|
Name |
Accession |
Description |
Interval |
E-value |
| cas_Csn1 |
TIGR01865 |
CRISPR subtype II/NMENI RNA-guided endonuclease Cas9/Csn1; CRISPR loci appear to be mobile ... |
43-1089 |
0e+00 |
|
CRISPR subtype II/NMENI RNA-guided endonuclease Cas9/Csn1; CRISPR loci appear to be mobile elements with a wide host range. This model represents a protein found only in CRISPR-containing species, near other CRISPR-associated proteins (cas), as part of the NMENI subtype of CRISPR/Cas locus. The species range so far for this protein is animal pathogens and commensals only.
Pssm-ID: 273840 Cd Length: 805 Bit Score: 924.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 43 KYSIGLDIGTNSVGWAVITDEYKVPSKKFKVLGNtdrhsiKKNLIGALLFDSGETAE-ATRLKRTARRRYTRRKNRICYL 121
Cdd:TIGR01865 1 EYILGLDIGIASVGWAIVEDDYKVPAAKRLIDGG------VRNFTGAELPKTGETAAlDRRLARGARRRIRRRKHRLLRL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 122 QEIFSNEMAKVDDSFFHRLEESFLVEEDKKHerhpifgnivdevayhekypTIYHLRKKLVDSTDKADLrlIYLALAHMI 201
Cdd:TIGR01865 75 QELFSREGSLTDFDFFSRLENSFLVEEDKRN--------------------TIYHLRKAALENKLKPDE--LYLALLHII 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 202 KFRGHFLIEgdlnpdnsdvdklfiqlvqtynqlfeenpinasgvdakailsarlsksrrlenliaqlpgekknglfgnli 281
Cdd:TIGR01865 133 KHRGHFLIE----------------------------------------------------------------------- 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 282 alslgltpnfksnfdlaedaklqlskdtyDDDLDnllaqigdqyadlflaaknlsdaillsdilrVNTEITKAPLSASMI 361
Cdd:TIGR01865 142 -----------------------------GNDFD-------------------------------TANKETGALLSAVMI 161
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 362 KRYDEHHQDLTLLKALVRQQLPEKYKEIFFDqskngyagyidggasqeefykfikpilekmdgteellvklnreDLLRKQ 441
Cdd:TIGR01865 162 NRYLEHEADLRTLKELILKKFPKKYKEIFSE-------------------------------------------TFLRNQ 198
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 442 RTFDNGSIPHQIHLGELHAILRRQEDFYPFlkdnrekiEKILTFRIPYYVGPLARGNSRFAwmtrkseetitpwnfeeVV 521
Cdd:TIGR01865 199 RGFYNGSIPRQLLLEELEAIFRKQREYYPF--------IKLLTFRIPYYIGPLAEGKSEFA-----------------FV 253
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 522 DKGASAQSFIERMTNFDKNLPNEKVLPKHSLLYEYFTVYNELTKVKYVTEGMRKPAFLSGEQKKAIVDLLFKTNRKVTVK 601
Cdd:TIGR01865 254 DKPASAENFIEKMTGKCTYLPEEKRAPKHSLLAEKFTVLNELNNVRIIILEQGETKILSKEEKQELLDLLFKKKKLTYKK 333
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 602 QLKEDYFKKIECFDSVEISGVEDR---FNASLGTYHDLLKIIKDKDFLDNEENEDILEDIVLTLTLFEDREMIEERLKTY 678
Cdd:TIGR01865 334 LRKLLGLSEDAIFKGLRYEGLDNAekaFNISLKTYHKLRKALGDKDLLDNPKNPKDLDEIVKILTLYKDREMIKKRLELY 413
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 679 AHLFDDKVMKQLKRRRYTGWGRLSRKLINGIRDKQSGKTILDFLKSDGFANRNFMQLIHDDSLTFKEDIQKAqvsgqgds 758
Cdd:TIGR01865 414 KDVLNEEQVKKLVRLHFTGWGRLSLKALRGIRPLMEQGKRYDEAILELGGNRNFMQNINDSQLLPKINITKA-------- 485
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 759 lhehiANLAGSPAIKKGILQTVKVVDELVKVMGrhKPENIVIEMARENQTTQKGQKNSRERMKRIEEGIKELGS----QI 834
Cdd:TIGR01865 486 -----KDEILNPVVKRALLQARKVVNELVKKYG--PPDKIVIEMAREEQGTNFGKRNSKERYKKNEDKIKEFASalgkEI 558
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 835 LKEHPVENTQLQNEKLYLYYLQNGRDMYVDQELDINRL---SDYDVDHIVPQSFLKDDSIDNKVLTRSDKNRGKSDNVPS 911
Cdd:TIGR01865 559 LKEEPTENSSKNILKLRLYYQQNGKCMYTGKEIDIDDLfdlSYYEIDHILPQSRSFDDSISNKVLVLASENQEKGDQTPY 638
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 912 E-EVVKKMKNYWRQLLNAKLITQRKFDNLTKAERGGLSELDKAGFIKRQLVETRQITKHVAQILDSRMNTKYDendklIR 990
Cdd:TIGR01865 639 EaEIVKKDSAFWNKFEAYVLISKRKSDKLTRAERGGLSDDDKAGFIDRNLNDTRYITRVVANYLKDRFNFHLK-----KR 713
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 991 EVKVITLKSKLVSDFRKDFQFYKVREINNYHHAHDAYLNAVVGTALIKKYPKLESEFVYGDYKVYDVRKMIAkseqeigK 1070
Cdd:TIGR01865 714 KVKVVTLKGQLTSQLRKKWGLYKKREINNYHHAHDAYINAVSTNALVKKFSQLEPEFRYKEYHNFDGRKKKK-------S 786
|
1050
....*....|....*....
gi 1682072386 1071 ATAKYFFYSNIMNFFKTEI 1089
Cdd:TIGR01865 787 ATDKKVKFSNPMEFFKQKV 805
|
|
| Csn1 |
cd09643 |
CRISPR/Cas system-associated protein Cas9; CRISPR (Clustered Regularly Interspaced Short ... |
43-1088 |
0e+00 |
|
CRISPR/Cas system-associated protein Cas9; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Very large protein containing McrA/HNH-nuclease related domain and a RuvC-like nuclease domain; signature gene for type II
Pssm-ID: 187774 [Multi-domain] Cd Length: 799 Bit Score: 909.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 43 KYSIGLDIGTNSVGWAVITDEYKVPSKKFKvlgntdrHSIKKNLIGALLFDSGETAE-ATRLKRTARRRYTRRKNRICYL 121
Cdd:cd09643 1 EYILGLDIGIASVGWAIVEDDYKVPAKKMI-------DCGVKIFTGAELFKTGETAAlDRRLARGARRRIRRRKHRLLRL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 122 QEIFSNEMAKVDDSFFHRLEESFLveedkkherhpifgnivdevAYHEKYPTIYHLRKKLVDSTDKADLrlIYLALAHMI 201
Cdd:cd09643 74 QELFAREGSLTDFDFFSRLEDSFL--------------------EYHKNYPTIYHLRKAALENKLKPDE--LYLALLHII 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 202 KFRGHFLIEGDLNPDNsdvdklfiqlvqtynqlfeenpinasgvdakailsarlsksrrlenliaqlpgekknglfgnli 281
Cdd:cd09643 132 KHRGHFLIEGDEDTTA---------------------------------------------------------------- 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 282 alslgltpnfksnfdlaedaklqlskdtydddldnllaqigdqyadlflaaknlsdaillsdilrvnTEITKAPLSASMI 361
Cdd:cd09643 148 -------------------------------------------------------------------DKETGALLSASMI 160
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 362 KRYDEHHQDLTLLKALVRQQLPEKYKEIFFDqskngyagyidggasqeefykfikpilekmdgteellvklnrEDLLRKQ 441
Cdd:cd09643 161 KRYDEHKADLRKLKELIKKEFFKKYKEIFGD------------------------------------------ETFLRNQ 198
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 442 RTFDNGSIPHQIHLGELHAILRRQEDFYPFlkdnrekiEKILTFRIPYYVGPLARGNSRFAWMTRKSEEtitpwnfeevv 521
Cdd:cd09643 199 RGFYNGSIPRQLLLEELEAIFRKQREYYPF--------EKILTFRIPYYIGPLAEGKSEFAWLTRPALS----------- 259
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 522 dkgasaQSFIERMTNFDKNLPNEKVLPKHSLLYEYFTVYNELTKVKYVTEgMRKPAFLSGEQKKAIVDLLFKTNRKVTVK 601
Cdd:cd09643 260 ------EAFIEKMTGKCTYLPEEKRAPKHSLLAEKFTVLNELNNLRIIEE-QGETKILSKEEKQELLDLLFKKNKLTYKQ 332
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 602 QLKEDYFKKIECFDSVEISG--VEDRFNASLGTYHDLLKIIKDKDFLDNEENEDILEDIVLTLTLFEDREMIEERLKTYA 679
Cdd:cd09643 333 KRKLLGLKEEEIFKGLRYEGlkAEKNFNISLKTYHDLRKALGKEFLKDLELNEKILDEIVKILTLYKDREMIEKILELYK 412
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 680 HLFDDKVMKQLKRRRYTGWGRLSRKLINGIRDKQSGKTILDFLKSDGFANRNfmQLIHDDSLTFKEDIQKAQVsgqgdsl 759
Cdd:cd09643 413 DLLNEEQLKKLLKRHFTGWGRLSLKALRGIRPLMEQGKRYDEAILELGGNHN--QKINSDELKFLPIIKKAQV------- 483
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 760 hehiANLAGSPAIKKGILQTVKVVDELVKVMGrhKPENIVIEMARENQtTQKGQKNSRERMKRIEEGIKELGS---QILK 836
Cdd:cd09643 484 ----KDEILNPVVKRALLQARKVVNELVKKYG--PPDKIVIEMARENG-TNKGTKNRKKRQKKNEDNIKEAASaleQKLK 556
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 837 EHPVENTQLQNEKLYLYYLQNGRDMYVDQELDINRL---SDYDVDHIVPQSFLKDDSIDNKVLTRSDKNRGKSDNVPSEE 913
Cdd:cd09643 557 ELPLDIKSKNILKLRLYYQQNGKCMYTGKEIDIDDLfdlSYYEIDHILPQSRSFDDSISNKVLVLASENQEKGDQTPYEE 636
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 914 VVKKMKNYWRQLLNAKLITQR---KFDNLtKAERgGLSELDKAGFIKRQLVETRQITKHVAQILDSRMNTKYDendklIR 990
Cdd:cd09643 637 IVSKMSAFWNKLEAAKLISQRgdsKKDRL-LLEK-GISDDEKAGFIDRNLNDTRYITRVVANYLKDRFNFHLK-----KR 709
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 991 EVKVITLKSKLVSDFRKDFQFYKVREINNYHHAHDAYLNAVVGTALIKKYPKLEsefVYGDYKVYDVRKMIAKSEQEIgk 1070
Cdd:cd09643 710 KVKVVTLKGQLTSQLRKKWGLYKKREINNYHHAHDAYINAVVTNALVKKFSQLE---RYKEYKRFDSEKGNKKTLDEN-- 784
|
1050
....*....|....*...
gi 1682072386 1071 ataKYFFYSNIMNFFKTE 1088
Cdd:cd09643 785 ---KKFFFANPMNFFKQE 799
|
|
| PTZ00164 |
PTZ00164 |
bifunctional dihydrofolate reductase-thymidylate synthase; Provisional |
1449-2058 |
0e+00 |
|
bifunctional dihydrofolate reductase-thymidylate synthase; Provisional
Pssm-ID: 240299 [Multi-domain] Cd Length: 514 Bit Score: 860.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1449 SQKPVCLVVAMTPKRGIGINNGLPWpHLTTDFKHFRRVTKTTPEEASrlngwlprkfaktgdsglpsPSVGKRFNAVVMG 1528
Cdd:PTZ00164 6 SLKDFSIVVAVTLKRGIGIGNSLPW-HIPEDMKFFSKITTYVREEKY--------------------EKSPKKQNAVIMG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1529 RKNWESMPRKFRPLVDRLNIVVSSSLKEEdiaaekpqaEGQQRVRVCASLPAALSLLEEEykDSVDQIFVVGGAGLYEAA 1608
Cdd:PTZ00164 65 RKTWESIPKKFRPLKNRINVVLSRTLTEE---------EADPGVLVFGSLEDALRLLAED--LSIEKIFIIGGASVYREA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1609 LSLGVASHLYITRVAREFPCDVFFPAFPGDDILSNKstaaqaaapaesvfvpfcpelgrekdneatyrpifISKTFSDNG 1688
Cdd:PTZ00164 134 LSANLLDKIYLTRVNSEYECDVFFPKIPESFFIVAI-----------------------------------VSQTFSTNG 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1689 VPYDFVVLEKRRKTDDAATAEPsnamssltstrettpvhglqapssaaaiapvLAWMDEEDRKKREQKELIRAVPHVHFR 1768
Cdd:PTZ00164 179 TSYDFVIYEKKNDDEEDLLGKI-------------------------------FGQMKMTGRKKSPKEQLYKACPSLKIR 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1769 GHEEFQYLDLIADIINNGRTMDDRTGVGVISKFGCTMRYSLDQAFPLLTTKRVFWKGVLEELLWFIRGDTNANHLSEKGV 1848
Cdd:PTZ00164 228 EHEEFQYLDLIADIIKNGNVKEDRTGVGTISKFGYQMRFDLRESFPLLTTKKVFLRGIIEELLWFIRGETNGNLLLDKGV 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1849 KIWDKNVTREFLDSRNLPHREVGDIGPGYGFQWRHFGAAYKDMHTDYTGQGVDQLKNVIQMLRTNPTDRRMLMTAWNPAA 1928
Cdd:PTZ00164 308 RIWEGNGSREFLDSRGLTHREENDLGPVYGFQWRHFGAEYKDMHDDYTGQGVDQLKNIIETIKNNPDDRRLILTAWNPSA 387
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1929 LDEMALPPCHLLCQFYVNDQKeLSCIMYQRSCDVGLGVPFNIASYSLLTLMVAHVCNLKPKEFIHFMGNTHVYTNHVEAL 2008
Cdd:PTZ00164 388 LDQMALPPCHLLSQFYVNDGK-LSCMMYQRSCDMGLGVPFNIASYALLTHMIAQVCGLRPGEFVHFLGDAHVYSNHVDAL 466
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1682072386 2009 KEQLRREPRPFPIVNILNKerIKEIDDFTAEDFEVVGYVPHGRIQMEMAV 2058
Cdd:PTZ00164 467 KEQLERVPYPFPTLKLKRE--VENIEDFTIEDIEVIGYVPHPKIKMEMAV 514
|
|
| Cas9_REC |
pfam16592 |
REC lobe of CRISPR-associated endonuclease Cas9; The REC lobe of Cas9 - the CRISPR-associated ... |
220-749 |
0e+00 |
|
REC lobe of CRISPR-associated endonuclease Cas9; The REC lobe of Cas9 - the CRISPR-associated endonuclease Cas9 - includes the REC1 and REC2 domains. REC1 forms an elongated, alpha-helical structure consisting of 25 alpha helices and two beta-sheets, whereas REC2 inserted within REC1 adopts a six-helix bundle structure. The REC lobe and the NUC lobe of Cas9 fold to present a positively charged groove at their interface which accommodates the negatively charged sgRNA:target DNA heteroduplex. CRISPR (clustered regularly interspaced short palindromic repeat)-Cas system occurs naturally in bacteria as a defence against invasion by phages or other mobile genetic elements. Cas9 is targeted to specific genomic locations by sgRNAs or single guide RNAs, in order to complex with invading DNA in order to cleave it and render it inactive.
Pssm-ID: 435447 Cd Length: 539 Bit Score: 589.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 220 VDKLFIQLVQTYNQLFEENPINASGVDAKAILSA-RLSKSRRLENLIAQLPGEK-KNGLFGNLIALSLGLTPNFKSNFDL 297
Cdd:pfam16592 1 VEESFQDLLNILYEQLENLELETQNVEIEKILKKtKISKKAKLDELLALPPNEKnSKKIFAEILKLILGNKADFTKIFEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 298 ------AEDAKLQLSKDTYDDDLDNLLAQIGDQYADLFLAAKNLSDAILLSDILRVNTEITKAPLSASMIKRYDEHHQDL 371
Cdd:pfam16592 81 ekfveePKKIKLSFSDSNYDEKIEELENQLGDEKAEIILILKKIYDWVVLSDILTVSTDNGKAYLSEAMVNRYDKHKEDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 372 TLLKALVRQQLPEKYKEIFFDQSKNGYAGYID----GGASQEEFYKFIKPILEKMDGTE--ELLVKLNREDLLRKQRTFD 445
Cdd:pfam16592 161 AQLKKVIKQNLSEKYNDMFRKEKKKGYSAYINgknnGKTSKEDFYKYIKKLINKVETSEaqYILSKIDNENFLPKQRTKS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 446 NGSIPHQIHLGELHAILRRQEDFYPFLKDNREKIEKILTFRIPYYVGPLARGNSRFAWMTRKSEETITPWNFEEVVDKGA 525
Cdd:pfam16592 241 NGSIPYQVHLQELKKIIKNQAEYYPFLKENQEKILKLLTFRIPYYVGPLAEKKSKFAWMKRKEQGKIYPWNFEQKVDIDK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 526 SAQSFIERMTNFDKNLPNEKVLPKHSLLYEYFTVYNELTKVKYVTEgmrkpaFLSGEQKKAIVDLLFKTNRKVTVKQLKE 605
Cdd:pfam16592 321 TAEAFITRMTNYCTYLPDEKVLPKNSLLYSKFTVLNELNKIKINGE------KISVELKQDIFNGLFKKNKKVTKKKLKD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 606 DYFKKIECFDSVEISGV--EDRFNASLGTYHDLLKIIkdKDFLDNEENEDILEDIVLTLTLFEDREMIEERL-KTYAHLF 682
Cdd:pfam16592 395 WLVKEGYNFKAVEIKGFdkENNFNNSLTTYIDLAKIF--GDFLDNPDNEDIIEDIIYWLTLFEDRKILKRRLqKKYSNLL 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 683 DDKVMKQLKRRRYTGWGRLSRKLINGIRDKQS---GKTILDFLKSDgfaNRNFMQLIHDDSLTFKEDIQK 749
Cdd:pfam16592 473 TEKQIKQILKLKYKGWGRLSKELLNGIRGADRqgeIKTIIDLLWND---NRNLMQLINDERLSFKEEIEK 539
|
|
| Thymidylat_synt |
pfam00303 |
Thymidylate synthase; This is a family of proteins that are flavin-dependent thymidylate ... |
1774-2054 |
2.39e-153 |
|
Thymidylate synthase; This is a family of proteins that are flavin-dependent thymidylate synthases.
Pssm-ID: 459753 Cd Length: 259 Bit Score: 474.60 E-value: 2.39e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1774 QYLDLIADIINNGRTMDDRTGVGVISKFGCTMRYSL-DQAFPLLTTKRVFWKGVLEELLWFIRGDTNANHLSEKGVKIWD 1852
Cdd:pfam00303 2 QYLDLLRDILENGTEKEDRTGTGTLSVFGYQMRFDLsDGEFPLLTTKKVFWKSIIHELLWFLRGDTNIKYLQENGVHIWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1853 knvtrEFLDsrnlphrEVGDIGPGYGFQWRHFGAaykdmhtdYTGQGVDQLKNVIQMLRTNPTDRRMLMTAWNPAALDEM 1932
Cdd:pfam00303 82 -----EWAD-------ENGDLGPVYGFQWRHWGA--------PDGGGIDQLAQVIDQLKNNPDSRRIIVSAWNPADLPKM 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1933 ALPPCHLLCQFYVNDqKELSCIMYQRSCDVGLGVPFNIASYSLLTLMVAHVCNLKPKEFIHFMGNTHVYTNHVEALKEQL 2012
Cdd:pfam00303 142 ALPPCHYLFQFYVDG-GKLSCQLYQRSADVFLGVPFNIASYALLTHMIAQVTGLEPGEFVHTIGDAHIYDNHVEQVKEQL 220
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1682072386 2013 RREPRPFPIVNILNKeriKEIDDFTAEDFEVVGYVPHGRIQM 2054
Cdd:pfam00303 221 TREPRPLPKLKINRK---VSIFDFTFEDFELEGYQPHPKIKA 259
|
|
| ThyA |
COG0207 |
Thymidylate synthase [Nucleotide transport and metabolism]; Thymidylate synthase is part of ... |
1774-2058 |
2.59e-139 |
|
Thymidylate synthase [Nucleotide transport and metabolism]; Thymidylate synthase is part of the Pathway/BioSystem: Thymidylate biosynthesis
Pssm-ID: 439977 Cd Length: 264 Bit Score: 434.92 E-value: 2.59e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1774 QYLDLIADIINNGRTMDDRTGVGVISKFGCTMRYSLDQAFPLLTTKRVFWKGVLEELLWFIRGDTNANHLSEKGVKIWDK 1853
Cdd:COG0207 3 QYLDLLRHILEEGTWKEDRTGTGTLSVFGYQMRFDLSEGFPLLTTKKVHWKSIIHELLWFLRGDTNIRYLRENGVKIWDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1854 NVTREfldsrnlphrevGDIGPGYGFQWRHFGAAykdmhtdyTGQGVDQLKNVIQMLRTNPTDRRMLMTAWNPAALDEMA 1933
Cdd:COG0207 83 WADEN------------GDLGPVYGKQWRSWPTP--------DGGTIDQIAQVIDQLKTNPDSRRLIVSAWNPAELDEMA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1934 LPPCHLLCQFYVNDQKeLSCIMYQRSCDVGLGVPFNIASYSLLTLMVAHVCNLKPKEFIHFMGNTHVYTNHVEALKEQLR 2013
Cdd:COG0207 143 LPPCHALFQFYVADGK-LSCQLYQRSADVFLGVPFNIASYALLTHMVAQVTGLEPGEFVHTIGDAHIYLNHLEQVKEQLS 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1682072386 2014 REPRPFPIVNILNKerIKEIDDFTAEDFEVVGYVPHGRIQMEMAV 2058
Cdd:COG0207 222 REPRPLPKLKINPK--VKSIFDFTFEDFELEGYDPHPAIKAPVAV 264
|
|
| Cas9 |
COG3513 |
CRISPR-Cas system type-II protein Cas9 [Defense mechanisms]; CRISPR-Cas system type-II protein ... |
42-1169 |
1.38e-130 |
|
CRISPR-Cas system type-II protein Cas9 [Defense mechanisms]; CRISPR-Cas system type-II protein Cas9 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 442735 [Multi-domain] Cd Length: 812 Bit Score: 432.08 E-value: 1.38e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 42 KKYSIGLDIGTNSVGWAVITDEYKVpskkfkvlgntdrHSIKKNLIGALLFDSGET-------AEATRLKRTARRRYTRR 114
Cdd:COG3513 2 DKYILGLDLGINSVGWAVLELDEDG-------------EPGEIIDAGVRIFDDGEDpksgeslAAARREARGARRRRRRR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 115 KNRICYLQEIFSNEMakvddsffhrleesFLVEEDKKHERHPifgnivdevayhekYPTIYHLRKKLVDstDKADLRLIY 194
Cdd:COG3513 69 KHRLRRLKRLLVEEG--------------LLPADDAERKALL--------------PLNPYELRAKALD--EKLSPEELG 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 195 LALAHMIKFRGHfliegdLNPDNSDVDKLfiqlvqtynqlfeenpinasgvDAKAILSARLSKSRRLENLIAQLPGEkkn 274
Cdd:COG3513 119 RALFHLAQRRGF------KSNRKTDSKDN----------------------ESGKVKDAIKELRERLEAKGARTVGE--- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 275 glfgnlialslgltpnfksnfdlaedaklqlskdtydddldnllaqigdqyadlFLAaknlsdaillsdilrvnteitka 354
Cdd:COG3513 168 ------------------------------------------------------YLY----------------------- 170
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 355 plsasmiKRYDEHHQdltllkalvrqqlpekykeiffdqskngyagyidggasqeefykfikpilekmdgteellvklnr 434
Cdd:COG3513 171 -------RRLQENGK----------------------------------------------------------------- 178
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 435 edlLRKQRTFDNGSIPHQIHLGELHAILRRQEDFYPFLKDN--REKIEKILTFRIPYYVGplargnsrfawmtrkseeti 512
Cdd:COG3513 179 ---VRNRKGDYDFYIPREDLEDEFEAIWAAQAEFGPALLTEelRDELLEIIFFQRPLKSG-------------------- 235
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 513 tpwnfeevvdkgasaqsfiERMTNFDKNLPNEKVLPKHSLLYEYFTVYNELTKVKYVTEGmRKPAFLSGEQKKAIVDLLF 592
Cdd:COG3513 236 -------------------KKLVGKCTFEPDEKRAPKASPLFQRFRILQKLNNLRIVDDG-GEERPLTLEERQKIIDLLE 295
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 593 KtNRKVTVKQLKEDYfkKIEcfDSVEISGVEDRFN-----ASLGTYHDLLKIIKDKDFldNEENEDILEDIVLTLTLFED 667
Cdd:COG3513 296 N-KKKLTFKKLRKLL--GLP--DGVIFKGFNYEDDdraklKGDKTYAKLAKIFGKAWL--NEFDPEILDDIVEALTLFKD 368
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 668 REMIEERLKTYAHLfDDKVMKQLKRRR-YTGWGRLSRKLINGIrdkqsgktiLDFLKSDgfanrnfmqlihddsLTFKED 746
Cdd:COG3513 369 DEELKEWLKKLYGL-DEEQAEALANLPlPDGYGNLSLKALRKI---------LPLLEEG---------------LDYDEA 423
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 747 IQKAQVSGQGDSLH--------EHIANLAGSPAIKKGILQTVKVVDELVKVMGrhKPENIVIEMARENQTTQKGQKNSRE 818
Cdd:COG3513 424 VKAAGYDHSSLEILdrlppigeEKRKGSIRNPVVHRALNQLRKVVNALIRKYG--KPDEIHIELARDLKKSKKERKEIQK 501
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 819 RMKRIEEGIKELGSQILKEHPVENTQLQNEKLYLYYLQNGRDMYVDQELDINRLSD--YDVDHIVPQSFLKDDSIDNKVL 896
Cdd:COG3513 502 RQRENEKAREKAREEIAEEGGGEPSRRDILKYRLWEEQNGRCPYTGKPISISDLLDgsVEIDHILPRSRTLDDSFNNKVL 581
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 897 TRSDKNRGKSDNVPSEEVVK----KMKNYWRQLLNAKLITQRKFDNLTKAERGglsELDKAGFIKRQLVETRQITKHVAQ 972
Cdd:COG3513 582 CLADANREKGNRTPYEALGGdeaeKWEEILARVENLKLIPQKKKKRFLKKELD---RDDDEGFIARQLNDTRYISRLAAE 658
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 973 ILDSRMNTKYdendklIREVKVITLKSKLVSDFRKDFQFYKV-------REINNYHHAHDAYLNAVVGTALIKKYPKLES 1045
Cdd:COG3513 659 YLKSLYPFED------KGKRKVRVVPGQLTAMLRRAWGLNKIlsddgekNRDDHRHHAIDALVIACTTQGLLQRLAKASR 732
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1046 EFVYgdykvydvrkmiakseqeigKATAKYFFYSNIMNFFKTeitlangeirkrplietngetgeivwdkgrDFATVRKV 1125
Cdd:COG3513 733 ERED--------------------AEKAEEHFPPPWDGFRQD------------------------------VAEAVDEI 762
|
1130 1140 1150 1160
....*....|....*....|....*....|....*....|....*
gi 1682072386 1126 LsmpqvnIVKKTEVQ-TGGFSKESILPKRNsDKLIARKKdWDPKK 1169
Cdd:COG3513 763 F------VSHAPRRKvTGQLHKETIYSTGE-GKVVLRKP-LTSLK 799
|
|
| thym_sym |
TIGR03284 |
thymidylate synthase; Members of this protein family are thymidylate synthase, an enzyme that ... |
1774-2058 |
5.78e-113 |
|
thymidylate synthase; Members of this protein family are thymidylate synthase, an enzyme that produces dTMP from dUMP. In prokaryotes, its gene usually is found close to that for dihydrofolate reductase, and in some systems the two enzymes are found as a fusion protein. This model excludes a set of related proteins (TIGR03283) that appears to replace this family in archaeal methanogens, where tetrahydrofolate is replaced by tetrahydromethanopterin. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]
Pssm-ID: 213790 [Multi-domain] Cd Length: 295 Bit Score: 360.99 E-value: 5.78e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1774 QYLDLIADIINNGRTMDDRTGVGVISKFGCTMRYSLDQAFPLLTTKRVFWKGVLEELLWFIRGDTNANHLSEKGVKIWD- 1852
Cdd:TIGR03284 1 QYLDLLRDILENGHQKGDRTGTGTISVFGYQMRFDLSKGFPLLTTKKVPFRLIASELLWFLKGDTNIRYLLDHNVNIWDe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1853 -------KNVTREFLDSRNLPHREV-------------GDIGPGYGFQWRHFGAAYkdmhtdytGQGVDQLKNVIQMLRT 1912
Cdd:TIGR03284 81 waferwvKSDDYNGPDMTDFGHRAQddpeeddefadkyGDLGPVYGKQWRSWATPD--------GETIDQIKNVIEMIKT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1913 NPTDRRMLMTAWNPAALDEMALPPCHLLCQFYVNDQKeLSCIMYQRSCDVGLGVPFNIASYSLLTLMVAHVCNLKPKEFI 1992
Cdd:TIGR03284 153 NPDSRRLIVSAWNPEDVPTMALPPCHTLFQFYVADGK-LSCQLYQRSADVFLGVPFNIASYALLTHLIAQETGLEVGEFV 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1682072386 1993 HFMGNTHVYTNHVEALKEQLRREPRPFPIVnILNKErIKEIDDFTAEDFEVVGYVPHGRIQMEMAV 2058
Cdd:TIGR03284 232 HTLGDAHLYSNHLEQAKLQLTREPRPLPTL-KLNPD-KKDIFDFEYEDIEIEGYDPHPAIKAPVAV 295
|
|
| TS_Pyrimidine_HMase |
cd00351 |
Thymidylate synthase and pyrimidine hydroxymethylase: Thymidylate synthase (TS) and ... |
1774-2009 |
1.97e-107 |
|
Thymidylate synthase and pyrimidine hydroxymethylase: Thymidylate synthase (TS) and deoxycytidylate hydroxymethylase (dCMP-HMase) are homologs that catalyze analogous alkylation of C5 of pyrimidine nucleotides. Both enzymes are involved in the biosynthesis of DNA precursors and are active as homodimers. However, they exhibit distinct pyrimidine base specificities and differ in the details of their catalyzed reactions. TS is biologically ubiquitous and catalyzes the conversion of dUMP and methylene-tetrahydrofolate (CH2THF) to dTMP and dihydrofolate (DHF). It also acts as a regulator of its own expression by binding and inactivating its own RNA. Due to its key role in the de novo pathway for thymidylate synthesis and, hence, DNA synthesis, it is one of the most conserved enzymes across species and phyla. TS is a well-recognized target for anticancer chemotherapy, as well as a valuable new target against infectious diseases. Interestingly, in several protozoa, a single polypeptide chain codes for both, dihydrofolate reductase (DHFR) and thymidylate synthase (TS), forming a bifunctional enzyme (DHFR-TS), possibly through gene fusion at a single evolutionary point. DHFR-TS is also active as a dimer. Virus encoded dCMP-HMase catalyzes the reversible conversion of dCMP and CH2THF to hydroxymethyl-dCMP and THF. This family also includes dUMP hydroxymethylase, which is encoded by several bacteriophages that infect Bacillus subtilis, for their own protection against the host restriction system, and contain hydroxymethyl-dUMP instead of dTMP in their DNA.
Pssm-ID: 238211 Cd Length: 215 Bit Score: 341.95 E-value: 1.97e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1774 QYLDLIADIINNGRT-MDDRTGVGVISKFGCTMRYSLDQAFPLLTTKRVFWKGVLEELLWFIRGDTNANHLSEKGVKIWD 1852
Cdd:cd00351 1 QYLDLWRKILEEGYRkTDDRTGTGTRSLFGAQLRFDLSEGFPLLTTKKVPWKSAIEELLWFLRGDTNAERLKEYGVSIWD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1853 KNVTREfldsrnlphrevGDIGPGYGFQWRHFGAAykdmhtdytGQGVDQLKNVIQMLRTNPTDRRMLMTAWNPAALDEM 1932
Cdd:cd00351 81 EWASKE------------GDLGYTYGFQWRHWGAP---------GQGVDQIEKVIEKLKNNPDSRRAIISAWNPADLDLM 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1682072386 1933 ALPPCHLLCQFYVNDQKeLSCIMYQRSCDVGLGVPFNIASYSLLTLMVAHVCNLKPKEFIHFMGNTHVYTNHVEALK 2009
Cdd:cd00351 140 ALPPCHTLIQFYVRNGK-LSLTLYQRSNDAFLGVPFNIASYALLTEMIARVTGLEPGEFIHTIGDAHIYENHLEQVK 215
|
|
| Cas9_PI |
pfam16595 |
PAM-interacting domain of CRISPR-associated endonuclease Cas9; Cas9_PI is a family found at ... |
1141-1397 |
2.97e-48 |
|
PAM-interacting domain of CRISPR-associated endonuclease Cas9; Cas9_PI is a family found at the C-terminal of bacterial type II CRISPR system Cas9 endonuclease. This domain adopts a novel protein fold that is unique to the Cas9 family. It is positioned in the structure-DNA-complex to recognize the PAM sequence on the non-complementary DNA strand of the crRNA. PAM sequence is protospacer-adjacent motifs on DNA. See family CRISPR-DR2, Rfam:RF01315. Cas9 carries two nuclease domains, HNH and RuvC, which cleave the DNA strands that are complementary and non-complementary to the 20 nucleotide guide sequence in crRNAs, respectively.
Pssm-ID: 435449 Cd Length: 264 Bit Score: 174.05 E-value: 2.97e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1141 TGGFSKESILP--KRNSDKLIARKKD---WDPKKYGGFDSPTVAYSVLVVAKVEKGKSKKLksvkeLLGITIMERSSFEK 1215
Cdd:pfam16595 1 KGGLFNQTILPahKKKGKGLIPLKKDergLDVEKYGGYSSLTAAYFSLVEYTGKKGKRKRT-----IEGVPLYLAAKIEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1216 NPI--DFLEAKGYKEVKKDLIIKLPKYSLFElENGRKRMLASAGE---LQKGNELALPSKYVNFLYLASHYEKLKGSPED 1290
Cdd:pfam16595 76 NKDllEYLEEKLGLKEPKIILPKIKKNSLIK-IDGFRMLLTGKTEnrlLKNAVQLVLSNDDEKYIKKIEKFVKKNKDDII 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1291 NEQKQLFVEQHKHYLDEIIEQISEFSKrVILADANLDKVLSAYNKHRDKPIREQAENIIHLFTLTNLGA-PAAFKYFDTT 1369
Cdd:pfam16595 155 EEKDGLTEEKNIKLYDELLDKMKNTIY-YKRPSNQGEKLEKLKEKFIKLSLEEKCKVLIEILKLTHANPtSADLKLIGGS 233
|
250 260 270
....*....|....*....|....*....|.
gi 1682072386 1370 IDRKRYTSTKEVLDA---TLIHQSITGLYET 1397
Cdd:pfam16595 234 KHAGRIKISNNISKAsniKLINQSVTGLYEK 264
|
|
| GFP |
pfam01353 |
Green fluorescent protein; |
2092-2302 |
2.51e-43 |
|
Green fluorescent protein;
Pssm-ID: 426217 Cd Length: 211 Bit Score: 157.73 E-value: 2.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 2092 MHMKLYMEGTVDNHHFKCTSEGEGKPYEGTQTMRIKVVEGgPLPFAFDILATSFLYgsKTFINHTQGiPDFFKQSFPEG- 2170
Cdd:pfam01353 1 MTHDLHMEGSVNGHEFDIVGGGNGNPNDGSLETKVKSTKG-ALPFSPYLLAPHL*Y--YQYLPFPDG-TSPFQAAVENGg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 2171 FTWERVTTYEDGGVLTATQDTSLQDGCLIYNVKIRGVNFTSNGPVMQKKTLGWEAFTETL-YPADGGLEGRNDMALKLVG 2249
Cdd:pfam01353 77 YQVHRTFKFEDGGVLTIVFTYTYEGGHIKGEFTFQGSGFPPDGPVMTKSLTGWDPSVEKMiPRNDKTLVGDINWSLKLTD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1682072386 2250 GSHLIANIKTTYRSKKP-AKNLKMPGVYYVDYRLERIKEANNETYVEQHEVAVA 2302
Cdd:pfam01353 157 GKRYRAQVVTNYTFAKPvPAGLKLPPPHFVFRKIERTGSKTEINLVEQQKAFVD 210
|
|
| dihyfolred_HdrA_Halo |
NF041386 |
dihydrofolate reductase HdrA; |
1456-1639 |
5.77e-07 |
|
dihydrofolate reductase HdrA;
Pssm-ID: 469277 [Multi-domain] Cd Length: 158 Bit Score: 51.49 E-value: 5.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1456 VVAMTPKRGIGINNGLPWPHLTTDFKHFR-RVtkttpeeasrlngwlprkfaktgdSGLPspsvgkrfnaVVMGRKNWES 1534
Cdd:NF041386 6 VAAVAENGVIGRDGELPWPSIPADKRQYReRV------------------------ADDP----------VILGRRTFES 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1535 MprkFRPLVDRLNIVVSSSLKEEDIAAekpqaegqqrVRVCASLPAALSLLEEeykDSVDQIFVVGGAGLYEaaLSLGVA 1614
Cdd:NF041386 52 M---RDDLPGSAQIVLSRSEREFDVET----------AHHAGGVDEAIEIAES---LGAERAYVLGGAAIYE--LFQPHV 113
|
170 180
....*....|....*....|....*
gi 1682072386 1615 SHLYITRVAREFPCDVFFPAFPGDD 1639
Cdd:NF041386 114 DRMVLSRVPGEYEGDAYYPEWDEDE 138
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| cas_Csn1 |
TIGR01865 |
CRISPR subtype II/NMENI RNA-guided endonuclease Cas9/Csn1; CRISPR loci appear to be mobile ... |
43-1089 |
0e+00 |
|
CRISPR subtype II/NMENI RNA-guided endonuclease Cas9/Csn1; CRISPR loci appear to be mobile elements with a wide host range. This model represents a protein found only in CRISPR-containing species, near other CRISPR-associated proteins (cas), as part of the NMENI subtype of CRISPR/Cas locus. The species range so far for this protein is animal pathogens and commensals only.
Pssm-ID: 273840 Cd Length: 805 Bit Score: 924.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 43 KYSIGLDIGTNSVGWAVITDEYKVPSKKFKVLGNtdrhsiKKNLIGALLFDSGETAE-ATRLKRTARRRYTRRKNRICYL 121
Cdd:TIGR01865 1 EYILGLDIGIASVGWAIVEDDYKVPAAKRLIDGG------VRNFTGAELPKTGETAAlDRRLARGARRRIRRRKHRLLRL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 122 QEIFSNEMAKVDDSFFHRLEESFLVEEDKKHerhpifgnivdevayhekypTIYHLRKKLVDSTDKADLrlIYLALAHMI 201
Cdd:TIGR01865 75 QELFSREGSLTDFDFFSRLENSFLVEEDKRN--------------------TIYHLRKAALENKLKPDE--LYLALLHII 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 202 KFRGHFLIEgdlnpdnsdvdklfiqlvqtynqlfeenpinasgvdakailsarlsksrrlenliaqlpgekknglfgnli 281
Cdd:TIGR01865 133 KHRGHFLIE----------------------------------------------------------------------- 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 282 alslgltpnfksnfdlaedaklqlskdtyDDDLDnllaqigdqyadlflaaknlsdaillsdilrVNTEITKAPLSASMI 361
Cdd:TIGR01865 142 -----------------------------GNDFD-------------------------------TANKETGALLSAVMI 161
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 362 KRYDEHHQDLTLLKALVRQQLPEKYKEIFFDqskngyagyidggasqeefykfikpilekmdgteellvklnreDLLRKQ 441
Cdd:TIGR01865 162 NRYLEHEADLRTLKELILKKFPKKYKEIFSE-------------------------------------------TFLRNQ 198
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 442 RTFDNGSIPHQIHLGELHAILRRQEDFYPFlkdnrekiEKILTFRIPYYVGPLARGNSRFAwmtrkseetitpwnfeeVV 521
Cdd:TIGR01865 199 RGFYNGSIPRQLLLEELEAIFRKQREYYPF--------IKLLTFRIPYYIGPLAEGKSEFA-----------------FV 253
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 522 DKGASAQSFIERMTNFDKNLPNEKVLPKHSLLYEYFTVYNELTKVKYVTEGMRKPAFLSGEQKKAIVDLLFKTNRKVTVK 601
Cdd:TIGR01865 254 DKPASAENFIEKMTGKCTYLPEEKRAPKHSLLAEKFTVLNELNNVRIIILEQGETKILSKEEKQELLDLLFKKKKLTYKK 333
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 602 QLKEDYFKKIECFDSVEISGVEDR---FNASLGTYHDLLKIIKDKDFLDNEENEDILEDIVLTLTLFEDREMIEERLKTY 678
Cdd:TIGR01865 334 LRKLLGLSEDAIFKGLRYEGLDNAekaFNISLKTYHKLRKALGDKDLLDNPKNPKDLDEIVKILTLYKDREMIKKRLELY 413
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 679 AHLFDDKVMKQLKRRRYTGWGRLSRKLINGIRDKQSGKTILDFLKSDGFANRNFMQLIHDDSLTFKEDIQKAqvsgqgds 758
Cdd:TIGR01865 414 KDVLNEEQVKKLVRLHFTGWGRLSLKALRGIRPLMEQGKRYDEAILELGGNRNFMQNINDSQLLPKINITKA-------- 485
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 759 lhehiANLAGSPAIKKGILQTVKVVDELVKVMGrhKPENIVIEMARENQTTQKGQKNSRERMKRIEEGIKELGS----QI 834
Cdd:TIGR01865 486 -----KDEILNPVVKRALLQARKVVNELVKKYG--PPDKIVIEMAREEQGTNFGKRNSKERYKKNEDKIKEFASalgkEI 558
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 835 LKEHPVENTQLQNEKLYLYYLQNGRDMYVDQELDINRL---SDYDVDHIVPQSFLKDDSIDNKVLTRSDKNRGKSDNVPS 911
Cdd:TIGR01865 559 LKEEPTENSSKNILKLRLYYQQNGKCMYTGKEIDIDDLfdlSYYEIDHILPQSRSFDDSISNKVLVLASENQEKGDQTPY 638
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 912 E-EVVKKMKNYWRQLLNAKLITQRKFDNLTKAERGGLSELDKAGFIKRQLVETRQITKHVAQILDSRMNTKYDendklIR 990
Cdd:TIGR01865 639 EaEIVKKDSAFWNKFEAYVLISKRKSDKLTRAERGGLSDDDKAGFIDRNLNDTRYITRVVANYLKDRFNFHLK-----KR 713
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 991 EVKVITLKSKLVSDFRKDFQFYKVREINNYHHAHDAYLNAVVGTALIKKYPKLESEFVYGDYKVYDVRKMIAkseqeigK 1070
Cdd:TIGR01865 714 KVKVVTLKGQLTSQLRKKWGLYKKREINNYHHAHDAYINAVSTNALVKKFSQLEPEFRYKEYHNFDGRKKKK-------S 786
|
1050
....*....|....*....
gi 1682072386 1071 ATAKYFFYSNIMNFFKTEI 1089
Cdd:TIGR01865 787 ATDKKVKFSNPMEFFKQKV 805
|
|
| Csn1 |
cd09643 |
CRISPR/Cas system-associated protein Cas9; CRISPR (Clustered Regularly Interspaced Short ... |
43-1088 |
0e+00 |
|
CRISPR/Cas system-associated protein Cas9; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Very large protein containing McrA/HNH-nuclease related domain and a RuvC-like nuclease domain; signature gene for type II
Pssm-ID: 187774 [Multi-domain] Cd Length: 799 Bit Score: 909.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 43 KYSIGLDIGTNSVGWAVITDEYKVPSKKFKvlgntdrHSIKKNLIGALLFDSGETAE-ATRLKRTARRRYTRRKNRICYL 121
Cdd:cd09643 1 EYILGLDIGIASVGWAIVEDDYKVPAKKMI-------DCGVKIFTGAELFKTGETAAlDRRLARGARRRIRRRKHRLLRL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 122 QEIFSNEMAKVDDSFFHRLEESFLveedkkherhpifgnivdevAYHEKYPTIYHLRKKLVDSTDKADLrlIYLALAHMI 201
Cdd:cd09643 74 QELFAREGSLTDFDFFSRLEDSFL--------------------EYHKNYPTIYHLRKAALENKLKPDE--LYLALLHII 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 202 KFRGHFLIEGDLNPDNsdvdklfiqlvqtynqlfeenpinasgvdakailsarlsksrrlenliaqlpgekknglfgnli 281
Cdd:cd09643 132 KHRGHFLIEGDEDTTA---------------------------------------------------------------- 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 282 alslgltpnfksnfdlaedaklqlskdtydddldnllaqigdqyadlflaaknlsdaillsdilrvnTEITKAPLSASMI 361
Cdd:cd09643 148 -------------------------------------------------------------------DKETGALLSASMI 160
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 362 KRYDEHHQDLTLLKALVRQQLPEKYKEIFFDqskngyagyidggasqeefykfikpilekmdgteellvklnrEDLLRKQ 441
Cdd:cd09643 161 KRYDEHKADLRKLKELIKKEFFKKYKEIFGD------------------------------------------ETFLRNQ 198
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 442 RTFDNGSIPHQIHLGELHAILRRQEDFYPFlkdnrekiEKILTFRIPYYVGPLARGNSRFAWMTRKSEEtitpwnfeevv 521
Cdd:cd09643 199 RGFYNGSIPRQLLLEELEAIFRKQREYYPF--------EKILTFRIPYYIGPLAEGKSEFAWLTRPALS----------- 259
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 522 dkgasaQSFIERMTNFDKNLPNEKVLPKHSLLYEYFTVYNELTKVKYVTEgMRKPAFLSGEQKKAIVDLLFKTNRKVTVK 601
Cdd:cd09643 260 ------EAFIEKMTGKCTYLPEEKRAPKHSLLAEKFTVLNELNNLRIIEE-QGETKILSKEEKQELLDLLFKKNKLTYKQ 332
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 602 QLKEDYFKKIECFDSVEISG--VEDRFNASLGTYHDLLKIIKDKDFLDNEENEDILEDIVLTLTLFEDREMIEERLKTYA 679
Cdd:cd09643 333 KRKLLGLKEEEIFKGLRYEGlkAEKNFNISLKTYHDLRKALGKEFLKDLELNEKILDEIVKILTLYKDREMIEKILELYK 412
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 680 HLFDDKVMKQLKRRRYTGWGRLSRKLINGIRDKQSGKTILDFLKSDGFANRNfmQLIHDDSLTFKEDIQKAQVsgqgdsl 759
Cdd:cd09643 413 DLLNEEQLKKLLKRHFTGWGRLSLKALRGIRPLMEQGKRYDEAILELGGNHN--QKINSDELKFLPIIKKAQV------- 483
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 760 hehiANLAGSPAIKKGILQTVKVVDELVKVMGrhKPENIVIEMARENQtTQKGQKNSRERMKRIEEGIKELGS---QILK 836
Cdd:cd09643 484 ----KDEILNPVVKRALLQARKVVNELVKKYG--PPDKIVIEMARENG-TNKGTKNRKKRQKKNEDNIKEAASaleQKLK 556
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 837 EHPVENTQLQNEKLYLYYLQNGRDMYVDQELDINRL---SDYDVDHIVPQSFLKDDSIDNKVLTRSDKNRGKSDNVPSEE 913
Cdd:cd09643 557 ELPLDIKSKNILKLRLYYQQNGKCMYTGKEIDIDDLfdlSYYEIDHILPQSRSFDDSISNKVLVLASENQEKGDQTPYEE 636
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 914 VVKKMKNYWRQLLNAKLITQR---KFDNLtKAERgGLSELDKAGFIKRQLVETRQITKHVAQILDSRMNTKYDendklIR 990
Cdd:cd09643 637 IVSKMSAFWNKLEAAKLISQRgdsKKDRL-LLEK-GISDDEKAGFIDRNLNDTRYITRVVANYLKDRFNFHLK-----KR 709
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 991 EVKVITLKSKLVSDFRKDFQFYKVREINNYHHAHDAYLNAVVGTALIKKYPKLEsefVYGDYKVYDVRKMIAKSEQEIgk 1070
Cdd:cd09643 710 KVKVVTLKGQLTSQLRKKWGLYKKREINNYHHAHDAYINAVVTNALVKKFSQLE---RYKEYKRFDSEKGNKKTLDEN-- 784
|
1050
....*....|....*...
gi 1682072386 1071 ataKYFFYSNIMNFFKTE 1088
Cdd:cd09643 785 ---KKFFFANPMNFFKQE 799
|
|
| PTZ00164 |
PTZ00164 |
bifunctional dihydrofolate reductase-thymidylate synthase; Provisional |
1449-2058 |
0e+00 |
|
bifunctional dihydrofolate reductase-thymidylate synthase; Provisional
Pssm-ID: 240299 [Multi-domain] Cd Length: 514 Bit Score: 860.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1449 SQKPVCLVVAMTPKRGIGINNGLPWpHLTTDFKHFRRVTKTTPEEASrlngwlprkfaktgdsglpsPSVGKRFNAVVMG 1528
Cdd:PTZ00164 6 SLKDFSIVVAVTLKRGIGIGNSLPW-HIPEDMKFFSKITTYVREEKY--------------------EKSPKKQNAVIMG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1529 RKNWESMPRKFRPLVDRLNIVVSSSLKEEdiaaekpqaEGQQRVRVCASLPAALSLLEEEykDSVDQIFVVGGAGLYEAA 1608
Cdd:PTZ00164 65 RKTWESIPKKFRPLKNRINVVLSRTLTEE---------EADPGVLVFGSLEDALRLLAED--LSIEKIFIIGGASVYREA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1609 LSLGVASHLYITRVAREFPCDVFFPAFPGDDILSNKstaaqaaapaesvfvpfcpelgrekdneatyrpifISKTFSDNG 1688
Cdd:PTZ00164 134 LSANLLDKIYLTRVNSEYECDVFFPKIPESFFIVAI-----------------------------------VSQTFSTNG 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1689 VPYDFVVLEKRRKTDDAATAEPsnamssltstrettpvhglqapssaaaiapvLAWMDEEDRKKREQKELIRAVPHVHFR 1768
Cdd:PTZ00164 179 TSYDFVIYEKKNDDEEDLLGKI-------------------------------FGQMKMTGRKKSPKEQLYKACPSLKIR 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1769 GHEEFQYLDLIADIINNGRTMDDRTGVGVISKFGCTMRYSLDQAFPLLTTKRVFWKGVLEELLWFIRGDTNANHLSEKGV 1848
Cdd:PTZ00164 228 EHEEFQYLDLIADIIKNGNVKEDRTGVGTISKFGYQMRFDLRESFPLLTTKKVFLRGIIEELLWFIRGETNGNLLLDKGV 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1849 KIWDKNVTREFLDSRNLPHREVGDIGPGYGFQWRHFGAAYKDMHTDYTGQGVDQLKNVIQMLRTNPTDRRMLMTAWNPAA 1928
Cdd:PTZ00164 308 RIWEGNGSREFLDSRGLTHREENDLGPVYGFQWRHFGAEYKDMHDDYTGQGVDQLKNIIETIKNNPDDRRLILTAWNPSA 387
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1929 LDEMALPPCHLLCQFYVNDQKeLSCIMYQRSCDVGLGVPFNIASYSLLTLMVAHVCNLKPKEFIHFMGNTHVYTNHVEAL 2008
Cdd:PTZ00164 388 LDQMALPPCHLLSQFYVNDGK-LSCMMYQRSCDMGLGVPFNIASYALLTHMIAQVCGLRPGEFVHFLGDAHVYSNHVDAL 466
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1682072386 2009 KEQLRREPRPFPIVNILNKerIKEIDDFTAEDFEVVGYVPHGRIQMEMAV 2058
Cdd:PTZ00164 467 KEQLERVPYPFPTLKLKRE--VENIEDFTIEDIEVIGYVPHPKIKMEMAV 514
|
|
| Cas9_REC |
pfam16592 |
REC lobe of CRISPR-associated endonuclease Cas9; The REC lobe of Cas9 - the CRISPR-associated ... |
220-749 |
0e+00 |
|
REC lobe of CRISPR-associated endonuclease Cas9; The REC lobe of Cas9 - the CRISPR-associated endonuclease Cas9 - includes the REC1 and REC2 domains. REC1 forms an elongated, alpha-helical structure consisting of 25 alpha helices and two beta-sheets, whereas REC2 inserted within REC1 adopts a six-helix bundle structure. The REC lobe and the NUC lobe of Cas9 fold to present a positively charged groove at their interface which accommodates the negatively charged sgRNA:target DNA heteroduplex. CRISPR (clustered regularly interspaced short palindromic repeat)-Cas system occurs naturally in bacteria as a defence against invasion by phages or other mobile genetic elements. Cas9 is targeted to specific genomic locations by sgRNAs or single guide RNAs, in order to complex with invading DNA in order to cleave it and render it inactive.
Pssm-ID: 435447 Cd Length: 539 Bit Score: 589.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 220 VDKLFIQLVQTYNQLFEENPINASGVDAKAILSA-RLSKSRRLENLIAQLPGEK-KNGLFGNLIALSLGLTPNFKSNFDL 297
Cdd:pfam16592 1 VEESFQDLLNILYEQLENLELETQNVEIEKILKKtKISKKAKLDELLALPPNEKnSKKIFAEILKLILGNKADFTKIFEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 298 ------AEDAKLQLSKDTYDDDLDNLLAQIGDQYADLFLAAKNLSDAILLSDILRVNTEITKAPLSASMIKRYDEHHQDL 371
Cdd:pfam16592 81 ekfveePKKIKLSFSDSNYDEKIEELENQLGDEKAEIILILKKIYDWVVLSDILTVSTDNGKAYLSEAMVNRYDKHKEDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 372 TLLKALVRQQLPEKYKEIFFDQSKNGYAGYID----GGASQEEFYKFIKPILEKMDGTE--ELLVKLNREDLLRKQRTFD 445
Cdd:pfam16592 161 AQLKKVIKQNLSEKYNDMFRKEKKKGYSAYINgknnGKTSKEDFYKYIKKLINKVETSEaqYILSKIDNENFLPKQRTKS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 446 NGSIPHQIHLGELHAILRRQEDFYPFLKDNREKIEKILTFRIPYYVGPLARGNSRFAWMTRKSEETITPWNFEEVVDKGA 525
Cdd:pfam16592 241 NGSIPYQVHLQELKKIIKNQAEYYPFLKENQEKILKLLTFRIPYYVGPLAEKKSKFAWMKRKEQGKIYPWNFEQKVDIDK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 526 SAQSFIERMTNFDKNLPNEKVLPKHSLLYEYFTVYNELTKVKYVTEgmrkpaFLSGEQKKAIVDLLFKTNRKVTVKQLKE 605
Cdd:pfam16592 321 TAEAFITRMTNYCTYLPDEKVLPKNSLLYSKFTVLNELNKIKINGE------KISVELKQDIFNGLFKKNKKVTKKKLKD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 606 DYFKKIECFDSVEISGV--EDRFNASLGTYHDLLKIIkdKDFLDNEENEDILEDIVLTLTLFEDREMIEERL-KTYAHLF 682
Cdd:pfam16592 395 WLVKEGYNFKAVEIKGFdkENNFNNSLTTYIDLAKIF--GDFLDNPDNEDIIEDIIYWLTLFEDRKILKRRLqKKYSNLL 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 683 DDKVMKQLKRRRYTGWGRLSRKLINGIRDKQS---GKTILDFLKSDgfaNRNFMQLIHDDSLTFKEDIQK 749
Cdd:pfam16592 473 TEKQIKQILKLKYKGWGRLSKELLNGIRGADRqgeIKTIIDLLWND---NRNLMQLINDERLSFKEEIEK 539
|
|
| Thymidylat_synt |
pfam00303 |
Thymidylate synthase; This is a family of proteins that are flavin-dependent thymidylate ... |
1774-2054 |
2.39e-153 |
|
Thymidylate synthase; This is a family of proteins that are flavin-dependent thymidylate synthases.
Pssm-ID: 459753 Cd Length: 259 Bit Score: 474.60 E-value: 2.39e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1774 QYLDLIADIINNGRTMDDRTGVGVISKFGCTMRYSL-DQAFPLLTTKRVFWKGVLEELLWFIRGDTNANHLSEKGVKIWD 1852
Cdd:pfam00303 2 QYLDLLRDILENGTEKEDRTGTGTLSVFGYQMRFDLsDGEFPLLTTKKVFWKSIIHELLWFLRGDTNIKYLQENGVHIWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1853 knvtrEFLDsrnlphrEVGDIGPGYGFQWRHFGAaykdmhtdYTGQGVDQLKNVIQMLRTNPTDRRMLMTAWNPAALDEM 1932
Cdd:pfam00303 82 -----EWAD-------ENGDLGPVYGFQWRHWGA--------PDGGGIDQLAQVIDQLKNNPDSRRIIVSAWNPADLPKM 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1933 ALPPCHLLCQFYVNDqKELSCIMYQRSCDVGLGVPFNIASYSLLTLMVAHVCNLKPKEFIHFMGNTHVYTNHVEALKEQL 2012
Cdd:pfam00303 142 ALPPCHYLFQFYVDG-GKLSCQLYQRSADVFLGVPFNIASYALLTHMIAQVTGLEPGEFVHTIGDAHIYDNHVEQVKEQL 220
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1682072386 2013 RREPRPFPIVNILNKeriKEIDDFTAEDFEVVGYVPHGRIQM 2054
Cdd:pfam00303 221 TREPRPLPKLKINRK---VSIFDFTFEDFELEGYQPHPKIKA 259
|
|
| ThyA |
COG0207 |
Thymidylate synthase [Nucleotide transport and metabolism]; Thymidylate synthase is part of ... |
1774-2058 |
2.59e-139 |
|
Thymidylate synthase [Nucleotide transport and metabolism]; Thymidylate synthase is part of the Pathway/BioSystem: Thymidylate biosynthesis
Pssm-ID: 439977 Cd Length: 264 Bit Score: 434.92 E-value: 2.59e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1774 QYLDLIADIINNGRTMDDRTGVGVISKFGCTMRYSLDQAFPLLTTKRVFWKGVLEELLWFIRGDTNANHLSEKGVKIWDK 1853
Cdd:COG0207 3 QYLDLLRHILEEGTWKEDRTGTGTLSVFGYQMRFDLSEGFPLLTTKKVHWKSIIHELLWFLRGDTNIRYLRENGVKIWDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1854 NVTREfldsrnlphrevGDIGPGYGFQWRHFGAAykdmhtdyTGQGVDQLKNVIQMLRTNPTDRRMLMTAWNPAALDEMA 1933
Cdd:COG0207 83 WADEN------------GDLGPVYGKQWRSWPTP--------DGGTIDQIAQVIDQLKTNPDSRRLIVSAWNPAELDEMA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1934 LPPCHLLCQFYVNDQKeLSCIMYQRSCDVGLGVPFNIASYSLLTLMVAHVCNLKPKEFIHFMGNTHVYTNHVEALKEQLR 2013
Cdd:COG0207 143 LPPCHALFQFYVADGK-LSCQLYQRSADVFLGVPFNIASYALLTHMVAQVTGLEPGEFVHTIGDAHIYLNHLEQVKEQLS 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1682072386 2014 REPRPFPIVNILNKerIKEIDDFTAEDFEVVGYVPHGRIQMEMAV 2058
Cdd:COG0207 222 REPRPLPKLKINPK--VKSIFDFTFEDFELEGYDPHPAIKAPVAV 264
|
|
| Cas9 |
COG3513 |
CRISPR-Cas system type-II protein Cas9 [Defense mechanisms]; CRISPR-Cas system type-II protein ... |
42-1169 |
1.38e-130 |
|
CRISPR-Cas system type-II protein Cas9 [Defense mechanisms]; CRISPR-Cas system type-II protein Cas9 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 442735 [Multi-domain] Cd Length: 812 Bit Score: 432.08 E-value: 1.38e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 42 KKYSIGLDIGTNSVGWAVITDEYKVpskkfkvlgntdrHSIKKNLIGALLFDSGET-------AEATRLKRTARRRYTRR 114
Cdd:COG3513 2 DKYILGLDLGINSVGWAVLELDEDG-------------EPGEIIDAGVRIFDDGEDpksgeslAAARREARGARRRRRRR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 115 KNRICYLQEIFSNEMakvddsffhrleesFLVEEDKKHERHPifgnivdevayhekYPTIYHLRKKLVDstDKADLRLIY 194
Cdd:COG3513 69 KHRLRRLKRLLVEEG--------------LLPADDAERKALL--------------PLNPYELRAKALD--EKLSPEELG 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 195 LALAHMIKFRGHfliegdLNPDNSDVDKLfiqlvqtynqlfeenpinasgvDAKAILSARLSKSRRLENLIAQLPGEkkn 274
Cdd:COG3513 119 RALFHLAQRRGF------KSNRKTDSKDN----------------------ESGKVKDAIKELRERLEAKGARTVGE--- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 275 glfgnlialslgltpnfksnfdlaedaklqlskdtydddldnllaqigdqyadlFLAaknlsdaillsdilrvnteitka 354
Cdd:COG3513 168 ------------------------------------------------------YLY----------------------- 170
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 355 plsasmiKRYDEHHQdltllkalvrqqlpekykeiffdqskngyagyidggasqeefykfikpilekmdgteellvklnr 434
Cdd:COG3513 171 -------RRLQENGK----------------------------------------------------------------- 178
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 435 edlLRKQRTFDNGSIPHQIHLGELHAILRRQEDFYPFLKDN--REKIEKILTFRIPYYVGplargnsrfawmtrkseeti 512
Cdd:COG3513 179 ---VRNRKGDYDFYIPREDLEDEFEAIWAAQAEFGPALLTEelRDELLEIIFFQRPLKSG-------------------- 235
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 513 tpwnfeevvdkgasaqsfiERMTNFDKNLPNEKVLPKHSLLYEYFTVYNELTKVKYVTEGmRKPAFLSGEQKKAIVDLLF 592
Cdd:COG3513 236 -------------------KKLVGKCTFEPDEKRAPKASPLFQRFRILQKLNNLRIVDDG-GEERPLTLEERQKIIDLLE 295
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 593 KtNRKVTVKQLKEDYfkKIEcfDSVEISGVEDRFN-----ASLGTYHDLLKIIKDKDFldNEENEDILEDIVLTLTLFED 667
Cdd:COG3513 296 N-KKKLTFKKLRKLL--GLP--DGVIFKGFNYEDDdraklKGDKTYAKLAKIFGKAWL--NEFDPEILDDIVEALTLFKD 368
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 668 REMIEERLKTYAHLfDDKVMKQLKRRR-YTGWGRLSRKLINGIrdkqsgktiLDFLKSDgfanrnfmqlihddsLTFKED 746
Cdd:COG3513 369 DEELKEWLKKLYGL-DEEQAEALANLPlPDGYGNLSLKALRKI---------LPLLEEG---------------LDYDEA 423
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 747 IQKAQVSGQGDSLH--------EHIANLAGSPAIKKGILQTVKVVDELVKVMGrhKPENIVIEMARENQTTQKGQKNSRE 818
Cdd:COG3513 424 VKAAGYDHSSLEILdrlppigeEKRKGSIRNPVVHRALNQLRKVVNALIRKYG--KPDEIHIELARDLKKSKKERKEIQK 501
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 819 RMKRIEEGIKELGSQILKEHPVENTQLQNEKLYLYYLQNGRDMYVDQELDINRLSD--YDVDHIVPQSFLKDDSIDNKVL 896
Cdd:COG3513 502 RQRENEKAREKAREEIAEEGGGEPSRRDILKYRLWEEQNGRCPYTGKPISISDLLDgsVEIDHILPRSRTLDDSFNNKVL 581
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 897 TRSDKNRGKSDNVPSEEVVK----KMKNYWRQLLNAKLITQRKFDNLTKAERGglsELDKAGFIKRQLVETRQITKHVAQ 972
Cdd:COG3513 582 CLADANREKGNRTPYEALGGdeaeKWEEILARVENLKLIPQKKKKRFLKKELD---RDDDEGFIARQLNDTRYISRLAAE 658
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 973 ILDSRMNTKYdendklIREVKVITLKSKLVSDFRKDFQFYKV-------REINNYHHAHDAYLNAVVGTALIKKYPKLES 1045
Cdd:COG3513 659 YLKSLYPFED------KGKRKVRVVPGQLTAMLRRAWGLNKIlsddgekNRDDHRHHAIDALVIACTTQGLLQRLAKASR 732
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1046 EFVYgdykvydvrkmiakseqeigKATAKYFFYSNIMNFFKTeitlangeirkrplietngetgeivwdkgrDFATVRKV 1125
Cdd:COG3513 733 ERED--------------------AEKAEEHFPPPWDGFRQD------------------------------VAEAVDEI 762
|
1130 1140 1150 1160
....*....|....*....|....*....|....*....|....*
gi 1682072386 1126 LsmpqvnIVKKTEVQ-TGGFSKESILPKRNsDKLIARKKdWDPKK 1169
Cdd:COG3513 763 F------VSHAPRRKvTGQLHKETIYSTGE-GKVVLRKP-LTSLK 799
|
|
| thyA |
PRK01827 |
thymidylate synthase; Reviewed |
1774-2058 |
1.00e-125 |
|
thymidylate synthase; Reviewed
Pssm-ID: 234984 Cd Length: 264 Bit Score: 396.44 E-value: 1.00e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1774 QYLDLIADIINNGRTMDDRTGVGVISKFGCTMRYSLDQAFPLLTTKRVFWKGVLEELLWFIRGDTNANHLSEKGVKIWDk 1853
Cdd:PRK01827 3 QYLDLLRKILDEGTKKNDRTGTGTLSVFGAQMRFDLSKGFPLLTTKKVHFKSIIHELLWFLRGDTNIAYLQENGVHIWD- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1854 nvtrEFLDsrnlphrEVGDIGPGYGFQWRHFGAAykdmhtdyTGQGVDQLKNVIQMLRTNPTDRRMLMTAWNPAALDEMA 1933
Cdd:PRK01827 82 ----EWAD-------ENGDLGPVYGKQWRSWPTP--------DGRHIDQISKVIEQLKTNPDSRRLIVSAWNPGELDKMA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1934 LPPCHLLCQFYVNDQKeLSCIMYQRSCDVGLGVPFNIASYSLLTLMVAHVCNLKPKEFIHFMGNTHVYTNHVEALKEQLR 2013
Cdd:PRK01827 143 LPPCHALFQFYVADGK-LSCQLYQRSADVFLGVPFNIASYALLTHMIAQQTGLKVGEFVHTIGDAHIYSNHLEQAREQLS 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1682072386 2014 REPRPFPIVnILNKErIKEIDDFTAEDFEVVGYVPHGRIQMEMAV 2058
Cdd:PRK01827 222 REPRPLPKL-VINPD-IKSIFDFEFEDFELEGYDPHPAIKAPVAV 264
|
|
| thym_sym |
TIGR03284 |
thymidylate synthase; Members of this protein family are thymidylate synthase, an enzyme that ... |
1774-2058 |
5.78e-113 |
|
thymidylate synthase; Members of this protein family are thymidylate synthase, an enzyme that produces dTMP from dUMP. In prokaryotes, its gene usually is found close to that for dihydrofolate reductase, and in some systems the two enzymes are found as a fusion protein. This model excludes a set of related proteins (TIGR03283) that appears to replace this family in archaeal methanogens, where tetrahydrofolate is replaced by tetrahydromethanopterin. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]
Pssm-ID: 213790 [Multi-domain] Cd Length: 295 Bit Score: 360.99 E-value: 5.78e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1774 QYLDLIADIINNGRTMDDRTGVGVISKFGCTMRYSLDQAFPLLTTKRVFWKGVLEELLWFIRGDTNANHLSEKGVKIWD- 1852
Cdd:TIGR03284 1 QYLDLLRDILENGHQKGDRTGTGTISVFGYQMRFDLSKGFPLLTTKKVPFRLIASELLWFLKGDTNIRYLLDHNVNIWDe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1853 -------KNVTREFLDSRNLPHREV-------------GDIGPGYGFQWRHFGAAYkdmhtdytGQGVDQLKNVIQMLRT 1912
Cdd:TIGR03284 81 waferwvKSDDYNGPDMTDFGHRAQddpeeddefadkyGDLGPVYGKQWRSWATPD--------GETIDQIKNVIEMIKT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1913 NPTDRRMLMTAWNPAALDEMALPPCHLLCQFYVNDQKeLSCIMYQRSCDVGLGVPFNIASYSLLTLMVAHVCNLKPKEFI 1992
Cdd:TIGR03284 153 NPDSRRLIVSAWNPEDVPTMALPPCHTLFQFYVADGK-LSCQLYQRSADVFLGVPFNIASYALLTHLIAQETGLEVGEFV 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1682072386 1993 HFMGNTHVYTNHVEALKEQLRREPRPFPIVnILNKErIKEIDDFTAEDFEVVGYVPHGRIQMEMAV 2058
Cdd:TIGR03284 232 HTLGDAHLYSNHLEQAKLQLTREPRPLPTL-KLNPD-KKDIFDFEYEDIEIEGYDPHPAIKAPVAV 295
|
|
| TS_Pyrimidine_HMase |
cd00351 |
Thymidylate synthase and pyrimidine hydroxymethylase: Thymidylate synthase (TS) and ... |
1774-2009 |
1.97e-107 |
|
Thymidylate synthase and pyrimidine hydroxymethylase: Thymidylate synthase (TS) and deoxycytidylate hydroxymethylase (dCMP-HMase) are homologs that catalyze analogous alkylation of C5 of pyrimidine nucleotides. Both enzymes are involved in the biosynthesis of DNA precursors and are active as homodimers. However, they exhibit distinct pyrimidine base specificities and differ in the details of their catalyzed reactions. TS is biologically ubiquitous and catalyzes the conversion of dUMP and methylene-tetrahydrofolate (CH2THF) to dTMP and dihydrofolate (DHF). It also acts as a regulator of its own expression by binding and inactivating its own RNA. Due to its key role in the de novo pathway for thymidylate synthesis and, hence, DNA synthesis, it is one of the most conserved enzymes across species and phyla. TS is a well-recognized target for anticancer chemotherapy, as well as a valuable new target against infectious diseases. Interestingly, in several protozoa, a single polypeptide chain codes for both, dihydrofolate reductase (DHFR) and thymidylate synthase (TS), forming a bifunctional enzyme (DHFR-TS), possibly through gene fusion at a single evolutionary point. DHFR-TS is also active as a dimer. Virus encoded dCMP-HMase catalyzes the reversible conversion of dCMP and CH2THF to hydroxymethyl-dCMP and THF. This family also includes dUMP hydroxymethylase, which is encoded by several bacteriophages that infect Bacillus subtilis, for their own protection against the host restriction system, and contain hydroxymethyl-dUMP instead of dTMP in their DNA.
Pssm-ID: 238211 Cd Length: 215 Bit Score: 341.95 E-value: 1.97e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1774 QYLDLIADIINNGRT-MDDRTGVGVISKFGCTMRYSLDQAFPLLTTKRVFWKGVLEELLWFIRGDTNANHLSEKGVKIWD 1852
Cdd:cd00351 1 QYLDLWRKILEEGYRkTDDRTGTGTRSLFGAQLRFDLSEGFPLLTTKKVPWKSAIEELLWFLRGDTNAERLKEYGVSIWD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1853 KNVTREfldsrnlphrevGDIGPGYGFQWRHFGAAykdmhtdytGQGVDQLKNVIQMLRTNPTDRRMLMTAWNPAALDEM 1932
Cdd:cd00351 81 EWASKE------------GDLGYTYGFQWRHWGAP---------GQGVDQIEKVIEKLKNNPDSRRAIISAWNPADLDLM 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1682072386 1933 ALPPCHLLCQFYVNDQKeLSCIMYQRSCDVGLGVPFNIASYSLLTLMVAHVCNLKPKEFIHFMGNTHVYTNHVEALK 2009
Cdd:cd00351 140 ALPPCHTLIQFYVRNGK-LSLTLYQRSNDAFLGVPFNIASYALLTEMIARVTGLEPGEFIHTIGDAHIYENHLEQVK 215
|
|
| thyA |
PRK13821 |
thymidylate synthase; Provisional |
1774-2058 |
2.28e-70 |
|
thymidylate synthase; Provisional
Pssm-ID: 184347 Cd Length: 323 Bit Score: 240.05 E-value: 2.28e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1774 QYLDLIADIINNGRTMDDRTGVGVISKFGCTMRYSLDQAFPLLTTKRVFWKGVLEELLWFIRGDTNANHLSEKGVKIWDK 1853
Cdd:PRK13821 3 QYLDLVRTILDTGTWQENRTGIRTISIPGAMLRFDLQQGFPAVTTKKLAFKSAIGELVGFLRASRSAADFRALGCKVWDQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1854 NVTrEFLDSRNLPHRE-VGDIGPGYGFQWRHFgAAYKDMHTDYTGQ---------------------------GVDQLKN 1905
Cdd:PRK13821 83 NAN-ENAQWLANPYRQgVDDLGDVYGVQWRQW-PGYKVLDASADAQiadatsrgfrivarfdedgapkvllykAIDQLRQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1906 VIQMLRTNPTDRRMLMTAWNPAALDEMALPPCHLLCQFYVNDQ-KELSCIMYQRSCDVGLGVPFNIASYSLLTLMVAHVC 1984
Cdd:PRK13821 161 CLDTIMNNPGSRRILFHGWNPAVLDEIALPACHLLYQFLPNVEtREISLCLYIRSNDVGLGTPFNLTEGAALLSLVGRLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1985 NLKPKEFIHFMGNTHVYTNHVEALKEQLRREPRPFPIVNIlnKERIKE-----------IDDFTAEDFEVVGYVPHGRIQ 2053
Cdd:PRK13821 241 GYTPRWFTYFIGDAHIYENQLDMLQEQLTREPYESPRLVI--SDRVPEyaktgvyepewLEKIEPSDFSLVGYRHHEPLT 318
|
....*
gi 1682072386 2054 MEMAV 2058
Cdd:PRK13821 319 APMAV 323
|
|
| Cas9_PI |
pfam16595 |
PAM-interacting domain of CRISPR-associated endonuclease Cas9; Cas9_PI is a family found at ... |
1141-1397 |
2.97e-48 |
|
PAM-interacting domain of CRISPR-associated endonuclease Cas9; Cas9_PI is a family found at the C-terminal of bacterial type II CRISPR system Cas9 endonuclease. This domain adopts a novel protein fold that is unique to the Cas9 family. It is positioned in the structure-DNA-complex to recognize the PAM sequence on the non-complementary DNA strand of the crRNA. PAM sequence is protospacer-adjacent motifs on DNA. See family CRISPR-DR2, Rfam:RF01315. Cas9 carries two nuclease domains, HNH and RuvC, which cleave the DNA strands that are complementary and non-complementary to the 20 nucleotide guide sequence in crRNAs, respectively.
Pssm-ID: 435449 Cd Length: 264 Bit Score: 174.05 E-value: 2.97e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1141 TGGFSKESILP--KRNSDKLIARKKD---WDPKKYGGFDSPTVAYSVLVVAKVEKGKSKKLksvkeLLGITIMERSSFEK 1215
Cdd:pfam16595 1 KGGLFNQTILPahKKKGKGLIPLKKDergLDVEKYGGYSSLTAAYFSLVEYTGKKGKRKRT-----IEGVPLYLAAKIEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1216 NPI--DFLEAKGYKEVKKDLIIKLPKYSLFElENGRKRMLASAGE---LQKGNELALPSKYVNFLYLASHYEKLKGSPED 1290
Cdd:pfam16595 76 NKDllEYLEEKLGLKEPKIILPKIKKNSLIK-IDGFRMLLTGKTEnrlLKNAVQLVLSNDDEKYIKKIEKFVKKNKDDII 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1291 NEQKQLFVEQHKHYLDEIIEQISEFSKrVILADANLDKVLSAYNKHRDKPIREQAENIIHLFTLTNLGA-PAAFKYFDTT 1369
Cdd:pfam16595 155 EEKDGLTEEKNIKLYDELLDKMKNTIY-YKRPSNQGEKLEKLKEKFIKLSLEEKCKVLIEILKLTHANPtSADLKLIGGS 233
|
250 260 270
....*....|....*....|....*....|.
gi 1682072386 1370 IDRKRYTSTKEVLDA---TLIHQSITGLYET 1397
Cdd:pfam16595 234 KHAGRIKISNNISKAsniKLINQSVTGLYEK 264
|
|
| DHFR |
cd00209 |
Dihydrofolate reductase (DHFR). Reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with ... |
1455-1697 |
4.05e-44 |
|
Dihydrofolate reductase (DHFR). Reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with NADPH as a cofactor. This is an essential step in the biosynthesis of deoxythymidine phosphate since 5,6,7,8-tetrahydrofolate is required to regenerate 5,10-methylenetetrahydrofolate which is then utilized by thymidylate synthase. Inhibition of DHFR interrupts thymidilate synthesis and DNA replication, inhibitors of DHFR (such as Methotrexate) are used in cancer chemotherapy. 5,6,7,8-tetrahydrofolate also is involved in glycine, serine, and threonine metabolism and aminoacyl-tRNA biosynthesis.
Pssm-ID: 238127 [Multi-domain] Cd Length: 158 Bit Score: 158.07 E-value: 4.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1455 LVVAMTPKRGIGINNGLPWpHLTTDFKHFRRVTKTtpeeasrlngwlprkfaktgdsglpspsvgkrfNAVVMGRKNWES 1534
Cdd:cd00209 3 LIVAVDENGVIGKDNKLPW-HLPEDLKHFKKTTTG---------------------------------NPVIMGRKTFES 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1535 MPRkfRPLVDRLNIVVSSSLKEEDiaaekpqAEGqqrVRVCASLPAALSLleeeYKDSVDQIFVVGGAGLYEAALSLgvA 1614
Cdd:cd00209 49 IPR--RPLPGRTNIVLSRQLDYQD-------AEG---VEVVHSLEEALEL----AENTVEEIFVIGGAEIYKQALPY--A 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1615 SHLYITRVAREFPCDVFFPAFpgddilsnkstaaqaaapaesvfvpfcpelgrekdNEATYRPIFISKTFSDNGVPYDFV 1694
Cdd:cd00209 111 DRLYLTRIHAEFEGDTFFPEI-----------------------------------DESEWELVSEEEVFEEDGYSYTFE 155
|
...
gi 1682072386 1695 VLE 1697
Cdd:cd00209 156 TYE 158
|
|
| GFP |
pfam01353 |
Green fluorescent protein; |
2092-2302 |
2.51e-43 |
|
Green fluorescent protein;
Pssm-ID: 426217 Cd Length: 211 Bit Score: 157.73 E-value: 2.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 2092 MHMKLYMEGTVDNHHFKCTSEGEGKPYEGTQTMRIKVVEGgPLPFAFDILATSFLYgsKTFINHTQGiPDFFKQSFPEG- 2170
Cdd:pfam01353 1 MTHDLHMEGSVNGHEFDIVGGGNGNPNDGSLETKVKSTKG-ALPFSPYLLAPHL*Y--YQYLPFPDG-TSPFQAAVENGg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 2171 FTWERVTTYEDGGVLTATQDTSLQDGCLIYNVKIRGVNFTSNGPVMQKKTLGWEAFTETL-YPADGGLEGRNDMALKLVG 2249
Cdd:pfam01353 77 YQVHRTFKFEDGGVLTIVFTYTYEGGHIKGEFTFQGSGFPPDGPVMTKSLTGWDPSVEKMiPRNDKTLVGDINWSLKLTD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1682072386 2250 GSHLIANIKTTYRSKKP-AKNLKMPGVYYVDYRLERIKEANNETYVEQHEVAVA 2302
Cdd:pfam01353 157 GKRYRAQVVTNYTFAKPvPAGLKLPPPHFVFRKIERTGSKTEINLVEQQKAFVD 210
|
|
| DHFR_1 |
pfam00186 |
Dihydrofolate reductase; |
1455-1639 |
2.07e-32 |
|
Dihydrofolate reductase;
Pssm-ID: 425512 [Multi-domain] Cd Length: 159 Bit Score: 124.58 E-value: 2.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1455 LVVAMTPKRGIGINNGLPWpHLTTDFKHFRRVTkttpeeasrlngwlprkfakTGdsglpspsvgkrfNAVVMGRKNWES 1534
Cdd:pfam00186 4 LIAAMDENGVIGKDNDLPW-HLPADLKHFKKLT--------------------TG-------------KPVIMGRKTFES 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1535 MPRkfrPLVDRLNIVVSSSlkeediaaEKPQAEGqqrVRVCASLPAALSLLEEEykdsvDQIFVVGGAGLYEAALSLgvA 1614
Cdd:pfam00186 50 IGR---PLPGRKNIVLTRN--------PDYKVDG---VEVVHSLEEALALAAEA-----EEIFIIGGAEIYAQALPL--A 108
|
170 180
....*....|....*....|....*
gi 1682072386 1615 SHLYITRVAREFPCDVFFPAFPGDD 1639
Cdd:pfam00186 109 DRLYITEIDAEFDGDTFFPEIDPSE 133
|
|
| FolA |
COG0262 |
Dihydrofolate reductase [Coenzyme transport and metabolism]; Dihydrofolate reductase is part ... |
1453-1641 |
6.38e-21 |
|
Dihydrofolate reductase [Coenzyme transport and metabolism]; Dihydrofolate reductase is part of the Pathway/BioSystem: Folate biosynthesis
Pssm-ID: 440032 [Multi-domain] Cd Length: 168 Bit Score: 91.84 E-value: 6.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1453 VCLVVAMTPKRGIG-INNGLPW-PHLTTDFKHFRRVTKttpeeasrlngwlprkfaktgdsglpspsvgkRFNAVVMGRK 1530
Cdd:COG0262 3 LILIVAVSLDGVIGgPDGDLPWlFPDPEDLAHFKELTA--------------------------------GADAVLMGRK 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1531 NWESMPRKF--RPLVDRLNIVVSSSLKEEDIAaekpqaegqqRVRVC-ASLPAALSLLEEEykdSVDQIFVVGGAGLYEA 1607
Cdd:COG0262 51 TYESIAGYWptRPLPGRPKIVLSRTLDEADWE----------GVTVVsGDLEEALAALKAA---GGKDIWVIGGGELYRQ 117
|
170 180 190
....*....|....*....|....*....|....*
gi 1682072386 1608 ALSLGVASHLYITRVAREFP-CDVFFPAFPGDDIL 1641
Cdd:COG0262 118 LLPAGLVDELYLTVVPVVLGeGDRLFPELDAPSRL 152
|
|
| folA |
PRK10769 |
type 3 dihydrofolate reductase; |
1453-1639 |
4.57e-16 |
|
type 3 dihydrofolate reductase;
Pssm-ID: 182714 [Multi-domain] Cd Length: 159 Bit Score: 77.86 E-value: 4.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1453 VCLVVAMTPKRGIGINNGLPWpHLTTDFKHFRRVTKTTPeeasrlngwlprkfaktgdsglpspsvgkrfnaVVMGRKNW 1532
Cdd:PRK10769 2 ISLIAALAVDRVIGMENAMPW-NLPADLAWFKRNTLNKP---------------------------------VIMGRHTW 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1533 ESMPRkfrPLVDRLNIVVSSslkeediaaekpQAEGQQRVRVCASLPAALSLLEEeykdsVDQIFVVGGAGLYEAALSLg 1612
Cdd:PRK10769 48 ESIGR---PLPGRKNIVISS------------QPGTDDRVTWVKSVDEALAAAGD-----VPEIMVIGGGRVYEQFLPK- 106
|
170 180
....*....|....*....|....*..
gi 1682072386 1613 vASHLYITRVAREFPCDVFFPAFPGDD 1639
Cdd:PRK10769 107 -AQRLYLTHIDAEVEGDTHFPDYEPDE 132
|
|
| HNH_4 |
pfam13395 |
HNH endonuclease; This HNH nuclease domain is found in CRISPR-related proteins. |
860-910 |
2.43e-14 |
|
HNH endonuclease; This HNH nuclease domain is found in CRISPR-related proteins.
Pssm-ID: 433172 [Multi-domain] Cd Length: 55 Bit Score: 69.19 E-value: 2.43e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1682072386 860 DMYVDQELDINRLSD---YDVDHIVPQSFLKDDSIDNKVLTRSDKNRGKSDNVP 910
Cdd:pfam13395 1 CPYTGEQISIDDLFSeknYDIDHILPYSRSFDDSFSNKVLVLRSANQEKGNRTP 54
|
|
| thy_syn_methano |
TIGR03283 |
thymidylate synthase, methanogen type; Thymidylate synthase makes dTMP for DNA synthesis, and ... |
1899-2001 |
2.10e-08 |
|
thymidylate synthase, methanogen type; Thymidylate synthase makes dTMP for DNA synthesis, and is among the most widely distributed of all enzymes. Members of this protein family are encoded within a completed genome sequence if and only if that species is one of the methanogenenic archaea. In these species, tetrahydromethanopterin replaces tetrahydrofolate, The member from Methanobacterium thermoautotrophicum was shown to behave as a thymidylate synthase based on similar side reactions (the exchange of a characteristic proton with water), although the full reaction was not reconstituted. Partial sequence data showed no similarity to known thymidylate synthases simply because the region sequenced was from a distinctive N-terminal region not found in other thymidylate synthases. Members of this protein family appear, therefore, to a novel, tetrahydromethanopterin-dependent thymidylate synthase. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]
Pssm-ID: 132326 Cd Length: 199 Bit Score: 56.67 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1899 GVDQLKNVIQMLRTNPTDRRMLMTAWNPAALDEMALPPCHLLCQFYVNDQK-ELSCIMyqRSCDVGLGVPFNIASYSLLT 1977
Cdd:TIGR03283 91 GIDQIDYIIERLNQSPNSRRAIAITWDPPQDIKVDEVPCLQLVQFLIRDNKlYLTAFF--RSNDVGGAWVANAIGLRRLQ 168
|
90 100
....*....|....*....|....
gi 1682072386 1978 LMVAHVCNLKPKEFIHFMGNTHVY 2001
Cdd:TIGR03283 169 EYVAEKVGVEPGTLTTHAISAHIY 192
|
|
| thyA |
PRK00956 |
thymidylate synthase; Provisional |
1900-2010 |
2.21e-08 |
|
thymidylate synthase; Provisional
Pssm-ID: 179181 Cd Length: 208 Bit Score: 56.53 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1900 VDQLKNVIQMLRTNPTDRRMLMTAWNPAALDEMALPPCHLLCQFYVNDQKELSCIMYqRSCDVGLGVPFNIASYSLLTLM 1979
Cdd:PRK00956 95 VDQIDYIIEKLKENKNSRRATAVTWNPYIDTKVDEVPCLQLVDFLIRDGKLYLTVLF-RSNDAGGAFHANAIGLIKLGEY 173
|
90 100 110
....*....|....*....|....*....|.
gi 1682072386 1980 VAHVCNLKPKEFIHFMGNTHVYTNHVEALKE 2010
Cdd:PRK00956 174 VAEKVGVELGTYTHHSVSAHIYERDWDYLEK 204
|
|
| dihyfolred_HdrA_Halo |
NF041386 |
dihydrofolate reductase HdrA; |
1456-1639 |
5.77e-07 |
|
dihydrofolate reductase HdrA;
Pssm-ID: 469277 [Multi-domain] Cd Length: 158 Bit Score: 51.49 E-value: 5.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1456 VVAMTPKRGIGINNGLPWPHLTTDFKHFR-RVtkttpeeasrlngwlprkfaktgdSGLPspsvgkrfnaVVMGRKNWES 1534
Cdd:NF041386 6 VAAVAENGVIGRDGELPWPSIPADKRQYReRV------------------------ADDP----------VILGRRTFES 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 1535 MprkFRPLVDRLNIVVSSSLKEEDIAAekpqaegqqrVRVCASLPAALSLLEEeykDSVDQIFVVGGAGLYEaaLSLGVA 1614
Cdd:NF041386 52 M---RDDLPGSAQIVLSRSEREFDVET----------AHHAGGVDEAIEIAES---LGAERAYVLGGAAIYE--LFQPHV 113
|
170 180
....*....|....*....|....*
gi 1682072386 1615 SHLYITRVAREFPCDVFFPAFPGDD 1639
Cdd:NF041386 114 DRMVLSRVPGEYEGDAYYPEWDEDE 138
|
|
| COG3472 |
COG3472 |
Uncharacterized conserved protein domain, often C-terminal to DUF262 [Function unknown]; |
850-927 |
1.76e-03 |
|
Uncharacterized conserved protein domain, often C-terminal to DUF262 [Function unknown];
Pssm-ID: 442695 [Multi-domain] Cd Length: 566 Bit Score: 43.45 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1682072386 850 LYLYYLQNG-RDMYVDQELDINRLSDY--DVDHIVPQSFLKD--------DSIDNKVLTRSDKNRGKSDNVPSEevvkkm 918
Cdd:COG3472 432 ILALLAKLGaRDFLSGQKIDLSNLFDNklEIHHIFPKAYLKKqgisrslyNSIANRTPLSARTNRKIGDKAPSE------ 505
|
....*....
gi 1682072386 919 knYWRQLLN 927
Cdd:COG3472 506 --YLAELEE 512
|
|
| |
