPPNfPVRFHPSDAIEF 621
Cdd:pfam00498 2 TIGRSPD-----CDIVLDDPSVSRRHAEIRYDgGGRFYLEDLGSTNGTFVNGQ-----RLGPE-PVRLKDGDVIRL 66
|
|
| PRK07045 |
PRK07045 |
putative monooxygenase; Reviewed |
73-417 |
2.97e-07 |
|
putative monooxygenase; Reviewed
Pssm-ID: 136171 [Multi-domain] Cd Length: 388 Bit Score: 52.99 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 73 VLVAGGGIGGLVFALAAKRKGFEVVVLERdmsaVRGEGKYRGPIQLQSNALAVLEAvdAGAADQVMDAGCITGNRVNGIV 152
Cdd:PRK07045 8 VLINGSGIAGVALAHLLGARGHSVTVVER----AARNRAQNGADLLKPSGIGVVRA--MGLLDDVFAAGGLRRDAMRLYH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 153 DGVsgswYIKFDTFTPAAERG---LPVTRVISRMTLQQILARAVGDDAILNDSHVVDFIDDGNKVTAILEDGRKFEGDLL 229
Cdd:PRK07045 82 DKE----LIASLDYRSASALGyfiLIPCEQLRRLLLAKLDGLPNVRLRFETSIERIERDADGTVTSVTLSDGERVAPTVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 230 VGADGIWSKVRKVLFgQSEATYSEYTCYTGIADFVPPDIDTVGYRVFLGHKQ---YFVSSDVGAGKMQwYAFHKEPAGG- 305
Cdd:PRK07045 158 VGADGARSMIRDDVL-RMPAERVPYATPMAFGTIALTDSVRECNRLYVDSNQglaYFYPIGDQATRLV-VSFPADEMQGy 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 306 -TDPENGKNKRLLEIFNGwcDNVVDLINATDEEAILRRDIYDRPPTFNWGKGRVTLLGDSVHAMQPNLGQGGCMAIEDGY 384
Cdd:PRK07045 236 lADTTRTKLLARLNEFVG--DESADAMAAIGAGTAFPLIPLGRMNLDRYHKRNVVLLGDAAHSIHPITGQGMNLAIEDAG 313
|
330 340 350
....*....|....*....|....*....|...
gi 1002264030 385 QLAVELEKSWQESaksgtpMDIVSSLRRYEKER 417
Cdd:PRK07045 314 ELGACLDLHLSGQ------IALADALERFERIR 340
|
|
| FHA_ArnA-like |
cd22680 |
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ... |
545-631 |
5.85e-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: 5.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 545 SLSIGSrsDPSNStasLALPLPQISENHATITCKNKAFYVTDNGSEHGTWITDNEgrryRVPPnfPVRFHPSDAIEFGsd 624
Cdd:cd22680 22 SVSIGR--DPENV---IVIPDPFVSRNHARITVDSNEIYIEDLGSTNGTFVNDFK----RIKG--PAKLHPNDIIKLG-- 88
|
....*..
gi 1002264030 625 KKAVFRV 631
Cdd:cd22680 89 RTTVLKV 95
|
|
| PRK06126 |
PRK06126 |
hypothetical protein; Provisional |
73-417 |
8.70e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 235704 [Multi-domain] Cd Length: 545 Bit Score: 51.92 E-value: 8.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 73 VLVAGGGIGGLVFALAAKRKGFEVVVLERdmsavrGEGKYRGPiqlQSNAlavleaVDA---------GAADQVMDAG-- 141
Cdd:PRK06126 10 VLIVGGGPVGLALALDLGRRGVDSILVER------KDGTAFNP---KANT------TSArsmehfrrlGIADEVRSAGlp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 142 ------CITGNRVNGI----------------VDGVSGSWyikfdtftPAAERGlpvTRvISRMTLQQIL---ARAVGDD 196
Cdd:PRK06126 75 vdyptdIAYFTRLTGYelarfrlpsareaitpVGGPDGSW--------PSPELP---HR-IPQKYLEPILlehAAAQPGV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 197 AILNDSHVVDFIDDGNKVTAILED-----GRKFEGDLLVGADGIWSKVRKVL----FGQSEATYSEYTCY--TGIADFVP 265
Cdd:PRK06126 143 TLRYGHRLTDFEQDADGVTATVEDldggeSLTIRADYLVGCDGARSAVRRSLgisyEGTSGLQRDLSIYIraPGLAALVG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 266 PDidtVGYRVFL------GHkqyFVSSDvgaGKMQWyAFHKEPAGGTDPENGKNKrlleifngWCDNVVDLINATDEEAI 339
Cdd:PRK06126 223 HD---PAWMYWLfnpdrrGV---LVAID---GRDEW-LFHQLRGGEDEFTIDDVD--------ARAFVRRGVGEDIDYEV 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 340 LRRDIYDR----PPTFnwGKGRVTLLGDSVHAMQPNLGQGGCMAIEDgyqlAVELekSWQESA--KSGTPMDIVSSlrrY 413
Cdd:PRK06126 285 LSVVPWTGrrlvADSY--RRGRVFLAGDAAHLFTPTGGYGMNTGIGD----AVNL--AWKLAAvlNGWAGPALLDS---Y 353
|
....
gi 1002264030 414 EKER 417
Cdd:PRK06126 354 EAER 357
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
532-633 |
8.84e-07 |
|
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
Pssm-ID: 441322 [Multi-domain] Cd Length: 96 Bit Score: 47.65 E-value: 8.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 532 DSQPIRLIRDEKKSLSIGSRSDpsnstASLALPLPQISENHATITCKNKAFYVTDNGSEHGTWItdnEGRRYRVppnfPV 611
Cdd:COG1716 9 GPLAGRRFPLDGGPLTIGRAPD-----NDIVLDDPTVSRRHARIRRDGGGWVLEDLGSTNGTFV---NGQRVTE----PA 76
|
90 100
....*....|....*....|..
gi 1002264030 612 RFHPSDAIEFGsdkKAVFRVKV 633
Cdd:COG1716 77 PLRDGDVIRLG---KTELRFRL 95
|
|
| FHA |
smart00240 |
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ... |
555-598 |
1.44e-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: 1.44e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1002264030 555 SNSTASLALPLPQISENHATITCK-NKAFYVTDNGSEHGTWITDN 598
Cdd:smart00240 6 SSEDCDIQLDGPSISRRHAVIVYDgGGRFYLIDLGSTNGTFVNGK 50
|
|
| COQ6 |
TIGR01989 |
ubiquinone biosynthesis monooxygenase COQ6; This model represents the monooxygenase ... |
209-417 |
3.48e-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: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 209 DDGNKVTAILEDGRKFEGDLLVGADGIWSKVRKvlFGQSEATYSEYTCYTGIA--DFVPPDIDTVGYRVFL--GHKQYFV 284
Cdd:TIGR01989 155 DNSNWVHITLSDGQVLYTKLLIGADGSNSNVRK--AANIDTTGWNYNQHAVVAtlKLEEATENDVAWQRFLptGPIALLP 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 285 SSDVGAGkMQWYAFHKEPAggtdpengKNKRLLEifngwcDNVVDLINA--------------TDEE-AILRRDIYDR-- 347
Cdd:TIGR01989 233 LPDNNST-LVWSTSPEEAL--------RLLSLPP------EDFVDALNAafdlgysdhpysylLDYAmEKLNEDIGFRte 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 348 --------PP-----------TFNWG--------KGRVTLLGDSVHAMQPNLGQGGCMAIEDGYQLAVELEKSWQESAKS 400
Cdd:TIGR01989 298 gskscfqvPPrvigvvdksraAFPLGlghadeyvTKRVALVGDAAHRVHPLAGQGVNLGFGDVASLVKALAEAVSVGADI 377
|
250
....*....|....*..
gi 1002264030 401 GTpmdiVSSLRRYEKER 417
Cdd:TIGR01989 378 GS----ISSLKPYERER 390
|
|
| FHA_PPP1R8 |
cd22674 |
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 ... |
537-630 |
4.09e-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: 4.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 537 RLIRDEKKSLSIGSRSDpsnsTASLALPLPQISENHATITC--KNKAFYVTDNGSEHGTWITDNegrryRVPPNFPVRFH 614
Cdd:cd22674 20 KLMIDEKKYYLFGRNSD----VCDFVLDHPSCSRVHAALVYhkHLNRVFLIDLGSTHGTFVGGI-----RLEPHKPQQLP 90
|
90
....*....|....*..
gi 1002264030 615 PSDAIEFG-SDKKAVFR 630
Cdd:cd22674 91 IDSTLRFGaSTRRYILR 107
|
|
| PRK06185 |
PRK06185 |
FAD-dependent oxidoreductase; |
73-472 |
8.09e-06 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 235729 [Multi-domain] Cd Length: 407 Bit Score: 48.70 E-value: 8.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 73 VLVAGGGIGGLVFALAAKRKGFEVVVLE------RDMsavRGEGKYRGPIQLQsNALAVLEAVDAGAADQVMDAGCITGN 146
Cdd:PRK06185 9 CCIVGGGPAGMMLGLLLARAGVDVTVLEkhadflRDF---RGDTVHPSTLELM-DELGLLERFLELPHQKVRTLRFEIGG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 147 RVNGIVDgvsgswyikFDTF-TPAaerglpvtRVISRMT----LQQILARAVGDDA--ILNDSHVVDFIDDGNKVTAIL- 218
Cdd:PRK06185 85 RTVTLAD---------FSRLpTPY--------PYIAMMPqwdfLDFLAEEASAYPNftLRMGAEVTGLIEEGGRVTGVRa 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 219 --EDGR-KFEGDLLVGADGIWSKVRK------VLFGQSeatyseytcytgiADFV------PPDiDTVGYRVFLGHKQYF 283
Cdd:PRK06185 148 rtPDGPgEIRADLVVGADGRHSRVRAlaglevREFGAP-------------MDVLwfrlprEPD-DPESLMGRFGPGQGL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 284 VSSDVG----AG----KMQWYAFHkepAGGTDPengKNKRLLEIFnGWCDNVVDLINATDEEAILRRDIyDRPPTfnWGK 355
Cdd:PRK06185 214 IMIDRGdywqCGyvipKGGYAALR---AAGLEA---FRERVAELA-PELADRVAELKSWDDVKLLDVRV-DRLRR--WHR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 356 GRVTLLGDSVHAMQPNLGQGGCMAIEDgyqlAVELEKSWQESAKSGTPMDivSSLRRYEKERILRVSVIHGLARMAAIMA 435
Cdd:PRK06185 284 PGLLCIGDAAHAMSPVGGVGINLAIQD----AVAAANILAEPLRRGRVSD--RDLAAVQRRREFPTRVTQALQRRIQRRL 357
|
410 420 430
....*....|....*....|....*....|....*...
gi 1002264030 436 TTYRPYLGVGLGPLSFLTKL-RIPHPGRVGGRfFIKYG 472
Cdd:PRK06185 358 LAPALAGRGPLGPPLLLRLLnRLPWLRRLPAR-LVGLG 394
|
|
| FHA_PS1-like |
cd22691 |
forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) ... |
566-632 |
1.07e-05 |
|
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: 44.72 E-value: 1.07e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002264030 566 PQISENHATI--TCKNKAFYVTDNGSEHGTWITDNegrryRVPPNFPVRFHPSDAIEFGSDKKaVFRVK 632
Cdd:cd22691 46 PSISRFHLEIriIPSRRKITLTDLSSVHGTWVNGQ-----RIEPGVPVELEEGDTVRLGASTR-VYRLH 108
|
|
| FHA_Cep170 |
cd22704 |
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ... |
522-635 |
1.08e-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: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 522 EWYLLptsSGDSQPIRLIRD------EKKSLSIGSRSdpsnstaslalplpqISENHATIT--CKNKAFYVTDNGSEHGT 593
Cdd:cd22704 1 SWCLV---SSDGTRHRLPRSmlfvgrEDCDLILQSRS---------------VDKQHAVITydQIDNEFKIKDLGSLNGT 62
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1002264030 594 WITDNegrryRVPPNFPVRFHPSDAIEFGSDKKaVFRVKVLS 635
Cdd:cd22704 63 FVNDS-----RIPEQTYITLKLGDSIRFGYDTN-VYRFEQLS 98
|
|
| FHA_RNF8 |
cd22663 |
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ... |
532-627 |
1.93e-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: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 532 DSQPIRLIRDEKKSLSIGsRSdPSNSTASLALPLPQISENHATITCKNK-AFYVTDNGSEHGTWITDNegrryRVPPNFP 610
Cdd:cd22663 9 GIDPLVLLLEDGKEVTVG-RG-LGVTYQLVSTCPLMISRNHCVLKKNDEgQWTIKDNKSLNGVWVNGE-----RIEPLKP 81
|
90
....*....|....*..
gi 1002264030 611 VRFHPSDAIEFGSDKKA 627
Cdd:cd22663 82 YPLNEGDLIQLGVPPEN 98
|
|
| PRK07333 |
PRK07333 |
ubiquinone biosynthesis hydroxylase; |
73-241 |
9.25e-05 |
|
ubiquinone biosynthesis hydroxylase;
Pssm-ID: 180935 [Multi-domain] Cd Length: 403 Bit Score: 45.36 E-value: 9.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 73 VLVAGGGIGGLVFALAAKRKGFE--VVVLE--------RDM--SAVRGegkyrGPIQLqSNALAVLEAVDAGAadQVMDA 140
Cdd:PRK07333 4 VVIAGGGYVGLALAVALKQAAPHlpVTVVDaapagawsRDPraSAIAA-----AARRM-LEALGVWDEIAPEA--QPITD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 141 GCITGNRVNGIVDGVsgswyikFDTFTPAAERGLPVTRVISRMTLQQILARAVGDDAI--LNDSHVVDFIDDGNKVTAIL 218
Cdd:PRK07333 76 MVITDSRTSDPVRPV-------FLTFEGEVEPGEPFAHMVENRVLINALRKRAEALGIdlREATSVTDFETRDEGVTVTL 148
|
170 180
....*....|....*....|...
gi 1002264030 219 EDGRKFEGDLLVGADGIWSKVRK 241
Cdd:PRK07333 149 SDGSVLEARLLVAADGARSKLRE 171
|
|
| FHA_Kanadaptin |
cd22677 |
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ... |
566-622 |
1.22e-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: 1.22e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002264030 566 PQISENHATI------TCKNKAFYVTDNGSEHGTWITDNegrryRVPPNFPVRFHPSDAIEFG 622
Cdd:cd22677 39 PSISRYHAVLqyrgdaDDHDGGFYLYDLGSTHGTFLNKQ-----RIPPKQYYRLRVGHVLKFG 96
|
|
| PRK06834 |
PRK06834 |
hypothetical protein; Provisional |
73-241 |
1.40e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235870 [Multi-domain] Cd Length: 488 Bit Score: 45.01 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 73 VLVAGGGIGGLVFALAAKRKGFEVVVLER----DMSAVRGEGkyrgpiqLQSNALAVLEavDAGAADQVMDAGCITGnrv 148
Cdd:PRK06834 6 VVIAGGGPTGLMLAGELALAGVDVAIVERrpnqELVGSRAGG-------LHARTLEVLD--QRGIADRFLAQGQVAQ--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 149 ngivdgVSGSWYIKFDTftpaaeRGLPvTRVISRMTLQQ-----ILARAVGDDA--ILNDSHVVDFIDDGNKVTAILEDG 221
Cdd:PRK06834 74 ------VTGFAATRLDI------SDFP-TRHNYGLALWQnhierILAEWVGELGvpIYRGREVTGFAQDDTGVDVELSDG 140
|
170 180
....*....|....*....|
gi 1002264030 222 RKFEGDLLVGADGIWSKVRK 241
Cdd:PRK06834 141 RTLRAQYLVGCDGGRSLVRK 160
|
|
| PRK08255 |
PRK08255 |
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase; |
73-429 |
1.68e-04 |
|
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase;
Pssm-ID: 236203 [Multi-domain] Cd Length: 765 Bit Score: 44.93 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 73 VLVAGGGIGGLVFALAAKRK--GFEVVVLERDmsavRGEGKYRGPIQLQSNALAVLEAVDAGAADQVMDAGcitgNRVNG 150
Cdd:PRK08255 3 IVCIGGGPAGLYFALLMKLLdpAHEVTVVERN----RPYDTFGWGVVFSDATLGNLRAADPVSAAAIGDAF----NHWDD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 151 IVdgvsgswyIKFdtftpaaeRGLPVTR------VISRMTLQQIL---ARAVGDDailndshvVDFIDDGNKVTAILEDG 221
Cdd:PRK08255 75 ID--------VHF--------KGRRIRSgghgfaGIGRKRLLNILqarCEELGVK--------LVFETEVPDDQALAADA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 222 rkfegDLLVGADGIWSKVRkvlfgqseatySEYtcytgiADFVPPDIDTVGYR-VFLG-HKQY----FVSSDVGAGKMQW 295
Cdd:PRK08255 131 -----DLVIASDGLNSRIR-----------TRY------ADTFQPDIDTRRCRfVWLGtHKVFdaftFAFEETEHGWFQA 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 296 YAFHKEPAGGT------------------DPENGKnKRLLEIFNGWCDNVVDLINATDeeaiLRRDIYDRPPTF---NW- 353
Cdd:PRK08255 189 HAYRFDDDTSTfivetpeevwraagldemSQEESI-AFCEKLFADYLDGHPLMSNASH----LRGSAWINFPRVvceRWv 263
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002264030 354 ---GKGRVTLLGDSVHAMQPNLGQGGCMAIEDGYQLAVELEKSwqesaksgtPMDIVSSLRRYEKERILRVSVIHGLAR 429
Cdd:PRK08255 264 hwnRRVPVVLMGDAAHTAHFSIGSGTKLALEDAIELARCLHEH---------PGDLPAALAAYEEERRVEVLRIQNAAR 333
|
|
| FHA_MDC1 |
cd22665 |
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ... |
548-625 |
1.96e-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: 1.96e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002264030 548 IGSrsDPSNStasLALPLPQISENHATITCKNKAFYVTDNGSEHGTWItdneGRRYRVPPNFPVRFHPSDAIEFGSDK 625
Cdd:cd22665 25 IGR--DPSCS---VVLPDKSVSKQHACIEVDGGTHLIEDLGSTNGTRI----GNKVRLKPNVRYELIDGDLLLFGDVK 93
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
75-101 |
2.25e-04 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 39.82 E-value: 2.25e-04
|
| FHA_FhaB-like |
cd22693 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
542-631 |
2.62e-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: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 542 EKKSLSIGSRSDpsnstASLALPLPQISENHATITCKNKAFYVTDNGSEHGTWITDNegrryRVppNFPVRFHPSDAIEF 621
Cdd:cd22693 16 DKSGITIGRADD-----NDLVLSDDFVSSRHARIYLQGSSWYLEDLGSTNGTFVNGN-----RV--TQPVVVQPGDTIRI 83
|
90
....*....|
gi 1002264030 622 GsdkKAVFRV 631
Cdd:cd22693 84 G---ATVFEV 90
|
|
| mhpA |
PRK06183 |
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase; |
334-387 |
4.90e-04 |
|
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
Pssm-ID: 235727 [Multi-domain] Cd Length: 500 Bit Score: 42.97 E-value: 4.90e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002264030 334 TDEEA-ILRRDIYdrppTFN------WGKGRVTLLGDSVHAMQPNLGQGGCMAIEDGYQLA 387
Cdd:PRK06183 261 TPDDAeLIRHAVY----TFHarvadrWRSGRVLLAGDAAHLMPPFAGQGMNSGIRDAANLA 317
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
73-108 |
5.15e-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: 5.15e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1002264030 73 VLVAGGGIGGLVFALAAKRKGFEVVVLERdMSAVRG 108
Cdd:COG1053 6 VVVVGSGGAGLRAALEAAEAGLKVLVLEK-VPPRGG 40
|
|
| PRK08849 |
PRK08849 |
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional |
205-417 |
6.34e-04 |
|
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional
Pssm-ID: 181564 [Multi-domain] Cd Length: 384 Bit Score: 42.45 E-value: 6.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 205 VDFIDDGNKVTaiLEDGRKFEGDLLVGADGIWSKVR-KVLFGQSEATYSEYTCYTGIADFVPPDIDT------VGYRVFL 277
Cdd:PRK08849 137 LEFSAEGNRVT--LESGAEIEAKWVIGADGANSQVRqLAGIGITAWDYRQHCMLINVETEQPQQDITwqqftpSGPRSFL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 278 ---GHKqyfvssdvgaGKMQWYafhKEPaggtdpengknKRLLEifngwcdnvvdLINATDEEaiLRRDIYDRPP----- 349
Cdd:PRK08849 215 plcGNQ----------GSLVWY---DSP-----------KRIKQ-----------LSAMNPEQ--LRSEILRHFPaelge 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264030 350 --TFNWG-------------KGRVTLLGDSVHAMQPNLGQGGCMAIEDGYQLAVELEKSWQESaksgtpmdiVSSLRRYE 414
Cdd:PRK08849 258 ikVLQHGsfpltrrhaqqyvKNNCVLLGDAAHTINPLAGQGVNLGFKDVDVLLAETEKQGVLN---------DASFARYE 328
|
...
gi 1002264030 415 KER 417
Cdd:PRK08849 329 RRR 331
|
|
| PRK08850 |
PRK08850 |
2-octaprenyl-6-methoxyphenol hydroxylase; Validated |
357-434 |
6.39e-04 |
|
2-octaprenyl-6-methoxyphenol hydroxylase; Validated
Pssm-ID: 236341 [Multi-domain] Cd Length: 405 Bit Score: 42.45 E-value: 6.39e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002264030 357 RVTLLGDSVHAMQPNLGQGGCMAIEDGYQLAVELEKSWQESAKSGTpmdiVSSLRRYEKERILRVsvihglARMAAIM 434
Cdd:PRK08850 283 RVALVGDAAHTIHPLAGQGVNLGLLDAASLAQEILALWQQGRDIGL----KRNLRGYERWRKAEA------AKMIAAM 350
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
73-102 |
6.48e-04 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 42.58 E-value: 6.48e-04
10 20 30
....*....|....*....|....*....|
gi 1002264030 73 VLVAGGGIGGLVFALAAKRKGFEVVVLERD 102
Cdd:COG0665 5 VVVIGGGIAGLSTAYHLARRGLDVTVLERG 34
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
73-101 |
7.86e-04 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 42.53 E-value: 7.86e-04
10 20
....*....|....*....|....*....
gi 1002264030 73 VLVAGGGIGGLVFALAAKRKGFEVVVLER 101
Cdd:COG1233 6 VVVIGAGIGGLAAAALLARAGYRVTVLEK 34
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
73-102 |
8.97e-04 |
|
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: 42.13 E-value: 8.97e-04
10 20 30
....*....|....*....|....*....|
gi 1002264030 73 VLVAGGGIGGLVFALAAKRKGFEVVVLERD 102
Cdd:COG1232 4 VAVIGGGIAGLTAAYRLAKAGHEVTVLEAS 33
|
|
| PRK07364 |
PRK07364 |
FAD-dependent hydroxylase; |
357-417 |
5.58e-03 |
|
FAD-dependent hydroxylase;
Pssm-ID: 236001 [Multi-domain] Cd Length: 415 Bit Score: 39.62 E-value: 5.58e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002264030 357 RVTLLGDSVHAMQPNLGQGGCMAIEDGYQLAVELEKSWQESAKSGTpmdiVSSLRRYEKER 417
Cdd:PRK07364 295 RLALVGDAAHCCHPVGGQGLNLGIRDAAALAQVLQTAHQRGEDIGS----LAVLKRYERWR 351
|
|
| FHA_Rv1747-like_rpt1 |
cd22694 |
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
537-605 |
5.62e-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: 36.54 E-value: 5.62e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002264030 537 RLIRDEKKSLSIGSrsDPSNStasLALPLPQISENHATITCKNKAFYVTDNGSEHGTWItdnEGRRYRV 605
Cdd:cd22694 9 ELRFDPGSSVRIGR--DPDAD---VRLDDPRVSRRHALLEFDGDGWVYTDLGSRNGTYL---NGRRVQQ 69
|
|
| PRK08274 |
PRK08274 |
FAD-dependent tricarballylate dehydrogenase TcuA; |
73-108 |
6.52e-03 |
|
FAD-dependent tricarballylate dehydrogenase TcuA;
Pssm-ID: 236214 [Multi-domain] Cd Length: 466 Bit Score: 39.47 E-value: 6.52e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1002264030 73 VLVAGGGIGGLVFALAAKRKGFEVVVLERDMSAVRG 108
Cdd:PRK08274 7 VLVIGGGNAALCAALAAREAGASVLLLEAAPREWRG 42
|
|
| FHA_EspA-like |
cd22698 |
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ... |
527-595 |
6.57e-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: 6.57e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002264030 527 PTSSGDSQPIRLIRDEkksLSIGSRSDpsnstASLALPLPQISENHATITCKNKAFYVTDNGSEHGTWI 595
Cdd:cd22698 7 QKGSEEGKDYELDQDE---FTIGRSSN-----NDIRLNDHSVSRHHARIVRQGDKCNLTDLGSTNGTFL 67
|
|
| |
