|
Name |
Accession |
Description |
Interval |
E-value |
| MrcB |
COG0744 |
Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall ... |
34-654 |
0e+00 |
|
Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440507 [Multi-domain] Cd Length: 630 Bit Score: 698.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 34 FRKFLVSCLLLGIVGLVAGVATFFVM-IKDAPKL-EKAKLVNPLSSKIYDKDGKLIYEYGKEKRTNIMYDQIPKLVENAF 111
Cdd:COG0744 11 LRRLLGLLLLLLAVLVLAALAGLVALyVADLPDPeELEDLALPQTSTIYDRDGTLIATLGDENREWVPLDQIPPHLKDAV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 112 LATEDARFYEHSGVDYKGTARAALVSLKGDYGSQGGSTITQQVIKNYFLSMEKTSKRKAQEIYLAYKLEQQYSKHEILEM 191
Cdd:COG0744 91 VAIEDRRFYEHGGVDPKGIARALVANLTAGGVVQGGSTITQQLVKNLFLSNERTLSRKLKEALLALKLERKYSKDEILEL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 192 YLNKVYLGNRSYGIATAVQNYYGKELKDLTLPEVAMLAGLMKAPNNYDPTKeqNIKKATERRNVVLKLMNRHGYITKKEM 271
Cdd:COG0744 171 YLNTVYFGRGAYGIEAAAQYYFGKSASDLTLAEAALLAGLVKAPSYYDPYR--NPEAAKERRNLVLDRMVEQGYITQAEA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 272 EEASKVPVTEgLKKATEQKEMPYPAFMDAVVKEVEKELPDVNIGSDGLEIYTTLDPKAQDFADKLLNKDIINYPNEKFQG 351
Cdd:COG0744 249 DAAKAEPLTL-VPPPNGAAAGKYPYFVDYVRRELEELLGEDDLYRGGLKIYTTLDPKLQKAAEKAVKNVLPEGKPGGLQA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 352 AFTFMDTKTGEVRAIGSGRGENKAVFkghNIAIELNRSAGSTMKPiFDYAPAIEYlKWATYHQIDDSPFKYSTGQ-EVRN 430
Cdd:COG0744 328 ALVVVDPKTGEVLAMVGGRDYGKSQF---NRATQAKRQPGSTFKP-FVYAAALEQ-GYTPATTVDDEPVTFPGGGwSPKN 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 431 ADRKHLGPITMRDALKTSRNIPAIKTAKEVGINRSKGFSEKLGITFNVAPTESTAIGTNEASPTEIAGAYAAFGNDGKYT 510
Cdd:COG0744 403 YDGRYRGPVTLREALANSLNTPAVRLAQEVGLDKVVDTARRLGITSPLDPNPSLALGTSEVSPLEMASAYATFANGGVYV 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 511 RPHFVKKVIYSDGKS-KSFEQKSKRVMKDSTAYMITDMLRTFVSSGLGTTANIGSLDIAGKTGTTNysleqiaqynlpes 589
Cdd:COG0744 483 EPHAITKVTDADGKVlYEAKPKCEQVISPEVAYLMTDMLQDVVTSGTGRAARLPGRPVAGKTGTTN-------------- 548
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1264348865 590 ATRDSWFAGYTPQYTMAVWTGYTKDSKDNYISSknTKIAQLIFKEMMSKF--ATDKSQFKMPNSVVQ 654
Cdd:COG0744 549 DNRDAWFVGYTPQLVTAVWVGNDDNSPMGYVTG--GSLPAPIWRDFMEAAleGLPVEDFPKPSGVVR 613
|
|
| PBP_1a_fam |
TIGR02074 |
penicillin-binding protein, 1A family; Bacterial that synthesize a cell wall of peptidoglycan ... |
94-637 |
0e+00 |
|
penicillin-binding protein, 1A family; Bacterial that synthesize a cell wall of peptidoglycan (murein) generally have several transglycosylases and transpeptidases for the task. This family consists of bifunctional transglycosylase/transpeptidase penicillin-binding proteins (PBP). In the Proteobacteria, this family includes PBP 1A but not the paralogous PBP 1B (TIGR02071). This family also includes related proteins, often designated PBP 1A, from other bacterial lineages. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273955 [Multi-domain] Cd Length: 531 Bit Score: 609.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 94 KRTNIMYDQIPKLVENAFLATEDARFYEHSGVDYKGTARAALVSLKGDYGSQGGSTITQQVIKNYFLSMEKTSKRKAQEI 173
Cdd:TIGR02074 1 RREYVPIDDIPENLINAFLAIEDRRFYDHFGIDLKGIGRAAVANITSGRVLEGGSTITQQLAKNLYLTNERTITRKIQEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 174 YLAYKLEQQYSKHEILEMYLNKVYLGNRSYGIATAVQNYYGKELKDLTLPEVAMLAGLMKAPNNYDPTKeqNIKKATERR 253
Cdd:TIGR02074 81 LLALKLEQKLSKDEILELYLNRIYFGNGAYGIEAAAQFYFGKSVNDLTLAEAAMLAGLPKAPSAYNPFK--NPERAKDRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 254 NVVLKLMNRHGYITKKEMEEASKVPVTEGLKKATEQKEmPYPAFMDAVVKEVEKELPDvNIGSDGLEIYTTLDPKAQDFA 333
Cdd:TIGR02074 159 NLVLSNMVENGYITAEEAEEAINEPIQLYLQTKKSEQY-KAPYFVDYVIQELEEEYGE-ELYTGGLKIYTTLDLDAQKAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 334 DKLLNKDIINY---PNEKFQGAFTFMDTKTGEVRAIGSGRGENKAVFkghNIAIELNRSAGSTMKPiFDYAPAIEYlKWA 410
Cdd:TIGR02074 237 EKVLNTGLRVAgrrDGDDLQAALVAIDPDTGAVRALVGGRDYGKSQF---NRATQAKRQPGSTFKP-FVYAAALEK-GLT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 411 TYHQIDDSPFKYS--TGQEVRNADRKHLGPITMRDALKTSRNIPAIKTAKEVGINRSKGFSEKLGITFNVAPTESTAIGT 488
Cdd:TIGR02074 312 PATIVNDEPITYNgnGPWSPKNYGGGYRGNVTLRQALAQSRNIPAVRLLQEVGLDKVVALAKRFGITSPLDPVLSLALGT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 489 NEASPTEIAGAYAAFGNDGKYTRPHFVKKVIYSDGKS-KSFEQKSKRVMKDSTAYMITDMLRTFVSSGLGTTANIGSLDI 567
Cdd:TIGR02074 392 VEVSPLEMASAYAVFANGGKYVEPHGIRKIVDRDGKViYENKPKTTQVISPATAYIMTDMLKGVVESGTGRSARLPGRPV 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 568 AGKTGTTNYSleqiaqynlpesatRDSWFAGYTPQYTMAVWTGYTkDSKDNYISSKNTKIAQLIFKEMMS 637
Cdd:TIGR02074 472 AGKTGTTQNW--------------RDAWFVGYTPYYVTAVWVGYD-DKKTLGKSGTGGGLAAPIWRDFMA 526
|
|
| MrcA |
COG5009 |
Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis]; |
32-654 |
0e+00 |
|
Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 444033 [Multi-domain] Cd Length: 785 Bit Score: 565.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 32 SFFRKFLVSCLLLGIVGLVAGVATFFVMIKDAPKLEKAKLVNP-LSSKIYDKDGKLIYEYGKEKRTNIMYDQIPKLVENA 110
Cdd:COG5009 2 RLLKILLILLLLLLLLGALAVAGLYLYLSPDLPDVETLKDYQPpTPSRVYSADGKLIAEFGEERRIPVPIEEIPPLLINA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 111 FLATEDARFYEHSGVDYKGTARAALVSLKGDYGSQGGSTITQQVIKNYFLSMEKTSKRKAQEIYLAYKLEQQYSKHEILE 190
Cdd:COG5009 82 FLAAEDKRFYEHPGVDPIGIARAAVVNLRTGRRVQGGSTITQQVAKNFLLSPERTLTRKIKEAILALRIEQELSKDEILE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 191 MYLNKVYLGNRSYGIATAVQNYYGKELKDLTLPEVAMLAGLMKAPNNYDPTKeqNIKKATERRNVVLKLMNRHGYITKKE 270
Cdd:COG5009 162 LYLNKIYLGHRAYGVAAAAQTYFGKSLDELTLAEAAMLAGLPKAPSRYNPIR--NPERALERRNYVLGRMLELGYITQAE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 271 MEEASKVPVTEGLKKATEQKEMPYpaFMDAVVKEVEKELPDVNIGSDGLEIYTTLDPKAQDFADKLLNKDIINY------ 344
Cdd:COG5009 240 YEAAKAEPLTARYHGASAEVDAPY--FAEMVRRELVERYGEDALYTGGLKVYTTLDPRLQEAAEKALRDGLLAYdrrhgy 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 345 ---------PNEKF------------------------------------------------------------------ 349
Cdd:COG5009 318 rgpeahldlAEEDWdealaevpdvgdlrpavvlevddksarvglrdgetgtlpleglkwarpyindnrrgpapksasdvl 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 350 ------------------------QGAFTFMDTKTGEVRAIGSGRGENKAVFkghNIAIELNRSAGSTMKPiFDYAPAIE 405
Cdd:COG5009 398 kpgdvirvrpvadggwrlrqipevQGALVALDPHTGAVLALVGGFDFEQSKF---NRATQAKRQPGSSFKP-FVYAAALD 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 406 Y-LKWATyhQIDDSPFKYSTGQEV-----RNADRKHLGPITMRDALKTSRNIPAIKTAKEVGINRSKGFSEKLGITFNVA 479
Cdd:COG5009 474 NgYTPAT--IINDAPIVFDDGGGGgvwrpKNYSGKFYGPTTLREALEKSRNLVTVRLLQDVGIDYVIDYAERFGIYSKLP 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 480 PTESTAIGTNEASPTEIAGAYAAFGNDGKYTRPHFVKKVIYSDGK----------------------SKSFEQKSKRVMK 537
Cdd:COG5009 552 PNLSLALGSGEVTPLEMARAYAVFANGGYRVEPYLIDRIEDRNGKviyradparacedcdaaewdgaEPRLPDPAEQVID 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 538 DSTAYMITDMLRTFVSSGLGTTANIGSLDIAGKTGTTNYSleqiaqynlpesatRDSWFAGYTPQYTMAVWTGYtkdskD 617
Cdd:COG5009 632 PRTAYQMTSMLRGVVQRGTGRRARALGRDIAGKTGTTNDS--------------KDAWFVGFTPDLVAGVWVGF-----D 692
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 1264348865 618 NYIS--SKNT--KIAQLIFKEMMSKFATDK--SQFKMPNSVVQ 654
Cdd:COG5009 693 DPRSlgRGETggRAALPIWIDFMKAALKDKpeKPFPVPEGIVT 735
|
|
| PBP_1b |
TIGR02071 |
penicillin-binding protein 1B; Bacterial that synthesize a cell wall of peptidoglycan (murein) ... |
83-656 |
1.32e-106 |
|
penicillin-binding protein 1B; Bacterial that synthesize a cell wall of peptidoglycan (murein) generally have several transglycosylases and transpeptidases for the task. This family consists of a particular bifunctional transglycosylase/transpeptidase in E. coli and other Proteobacteria, designated penicillin-binding protein 1B. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273952 [Multi-domain] Cd Length: 730 Bit Score: 344.40 E-value: 1.32e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 83 DGKLI---YEYGKEKRTNIMYDQIPKLVENAFLATEDARFYEHSGVDYKGTARAALVSLKGDYGSQGGSTITQQVIKNYF 159
Cdd:TIGR02071 132 DPKLIamlYSPNGEQRLFVPRDQFPELLVDTLLATEDRDFYEHDGISLYSIGRAVWVNLTAGRTVQGGSTLTQQLVKNLF 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 160 LSMEKTSKRKAQEIYLAYKLEQQYSKHEILEMYLNKVYLGNRS----YGIATAVQNYYGKELKDLTLPEVAMLAGLMKAP 235
Cdd:TIGR02071 212 LSNERSLWRKANEAYMALILDARYSKDRILELYLNEVYLGQSGddaiHGFPLASQYYFGRPLGELSLDQVALLVGMVKGP 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 236 NNYDPTKeqNIKKATERRNVVLKLMNRHGYITKKEMEEASKVPVteGLKKaTEQKEMPYPAFMDAVVKEVEKELPDVNIG 315
Cdd:TIGR02071 292 SYYNPWR--NPDRALERRNLVLRLLQEQKIIDDEEYDMLSARPL--GVQK-KGGIISRQPAFLQLVRRELRQKLGDKVKD 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 316 SDGLEIYTTLDPKAQDFADKLLNKDIINYPNEK----FQGAFTFMDTKTGEVRAIGSGRgenKAVFKGHNIAIELNRSAG 391
Cdd:TIGR02071 367 LSGLRIFTTLDPVSQSAAEQAVQETIPALKKKKklpdLEAAMVVTDRFTGEVRAMVGGS---DPQFAGFNRALQARRQIG 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 392 STMKPiFDYAPAIEYL-KWATYHQIDDSPF--KYSTGQ--EVRNADRKHLGPITMRDALKTSRNIPAIKTAKEVGINRSK 466
Cdd:TIGR02071 444 SLVKP-AVYLTALSQPdKYRLNTWIEDQPLsiKLSNGQvwSPQNYDRRYSGTVMLYDALAHSLNIPTVNLGMKVGLPKVS 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 467 GFSEKLGITFNVA-PTESTAIGTNEASPTEIAGAYAAFGNDGKYTRPHFVKKVIYSDGK--SKSFEQKSKRVMKDStAYM 543
Cdd:TIGR02071 523 QTWNKLGINKDEIpPVPSMLLGAINLTPYEVAQLYQTIASGGNRAPLSAVRSVLDEDGKvlYQSDPQAEQAVPSQA-AYL 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 544 ITDMLRTFVSSGLGTTANI--GSLDIAGKTGTTNYSleqiaqynlpesatRDSWFAGYTPQYTMAVWTGytkdsKDNyis 621
Cdd:TIGR02071 602 TLYAMQQVVQRGTARSLGAdfPSLSLAGKTGTTNDN--------------RDSWFAGIDGKEVTIIWLG-----RDD--- 659
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1264348865 622 SKNTKI-----AQLIFKEMMSKFATDKSQFKMPNSVVQEG 656
Cdd:TIGR02071 660 NGPTKLtgasgALQVYARYLSYQTPEPLLLVPPEGIDWFG 699
|
|
| PbpC |
COG4953 |
Membrane carboxypeptidase/penicillin-binding protein PbpC [Cell wall/membrane/envelope ... |
33-610 |
3.24e-89 |
|
Membrane carboxypeptidase/penicillin-binding protein PbpC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 443980 [Multi-domain] Cd Length: 773 Bit Score: 299.05 E-value: 3.24e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 33 FFRKFLVSCLLLGiVGLVAGVATFfvmikdAPKLEKAKlvnPLSSKIYDKDGKLIYEY--GKEK-RTNIMYDQIPKLVEN 109
Cdd:COG4953 10 RLLALLLALLLLA-LALWALDRLF------PLPLLFAV---PYSTVVLDRDGTLLRAFlaADGQwRLPVPLDEVSPRYLQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 110 AFLATEDARFYEHSGVDYKGTARAALVSLKGDYGSQGGSTITQQVIKnyfLSmEKTSK---RKAQEIYLAYKLEQQYSKH 186
Cdd:COG4953 80 ALLAYEDRRFYYHPGVNPLALLRAAWQNLRSGRIVSGGSTLTMQVAR---LL-EPRPRtlsGKLRQILRALQLERRYSKD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 187 EILEMYLNKVYLGNRSYGIATAVQNYYGKELKDLTLPEVAMLAGLMKAPNNYDPTKeqNIKKATERRNVVLKLMNRHGYI 266
Cdd:COG4953 156 EILELYLNLAPYGGNIEGVEAASLAYFGKPPSRLSLAEAALLAVLPQAPSRRRPDR--NPERARAARDRVLARLAEAGVI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 267 TKKEMEEASKVPVteglkkATEQKEMPY--PAFMDAVVKEvekelpdvniGSDGLEIYTTLDPKAQDFADKLLnKDIIN- 343
Cdd:COG4953 234 DAEEAALALLEPV------PARRRPLPQlaPHLARRLLRQ----------LPGGTRIRTTLDAGLQRRLERLV-RRYVRr 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 344 -YPNEKFQGAFTFMDTKTGEVRA-IGSGRGENKAVFkGHNIAIELNRSAGSTMKPiFDYAPAIEylkwatyhQ------- 414
Cdd:COG4953 297 lKQNGIHNAAVLVVDNRTGEVLAyVGSADFFDASRQ-GQVDMVRALRSPGSTLKP-FLYGLALD--------Qglihpet 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 415 -IDDSP--FK-YSTgqevRNADRKHLGPITMRDALKTSRNIPAIKTAKEVGINRSKGFSEKLGITfNVAPTEST-----A 485
Cdd:COG4953 367 lLADVPtsFGgYRP----ENFDGTFQGPVSAREALARSLNIPAVRLLEALGPARFYARLRRAGLR-LLLPPAEHyglslI 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 486 IGTNEASPTEIAGAYAAFGNDGKYTRPHFVKkviysdgksKSFEQKSKRVMKDSTAYMITDMLrtfvsSGL---GTTANI 562
Cdd:COG4953 442 LGGAEVTLEELVGLYAALARGGEARPLRLLA---------GEPASPGRRLLSPGAAWLVRDIL-----SDVprpDGAFGW 507
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1264348865 563 GSLD----IAGKTGTTnysleqiaqYNLpesatRDSWFAGYTPQYTMAVWTG 610
Cdd:COG4953 508 RALDspppIAWKTGTS---------YGF-----RDAWAVGFTGRYTVGVWVG 545
|
|
| Transgly |
pfam00912 |
Transglycosylase; The penicillin-binding proteins are bifunctional proteins consisting of ... |
83-261 |
2.83e-87 |
|
Transglycosylase; The penicillin-binding proteins are bifunctional proteins consisting of transglycosylase and transpeptidase in the N- and C-terminus respectively. The transglycosylase domain catalyzes the polymerization of murein glycan chains.
Pssm-ID: 459993 [Multi-domain] Cd Length: 177 Bit Score: 274.40 E-value: 2.83e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 83 DGKLIYEYGKEKRTNIMYDQIPKLVENAFLATEDARFYEHSGVDYKGTARAALVSLKGDYGSQGGSTITQQVIKNYFLSM 162
Cdd:pfam00912 1 DGTLLAELGEENREYVPLDDIPPALKNAVLAIEDRRFYEHGGVDPKGIARALLSNLRSGRIVQGGSTITQQLAKNLFLTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 163 EKTSKRKAQEIYLAYKLEQQYSKHEILEMYLNKVYLGNRSYGIATAVQNYYGKELKDLTLPEVAMLAGLMKAPNNYDPTK 242
Cdd:pfam00912 81 ERTLTRKLKEAVLALKLERRYSKDEILEAYLNTVYFGRGAYGIEAAARAYFGKDASDLTLAEAALLAGLPQAPSRYNPLR 160
|
170
....*....|....*....
gi 1264348865 243 eqNIKKATERRNVVLKLMN 261
Cdd:pfam00912 161 --NPERAKRRRNLVLDRMV 177
|
|
| mrcA |
PRK11636 |
penicillin-binding protein 1a; Provisional |
34-617 |
2.82e-78 |
|
penicillin-binding protein 1a; Provisional
Pssm-ID: 183248 [Multi-domain] Cd Length: 850 Bit Score: 270.85 E-value: 2.82e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 34 FRKFL----VSCLLLGivglvagVATFFVMIK-------DAPKLEKAKLVNPLssKIYDKDGKLIYEYGKEKRTNIMYDQ 102
Cdd:PRK11636 3 FVKYLlilaVCCILLG-------AGSIYGLYRyiepqlpDVATLKDVRLQTPM--QVYSADGELIAQYGEKRRIPLTLDQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 103 IPKLVENAFLATEDARFYEHSGVDYKGTARAALVSLKGDYGSQGGSTITQQVIKNYFLSMEKTSKRKAQEIYLAYKLEQQ 182
Cdd:PRK11636 74 IPPEMVKAFIATEDSRFYEHHGVDPVGIFRAASVALFSGHASQGASTITQQLARNFFLSPERTLMRKIKEAFLAIRIEQL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 183 YSKHEILEMYLNKVYLGNRSYGIATAVQNYYGKELKDLTLPEVAMLAGLMKAPNNYDPTKEQNikKATERRNVVLKLMNR 262
Cdd:PRK11636 154 LTKDEILELYLNKIYLGYRAYGVGAAAQVYFGKTVDQLTLSEMAVIAGLPKAPSTFNPLYSMD--RAVARRNVVLSRMLD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 263 HGYITKKEMEEASKVPVTEGLKKATEQKEMPYPAFMdaVVKEVEKELPDvNIGSDGLEIYTTLDPKAQDFADKLLNKDII 342
Cdd:PRK11636 232 EGYITQAQYDQARSEPIVANYHAPEIAFSAPYLSEM--VRQEMYNRYGE-NAYEDGYRVYTTITRKVQQAAQQAVRNNVL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 343 NY---------------------PNEKF---------------------------------------------------- 349
Cdd:PRK11636 309 DYdmrhgyrgpanvlwkvgesawDNKKItdtlkalptygpllpavvtsanpqeatamladgssvalpmegvrwarpyrsd 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 350 --QG-----------------------------------AFTFMDTKTGEVRAIGSGRGENKAVFkghNIAIELNRSAGS 392
Cdd:PRK11636 389 tqQGptprkvtdvvqtgqqiwvrqvddawwlaqvpdvnsALVSINPQNGAVMALVGGFDFNQSKF---NRATQALRQVGS 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 393 TMKPiFDYAPAIEY-LKWATYhqIDDSP---FKYSTGQEVR--NADRKHLGPITMRDALKTSRNIPAIKTAKEVGINRSK 466
Cdd:PRK11636 466 NIKP-FLYTAAMDKgLTLASM--LNDVPisrWDAGAGSDWRpkNSPPQYAGPIRLRQGLGQSKNVVMVRAMRAMGVDYAA 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 467 GFSEKLGI-TFNVAPTESTAIGTNEASPTEIAGAYAAFGNDGKYTRPHFVKK------------------------VIYS 521
Cdd:PRK11636 543 EYLQRFGFpAQNIVHTESLALGSASFTPMQVARGYAVMANGGFLVDPYFISKiendqggvifeakpkvacpecdipVIYG 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 522 D-GKSKSFEQKS-------------------------KRVMKDST------------AYMITDMLRTFVS-----SGLGT 558
Cdd:PRK11636 623 DtQKSNVLENDDvenvatsqeqqnssvpmpqleqanqALVAQNGAqeyaphvintplAFLIKSALNTNIFgepgwMGTGW 702
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1264348865 559 TA--NIGSLDIAGKTGTTNYSleqiaqynlpesatRDSWFAGYTPQYTMAVWTGYTKDSKD 617
Cdd:PRK11636 703 RAgrDLKRRDIGGKTGTTNSS--------------KDAWFSGYGPGVVTSVWIGFDDHRRD 749
|
|
| PRK14850 |
PRK14850 |
penicillin-binding protein 1b; Provisional |
86-610 |
2.82e-76 |
|
penicillin-binding protein 1b; Provisional
Pssm-ID: 237835 [Multi-domain] Cd Length: 764 Bit Score: 263.63 E-value: 2.82e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 86 LIYEYGKEKRTNIMYDQIPKLVENAFLATEDARFYEHSGVDYKGTARAALVSLKGDYGSQGGSTITQQVIKNYFLSMEKT 165
Cdd:PRK14850 148 MLYSPEGKKRLFIPRNQYPEMLIKTLLAIEDKYFYEHDGIHLSSIGRAFLVNLMSGHTIQGGSTLTQQLVKNLFLTNTRS 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 166 SKRKAQEIYLAYKLEQQYSKHEILEMYLNKVYLG----NRSYGIATAVQNYYGKELKDLTLPEVAMLAGLMKAPNNYDPT 241
Cdd:PRK14850 228 LWRKINEIYMALILDRFYSKDRILELYLNEVYLGqdgnEQIRGFPLASIYYFGRPINELNLDQYALLVGMVKGASLYNPW 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 242 KeqNIKKATERRNVVLKLMNRHGYITKKEMEEASKVPVteglkkATEQKE---MPYPAFMDAVVKEVEKELPDVNIGSDG 318
Cdd:PRK14850 308 T--NPNLTLKRRNLVLFLLYKQKVITRKLYKDLCSRPL------NVQSKGniiSSHPAFIQLVCEEFHKKIHYPFKNFSG 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 319 LEIYTTLDPKAQDFADKLLNKDI----INYPNEKFQGAFTFMDTKTGEVRAIgsgRGENKAVFKGHNIAIELNRSAGSTM 394
Cdd:PRK14850 380 TKIFTTLDYISQNAAEQAVKIGIpilkRKKRLKDLEVAMVIIDRFSGEVRAL---IGSSKPEFNGYNRALKARRSIGSLS 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 395 KPIFdYAPAI---EYLKWATYhqIDDSP--FKYSTGQ--EVRNADRKHLGPITMRDALKTSRNIPAIKTAKEVGINRSKG 467
Cdd:PRK14850 457 KPIT-YLTALsqpEKYHLNTW--ISDTPisIKLDNGQywTPKNNNFSFSGKVMLIDALIHSINIPTVHLSINLGLKKLVD 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 468 FSEKLGITFN-VAPTESTAIGTNEASPTEIAGAYAAFGNDGKYTRPHFVKKVIYSDGK--SKSFEQkSKRVMKDSTAYMI 544
Cdd:PRK14850 534 SWILLGISSNyITPLPSISLGAINLTPMEVAQVFQIIGSGGYKSSLSSIRSIISDDNKvlYQNFPQ-SKHVESSQASYLT 612
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 545 TDMLRTFVSSglGTTANIG----SLDIAGKTGTTNYSleqiaqynlpesatRDSWFAGYTPQYTMAVWTG 610
Cdd:PRK14850 613 LYAMQQVVKS--GTAKSLGtifkEFSLAGKTGTTNNL--------------VDSWFVGIDGKQVVITWIG 666
|
|
| mrcB |
PRK09506 |
bifunctional glycosyl transferase/transpeptidase; Reviewed |
83-618 |
3.22e-76 |
|
bifunctional glycosyl transferase/transpeptidase; Reviewed
Pssm-ID: 236544 [Multi-domain] Cd Length: 830 Bit Score: 264.71 E-value: 3.22e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 83 DGKLI---YEYGKEKRTNIMYDQIPKLVENAFLATEDARFYEHSGVDYKGTARAALVSLKGDYGSQGGSTITQQVIKNYF 159
Cdd:PRK09506 196 DPRLItmlQSPNGEQRLFVPRSGFPDLLVDTLLATEDRHFYEHDGISLYSIGRAVLANLTAGRTVQGGSTLTQQLVKNLF 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 160 LSMEKTSKRKAQEIYLAYKLEQQYSKHEILEMYLNKVYLG----NRSYGIATAVQNYYGKELKDLTLPEVAMLAGLMKAP 235
Cdd:PRK09506 276 LSNERSLWRKANEAYMALIMDARYSKDRILELYLNEVYLGqsgdDQIRGFPLASLYYFGRPVEELSLDQQALLVGMVKGA 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 236 NNYDPTKeqNIKKATERRNVVLKLMNRHGYITKKEMEEASKVPVteGLKKATEQKeMPYPAFMDAVVKEVEKELPD-VNI 314
Cdd:PRK09506 356 SLYNPWR--NPKLALERRNLVLRLLQQQQIIDQELYDMLSARPL--GVQPKGGVI-SPQPAFMQMVRQELQAKLGDkVKD 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 315 GSdGLEIYTTLDPKAQDFADKLLNKDIINYPNEK----FQGAFTFMDTKTGEVRAIGSGrgeNKAVFKGHNIAIELNRSA 390
Cdd:PRK09506 431 LS-GVKIFTTLDPVSQDAAEKAVEEGIPALKKQRklsdLETAMVVVDRFSGEVRAMVGG---SEPQFAGYNRAMQARRSI 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 391 GSTMKPIFDYAPAIEYLKWATYHQIDDSP--FKYSTGQ--EVRNADRKHLGPITMRDALKTSRNIPAIKTAKEVGINRSK 466
Cdd:PRK09506 507 GSLAKPATYLTALSQPDKYRLNTWIADAPisLRQPNGQvwSPQNDDRRFSGRVMLVDALTRSMNVPTVNLGMALGLPAVT 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 467 GFSEKLGITFNV-APTESTAIGTNEASPTEIAGAYAAFGNDGKYTRPHFVKKVIYSDGKS--KSFEQkSKRVMKDSTAYM 543
Cdd:PRK09506 587 DTWIKLGVPKDQlNPVPAMLLGALNLTPIEVAQAFQTIASGGNRAPLSALRSVIAEDGKVlyQSFPQ-AERAVPAQAAYL 665
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1264348865 544 ITDMLRTFVSSGLGT--TANIGSLDIAGKTGTTNysleqiaqyNLpesatRDSWFAGYTPQYTMAVWTGytkdsKDN 618
Cdd:PRK09506 666 TLYTMQQVVQRGTGRqlGAKYPNLHLAGKTGTTN---------DL-----VDSWFAGIDGKEVTITWVG-----RDN 723
|
|
| Transpeptidase |
pfam00905 |
Penicillin binding protein transpeptidase domain; The active site serine (residue 337 in Swiss: ... |
351-636 |
1.03e-42 |
|
Penicillin binding protein transpeptidase domain; The active site serine (residue 337 in Swiss:P14677) is conserved in all members of this family.
Pssm-ID: 425939 [Multi-domain] Cd Length: 296 Bit Score: 157.58 E-value: 1.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 351 GAFTFMDTKTGEVRAIGSGRGENKAVFKGH--NIAIELNRSAGSTMKPiFDYAPAIEYLKWATYHQIDDSPFKYSTGQEV 428
Cdd:pfam00905 1 GSAVVLDPKTGEVLAMVGKPSYDPNGFIGPlrNRAVTSRYEPGSTFKP-FTALAALDNGVLKPDETIFDWPGKQQGGKSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 429 RNADRKHLGPITMRDALKTSRNIPAIKTAKEVGINRSK------GFSEKLGITF------------NVAPTESTAIGTNe 490
Cdd:pfam00905 80 GDWNQDQVGIGTLRQALEYSSNWYMQKLAQKLGADKLRsylkkfGYGNKTGIGLpgenagyltpywLEGATASFGIGLT- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 491 ASPTEIAGAYAAFGNDGKYTRPHFVKKVIYSDGKsksfEQKSKRVMKDSTAYMITDMLRTFVSSGLGT-TANIGSLDIAG 569
Cdd:pfam00905 159 ITPLQQAQAYAAIANGGKLVPPHLVKSIEDKVDP----KVLNKLPISKSTAEKVKDMLRLVVNDGTGTgTAAVPGYKVAG 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1264348865 570 KTGTTNYSLEQIAQYNlpeSATRDSWFAGYT----PQYTMAVwtgyTKDSKDNYISSkntKIAQLIFKEMM 636
Cdd:pfam00905 235 KTGTAQVAGPKGGGYY---DGAQIGWFVGYApadnPKYAFAV----LIDDPKRYYGG---KVAAPIFKDIL 295
|
|
| FtsI |
COG0768 |
Cell division protein FtsI, peptidoglycan transpeptidase (Penicillin-binding protein 2) [Cell ... |
301-607 |
1.73e-41 |
|
Cell division protein FtsI, peptidoglycan transpeptidase (Penicillin-binding protein 2) [Cell cycle control, cell division, chromosome partitioning, Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440531 [Multi-domain] Cd Length: 568 Bit Score: 160.76 E-value: 1.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 301 VVKEVEKELPDVNiGSDgleIYTTLDPKAQDFADKLLNKDIINYPNEKfqGAFTFMDTKTGEVRAIGSGRGENKAVFKGH 380
Cdd:COG0768 205 VIRDLGEEKPPVP-GKD---LVLTIDSDLQKIAEEALKKAVEEYKAKS--GAVVVMDPKTGEILAMASYPSFDPNLFVGG 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 381 NIAIELNRSA------GSTMKPIFDYApAIEYLKWATYHQIDDSPFKYSTGQEVRNADRKHLGPITMRDALKTSRNIPAI 454
Cdd:COG0768 279 PDEPLRNRAVqgtyepGSTFKPFTAAA-ALEEGVITPDTTFDCPGYYRVGGRTIRDWDRGGHGTLTLTEALAKSSNVGFY 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 455 KTAKEVGINR-----SK-GFSEKLGITF------NVAPTE--------STAIG-TNEASPTEIAGAYAAFGNDGKYTRPH 513
Cdd:COG0768 358 KLALRLGIDKlydylKKfGLGQKTGIDLpgeasgLLPSPKrwypgetaTMSIGqGLSVTPLQLAQAYAAIANGGVLVKPH 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 514 FVKKVIYSDGKS-KSFEQKSKRVMKDSTAYMITDMLRTFVSSGLGT--TANIGSLDIAGKTGTT-NYSLEQIAQYNLpes 589
Cdd:COG0768 438 LVKEIVDPDGEVvKEEPEVLRRVISPETAETVREGMEGVVNEPGGTarRAAIPGYRVAGKTGTAqVVDIGNGGYYKG--- 514
|
330 340
....*....|....*....|..
gi 1264348865 590 aTRDSWFAGYT----PQYTMAV 607
Cdd:COG0768 515 -RHIASFVGFApadnPRYAVAV 535
|
|
| PRK13481 |
PRK13481 |
glycosyltransferase; Provisional |
92-274 |
2.95e-40 |
|
glycosyltransferase; Provisional
Pssm-ID: 184078 [Multi-domain] Cd Length: 232 Bit Score: 148.41 E-value: 2.95e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 92 KEKRTNIMYDQIPKLVENAFLATEDARFYEHSGVDYKGTARAALVSLkGDYGSQGGSTITQQVIKNYFLSMEKTSKRKAQ 171
Cdd:PRK13481 42 ENKSSFVSADNMPEYVKGAFISMEDERFYKHHGFDLKGTTRALFSTI-SDRDVQGGSTITQQVVKNYFYDNERSFTRKVK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 172 EIYLAYKLEQQYSKHEILEMYLNKVYLGNRSYGIATAVQNYYG-------KELKDLTLPEVAMLAGLMKAPNNYDPTKEQ 244
Cdd:PRK13481 121 ELFVAHRVEKQYSKNEILSFYLNNIYFGDNQYTLEGAANHYFGttvnknsTTMSHITVLQSAILASKVNAPSVYNINDMS 200
|
170 180 190
....*....|....*....|....*....|
gi 1264348865 245 NikKATERRNVVLKLMNRHGYITKKEMEEA 274
Cdd:PRK13481 201 E--NFTQRVSTNLEKMKQQNYINETQYQQA 228
|
|
| PRK11240 |
PRK11240 |
penicillin-binding protein 1C; Provisional |
110-610 |
9.12e-32 |
|
penicillin-binding protein 1C; Provisional
Pssm-ID: 183049 [Multi-domain] Cd Length: 772 Bit Score: 132.90 E-value: 9.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 110 AFLATEDARFYEHSGVDYKGTARAALVSLKGDYGSQGGSTITQQVIKnYFLSMEKTSKRKAQEIYLAYKLEQQYSKHEIL 189
Cdd:PRK11240 77 ALINYEDRWFWKHPGVNPFSVARAAWQDLTSGRVISGGSTLTMQVAR-LLDPHPRTFGGKIRQLWRALQLEWHLSKREIL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 190 EMYLNKVYLGNRSYGIATAVQNYYGKELKDLTLPEVAMLAGLMKAPNNYDPTKEQniKKATERRNVVLKLMNRHGYITKK 269
Cdd:PRK11240 156 TLYLNRAPFGGTLQGIGAASWAYLGKSPANLSYAEAALLAVLPQAPSRLRPDRWP--ERAEAARNKVLERMAEQGVWSAE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 270 EMEEASKVPVTeglkKATEQkeMPY--PAFMDAVVKEVEKELpdvnigsdgleIYTTLDPKAQDFADKLLnkdiINYPN- 346
Cdd:PRK11240 234 QVKESREEPVW----LAPRQ--MPQlaPLFARMMLGKSKSDK-----------IVTTLDAGLQRRLEDLA----LNWKGr 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 347 --EKFQGAFTFMDTKTGEVRA-IGSGRGENKAVFkGHNIAIELNRSAGSTMKPiFDYAPAIE--YLKWATYHQidDSPFK 421
Cdd:PRK11240 293 lpPRSSLAMIVVDHTDMAVRGwVGSVDLNDDSRF-GHVDMVNAIRSPGSVLKP-FVYGLALDdgLIHPASLLQ--DVPRR 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 422 YStgqEVR--NADRKHLGPITMRDALKTSRNIPAIKTAKEVGinrSKGFSEKL---GITFNV----APTESTAIGTNEAS 492
Cdd:PRK11240 369 TG---DYRpgNFDSGFHGPVSMSEALVRSLNLPAVQVLEAYG---PKRFAAKLrnvGLPLYLpagaEPNLSLILGGAGAR 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 493 PTEIAGAYAAFGNDGKYTRPHFVKKVIYSDgksksfeqksKRVMKDSTAYMITDMLrtfvsSGLGTTANIGSL----DIA 568
Cdd:PRK11240 443 LEDMVAAYSAFARHGKAAKLRLQPDDPLLE----------RPLMSPGAAWIIRRIM-----ADEAQPLPDAALprvvPLA 507
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1264348865 569 GKTGTTnYSLeqiaqynlpesatRDSWFAGYTPQYTMAVWTG 610
Cdd:PRK11240 508 WKTGTS-YGY-------------RDAWAIGVNARYVIGIWTG 535
|
|
| pbp2_mrdA |
TIGR03423 |
penicillin-binding protein 2; Members of this protein family are penicillin-binding protein 2 ... |
318-607 |
1.85e-17 |
|
penicillin-binding protein 2; Members of this protein family are penicillin-binding protein 2 (PBP-2), a protein whose gene (designated pbpA or mrdA) generally is found next to the gene for RodA, a protein required for rod (bacillus) shape in many bacteria. PBP-2 acts as a transpeptidase for cell elongation (hence, rod-shape). [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 274573 [Multi-domain] Cd Length: 592 Bit Score: 86.81 E-value: 1.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 318 GLEIYTTLDPKAQDFADKLLnkdiinyPNEKfqGAFTFMDTKTGEVRAIGS---------GRGENKAVFKghniaiEL-- 386
Cdd:TIGR03423 225 GKDLVLTIDARLQQAAEKAL-------GGRR--GAVVVMDPRTGEILAMVStpsfdpnlfVDGISSKDYK------ALln 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 387 -------NRSA------GSTMKPiFDYAPAIEYLKWATYHQIDDSPFKYSTGQEVRNADRKHLGPITMRDALKTSRNIPA 453
Cdd:TIGR03423 290 dpdrpllNRAIqgvyppGSTFKP-VVALAALEEGVITPETRIYCPGYFQLGGRRFRCWKRGGHGRVDLRKAIEESCDVYF 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 454 IKTAKEVGINR----SK--GFSEKLGITF-----NVAPTE-----------------STAIGT--NEASPTEIAGAYAAF 503
Cdd:TIGR03423 369 YQLALRLGIDKiaeyAKrfGFGQKTGIDLpgeksGLVPSRewkrkrfgqpwypgdtlNVSIGQgyVLVTPLQLAVATAAL 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 504 GNDGKYTRPHFVKKVIYSDGKS-KSFEQKSKRVMKDSTAYM--ITDMLRTFVSSGLGTTANIG---SLDIAGKTGTT-NY 576
Cdd:TIGR03423 449 ANGGKLYKPHLVKSIEDPDGGVvRRTEPEVLRPLPISPENLdvVREGMRDVVNGPGGTARRARlglPYKMAGKTGTAqVV 528
|
330 340 350
....*....|....*....|....*....|....*....
gi 1264348865 577 SLEQIAQYN---LPESaTRD-SWFAGYTP----QYTMAV 607
Cdd:TIGR03423 529 SLKQGEKYDaeqIPER-LRDhALFVAFAPydnpKIAVAV 566
|
|
| Pro-rich |
pfam15240 |
Proline-rich protein; This family includes several eukaryotic proline-rich proteins. |
699-826 |
1.84e-13 |
|
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
Pssm-ID: 464580 [Multi-domain] Cd Length: 167 Bit Score: 68.91 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 699 SEPNNGSDQGNTPPPksGSDQGNTPPPNNSNGQGNTPSPKSGSDQgntPPPNNGNGQGNTPPPKSGS----DQGNTPPPK 774
Cdd:pfam15240 33 SEEEGQSQQGGQGPQ--GPPPGGFPPQPPASDDPPGPPPPGGPQQ---PPPQGGKQKPQGPPPQGGPrpppGKPQGPPPQ 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1264348865 775 SGSDQGNTPPPNNGSG---QGNTPSPKSGSDQGNTPPPNnGDGHGTPPPPSNDGN 826
Cdd:pfam15240 108 GGNQQQGPPPPGKPQGpppQGGGPPPQGGNQQGPPPPPP-GNPQGPPQRPPQPGN 161
|
|
| Pro-rich |
pfam15240 |
Proline-rich protein; This family includes several eukaryotic proline-rich proteins. |
701-820 |
6.92e-11 |
|
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
Pssm-ID: 464580 [Multi-domain] Cd Length: 167 Bit Score: 61.59 E-value: 6.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 701 PNNGSDQGNTPPPKSGSDQGNTPPPNNSNGQG----NTPSPKSGSDQGntPPPNNGNGQGNTPPPksGSDQGntPPPksg 776
Cdd:pfam15240 56 PQPPASDDPPGPPPPGGPQQPPPQGGKQKPQGpppqGGPRPPPGKPQG--PPPQGGNQQQGPPPP--GKPQG--PPP--- 126
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1264348865 777 sdQGNTPPPNNGSGQGnTPSPKSGSDQGNTPPPNNGDGHGTPPP 820
Cdd:pfam15240 127 --QGGGPPPQGGNQQG-PPPPPPGNPQGPPQRPPQPGNPQGPPQ 167
|
|
| Drf_FH1 |
pfam06346 |
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ... |
708-831 |
1.02e-08 |
|
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.
Pssm-ID: 461881 [Multi-domain] Cd Length: 157 Bit Score: 55.26 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 708 GNTPPPKSGSDQGNTPPPNNSNGQGNTPSPKSGSDQGNTPPPNNGNGQGNTPPPKSGSDQGNTPPPKSGSDQGNTPPPNN 787
Cdd:pfam06346 9 DSSTIPLPPGACIPTPPPLPGGGGPPPPPPLPGSAAIPPPPPLPGGTSIPPPPPLPGAASIPPPPPLPGSTGIPPPPPLP 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1264348865 788 GS-GQGNTPSPKSGSDQGNTPPPNNGDGHGTPPPPSNDGNIGEDP 831
Cdd:pfam06346 89 GGaGIPPPPPPLPGGAGVPPPPPPLPGGPGIPPPPPFPGGPGIPP 133
|
|
| Drf_FH1 |
pfam06346 |
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ... |
711-821 |
3.95e-08 |
|
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.
Pssm-ID: 461881 [Multi-domain] Cd Length: 157 Bit Score: 53.34 E-value: 3.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 711 PPPKSGsdqGNTPPPNNSNGQGNTPSPKSGSDQGNTPPPNNGNGQGNTPPPKSGSDQGNTPPPKSGSDQGNTPPPNNGSG 790
Cdd:pfam06346 3 PPPLPG---DSSTIPLPPGACIPTPPPLPGGGGPPPPPPLPGSAAIPPPPPLPGGTSIPPPPPLPGAASIPPPPPLPGST 79
|
90 100 110
....*....|....*....|....*....|.
gi 1264348865 791 QGNTPSPKSGSDQGNTPPPNNGDGHGTPPPP 821
Cdd:pfam06346 80 GIPPPPPLPGGAGIPPPPPPLPGGAGVPPPP 110
|
|
| PHA03418 |
PHA03418 |
hypothetical E4 protein; Provisional |
701-821 |
4.68e-08 |
|
hypothetical E4 protein; Provisional
Pssm-ID: 177646 [Multi-domain] Cd Length: 230 Bit Score: 54.74 E-value: 4.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 701 PNNGSDQGNTPPPKSGSDQGNTPP----PNNSNGQGNTPSPKSGSDQGNTPPPNNGNGQGNTPPPKSGSDQG-----NTP 771
Cdd:PHA03418 52 PSPPPDPPLTPRPPAQPNGHNKPPvtkqPGGEGTEEDHQAPLAADADDDPRPGKRSKADEHGPAPGRAALAPfkldlDQD 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1264348865 772 PPKSGSDqgntPPPNNGSGQGNTPsPKSGSDqgNTPPPNNGDG--HGTPPPP 821
Cdd:PHA03418 132 PLHGDPD----PPPGATGGQGEEP-PEGGEE--SQPPLGEGEGavEGHPPPL 176
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
704-832 |
4.69e-08 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 56.58 E-value: 4.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 704 GSDQGNTPPPKSGSDQGNTPPPNNSNGQ---GNTPSPKSGS-----DQGNTP--PPNNGNGQGNTPPPKSGSDQGNTPPP 773
Cdd:COG5164 93 AGNTGGTTPAGDGGATGPPDDGGATGPPddgGSTTPPSGGSttppgDGGSTPpgPGSTGPGGSTTPPGDGGSTTPPGPGG 172
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1264348865 774 KSGS--DQGNTPPPNNGSGQGNTPSPKSGSDQGNTPPPNNGDGHGTPPPPSNDGNIGEDPA 832
Cdd:COG5164 173 STTPpdDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQ 233
|
|
| Drf_FH1 |
pfam06346 |
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ... |
723-831 |
5.47e-08 |
|
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.
Pssm-ID: 461881 [Multi-domain] Cd Length: 157 Bit Score: 52.95 E-value: 5.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 723 PPPNNSNGQGNTPSPksGSDQGNTPPPNNGNGQGNTPPPKSGSDQGNTPPPKSGSDQGNTPPPNNGSGQGNTPSPKSGSD 802
Cdd:pfam06346 2 PPPPLPGDSSTIPLP--PGACIPTPPPLPGGGGPPPPPPLPGSAAIPPPPPLPGGTSIPPPPPLPGAASIPPPPPLPGST 79
|
90 100
....*....|....*....|....*....
gi 1264348865 803 QGNTPPPNNGDGHGTPPPPSNDGNIGEDP 831
Cdd:pfam06346 80 GIPPPPPLPGGAGIPPPPPPLPGGAGVPP 108
|
|
| Drf_FH1 |
pfam06346 |
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ... |
708-825 |
2.81e-07 |
|
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.
Pssm-ID: 461881 [Multi-domain] Cd Length: 157 Bit Score: 51.02 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 708 GNTPPPKSGSDQGNTPPPNNSNGQGNTPSPKSGSDQGNTPPPNNGNGQGNTPPPKSGSDQGNTPPPKSGSDQGNTPPPNN 787
Cdd:pfam06346 21 IPTPPPLPGGGGPPPPPPLPGSAAIPPPPPLPGGTSIPPPPPLPGAASIPPPPPLPGSTGIPPPPPLPGGAGIPPPPPPL 100
|
90 100 110
....*....|....*....|....*....|....*....
gi 1264348865 788 GSGQGNTPSPKS-GSDQGNTPPPNNGDGHGTPPPPSNDG 825
Cdd:pfam06346 101 PGGAGVPPPPPPlPGGPGIPPPPPFPGGPGIPPPPPGMG 139
|
|
| dermokine |
cd21118 |
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ... |
699-831 |
7.88e-07 |
|
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.
Pssm-ID: 411053 [Multi-domain] Cd Length: 495 Bit Score: 52.69 E-value: 7.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 699 SEPNNGSDQGNTPPPKSGSDQGNTpppnNSNGQGNTPSPKSGSDQGNTPPPNNGN--GQGNTPPPKSGSDQGNTPPPKSG 776
Cdd:cd21118 192 TVRGNNQNSGCTNPPPSGSHESFS----NSGGSSSSGSSGSQGSHGSNGQGSSGSsgGQGNGGNNGSSSSNSGNSGGSNG 267
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1264348865 777 SDQGNTPPPNNGSGQGNTPSPKSGSDQGNTPppnnGDGHGTPPPPSNDGNIGEDP 831
Cdd:cd21118 268 GSSGNSGSGSGGSSSGGSNGWGGSSSSGGSG----GSGGGNKPECNNPGNDVRMA 318
|
|
| Drf_FH1 |
pfam06346 |
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ... |
711-821 |
3.95e-06 |
|
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.
Pssm-ID: 461881 [Multi-domain] Cd Length: 157 Bit Score: 47.56 E-value: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 711 PPPKSGSDQGNTPPPNNSNGQGNTPSPKSGSDQGNTPPPNNGNGQGNTPPPKSGSDQGNTPPPKSGSDQGNTPPPNNGSG 790
Cdd:pfam06346 36 PPPLPGSAAIPPPPPLPGGTSIPPPPPLPGAASIPPPPPLPGSTGIPPPPPLPGGAGIPPPPPPLPGGAGVPPPPPPLPG 115
|
90 100 110
....*....|....*....|....*....|.
gi 1264348865 791 QGNTPSPKSGSDQGNTPPPNngDGHGTPPPP 821
Cdd:pfam06346 116 GPGIPPPPPFPGGPGIPPPP--PGMGMPPPP 144
|
|
| Med15 |
pfam09606 |
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ... |
703-826 |
7.67e-06 |
|
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.
Pssm-ID: 312941 [Multi-domain] Cd Length: 732 Bit Score: 49.62 E-value: 7.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 703 NGSDQGNTPPPKSGSDQGNTPPPNN--------SNGQGNTPSPKSGSDQGNTPPPNNGNGQGNTPPPKSGSDQGNTPPPK 774
Cdd:pfam09606 88 NLAGQGTRPQMMGPMGPGPGGPMGQqmggpgtaSNLLASLGRPQMPMGGAGFPSQMSRVGRMQPGGQAGGMMQPSSGQPG 167
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1264348865 775 SGsdQGNTPPPNNGSGQGNTPSPKSGSDQGNTPPPNNGDGHGTPPPPSNDGN 826
Cdd:pfam09606 168 SG--TPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGA 217
|
|
| pullulan_Gpos |
TIGR02102 |
pullulanase, extracellular, Gram-positive; Pullulan is an unusual, industrially important ... |
754-833 |
8.18e-06 |
|
pullulanase, extracellular, Gram-positive; Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although pullulan itself may not be the natural substrate. In contrast, a glycogen debranching enzyme such GlgX, homologous to this family, can release glucose at alpha,1-6 linkages from glycogen first subjected to limit degradation by phosphorylase. Characterized members of this family include a surface-located pullulanase from Streptococcus pneumoniae () and an extracellular bifunctional amylase/pullulanase with C-terminal pullulanase activity (.
Pssm-ID: 273973 [Multi-domain] Cd Length: 1111 Bit Score: 49.86 E-value: 8.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 754 GQGNTPPPKSGSDQGNTPPPKSGSDQGNTPPPNNGSGQGNTPSPKSGSDQGNTPPPNNGDGHGTPPPPSNDGNIGEDPAN 833
Cdd:TIGR02102 1009 APEKTPPPPEHEPQAPKPPTQDPDGSKPKDKVDPKDNKDPLTPPGSDDENGETPKGNEEKKEEQPDKGANLPNTGTKNSN 1088
|
|
| dermokine |
cd21118 |
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ... |
701-834 |
9.05e-06 |
|
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.
Pssm-ID: 411053 [Multi-domain] Cd Length: 495 Bit Score: 49.23 E-value: 9.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 701 PNNGSD-QGNTPPPKSGSDQGN-------TPPPNNSNGQGNTPSPKSGSDQGNTPPPNNGNGQGNTPPPKSGSDQGNtpp 772
Cdd:cd21118 175 LNYGTNsQGAVAQPGYGTVRGNnqnsgctNPPPSGSHESFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSGGQGNGGN--- 251
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1264348865 773 pkSGSDQGNTPPPNNGSGQGNTPSPKSGSDQGNTPPPNNGDGHGTPPPPSNDGNIGEDPANN 834
Cdd:cd21118 252 --NGSSSSNSGNSGGSNGGSSGNSGSGSGGSSSGGSNGWGGSSSSGGSGGSGGGNKPECNNP 311
|
|
| PHA03418 |
PHA03418 |
hypothetical E4 protein; Provisional |
711-831 |
2.01e-05 |
|
hypothetical E4 protein; Provisional
Pssm-ID: 177646 [Multi-domain] Cd Length: 230 Bit Score: 46.66 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 711 PPPKSGSDQGNTPPPNNSNgqgnTPSPKSGSDQGNTP-----PPNNGNGQGNTPPPKSGSDQGNTPPPKSGSDqGNTPPP 785
Cdd:PHA03418 42 PNPQEDPDKNPSPPPDPPL----TPRPPAQPNGHNKPpvtkqPGGEGTEEDHQAPLAADADDDPRPGKRSKAD-EHGPAP 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1264348865 786 NNGSGQ-------------GNTPSPKSGSDQGNTPPpnNGDGHGTPPPPSNDGNIGEDP 831
Cdd:PHA03418 117 GRAALApfkldldqdplhgDPDPPPGATGGQGEEPP--EGGEESQPPLGEGEGAVEGHP 173
|
|
| PRK15319 |
PRK15319 |
fibronectin-binding autotransporter adhesin ShdA; |
726-793 |
2.45e-05 |
|
fibronectin-binding autotransporter adhesin ShdA;
Pssm-ID: 185219 [Multi-domain] Cd Length: 2039 Bit Score: 48.16 E-value: 2.45e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1264348865 726 NNSNGQGNTPSpKSGSDQGNTPPPNNGNGQGNTPPPKSGSDQGNTPPPKSGSDQGNTPPPNNGSGQGN 793
Cdd:PRK15319 1671 DDDSGGDDTPS-DGGDDGGNVTPPDDGGDGGNVTPPDDGGDGGDVTPPDHGGDVAPQYRADIGAYMGN 1737
|
|
| Pneumo_att_G |
pfam05539 |
Pneumovirinae attachment membrane glycoprotein G; |
662-809 |
1.06e-04 |
|
Pneumovirinae attachment membrane glycoprotein G;
Pssm-ID: 114270 [Multi-domain] Cd Length: 408 Bit Score: 45.42 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 662 KGEKRDSPPNTKIVNTTEQPSENKQKEKQKKLEEQkqSEPNNGSdQGNTPPpkSGSDQGNTPPPNNSNGQGNTPSPKSGS 741
Cdd:pfam05539 180 WPTEVSHPTYPSQVTPQSQPATQGHQTATANQRLS--STEPVGT-QGTTTS--SNPEPQTEPPPSQRGPSGSPQHPPSTT 254
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1264348865 742 DQGNTpppNNGNGQGNTPPPKSGSDQGN--------TPPPKSGSDQGNTPPPNngsgqgNTPSPKSGSDQGNTPPP 809
Cdd:pfam05539 255 SQDQS---TTGDGQEHTQRRKTPPATSNrrsphstaTPPPTTKRQETGRPTPR------PTATTQSGSSPPHSSPP 321
|
|
| PRK15319 |
PRK15319 |
fibronectin-binding autotransporter adhesin ShdA; |
756-802 |
2.05e-04 |
|
fibronectin-binding autotransporter adhesin ShdA;
Pssm-ID: 185219 [Multi-domain] Cd Length: 2039 Bit Score: 45.07 E-value: 2.05e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1264348865 756 GNTPPPKSGSDQGNTPPPKSGSDQGNTPPPNNGSGQGNTPSPKSGSD 802
Cdd:PRK15319 1676 GDDTPSDGGDDGGNVTPPDDGGDGGNVTPPDDGGDGGDVTPPDHGGD 1722
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
699-833 |
2.75e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 44.78 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 699 SEPNNGSDQGNTPPPKSGSDQG---NTPPPNNSNGQGNTPS-PKSGSDQGNTP-PPNNGNGQGNTPPPKSGSDQG-NTPP 772
Cdd:PHA03307 284 PASSSSSPRERSPSPSPSSPGSgpaPSSPRASSSSSSSRESsSSSTSSSSESSrGAAVSPGPSPSRSPSPSRPPPpADPS 363
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1264348865 773 PKSGSDQGNTPPPNNGSGQGNTPSPKSGSDQGNTPPPNNGDGHGT-----PPPPSNDGNIGEDPAN 833
Cdd:PHA03307 364 SPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPagrprPSPLDAGAASGAFYAR 429
|
|
| BimA_first |
NF040984 |
trimeric autotransporter actin-nucleating factor BimA; BimA (B. pseudomallei intracellular ... |
729-818 |
4.43e-04 |
|
trimeric autotransporter actin-nucleating factor BimA; BimA (B. pseudomallei intracellular motility protein A) is a trimeric autotransporter, homologous in its C-terminal half to a number of trimeric autotransporter adhesins. It is a virulence factor that nucleates actin, so that actin polymerization can drive escape by B. pseudomallei out of one cell and into a neighboring cell. HMM NF040983 describes a homolog with similar activity but substantial difference in sequence architecture in the N-terminal region.
Pssm-ID: 468914 [Multi-domain] Cd Length: 517 Bit Score: 43.71 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 729 NGQGNTPSPKSGSDQGNTPPPNNGNGQGNTPPPKSGSDqGNTPPPksgsdqgntPPPNNGSGqGNTPSPksgsdqgntPP 808
Cdd:NF040984 37 DAEANPPEPPGGTNIPVPPPMPGGGANIPVPPPMPGGG-ANIPPP---------PPPPGGIG-GATPSP---------PP 96
|
90
....*....|...
gi 1264348865 809 --PNNGD-GHGTP 818
Cdd:NF040984 97 ltPVNGNpGASTP 109
|
|
| Mucin-like |
pfam16058 |
Mucin-like; This region is found repeated at the C-terminus (C-tail) of bile salt-activated ... |
728-824 |
4.47e-04 |
|
Mucin-like; This region is found repeated at the C-terminus (C-tail) of bile salt-activated lipase, where is O-glycosylated. This region is composed of biased amino acid composition that is likely to be disordered. The region contains many repeats of an approximately 11 residue degenerate repeat.
Pssm-ID: 464997 [Multi-domain] Cd Length: 94 Bit Score: 40.10 E-value: 4.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 728 SNGQGNTPSPKSGSdqgNTPPPNNGNGQGNTPPPKSGSDQGNTPPPKSGSDqgnTPPPNNGSGQGNTPSPKSGSDQGNTP 807
Cdd:pfam16058 2 SSSITEPPRDPSGS---YGEPPRAPSSSYTEPQRDPSSSITEPPADPSSSY---TEPPRDPSGSYTEPQRDPSSSSTEPQ 75
|
90
....*....|....*..
gi 1264348865 808 PPNNGDGHGTPPPPSND 824
Cdd:pfam16058 76 RDPSSSITEPPRDPSGS 92
|
|
| pullulan_Gpos |
TIGR02102 |
pullulanase, extracellular, Gram-positive; Pullulan is an unusual, industrially important ... |
730-800 |
5.25e-04 |
|
pullulanase, extracellular, Gram-positive; Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although pullulan itself may not be the natural substrate. In contrast, a glycogen debranching enzyme such GlgX, homologous to this family, can release glucose at alpha,1-6 linkages from glycogen first subjected to limit degradation by phosphorylase. Characterized members of this family include a surface-located pullulanase from Streptococcus pneumoniae () and an extracellular bifunctional amylase/pullulanase with C-terminal pullulanase activity (.
Pssm-ID: 273973 [Multi-domain] Cd Length: 1111 Bit Score: 43.69 E-value: 5.25e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1264348865 730 GQGNTPSPKSGSDQGNTPPPNNGNGQGNTPPPKSGSDQGNTPPPKSGSDQGNTPPPNNGSGQGNTPS----PKSG 800
Cdd:TIGR02102 1009 APEKTPPPPEHEPQAPKPPTQDPDGSKPKDKVDPKDNKDPLTPPGSDDENGETPKGNEEKKEEQPDKganlPNTG 1083
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
710-833 |
5.65e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 43.62 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 710 TPPPKSGSDQGNTPPPnnsnGQGNTPSPKSGSD--QGNTPPPNNGNGQGNTPPPKSGSDQGNTPPPKSGsdqgnTPPPNN 787
Cdd:PHA03307 52 AVTVVAGAAACDRFEP----PTGPPPGPGTEAPanESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDP-----PPPTPP 122
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1264348865 788 GSGQGNTPSPKSGSDQGNTPPPNNGDGHGTPPPPSNDGNIGEDPAN 833
Cdd:PHA03307 123 PASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAAS 168
|
|
| PRK15319 |
PRK15319 |
fibronectin-binding autotransporter adhesin ShdA; |
768-812 |
5.90e-04 |
|
fibronectin-binding autotransporter adhesin ShdA;
Pssm-ID: 185219 [Multi-domain] Cd Length: 2039 Bit Score: 43.92 E-value: 5.90e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1264348865 768 GNTPPPKSGSDQGNTPPPNNGSGQGNTPSPKSGSDQGNTPPPNNG 812
Cdd:PRK15319 1676 GDDTPSDGGDDGGNVTPPDDGGDGGNVTPPDDGGDGGDVTPPDHG 1720
|
|
| pullulan_Gpos |
TIGR02102 |
pullulanase, extracellular, Gram-positive; Pullulan is an unusual, industrially important ... |
745-814 |
5.92e-04 |
|
pullulanase, extracellular, Gram-positive; Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although pullulan itself may not be the natural substrate. In contrast, a glycogen debranching enzyme such GlgX, homologous to this family, can release glucose at alpha,1-6 linkages from glycogen first subjected to limit degradation by phosphorylase. Characterized members of this family include a surface-located pullulanase from Streptococcus pneumoniae () and an extracellular bifunctional amylase/pullulanase with C-terminal pullulanase activity (.
Pssm-ID: 273973 [Multi-domain] Cd Length: 1111 Bit Score: 43.69 E-value: 5.92e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1264348865 745 NTPPPNNGNGQGNTPPPKSGSDQGNTPPPKSGSDQGNTPPPNNGSGQGNTP--SPKSGSDQG--NTPPPNNGDG 814
Cdd:TIGR02102 1012 KTPPPPEHEPQAPKPPTQDPDGSKPKDKVDPKDNKDPLTPPGSDDENGETPkgNEEKKEEQPdkGANLPNTGTK 1085
|
|
| Herpes_LMP1 |
pfam05297 |
Herpesvirus latent membrane protein 1 (LMP1); This family consists of several latent membrane ... |
701-831 |
6.37e-04 |
|
Herpesvirus latent membrane protein 1 (LMP1); This family consists of several latent membrane protein 1 or LMP1s mostly from Epstein-Barr virus. LMP1 of EBV is a 62-65 kDa plasma membrane protein possessing six membrane spanning regions, a short cytoplasmic N-terminus and a long cytoplasmic carboxy tail of 200 amino acids. EBV latent membrane protein 1 (LMP1) is essential for EBV-mediated transformation and has been associated with several cases of malignancies. EBV-like viruses in Cynomolgus monkeys (Macaca fascicularis) have been associated with high lymphoma rates in immunosuppressed monkeys
Pssm-ID: 283060 Cd Length: 386 Bit Score: 43.09 E-value: 6.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 701 PNNGSDQGNTPPPKSgSDQGNTPPPNNSNGQGNTPSPK---SGSDQGNTPPPNNGNGQGNTPPPKSGSDQgntpppkSGS 777
Cdd:pfam05297 245 PGGGPDNGPQDPDNT-DDNGPQDPDNTDDNGPHDPLPQdpdNTDDNGPQDPDNTADNGPHDPLPHNPSDS-------AGN 316
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1264348865 778 DQGntpPPN---NGSGQGNTPSPKSGSDQGNTPPPNNGDGHGTPPPP------SNDGNIGEDP 831
Cdd:pfam05297 317 DGG---PPNlteEVENKGGDQGPPLMTDGGGGHSHDSGHGGGDPHLPtlllgsSGSGGDDDDP 376
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
710-834 |
6.87e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 43.62 E-value: 6.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 710 TPPPKSGSDQGNTPPPNNSNGQGNTPSPKSGSDQGNTPPP----NNGNGQ---GNTPPPKSGSD---QGNTPPPKSGSDQ 779
Cdd:PHA03307 185 APSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPgrsaADDAGAsssDSSSSESSGCGwgpENECPLPRPAPIT 264
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1264348865 780 GNTPP----PNNGSGQGNTPSPKSGSDQGNTPP--PNNGDGHGTPPPPSNDGNIGEDPANN 834
Cdd:PHA03307 265 LPTRIweasGWNGPSSRPGPASSSSSPRERSPSpsPSSPGSGPAPSSPRASSSSSSSRESS 325
|
|
| PRK09418 |
PRK09418 |
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase; |
733-806 |
1.21e-03 |
|
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;
Pssm-ID: 236504 [Multi-domain] Cd Length: 780 Bit Score: 42.39 E-value: 1.21e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1264348865 733 NTPSPKSGSDQGNTPPPNNG-NGQGNTPPPKSGSDQGN--TPPPKSGSDQGNTPPPNNGSGQGNTPSPKSGSDQGNT 806
Cdd:PRK09418 656 NDDDKETGGENPTTPPTGEGdNGENPTTPPTGEGNNGEnpTTPPTGEGNNGGNPTTPSTDEGNNAGSGQTTTDNQNS 732
|
|
| dermokine |
cd21118 |
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ... |
729-830 |
1.35e-03 |
|
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.
Pssm-ID: 411053 [Multi-domain] Cd Length: 495 Bit Score: 42.29 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 729 NGQGNTPSPKSGSDQGNTPPPNNGNGQGNTPPPKSGSDQGNTPPPKSGSDQGNTPPPNNGS-GQGNTPSPKSGSDQGntp 807
Cdd:cd21118 119 NSWQGSGGHGAYGSQGGPGVQGHGIPGGTGGPWASGGNYGTNSLGGSVGQGGNGGPLNYGTnSQGAVAQPGYGTVRG--- 195
|
90 100
....*....|....*....|...
gi 1264348865 808 ppNNGDGHGTPPPPSNDGNIGED 830
Cdd:cd21118 196 --NNQNSGCTNPPPSGSHESFSN 216
|
|
| pullulan_Gpos |
TIGR02102 |
pullulanase, extracellular, Gram-positive; Pullulan is an unusual, industrially important ... |
709-793 |
1.94e-03 |
|
pullulanase, extracellular, Gram-positive; Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although pullulan itself may not be the natural substrate. In contrast, a glycogen debranching enzyme such GlgX, homologous to this family, can release glucose at alpha,1-6 linkages from glycogen first subjected to limit degradation by phosphorylase. Characterized members of this family include a surface-located pullulanase from Streptococcus pneumoniae () and an extracellular bifunctional amylase/pullulanase with C-terminal pullulanase activity (.
Pssm-ID: 273973 [Multi-domain] Cd Length: 1111 Bit Score: 41.77 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 709 NTPPPKSGSDQGNTPPpnnsngqgntpsPKSGSDQGNTPPPNNGNGQGNTPPPKSGSDQGNTP--PPKSGSDQG--NTPP 784
Cdd:TIGR02102 1012 KTPPPPEHEPQAPKPP------------TQDPDGSKPKDKVDPKDNKDPLTPPGSDDENGETPkgNEEKKEEQPdkGANL 1079
|
....*....
gi 1264348865 785 PNNGSGQGN 793
Cdd:TIGR02102 1080 PNTGTKNSN 1088
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
703-821 |
2.05e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.08 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 703 NGSDQGNTPPPKSGSDQGNTPPPNNSNGQGN---TPSPKSGSDQGNTPPPNNGNGQGNTPPPKSGSDQGNTPPPKSGSDQ 779
Cdd:PHA03307 80 PANESRSTPTWSLSTLAPASPAREGSPTPPGpssPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASP 159
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1264348865 780 GNTPPPNNGSGQGNTPSPK------SGSDQGNTPPPNNGDGHGTPPPP 821
Cdd:PHA03307 160 AAVASDAASSRQAALPLSSpeetarAPSSPPAEPPPSTPPAAASPRPP 207
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
706-832 |
2.19e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 41.51 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 706 DQGNTPPPKSGSDQGNTPPPNNSNGQGNTPSPKSGSDQGNTPPPNNGNGQGNTPPPKSGSDQGNTPPPKSGSDQGNTPPP 785
Cdd:PRK07764 630 AGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATP 709
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1264348865 786 NNGSGQGNTPSPKSGSDQGNTPPPNNGDGHGTPPPPSNDGNIGEDPA 832
Cdd:PRK07764 710 PAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPA 756
|
|
| PHA03419 |
PHA03419 |
E4 protein; Provisional |
712-831 |
2.65e-03 |
|
E4 protein; Provisional
Pssm-ID: 223079 [Multi-domain] Cd Length: 200 Bit Score: 39.93 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 712 PPKSGSDQGNTPPPNNSNGQgntPSPKSGSDQGNTP--PPNNGNGQGNTPPPKSGSDQGNTPPpksgsDQGNTPPPNngs 789
Cdd:PHA03419 53 PPTTPHPSSQPPPCPPSPGH---PPQTNDTHEKDLAlqPPPGGKKKEKKKKETEKPAQGGEKP-----DQGPEAKGE--- 121
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1264348865 790 GQGNTPspksgsdqgNTPPPNNgdghgTPPPPSNDGNIGEDP 831
Cdd:PHA03419 122 GEGHEP---------EDPPPED-----TPPPPGGEGEVEGGP 149
|
|
| PRK15319 |
PRK15319 |
fibronectin-binding autotransporter adhesin ShdA; |
699-752 |
3.37e-03 |
|
fibronectin-binding autotransporter adhesin ShdA;
Pssm-ID: 185219 [Multi-domain] Cd Length: 2039 Bit Score: 41.22 E-value: 3.37e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1264348865 699 SEPNNGSDQGNTPPPKSGSDQGNTPPPNNSNGQGNTPSPKSGSDQGNTPPPNNG 752
Cdd:PRK15319 1667 AQSDDDDSGGDDTPSDGGDDGGNVTPPDDGGDGGNVTPPDDGGDGGDVTPPDHG 1720
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
704-835 |
3.41e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 40.72 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 704 GSDQGNTPPPKSGSDQGNTPPPNNSNGQGNTPSPKSGSDQG--NTPPPNNGNGQGNTPPpkSGSDQGNTPPPKSGSDQGN 781
Cdd:PHA03169 105 PSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGphEPAPPESHNPSPNQQP--SSFLQPSHEDSPEEPEPPT 182
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1264348865 782 TPPPNNGSGQGNTPSPKSGSDQGNTP----PPNNGDGHGTPPPPSNDGNIGED-PANNE 835
Cdd:PHA03169 183 SEPEPDSPGPPQSETPTSSPPPQSPPdepgEPQSPTPQQAPSPNTQQAVEHEDePTEPE 241
|
|
| Herpes_LMP1 |
pfam05297 |
Herpesvirus latent membrane protein 1 (LMP1); This family consists of several latent membrane ... |
700-831 |
3.61e-03 |
|
Herpesvirus latent membrane protein 1 (LMP1); This family consists of several latent membrane protein 1 or LMP1s mostly from Epstein-Barr virus. LMP1 of EBV is a 62-65 kDa plasma membrane protein possessing six membrane spanning regions, a short cytoplasmic N-terminus and a long cytoplasmic carboxy tail of 200 amino acids. EBV latent membrane protein 1 (LMP1) is essential for EBV-mediated transformation and has been associated with several cases of malignancies. EBV-like viruses in Cynomolgus monkeys (Macaca fascicularis) have been associated with high lymphoma rates in immunosuppressed monkeys
Pssm-ID: 283060 Cd Length: 386 Bit Score: 40.40 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 700 EPNNGSDQGNTPPPKSGSdqGNTPPPNNSN------GQGNTPSPKSGSDQGNTPPPNNGNGQGNTPP----PKSGSDQGN 769
Cdd:pfam05297 214 ESDSNSNEGRHHLLVSGA--GDGPPLCSQNlgapggGPDNGPQDPDNTDDNGPQDPDNTDDNGPHDPlpqdPDNTDDNGP 291
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1264348865 770 TPPPKSGSDQGNTPPPNNGS-GQGNTPSP--------KSGSDQGntpPPNNGDGHGTPPPPSNDGniGEDP 831
Cdd:pfam05297 292 QDPDNTADNGPHDPLPHNPSdSAGNDGGPpnlteeveNKGGDQG---PPLMTDGGGGHSHDSGHG--GGDP 357
|
|
| Pro-rich |
pfam15240 |
Proline-rich protein; This family includes several eukaryotic proline-rich proteins. |
725-823 |
4.86e-03 |
|
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
Pssm-ID: 464580 [Multi-domain] Cd Length: 167 Bit Score: 38.87 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 725 PNNSNGQGNTPSPKSGsDQGNTPPPNNGNgQGntPPPksgsdqGNTPPPKSGSDQGNTPPPNNGSGQ-----GNT----- 794
Cdd:pfam15240 19 SSEDVSQEDSPSLISE-EEGQSQQGGQGP-QG--PPP------GGFPPQPPASDDPPGPPPPGGPQQpppqgGKQkpqgp 88
|
90 100 110
....*....|....*....|....*....|....
gi 1264348865 795 -----PSPKSGSDQGntPPPNNGDGHGTPPPPSN 823
Cdd:pfam15240 89 ppqggPRPPPGKPQG--PPPQGGNQQQGPPPPGK 120
|
|
| Drf_FH1 |
pfam06346 |
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ... |
711-795 |
6.66e-03 |
|
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.
Pssm-ID: 461881 [Multi-domain] Cd Length: 157 Bit Score: 38.31 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 711 PPPKSGSDQGNTPPP-NNSNGQGNTPSPKSGSDQGNTPPPNNGNGQGNTPPPKSGSDQGnTPPPKSGsdQGNTPPPNNGS 789
Cdd:pfam06346 72 PPPLPGSTGIPPPPPlPGGAGIPPPPPPLPGGAGVPPPPPPLPGGPGIPPPPPFPGGPG-IPPPPPG--MGMPPPPPFGF 148
|
....*.
gi 1264348865 790 GQGNTP 795
Cdd:pfam06346 149 GVPAAP 154
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
651-820 |
6.94e-03 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 40.14 E-value: 6.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 651 SVVQEGSE--LRIKGEKRDSPPNTKIVNTTEQPSENKQKEKQKKLEEQKQSEPNNGSDQGNTPPPKSGSDQGNTPPPNNS 728
Cdd:pfam03154 125 SVNDEGSSdpKDIDQDNRSTSPSIPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAP 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 729 N--GQGNTPSPKSGSDQGNTPPPNNGNGQGNT------PPPKSGSDQGNTPPPKSGSDQGNTPPPN-NGSGQ-------- 791
Cdd:pfam03154 205 SvpPQGSPATSQPPNQTQSTAAPHTLIQQTPTlhpqrlPSPHPPLQPMTQPPPPSQVSPQPLPQPSlHGQMPpmphslqt 284
|
170 180
....*....|....*....|....*....
gi 1264348865 792 GNTPSPKSGSDQGNTPPPNNGDGHGTPPP 820
Cdd:pfam03154 285 GPSHMQHPVPPQPFPLTPQSSQSQVPPGP 313
|
|
| PRK15319 |
PRK15319 |
fibronectin-binding autotransporter adhesin ShdA; |
780-828 |
7.28e-03 |
|
fibronectin-binding autotransporter adhesin ShdA;
Pssm-ID: 185219 [Multi-domain] Cd Length: 2039 Bit Score: 40.07 E-value: 7.28e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1264348865 780 GNTPPPNNGSGQGNTPSPKSGSDQGNTPPPNNGDGHGTPPPPSNDGNIG 828
Cdd:PRK15319 1676 GDDTPSDGGDDGGNVTPPDDGGDGGNVTPPDDGGDGGDVTPPDHGGDVA 1724
|
|
| SOBP |
pfam15279 |
Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual ... |
699-822 |
8.42e-03 |
|
Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual disability. It carries a zinc-finger of the zf-C2H2 type at the N-terminus, and a highly characteriztic C-terminal PhPhPhPhPhPh motif. The deduced 873-amino acid protein contains an N-terminal nuclear localization signal (NLS), followed by 2 FCS-type zinc finger motifs, a proline-rich region (PR1), a putative RNA-binding motif region, and a C-terminal NLS embedded in a second proline-rich motif. SOBP is expressed in various human tissues, including developing mouse brain at embryonic day 14. In postnatal and adult mouse brain SOBP is expressed in all neurons, with intense staining in the limbic system. Highest expression is in layer V cortical neurons, hippocampus, pyriform cortex, dorsomedial nucleus of thalamus, amygdala, and hypothalamus. Postnatal expression of SOBP in the limbic system corresponds to a time of active synaptogenesis. the family is also referred to as Jackson circler, JXC1. In seven affected siblings from a consanguineous Israeli Arab family with mental retardation, anterior maxillary protrusion, and strabismus mutations were found in this protein.
Pssm-ID: 464609 [Multi-domain] Cd Length: 325 Bit Score: 39.41 E-value: 8.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 699 SEPNNGSDQGNTP--PPKSGSDQGNTPPPNNSN---------GQGNTPSP---KSGSDQGNTPPPNNGNGQGNTPPPKSG 764
Cdd:pfam15279 149 HRPGLHPPLGRPPgsPPMSMTPRGLLGKPQQHPppsplpafmEPSSMPPPflrPPPSIPQPNSPLSNPMLPGIGPPPKPP 228
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1264348865 765 SDQGntpPPKSGSDQ---GNTPPPNNGSGQGNTPSPKsgsdqgnTPPPNNGDGHGTPPPPS 822
Cdd:pfam15279 229 RNLG---PPSNPMHRppfSPHHPPPPPTPPGPPPGLP-------PPPPRGFTPPFGPPFPP 279
|
|
| PTZ00441 |
PTZ00441 |
sporozoite surface protein 2 (SSP2); Provisional |
701-835 |
8.51e-03 |
|
sporozoite surface protein 2 (SSP2); Provisional
Pssm-ID: 240420 [Multi-domain] Cd Length: 576 Bit Score: 39.56 E-value: 8.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 701 PNNgsDQGNTPPPKSGSDqGN------TPP-----PNNSNGQGNTPSPKSGSDQ------GNTPPPNNGNGQGNTPPPKS 763
Cdd:PTZ00441 323 PDN--PQDPVPPPNEGKD-GNpneenlFPPgddevPDESNVPPNPPNVPGGSNSefssdvENPPNPPNPDIPEQEPNIPE 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 764 GSDQGNTP-----PPKSGSDQGNTP--PPNNGSGQGNTPSPKSGSDQGNTPPPNNGDGHG---------TPPPPSNDGNI 827
Cdd:PTZ00441 400 DSNKEVPEdvpmePEDDRDNNFNEPkkPENKGDGQNEPVIPKPLDNERDQSNKNKQVNPGnrhnsedryTRPHGRNNENR 479
|
....*...
gi 1264348865 828 GEDPANNE 835
Cdd:PTZ00441 480 NYNNKNSD 487
|
|
| PBP1 |
COG5180 |
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ... |
634-824 |
9.03e-03 |
|
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];
Pssm-ID: 444064 [Multi-domain] Cd Length: 548 Bit Score: 39.66 E-value: 9.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 634 EMMSKFATDKSQFKMPNSVVQEGSELRIKGEKRDSPPNTKIVNTTEQPSENKQKEKQKkleeqkqsePNNGSDQGNTPpp 713
Cdd:COG5180 284 EAGSEPQSDAPEAETARPIDVKGVASAPPATRPVRPPGGARDPGTPRPGQPTERPAGV---------PEAASDAGQPP-- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 714 kSGSDQGNTPPPNNsNGQGNTPSPksGSDQGNTPPPNNGNGQgntPPPKSGSDQGNTPPPKSGsDQGNTPPPNNGSGQGN 793
Cdd:COG5180 353 -SAYPPAEEAVPGK-PLEQGAPRP--GSSGGDGAPFQPPNGA---PQPGLGRRGAPGPPMGAG-DLVQAALDGGGRETAS 424
|
170 180 190
....*....|....*....|....*....|...
gi 1264348865 794 TPSPKSGSDQGNTPPPNNGDGH--GTPPPPSND 824
Cdd:COG5180 425 LGGAAGGAGQGPKADFVPGDAEsvSGPAGLADQ 457
|
|
| PRK10856 |
PRK10856 |
cytoskeleton protein RodZ; |
717-809 |
9.30e-03 |
|
cytoskeleton protein RodZ;
Pssm-ID: 236776 [Multi-domain] Cd Length: 331 Bit Score: 39.24 E-value: 9.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264348865 717 SDQGNTPPP-NNSNGQGNTPSPKSGSDQGNTPPPNNGNGQGNTPPPKSGSDQGNTPPPKSGSDQGNTPPPNNGSGQGNTP 795
Cdd:PRK10856 155 SQNSGQSVPlDTSTTTDPATTPAPAAPVDTTPTNSQTPAVATAPAPAVDPQQNAVVAPSQANVDTAATPAPAAPATPDGA 234
|
90
....*....|....
gi 1264348865 796 SPKSGSDQGNTPPP 809
Cdd:PRK10856 235 APLPTDQAGVSTPA 248
|
|
| |
