|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1-530 |
0e+00 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 757.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 1 MTIYIILAAVVGAGIGFYVGRVLLLKLFKEQEEQATERAKLIIREAEVKAETQKKDKMLEAKEHFLKLKVEHEEESNRKK 80
Cdd:PRK12704 2 MLLIIILIALVALVVGAVIGYFVRKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 81 NIILQNENKVKQREQQVTKQLEDLKRKEQENDVLKDKLNQQLEGFNKRKEDLEAQfrdkqakveqdHHEILSRLERIANL 160
Cdd:PRK12704 82 NELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEEL-----------IEEQLQELERISGL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 161 SAEEAREQLVENLKSEASTRASSYIKDIVAEAKLTATKEAKKVVIETIQRTAAEHAIENCVSIFNIESDDIKGKIIGREG 240
Cdd:PRK12704 151 TAEEAKEILLEKVEEEARHEAAVLIKEIEEEAKEEADKKAKEILAQAIQRCAADHVAETTVSVVNLPNDEMKGRIIGREG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 241 RNIRALEAATGVEIIVDDTPEAIIISGFDPVRREIARLSLHRLVADGRIHPARIEEVVSKTKKSIEDEIVEIGERTAIDL 320
Cdd:PRK12704 231 RNIRALETLTGVDLIIDDTPEAVILSGFDPIRREIARLALEKLVQDGRIHPARIEEMVEKARKEVDEEIREEGEQAVFEL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 321 GIHGLHPELIKMVGRMRFRSSYGQNLLQHSREVANLCATMAAELGLNVKHAKRAGLLHDIGKVTTEEPELPHAIIGMQLA 400
Cdd:PRK12704 311 GIHGLHPELIKLLGRLKYRTSYGQNVLQHSIEVAHLAGLMAAELGLDVKLAKRAGLLHDIGKALDHEVEGSHVEIGAELA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 401 QQYKEHPDVCNAIGAHHDEIEMTAMISPIIQSCDAISGSRPGARREIMESYIKRLKELEETAHSFEGVNQCYAIQAGREL 480
Cdd:PRK12704 391 KKYKESPVVINAIAAHHGDEEPTSIEAVLVAAADAISAARPGARRETLENYIKRLEKLEEIANSFEGVEKAYAIQAGREI 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 937828587 481 RVMVDADNVTDERASQLSFDISQKIEKEMQYPGQIKITVIREMRSVSYAK 530
Cdd:PRK12704 471 RVIVKPDKVDDLQAVRLARDIAKKIEEELQYPGQIKVTVIRETRAVEYAK 520
|
|
| RNase_Y |
TIGR03319 |
ribonuclease Y; Members of this family are RNase Y, an endoribonuclease. The member from ... |
6-530 |
0e+00 |
|
ribonuclease Y; Members of this family are RNase Y, an endoribonuclease. The member from Bacillus subtilis, YmdA, has been shown to be involved in turnover of yitJ riboswitch. [Transcription, Degradation of RNA]
Pssm-ID: 188306 [Multi-domain] Cd Length: 514 Bit Score: 625.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 6 ILAAVVGAGIGFYVGRVLLLKLFKEQEEQATERAKLIIREAEVKAETQKKDKMLEAKEHFLKLKVEHEEESNRKKNIILQ 85
Cdd:TIGR03319 1 ILLALVALIVGLIIGYLLRKRIAEKKLGSAEELAKRIIEEAKKEAETLKKEALLEAKEEVHKLRAELERELKERRNELQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 86 NENKVKQREQQVTKQLEDLKRKEQENDVLKDKLNQQlegfnkrkedlEAQFRDKQAKVEQDHHEILSRLERIANLSAEEA 165
Cdd:TIGR03319 81 LERRLLQREETLDRKMESLDKKEENLEKKEKELSNK-----------EKNLDEKEEELEELIAEQREELERISGLTQEEA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 166 REQLVENLKSEASTRASSYIKDIVAEAKLTATKEAKKVVIETIQRTAAEHAIENCVSIFNIESDDIKGKIIGREGRNIRA 245
Cdd:TIGR03319 150 KEILLEEVEEEARHEAAKLIKEIEEEAKEEADKKAKEILATAIQRYAGDHVAETTVSVVNLPNDEMKGRIIGREGRNIRA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 246 LEAATGVEIIVDDTPEAIIISGFDPVRREIARLSLHRLVADGRIHPARIEEVVSKTKKSIEDEIVEIGERTAIDLGIHGL 325
Cdd:TIGR03319 230 LETLTGVDLIIDDTPEAVILSGFDPVRREIARMALEKLIQDGRIHPARIEEMVEKATKEVDNAIREEGEQAAFDLGVHGL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 326 HPELIKMVGRMRFRSSYGQNLLQHSREVANLCATMAAELGLNVKHAKRAGLLHDIGKVTTEEPELPHAIIGMQLAQQYKE 405
Cdd:TIGR03319 310 HPELIKLLGRLKFRTSYGQNVLQHSIEVAHLAGIMAAELGEDVKLAKRAGLLHDIGKAVDHEVEGSHVEIGAELAKKYKE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 406 HPDVCNAIGAHHDEIEMTAMISPIIQSCDAISGSRPGARREIMESYIKRLKELEETAHSFEGVNQCYAIQAGRELRVMVD 485
Cdd:TIGR03319 390 SPEVVNAIAAHHGDVEPTSIEAVLVAAADALSAARPGARRESLENYIKRLEKLEEIANSFEGVEKSYAIQAGREIRVMVK 469
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 937828587 486 ADNVTDERASQLSFDISQKIEKEMQYPGQIKITVIREMRSVSYAK 530
Cdd:TIGR03319 470 PEKISDDQAVVLARDIAKKIEEELEYPGQIKVTVIRETRAVEYAK 514
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
3-530 |
1.91e-156 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 455.71 E-value: 1.91e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 3 IYIILAAVVGAGIGFYVGRvlllkLFKEQeeQATERAKLIIREAEVKAETQKKDKMLEAKEHFLKLKVEHEEESNRKKNI 82
Cdd:PRK12705 6 LLVILLLLIGLLLGVLVVL-----LKKRQ--RLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 83 ILQNENKVKQREQQVTKQLEDLKRKEQENDVLKDKLNQQLEGFNKRKEDLEAqfrdkqakveqdhheilsRLERIANLSA 162
Cdd:PRK12705 79 LQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSARELELEELEKQLDN------------------ELYRVAGLTP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 163 EEAREQLVENLKSEASTRASSYIKDIVAEAKLTATKEAKKVVIETIQRTAAEHAIENCVSIFNIESDDIKGKIIGREGRN 242
Cdd:PRK12705 141 EQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKAQNILAQAMQRIASETASDLSVSVVPIPSDAMKGRIIGREGRN 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 243 IRALEAATGVEIIVDDTPEAIIISGFDPVRREIARLSLHRLVADGRIHPARIEEVVSKTKKSIEDEIVEIGERTAIDLGI 322
Cdd:PRK12705 221 IRAFEGLTGVDLIIDDTPEAVVISSFNPIRREIARLTLEKLLADGRIHPARIEEYVQKANEEFKQKIYEIGEEVLEELGI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 323 HGLHPELIKMVGRMRFRSSYGQNLLQHSREVANLCATMAAELGLNVKHAKRAGLLHDIGKVTTEEPELPHAIIGMQLAQQ 402
Cdd:PRK12705 301 FDLKPGLVRLLGRLYFRTSYGQNVLSHSLEVAHLAGIIAAEIGLDPALAKRAGLLHDIGKSIDRESDGNHVEIGAELARK 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 403 YKEHPDVCNAIGAHHDEIEMTAMISPIIQSCDAISGSRPGARREIMESYIKRLKELEETAHSFEGVNQCYAIQAGRELRV 482
Cdd:PRK12705 381 FNEPDEVINAIASHHNKVNPETVYSVLVQIADALSAARPGARRESLDEYVQRLEELEQIAESFPGVEKAYAIQAGRELRV 460
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 937828587 483 MVDADNVTDERASQLSFDISQKIEKEMQYPGQIKITVIREMRSVSYAK 530
Cdd:PRK12705 461 IVEPEKVSDAQATLLARDIAKKIENDLTYPGPIKVTLIRETRAVEYAR 508
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
6-530 |
1.92e-145 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 428.90 E-value: 1.92e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 6 ILAAVVGAGIGFYVGRVLL---LKLFKEQEE---------------QATERAKLIIREAEVKAETQKKDKMLEAKEHFLK 67
Cdd:PRK00106 4 IIILVVSALIGLVIGYVLIsikMKSAKEAAEltllnaeqeavnlrgKAERDAEHIKKTAKRESKALKKELLLEAKEEARK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 68 LKVEHEEESNRKKNIILQNENKVKQREQQVTKQLEDLKRKEQENDVLKDKLNQQLEGFNKRKEDLEAQFRDKQAKveqdh 147
Cdd:PRK00106 84 YREEIEQEFKSERQELKQIESRLTERATSLDRKDENLSSKEKTLESKEQSLTDKSKHIDEREEQVEKLEEQKKAE----- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 148 heilsrLERIANLSAEEAREQLVENLKSEASTRASSYIKDIVAEAKLTATKEAKKVVIETIQRTAAEHAIENCVSIFNIE 227
Cdd:PRK00106 159 ------LERVAALSQAEAREIILAETENKLTHEIATRIREAEREVKDRSDKMAKDLLAQAMQRLAGEYVTEQTITTVHLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 228 SDDIKGKIIGREGRNIRALEAATGVEIIVDDTPEAIIISGFDPVRREIARLSLHRLVADGRIHPARIEEVVSKTKKSIED 307
Cdd:PRK00106 233 DDNMKGRIIGREGRNIRTLESLTGIDVIIDDTPEVVVLSGFDPIRREIARMTLESLIKDGRIHPARIEELVEKNRLEMDN 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 308 EIVEIGERTAIDLGIHGLHPELIKMVGRMRFRSSYGQNLLQHSREVANLCATMAAELGLNVKHAKRAGLLHDIGKVTTEE 387
Cdd:PRK00106 313 RIREYGEAAAYEIGAPNLHPDLIKIMGRLQFRTSYGQNVLRHSVEVGKLAGILAGELGENVALARRAGFLHDMGKAIDRE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 388 PELPHAIIGMQLAQQYKEHPDVCNAIGAHHDEIEMTAMISPIIQSCDAISGSRPGARREIMESYIKRLKELEETAHSFEG 467
Cdd:PRK00106 393 VEGSHVEIGMEFARKYKEHPVVVNTIASHHGDVEPESVIAVIVAAADALSSARPGARNESMENYIKRLRDLEEIANSFDG 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 937828587 468 VNQCYAIQAGRELRVMVDADNVTDERASQLSFDISQKIEKEMQYPGQIKITVIREMRSVSYAK 530
Cdd:PRK00106 473 VQNSFALQAGREIRIMVQPEKISDDQVTILAHKVREKIENNLDYPGNIKVTVIRELRAVDYAK 535
|
|
| KH-I_RNaseY |
cd22431 |
type I K homology (KH) RNA-binding domain found in ribonuclease Y (RNase Y) and similar ... |
218-296 |
1.58e-43 |
|
type I K homology (KH) RNA-binding domain found in ribonuclease Y (RNase Y) and similar proteins; RNase Y is an endoribonuclease that initiates mRNA decay. It initiates the decay of all SAM-dependent riboswitches, such as yitJ riboswitch. RNase Y is involved in processing of the gapA operon mRNA and it cleaves between cggR and gapA. It is also the decay-initiating endonuclease for rpsO mRNA. It plays a role in degradation of type I toxin-antitoxin system bsrG/SR4 RNAs and also a minor role in degradation of type I toxin-antitoxin system bsrE/SR5 degradation.
Pssm-ID: 411859 [Multi-domain] Cd Length: 79 Bit Score: 148.88 E-value: 1.58e-43
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 937828587 218 ENCVSIFNIESDDIKGKIIGREGRNIRALEAATGVEIIVDDTPEAIIISGFDPVRREIARLSLHRLVADGRIHPARIEE 296
Cdd:cd22431 1 ERTVSTVNLPNDEMKGRIIGREGRNIRAFEAATGVDLIIDDTPEAVILSGFDPVRREVARRTLEKLVEDGRIHPARIEE 79
|
|
| RnaY |
COG1418 |
HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal ... |
327-524 |
1.07e-38 |
|
HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal structure and biogenesis, General function prediction only];
Pssm-ID: 441028 [Multi-domain] Cd Length: 191 Bit Score: 140.03 E-value: 1.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 327 PELIKMVgrMRFRSSYGQNLLQHSREVANLCATMAAELGLNVKHAKRAGLLHDIGKVTTEEPELPHAIIGMQLAQQYK-- 404
Cdd:COG1418 2 PELIKLV--KYLRTSYGQHDLQHSLRVAKLAGLIAAEEGADVEVAKRAALLHDIGKAKDHEVEGSHAEIGAELARKYLes 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 405 ------EHPDVCNAIGAHHDE--IEMTAMISPIIQSCDAISGSrpGArreimesyikrlkeleetahsfEGVNQCYAI-- 474
Cdd:COG1418 80 lgfpeeEIEAVVHAIEAHSFSggIEPESLEAKIVQDADRLDAL--GA----------------------IGVARAFAIgg 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 475 QAGRELR---------VMVDADNVTDERASQLSFDISQKIEKEMQ-YPgqikITVIREMR 524
Cdd:COG1418 136 QAGRELRdpedtainhFYEKLLKLKDLMATELARDIAKKREEFMEeFP----VTVIRETR 191
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
5-215 |
4.82e-37 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 135.78 E-value: 4.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 5 IILAAVVGAGIGFYVGRVLLLKLFKEQEEQATERAKLIIREAEVKAETQKKDKMLEAKEHFLKLKVEHEEESNRKKNIIL 84
Cdd:pfam12072 2 IIILAIIALVVGFVVGYLVRKSIAEAKIGSAEELAKRIIEEAKKEAETKKKEALLEAKEEIHKLRAEAERELKERRNELQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 85 QNENKVKQREQQVTKQLEDLKRKEQendvlkdKLNQQLEGFNKRKEDLEAqfrdKQAKVEQDHHEILSRLERIANLSAEE 164
Cdd:pfam12072 82 RQERRLLQKEETLDRKDESLEKKEE-------SLEKKEKELEAQQQQLEE----KEEELEELIEEQRQELERISGLTSEE 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 937828587 165 AREQLVENLKSEASTRASSYIKDIVAEAKLTATKEAKKVVIETIQRTAAEH 215
Cdd:pfam12072 151 AKEILLDEVEEELRHEAAVMIKEIEEEAKEEADKKAKEIIALAIQRCAADH 201
|
|
| Krr1 |
COG1094 |
rRNA processing protein Krr1/Pno1, contains KH domain [Translation, ribosomal structure and ... |
229-311 |
1.41e-19 |
|
rRNA processing protein Krr1/Pno1, contains KH domain [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440711 [Multi-domain] Cd Length: 177 Bit Score: 86.03 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 229 DDIKGKIIGREGRNIRALEAATGVEIIVDDTPEAiIISGFDPVrrEIARLSLHRLVaDGRIHPArIEEVVSKTKKSIEDE 308
Cdd:COG1094 98 DRIKGRIIGREGRTRRIIEELTGVDISIYGKTVA-IIGDFDQV--EIAREAIEMLI-DGRIHPT-VYEFLEKARRELKRR 172
|
...
gi 937828587 309 IVE 311
Cdd:COG1094 173 RLE 175
|
|
| HDIG |
TIGR00277 |
HDIG domain; This domain is found in a few known nucleotidyltransferes and in a large number ... |
342-417 |
2.35e-19 |
|
HDIG domain; This domain is found in a few known nucleotidyltransferes and in a large number of uncharacterized proteins. It contains four widely separated His residues, the second of which is part of an invariant dipeptide His-Asp in a region matched approximately by the motif HDIG. This model may annotate homologous domains in which one or more of the His residues is conserved but misaligned, and some probable false-positive hits.
Pssm-ID: 272994 [Multi-domain] Cd Length: 80 Bit Score: 82.38 E-value: 2.35e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 937828587 342 YGQNLLQHSREVANLCATMAAELGLNVKHAKRAGLLHDIGKVTTEEP--ELPHAIIGMQLAQQYKEHPDVCNAIGAHH 417
Cdd:TIGR00277 1 YGQNVLQHSLEVAKLAEALARELGLDVELARRGALLHDIGKPITREGviFESHVVVGAEIARKYGEPLEVIDIIAEHH 78
|
|
| HD |
pfam01966 |
HD domain; HD domains are metal dependent phosphohydrolases. |
346-430 |
2.68e-11 |
|
HD domain; HD domains are metal dependent phosphohydrolases.
Pssm-ID: 460398 [Multi-domain] Cd Length: 110 Bit Score: 60.71 E-value: 2.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 346 LLQHSREVANLCATMAAELG-LNVKHAKRAGLLHDIGKVTT------EEPELPHAIIGMQLAQQYKEHP---DVCNAIGA 415
Cdd:pfam01966 1 RLEHSLRVALLARELAEELGeLDRELLLLAALLHDIGKGPFgdekpeFEIFLGHAVVGAEILRELEKRLgleDVLKLILE 80
|
90
....*....|....*
gi 937828587 416 HHDEIEMTAMISPII 430
Cdd:pfam01966 81 HHESWEGAGYPEEIS 95
|
|
| HDGYP |
COG2206 |
HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal ... |
223-441 |
4.25e-11 |
|
HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal transduction mechanisms];
Pssm-ID: 441808 [Multi-domain] Cd Length: 316 Bit Score: 64.22 E-value: 4.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 223 IFNIESDDIKGKIIGREGRNIRALEAATGVEIIVDDTPEAIIISGFDPVRREIARLSLHRLVADGRIHPARIEEVVSKTK 302
Cdd:COG2206 32 LLLLLLLLLALLALLLLLLLLLALLALLLALLALLLLLLLLLLLLSLLLAVALLLAELLLLLAALESLLAELFEELRLGL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 303 KSIEDEIVEIGERTAIDLgihglhpeLIKMVGRMRFRSSYgqnLLQHSREVANLCATMAAELGLN---VKHAKRAGLLHD 379
Cdd:COG2206 112 LEELKKLVEELDELLPDA--------LLALLAALDAKDPY---TYGHSVRVAVLALALARELGLSeeeLEDLGLAALLHD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 380 IGKV-------------TTEEPELP--HAIIGMQLAQQYKEHPDVCNAIGAHH--------------DEIEMTAMISPII 430
Cdd:COG2206 181 IGKIgipdeilnkpgklTDEEFEIIkkHPEYGYEILKKLPGLSEVAEIVLQHHerldgsgyprglkgEEIPLLARILAVA 260
|
250
....*....|.
gi 937828587 431 QSCDAISGSRP 441
Cdd:COG2206 261 DVYDALTSDRP 271
|
|
| HDc |
smart00471 |
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ... |
342-445 |
1.48e-09 |
|
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic nucleotide phosphodiesterases (PDEc). This profile/HMM does not detect HD homologues in bacterial glycine aminoacyl-tRNA synthetases (beta subunit).
Pssm-ID: 214679 [Multi-domain] Cd Length: 124 Bit Score: 56.15 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 342 YGQNLLQHSREVANLCATMAAELGL-NVKHAKRAGLLHDIGKVTT-------EEPELPHAIIGMQLAQQYKEHPDVCN-- 411
Cdd:smart00471 1 SDYHVFEHSLRVAQLAAALAEELGLlDIELLLLAALLHDIGKPGTpdsflvkTSVLEDHHFIGAEILLEEEEPRILEEil 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 937828587 412 --AIGAHHDEIEMTAM--ISP---IIQSCDAISGSRPGARR 445
Cdd:smart00471 81 rtAILSHHERPDGLRGepITLearIVKVADRLDALRADRRY 121
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
30-202 |
7.52e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 7.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 30 EQEEQATERAKLIIREAEV--KAETQKKDKMLEAKEHFLKLKVEH--EEESNRKKNIILQNENKVKQREQQVTKQLEDLK 105
Cdd:PTZ00121 1567 EEAKKAEEDKNMALRKAEEakKAEEARIEEVMKLYEEEKKMKAEEakKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEK 1646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 106 RK-------EQENDVLKDKLNQQLEGFNKRKEDLEAQFRDKQAKVEQDHH--EILSRLERIANLSAEEAREqlVENLKSE 176
Cdd:PTZ00121 1647 KKaeelkkaEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKeaEEAKKAEELKKKEAEEKKK--AEELKKA 1724
|
170 180
....*....|....*....|....*.
gi 937828587 177 ASTRassyiKDIVAEAKLTATKEAKK 202
Cdd:PTZ00121 1725 EEEN-----KIKAEEAKKEAEEDKKK 1745
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
29-218 |
1.40e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 29 KEQEEQATERAKLIIREAEVKAETQKKDKMLEAKEHFLKLKVEHEEESNRKKNIILQNENKVKQREQQVTKQLEDLKRKE 108
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 109 QENDVLKDKLNQQLEGFNKRKEDLEAQFRDKQAKVEQDHHEILSRL-ERIANLSAEEAREQLVENLKSEASTRASSYIKD 187
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEaELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
170 180 190
....*....|....*....|....*....|.
gi 937828587 188 IVAEAKLTATKEAKKVVIETIQRTAAEHAIE 218
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEE 436
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
21-216 |
1.46e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 21 RVLLLKLFKEQEEQATERAKLIIREAEVKAETQKKDKmLEAKEHFLKLKVEHEEESNRKKNiilQNENKVKQREQQVTKQ 100
Cdd:COG1196 228 ELLLLKLRELEAELEELEAELEELEAELEELEAELAE-LEAELEELRLELEELELELEEAQ---AEEYELLAELARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 101 LEDLKRKEQENDVLKDKLNQQLEGFNKRKEDLEAQFRDKQAKVEQDHHEILSRLERIANlsAEEAREQLVENLKSEASTR 180
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE--AEEALLEAEAELAEAEEEL 381
|
170 180 190
....*....|....*....|....*....|....*.
gi 937828587 181 ASSYIKDIVAEAKLTATKEAKKVVIETIQRTAAEHA 216
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
|
| Cas3''_I |
cd09641 |
CRISPR/Cas system-associated protein Cas3''; CRISPR (Clustered Regularly Interspaced Short ... |
340-417 |
3.92e-06 |
|
CRISPR/Cas system-associated protein Cas3''; 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; HD-like nuclease, specifically digesting double-stranded oligonucleotides and preferably cleaving at G:C pairs; signature gene for Type I
Pssm-ID: 193608 [Multi-domain] Cd Length: 200 Bit Score: 47.65 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 340 SSYGQNLLQHSREVANLCATMA--------AELGLNVKHAKRAGLLHDIGKVTTE----------------EPELPHAII 395
Cdd:cd09641 3 SGPWQPLLEHLLDVAAWDAELAeefarklgLELGLSRELLALAGLLHDLGKATPAfqkylrggkealregkRKEVRHSLL 82
|
90 100 110
....*....|....*....|....*....|
gi 937828587 396 GMQLAQQYKEHPD--------VCNAIGAHH 417
Cdd:cd09641 83 GALLLYELLKELGldeelallLAYAIAGHH 112
|
|
| cas3_HD |
TIGR01596 |
CRISPR-associated endonuclease Cas3-HD; CRISPR/Cas systems are widespread, mobile systems for ... |
346-487 |
6.01e-06 |
|
CRISPR-associated endonuclease Cas3-HD; CRISPR/Cas systems are widespread, mobile systems for host defense against invasive elements such as phage. In these systems, Cas3 designates one of the core proteins shared widely by multiple types of CRISPR/Cas system. This model represents an HD-like endonuclease that occurs either separately or as the N-terminal region of Cas3, the helicase-containing CRISPR-associated protein.
Pssm-ID: 273711 [Multi-domain] Cd Length: 176 Bit Score: 46.81 E-value: 6.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 346 LLQHSREVANLCATM-------AAELGLNVKH-AKRAGLLHDIGKVTTE-------------EPELPHAIIGMQLAQQYK 404
Cdd:TIGR01596 1 LKEHLLDVAAVAEALpalrprlAEKLGLELRElLKLAGLLHDLGKASPAfqkklrkaeergdRGEVRHSTLSAALLYDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 405 EHPD--------VCNAIGAHHDEIEMTAMISPIIQSCDAISGSRPGARREIMESYIKRLKELEETAHSFEGVNqcyAIQA 476
Cdd:TIGR01596 81 EELGleeelallLALAIAGHHGGLIDDDDLEELLELLERELEEALGELLEELEELLDEVLKALPLRLLLDKEE---PIEL 157
|
170
....*....|....*
gi 937828587 477 GRELR----VMVDAD 487
Cdd:TIGR01596 158 YLLARllfgLLVDAD 172
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
30-321 |
6.13e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 6.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 30 EQEEQATERAKLIIREAEVKAETQKKDKMLEAKEHFLKLKVEHEEESNRKKNIILQNENKVKQREQQVTKQLEDLKRKEQ 109
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 110 ENDVL----------KDKLNQQLEGFNKRKEDLEAQFRDKQAKVEQDHHEILSRLERIANLSAEEAREQLVENLKSEAST 179
Cdd:COG1196 422 ELEELeealaeleeeEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 180 RASSYIKDIVAEAKLTATKEAKKVVIETIQ-----RTAAEHAIENCVSIFNIESDDIKGKIIG-----REGR-NIRALEA 248
Cdd:COG1196 502 DYEGFLEGVKAALLLAGLRGLAGAVAVLIGveaayEAALEAALAAALQNIVVEDDEVAAAAIEylkaaKAGRaTFLPLDK 581
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 937828587 249 ATGVEIIVDDTP-----EAIIISGFDPVRREIARLSLHRLVADGRIHPARIEEVVSKTKKSIEDEIVEIGERTAIDLG 321
Cdd:COG1196 582 IRARAALAAALArgaigAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAG 659
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
29-218 |
1.08e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 29 KEQEEQATERAKLIIREAEVKAETQKKDKMLEAKEHFLKLKVEHEEESNRKKNIILQNENKVKQREQQVTKQLEDLKRKE 108
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 109 QENDVLKDKLNQQLEgfnkRKEDLEAQFRDKQAKVEQDHHEILSRLERIANLSAEEAR-EQLVENLKSEASTRASSYIKD 187
Cdd:COG1196 351 EELEEAEAELAEAEE----ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEElEEAEEALLERLERLEEELEEL 426
|
170 180 190
....*....|....*....|....*....|.
gi 937828587 188 IVAEAKLTATKEAKKVVIETIQRTAAEHAIE 218
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
|
| YqeK |
COG1713 |
Diadenosine tetraphosphatase YqeK or a related HD superfamily phosphohydrolase [Signal ... |
347-417 |
1.23e-05 |
|
Diadenosine tetraphosphatase YqeK or a related HD superfamily phosphohydrolase [Signal transduction mechanisms, General function prediction only];
Pssm-ID: 441319 [Multi-domain] Cd Length: 184 Bit Score: 45.88 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 347 LQHSREVANLCATMAAELGLNVKHAKRAGLLHDIGK--------------------VTTEEPELPHAIIGMQLAQQ-YKE 405
Cdd:COG1713 19 YEHTLGVAETAVELAERYGVDVEKAELAGLLHDYAKelppeellelakeygldldeLEEYNPELLHGPVGAYLAKEeFGI 98
|
90
....*....|...
gi 937828587 406 H-PDVCNAIgAHH 417
Cdd:COG1713 99 TdEEILNAI-RYH 110
|
|
| HDc |
cd00077 |
Metal dependent phosphohydrolases with conserved 'HD' motif |
344-431 |
2.39e-05 |
|
Metal dependent phosphohydrolases with conserved 'HD' motif
Pssm-ID: 238032 [Multi-domain] Cd Length: 145 Bit Score: 44.25 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 344 QNLLQHSREVANLCATMAAELGL---NVKHAKRAGLLHDIGKVTT--------EEPELPHAIIGMQLAQQ------YKEH 406
Cdd:cd00077 1 EHRFEHSLRVAQLARRLAEELGLseeDIELLRLAALLHDIGKPGTpdaiteeeSELEKDHAIVGAEILREllleevIKLI 80
|
90 100
....*....|....*....|....*
gi 937828587 407 PDVCNAIGAHHDEIEMTAMISPIIQ 431
Cdd:cd00077 81 DELILAVDASHHERLDGLGYPDGLK 105
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
26-211 |
5.45e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 5.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 26 KLFKEQEEQATERAKLIIREAEVKAETQKKDKMLEAKEHFLKLKVEH----EEESNRKKNIILQNENKVKQREQQVTKQL 101
Cdd:PTZ00121 1619 KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEeakkAEEDKKKAEEAKKAEEDEKKAAEALKKEA 1698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 102 EDLKRKEQendvlkdkLNQQLEGFNKRKEDLEAQFRDKQAKVEQDHHEILSRLERIANLSAEEAREQLVENLKSEASTRA 181
Cdd:PTZ00121 1699 EEAKKAEE--------LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKA 1770
|
170 180 190
....*....|....*....|....*....|
gi 937828587 182 SSYIKDIVAEAKLTATKEAKKVVIETIQRT 211
Cdd:PTZ00121 1771 EEIRKEKEAVIEEELDEEDEKRRMEVDKKI 1800
|
|
| HDOD |
pfam08668 |
HDOD domain; |
332-418 |
6.31e-05 |
|
HDOD domain;
Pssm-ID: 430141 [Multi-domain] Cd Length: 196 Bit Score: 44.14 E-value: 6.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 332 MVGRMRFRSSYG---QNLLQHSREVANLCATMAAELGLNVkhAKR---AGLLHDIGKV---------------------- 383
Cdd:pfam08668 78 VKRIFRGTPPLGfdlKGFWEHSLACALAARLLARRLGLDD--PEEaflAGLLHDIGKLillsllpdkyeellekaaeegi 155
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 937828587 384 ---TTEEPELP--HAIIGMQLAQQYKEHPDVCNAIGAHHD 418
Cdd:pfam08668 156 sllEAERELLGtdHAEVGAALLERWNLPEELVEAIAYHHN 195
|
|
| nadD |
PRK07152 |
nicotinate-nucleotide adenylyltransferase; |
347-387 |
6.72e-05 |
|
nicotinate-nucleotide adenylyltransferase;
Pssm-ID: 235947 [Multi-domain] Cd Length: 342 Bit Score: 44.94 E-value: 6.72e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 937828587 347 LQHSREVANLCATMAAELGLNVKHAKRAGLLHDIGKVTTEE 387
Cdd:PRK07152 198 YKHCLRVAQLAAELAKKNNLDPKKAYYAGLYHDITKEWDEE 238
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
21-206 |
7.88e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 7.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 21 RVLLLKLFKEQEEQATERAKLIIREAEVKAETQKKdKMLEAKEHFLKLKveHEEESNRKKNIILQNENKVKQREQQVTKQ 100
Cdd:PTZ00121 1634 KVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK-KAEEDKKKAEEAK--KAEEDEKKAAEALKKEAEEAKKAEELKKK 1710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 101 LEDLKRKEQEndVLKDKLNQQLEGFNKRKEDLEAQFRDKQAKVEQDHHEILSRLERIANLSAEEAREQLVENLKSEASTR 180
Cdd:PTZ00121 1711 EAEEKKKAEE--LKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEE 1788
|
170 180
....*....|....*....|....*.
gi 937828587 181 ASSyiKDIVAEAKLTATKEAKKVVIE 206
Cdd:PTZ00121 1789 DEK--RRMEVDKKIKDIFDNFANIIE 1812
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
29-202 |
1.41e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 29 KEQEEQATERAKLI---IREAEVKAETQKKDKMLEAKEHFLKLKVEHEEESNRKKNIILQNENKVKQREQQVTKQLEDLK 105
Cdd:COG1196 320 ELEEELAELEEELEeleEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 106 RKEQENDVLKDKLNQQLEGFNKRKEDLEAQFRDKQAKVEQDHHEILSRLERIANLSAEEAR-EQLVENLKSEASTRASSY 184
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAlLELLAELLEEAALLEAAL 479
|
170
....*....|....*...
gi 937828587 185 IKDIVAEAKLTATKEAKK 202
Cdd:COG1196 480 AELLEELAEAAARLLLLL 497
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
29-214 |
1.82e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 29 KEQEEQATERAKLIIREAEVKAEtQKKDKMLEAKEHFLKLKVEHEEESNRKKNIILQNENKVKQREQQVTKQLEDLKRKE 108
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLE-ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 109 QENDVLKDKLNQQLEGFNKRKEDLEAQFRDKQAkvEQDHHEILSRL--ERIANLSAEEAREQLVENLKSEASTRASSYIK 186
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEA--EEALLERLERLeeELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
170 180
....*....|....*....|....*...
gi 937828587 187 DIVAEAKLTATKEAKKVVIETIQRTAAE 214
Cdd:COG1196 454 LEEEEEALLELLAELLEEAALLEAALAE 481
|
|
| HDOD |
COG1639 |
HD-like signal output (HDOD) domain, no enzymatic activity [Signal transduction mechanisms]; |
344-418 |
2.61e-04 |
|
HD-like signal output (HDOD) domain, no enzymatic activity [Signal transduction mechanisms];
Pssm-ID: 441246 [Multi-domain] Cd Length: 244 Bit Score: 42.65 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 344 QNLLQHSREVANLCATMAAELG-LNVKHAKRAGLLHDIGKV---------------TTEEPELP------------HAII 395
Cdd:COG1639 103 RRFWRHSLAVAAAARALARRLGlLDPEEAFLAGLLHDIGKLvllslfpeeyaellaLAEADGLSlaeaerevlgtdHAEL 182
|
90 100
....*....|....*....|...
gi 937828587 396 GMQLAQQYKEHPDVCNAIGAHHD 418
Cdd:COG1639 183 GAALARKWGLPEELVEAIRYHHD 205
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
76-219 |
5.94e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 5.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 76 SNRKKNIILQNENKVKQREQQVTKQLEDLKRKEQENDVLKDK---LNQQLEGFNKRKEDLEAQFRDKQAKVEQDHHEILS 152
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKEleeLEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 937828587 153 RLERIANLSAE----EAREQLVENLKSEASTRASSYIKDIVA-EAKLTATKEAKKVVIETIQRTAAEHAIEN 219
Cdd:TIGR02168 745 LEERIAQLSKEltelEAEIEELEERLEEAEEELAEAEAEIEElEAQIEQLKEELKALREALDELRAELTLLN 816
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
29-206 |
8.10e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 8.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 29 KEQEEQATERAKLIIREAEVKAETQKKDKMLEAKehflklkvEHEEESNRKKNIILQNENKVKQREQQVTKQLEDLKRKE 108
Cdd:PTZ00121 1606 KMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLK--------KKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA 1677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 109 QENDVLKDKLNQQLEGFNKRKEDLEA--QFRDKQAKvEQDHHEILSRLERIANLSAEEAREQLVENLKSEASTRASSYIK 186
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALKKEAEEAKKaeELKKKEAE-EKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK 1756
|
170 180
....*....|....*....|
gi 937828587 187 DIVAEAKLTATKEAKKVVIE 206
Cdd:PTZ00121 1757 KKIAHLKKEEEKKAEEIRKE 1776
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
30-168 |
8.42e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.36 E-value: 8.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 30 EQEEQATERAKLIIREAEVKAETQKKDKmlEAKEHFLKLKVEHEEesnRKKNIILQNENKVKQREQQVTKQLEDLKRKEQ 109
Cdd:TIGR02169 180 EEVEENIERLDLIIDEKRQQLERLRRER--EKAERYQALLKEKRE---YEGYELLKEKEALERQKEAIERQLASLEEELE 254
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 937828587 110 ENDVLKDKLNQQLEGFNKRKEDLEAQFRDK----QAKVEQDHHEILSRLERIANLSAEEAREQ 168
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeQLRVKEKIGELEAEIASLERSIAEKEREL 317
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
23-219 |
1.26e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.58 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 23 LLLKLFKEQEEQATERAKLIIREAEVKAETQKKDKMLEAKEHFLKLKV-EHEEESNRKKNIILQNENKVKQREQQVTKQL 101
Cdd:TIGR02168 229 LLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVsELEEEIEELQKELYALANEISRLEQQKQILR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 102 EDLKRKEQENdvlkDKLNQQLEGFNKRKEDLEAQFRDKQAKVEQDHHEILSRLERIANLSAE-EAREQLVENLKSEASTR 180
Cdd:TIGR02168 309 ERLANLERQL----EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAElEELESRLEELEEQLETL 384
|
170 180 190
....*....|....*....|....*....|....*....
gi 937828587 181 ASSYikdivAEAKLTATKEAKKVVIETIQRTAAEHAIEN 219
Cdd:TIGR02168 385 RSKV-----AQLELQIASLNNEIERLEARLERLEDRRER 418
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
26-196 |
1.56e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 26 KLFKEQEEQATERAKLIIREAEVKAETQKKDKMLEAKEHFLKLkveheEESNRKKNIILQNENKVKQREQQVTKQLEDLK 105
Cdd:COG4717 92 ELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQEL-----EALEAELAELPERLEELEERLEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 106 RKEQENDVLKDKLNQQLEGFNKRKEDLEAQFRDKQAKVEQDHHEILSRLERianlsAEEAREQLVENLKSEASTRASSYI 185
Cdd:COG4717 167 ELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE-----AQEELEELEEELEQLENELEAAAL 241
|
170
....*....|.
gi 937828587 186 KDIVAEAKLTA 196
Cdd:COG4717 242 EERLKEARLLL 252
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
29-218 |
1.87e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 40.71 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 29 KEQEEQ------ATERAKLIirEAEVKAETQKKDKMLEAKEHFLKLKVEHEEESNRKKNIILQNEN-KVKQREQQVTKQL 101
Cdd:pfam15709 355 REQEEQrrlqqeQLERAEKM--REELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQeRARQQQEEFRRKL 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 102 EDLKRKEQENDVLKDKLNQQlegfnkRKEDLEAQFRDKQakveqdhheilsrlERIANLSAEEAREQLVENLKSEASTRA 181
Cdd:pfam15709 433 QELQRKKQQEEAERAEAEKQ------RQKELEMQLAEEQ--------------KRLMEMAEEERLEYQRQKQEAEEKARL 492
|
170 180 190
....*....|....*....|....*....|....*..
gi 937828587 182 SsyikdivAEAKLTATKEAKKVVIETIQRTAAEHAIE 218
Cdd:pfam15709 493 E-------AEERRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
37-218 |
2.34e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 37 ERAKLIIREAEVKAETQKKDKmlEAKEHFLKLKvehEEESNRKKNIILQNENKVKQREQQVTKQLEDLKRKEQENDVLKD 116
Cdd:COG1196 189 ERLEDILGELERQLEPLERQA--EKAERYRELK---EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 117 KLNQQLEGFNKRKEDLEAQFRDKQA-------KVEQDHHEILSRLERIANLSAEEAREQL-VENLKSEASTRASSYIKDI 188
Cdd:COG1196 264 ELEAELEELRLELEELELELEEAQAeeyellaELARLEQDIARLEERRRELEERLEELEEeLAELEEELEELEEELEELE 343
|
170 180 190
....*....|....*....|....*....|
gi 937828587 189 VAEAKLTATKEAKKVVIETIQRTAAEHAIE 218
Cdd:COG1196 344 EELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
30-202 |
2.54e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 30 EQEEQATERAKLIIREAEVKAETQKKDKMLEAKEHFLKLKVEHEEESNRKKNIILQNENKVKQREqqvTKQLEDLKRKEQ 109
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADE---LKKAEELKKAEE 1562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 110 ENDVLKDKLNQQLEGFNKRKEDLEAQFRDKQAKveqdhhEILSRLERIANLSAEEAREQLVENLKSEaSTRASSYIKDIV 189
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIE------EVMKLYEEEKKMKAEEAKKAEEAKIKAE-ELKKAEEEKKKV 1635
|
170
....*....|...
gi 937828587 190 AEAKLTATKEAKK 202
Cdd:PTZ00121 1636 EQLKKKEAEEKKK 1648
|
|
| KH_1 |
pfam00013 |
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ... |
233-267 |
3.01e-03 |
|
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause paraneoplastic opsoclonus ataxia.
Pssm-ID: 459630 [Multi-domain] Cd Length: 65 Bit Score: 36.11 E-value: 3.01e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 937828587 233 GKIIGREGRNIRALEAATGVEIIVDD-----TPEAIIISG 267
Cdd:pfam00013 12 GLIIGKGGSNIKEIREETGAKIQIPPsesegNERIVTITG 51
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
31-171 |
3.70e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.11 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 31 QEEQATERAKliIREAE-VKAETQKKDKMLEAK-EHFLKLKVEHEE------ESNRKKNIILQNENKVKQREQQV----- 97
Cdd:pfam17380 367 QEEIAMEISR--MRELErLQMERQQKNERVRQElEAARKVKILEEErqrkiqQQKVEMEQIRAEQEEARQREVRRleeer 444
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 937828587 98 TKQLEDLKRKEQENDVLKDKLNQQLEGFNKRKEDLEAQFRDKQAKVEQDHHEILSRLE-RIANLSAEEAREQLVE 171
Cdd:pfam17380 445 AREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEeRKQAMIEEERKRKLLE 519
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
29-218 |
4.10e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 29 KEQEEQATERAKLIIREAEV-KAETQKKDKMLEA---KEHFLKLKVEHEE---ESNRKKNIILQNENKVKQREQQVTKQL 101
Cdd:PTZ00121 1328 KKKADAAKKKAEEAKKAAEAaKAEAEAAADEAEAaeeKAEAAEKKKEEAKkkaDAAKKKAEEKKKADEAKKKAEEDKKKA 1407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 102 EDLKRKEQEN---DVLKDKLNQQLEGFNKRKEDLEAQFRD---KQAKVEQDHHEILSRLERIANlsAEEAREQLVENLKS 175
Cdd:PTZ00121 1408 DELKKAAAAKkkaDEAKKKAEEKKKADEAKKKAEEAKKADeakKKAEEAKKAEEAKKKAEEAKK--ADEAKKKAEEAKKA 1485
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 937828587 176 EASTRASSYIKDIVAEAKLTAtkEAKKVVIETIQRTAAEHAIE 218
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAA--EAKKKADEAKKAEEAKKADE 1526
|
|
| PRK13763 |
PRK13763 |
putative RNA-processing protein; Provisional |
231-290 |
4.74e-03 |
|
putative RNA-processing protein; Provisional
Pssm-ID: 237494 [Multi-domain] Cd Length: 180 Bit Score: 38.31 E-value: 4.74e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 231 IKGKIIGREGRNIRALEAATGVEIIVDDTPEAIIisGfDPVRREIARLSLHRLVaDGRIH 290
Cdd:PRK13763 105 IKGRIIGEGGKTRRIIEELTGVDISVYGKTVAII--G-DPEQVEIAREAIEMLI-EGAPH 160
|
|
| arCOG04150 |
TIGR03665 |
arCOG04150 universal archaeal KH domain protein; This family of proteins is universal among ... |
231-290 |
4.77e-03 |
|
arCOG04150 universal archaeal KH domain protein; This family of proteins is universal among the 41 archaeal genomes analyzed, and is not observed outside of the archaea. The proteins contain a single KH domain (pfam00013) which is likely to confer the ability to bind RNA.
Pssm-ID: 274711 [Multi-domain] Cd Length: 172 Bit Score: 37.93 E-value: 4.77e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 231 IKGKIIGREGRNIRALEAATGVEIIVDDTPEAIIisGfDPVRREIARLSLHRLVaDGRIH 290
Cdd:TIGR03665 99 IKGRIIGEGGKTRRIIEELTGVSISVYGKTVGII--G-DPEQVQIAREAIEMLI-EGAPH 154
|
|
| KH-I_PNPase |
cd02393 |
type I K homology (KH) RNA-binding domain found in polyribonucleotide nucleotidyltransferase ... |
233-258 |
5.20e-03 |
|
type I K homology (KH) RNA-binding domain found in polyribonucleotide nucleotidyltransferase (PNPase) and similar proteins; PNPase, also called polynucleotide phosphorylase, is a polyribonucleotide nucleotidyl transferase that degrades mRNA in prokaryotes and plant chloroplasts. It catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction. It is also involved, along with RNase II, in tRNA processing. The C-terminal region of PNPase contains domains homologous to those in other RNA binding proteins: a KH domain and an S1 domain. The model corresponds to the KH domain.
Pssm-ID: 411803 [Multi-domain] Cd Length: 70 Bit Score: 35.53 E-value: 5.20e-03
10 20
....*....|....*....|....*.
gi 937828587 233 GKIIGREGRNIRALEAATGVEIIVDD 258
Cdd:cd02393 16 GDVIGPGGKTIRAIIEETGAKIDIED 41
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
29-219 |
5.57e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 39.02 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 29 KEQEEQATERAKLIIREAEVKAEtQKKDKMLEAKEHFLKLKVEHEEESNRKKNiilQNENKVKQREQQvtKQLEDLKRKE 108
Cdd:PRK09510 68 QQQQKSAKRAEEQRKKKEQQQAE-ELQQKQAAEQERLKQLEKERLAAQEQKKQ---AEEAAKQAALKQ--KQAEEAAAKA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 109 QENDVLKDKLNQQLEGFNKRKEDLEAQFRDKQAKVEQDHHEILSRLERIANLSAE---------EAREQLVENLKSEAST 179
Cdd:PRK09510 142 AAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAaeakkkaeaEAKKKAAAEAKKKAAA 221
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 937828587 180 RASSYIKDIVAEAKLTATKEAKKVVIETIQRTAAEHAIEN 219
Cdd:PRK09510 222 EAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDD 261
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
29-214 |
5.59e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 39.47 E-value: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 29 KEQEEQATERAKLIIREAEVKAETQKKDKMLEAKEHFLKLKVEHEEESNRKKNIilqNENKVKQREQQVTKQLEDLKRKE 108
Cdd:pfam02029 87 KEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEY---QENKWSTEVRQAEEEGEEEEDKS 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 109 QEndvlkdklNQQLEGFNKRKEDLEAQFRDKQAKVEQDHHEILSRLERIANLSAEEAREQLVENLKSEASTRASSYIKDi 188
Cdd:pfam02029 164 EE--------AEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQ- 234
|
170 180
....*....|....*....|....*.
gi 937828587 189 VAEAKLTATKEAKKvVIETIQRTAAE 214
Cdd:pfam02029 235 EREEEAEVFLEAEQ-KLEELRRRRQE 259
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
26-191 |
6.73e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 39.23 E-value: 6.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 26 KLFKEQEEQATERAKLIIREAEVKAETQKKDKMLEAK-----EHFLKLKVEHEEES---NRKKNIILQNE--NKVKQREQ 95
Cdd:PHA02562 230 KTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKikskiEQFQKVIKMYEKGGvcpTCTQQISEGPDriTKIKDKLK 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 96 QVTKQLEDLKRKEQENDVLKDKLNQQLEGFNKRKEDLEAQFRDKQAKVEQ--DHHEILSRLERiANLSAEEAREQLVENL 173
Cdd:PHA02562 310 ELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKakKVKAAIEELQA-EFVDNAEELAKLQDEL 388
|
170 180
....*....|....*....|..
gi 937828587 174 KSEASTRASS----YIKDIVAE 191
Cdd:PHA02562 389 DKIVKTKSELvkekYHRGIVTD 410
|
|
| KH |
smart00322 |
K homology RNA-binding domain; |
233-265 |
7.04e-03 |
|
K homology RNA-binding domain;
Pssm-ID: 197652 [Multi-domain] Cd Length: 68 Bit Score: 35.35 E-value: 7.04e-03
10 20 30
....*....|....*....|....*....|...
gi 937828587 233 GKIIGREGRNIRALEAATGVEIIVDDTPEAIII 265
Cdd:smart00322 15 GLIIGKGGSTIKKIEEETGVKIDIPGPGSEERV 47
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
74-216 |
8.39e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 38.63 E-value: 8.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937828587 74 EESNRKKNIILQNENKVKQREQQVTKQLEDLKRKEQENdvlKDKLnQQLEgfnkrKEDLEAQFRDKQAkveqdhhEILSR 153
Cdd:PRK09510 62 EQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAE---QERL-KQLE-----KERLAAQEQKKQA-------EEAAK 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 937828587 154 LERIANLSAEEAREQLVENLKSEA---STRASSYIKDIVAEAKLTATKEAKKVVIETIQRTAAEHA 216
Cdd:PRK09510 126 QAALKQKQAEEAAAKAAAAAKAKAeaeAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEA 191
|
|
| |
