|
Name |
Accession |
Description |
Interval |
E-value |
| RNase_Y |
TIGR03319 |
ribonuclease Y; Members of this family are RNase Y, an endoribonuclease. The member from ... |
21-519 |
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: 774.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 21 YVVARNLLLQKQSQARQTAEDIVNQAHKEADNIKKEKLLEAKEENQILREQTEAELRERRSELQRQETRLLQKEENLERK 100
Cdd:TIGR03319 16 YLLRKRIAEKKLGSAEELAKRIIEEAKKEAETLKKEALLEAKEEVHKLRAELERELKERRNELQRLERRLLQREETLDRK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 101 SDLLDKKDEILEQKESKIEEKQQQVDAKESSVQTLIMKHEQELERISGLTQEEAINEQLQRVEEELSQDIAVLVKEKEKE 180
Cdd:TIGR03319 96 MESLDKKEENLEKKEKELSNKEKNLDEKEEELEELIAEQREELERISGLTQEEAKEILLEEVEEEARHEAAKLIKEIEEE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 181 AKEKVDKTAKELLATAVQRLAADHTSESTVSVVNLPNDEMKGRIIGREGRNIRTLETLTGIDLIIDDTPEAVILSGFDPI 260
Cdd:TIGR03319 176 AKEEADKKAKEILATAIQRYAGDHVAETTVSVVNLPNDEMKGRIIGREGRNIRALETLTGVDLIIDDTPEAVILSGFDPV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 261 RREIARTALVNLVSDGRIHPGRIEDMVEKARKEVDDIIREAGEQATFEVNAHNMHPDLVKIVGRLNYRTSYGQNVLKHSI 340
Cdd:TIGR03319 256 RREIARMALEKLIQDGRIHPARIEEMVEKATKEVDNAIREEGEQAAFDLGVHGLHPELIKLLGRLKFRTSYGQNVLQHSI 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 341 EVAHLASMLAAELGEDETLAKRAGLLHDVGKAIDHEVEGSHVEIGVELAKKYGENETVINAIHSHHGDVEPTSIISILVA 420
Cdd:TIGR03319 336 EVAHLAGIMAAELGEDVKLAKRAGLLHDIGKAVDHEVEGSHVEIGAELAKKYKESPEVVNAIAAHHGDVEPTSIEAVLVA 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 421 AADALSAARPGARKETLENYIRRLERLETLSESYDGVEKAFAIQAGREIRVIVSPEEIDDLKSYRLARDIKNQIEDELQY 500
Cdd:TIGR03319 416 AADALSAARPGARRESLENYIKRLEKLEEIANSFEGVEKSYAIQAGREIRVMVKPEKISDDQAVVLARDIAKKIEEELEY 495
|
490
....*....|....*....
gi 616394879 501 PGHIKVTVVRETRAVEYAK 519
Cdd:TIGR03319 496 PGQIKVTVIRETRAVEYAK 514
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
21-519 |
0e+00 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 770.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 21 YVVARNLLLQKQSQARQTAEDIVNQAHKEADNIKKEKLLEAKEENQILREQTEAELRERRSELQRQETRLLQKEENLERK 100
Cdd:PRK12704 22 YFVRKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 101 SDLLDKKDEILEQKESKIEEKQQQVDAKESSVQTLIMKHEQELERISGLTQEEAINEQLQRVEEELSQDIAVLVKEKEKE 180
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEILLEKVEEEARHEAAVLIKEIEEE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 181 AKEKVDKTAKELLATAVQRLAADHTSESTVSVVNLPNDEMKGRIIGREGRNIRTLETLTGIDLIIDDTPEAVILSGFDPI 260
Cdd:PRK12704 182 AKEEADKKAKEILAQAIQRCAADHVAETTVSVVNLPNDEMKGRIIGREGRNIRALETLTGVDLIIDDTPEAVILSGFDPI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 261 RREIARTALVNLVSDGRIHPGRIEDMVEKARKEVDDIIREAGEQATFEVNAHNMHPDLVKIVGRLNYRTSYGQNVLKHSI 340
Cdd:PRK12704 262 RREIARLALEKLVQDGRIHPARIEEMVEKARKEVDEEIREEGEQAVFELGIHGLHPELIKLLGRLKYRTSYGQNVLQHSI 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 341 EVAHLASMLAAELGEDETLAKRAGLLHDVGKAIDHEVEGSHVEIGVELAKKYGENETVINAIHSHHGDVEPTSIISILVA 420
Cdd:PRK12704 342 EVAHLAGLMAAELGLDVKLAKRAGLLHDIGKALDHEVEGSHVEIGAELAKKYKESPVVINAIAAHHGDEEPTSIEAVLVA 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 421 AADALSAARPGARKETLENYIRRLERLETLSESYDGVEKAFAIQAGREIRVIVSPEEIDDLKSYRLARDIKNQIEDELQY 500
Cdd:PRK12704 422 AADAISAARPGARRETLENYIKRLEKLEEIANSFEGVEKAYAIQAGREIRVIVKPDKVDDLQAVRLARDIAKKIEEELQY 501
|
490
....*....|....*....
gi 616394879 501 PGHIKVTVVRETRAVEYAK 519
Cdd:PRK12704 502 PGQIKVTVIRETRAVEYAK 520
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
32-519 |
0e+00 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 534.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 32 QSQARQTAEDIVNQAHKEADNIKKEKLLEAKEENQILREQTEAELRERRSELQRQETRLLQKEENLERKSDLLDKKDEIL 111
Cdd:PRK00106 48 RGKAERDAEHIKKTAKRESKALKKELLLEAKEEARKYREEIEQEFKSERQELKQIESRLTERATSLDRKDENLSSKEKTL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 112 EQKESKIEEKQQQVDAKESSVQTLIMKHEQELERISGLTQEEAINEQLQRVEEELSQDIAVLVKEKEKEAKEKVDKTAKE 191
Cdd:PRK00106 128 ESKEQSLTDKSKHIDEREEQVEKLEEQKKAELERVAALSQAEAREIILAETENKLTHEIATRIREAEREVKDRSDKMAKD 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 192 LLATAVQRLAADHTSESTVSVVNLPNDEMKGRIIGREGRNIRTLETLTGIDLIIDDTPEAVILSGFDPIRREIARTALVN 271
Cdd:PRK00106 208 LLAQAMQRLAGEYVTEQTITTVHLPDDNMKGRIIGREGRNIRTLESLTGIDVIIDDTPEVVVLSGFDPIRREIARMTLES 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 272 LVSDGRIHPGRIEDMVEKARKEVDDIIREAGEQATFEVNAHNMHPDLVKIVGRLNYRTSYGQNVLKHSIEVAHLASMLAA 351
Cdd:PRK00106 288 LIKDGRIHPARIEELVEKNRLEMDNRIREYGEAAAYEIGAPNLHPDLIKIMGRLQFRTSYGQNVLRHSVEVGKLAGILAG 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 352 ELGEDETLAKRAGLLHDVGKAIDHEVEGSHVEIGVELAKKYGENETVINAIHSHHGDVEPTSIISILVAAADALSAARPG 431
Cdd:PRK00106 368 ELGENVALARRAGFLHDMGKAIDREVEGSHVEIGMEFARKYKEHPVVVNTIASHHGDVEPESVIAVIVAAADALSSARPG 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 432 ARKETLENYIRRLERLETLSESYDGVEKAFAIQAGREIRVIVSPEEIDDLKSYRLARDIKNQIEDELQYPGHIKVTVVRE 511
Cdd:PRK00106 448 ARNESMENYIKRLRDLEEIANSFDGVQNSFALQAGREIRIMVQPEKISDDQVTILAHKVREKIENNLDYPGNIKVTVIRE 527
|
....*...
gi 616394879 512 TRAVEYAK 519
Cdd:PRK00106 528 LRAVDYAK 535
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
27-519 |
1.25e-176 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 506.94 E-value: 1.25e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 27 LLLQKQSQARQTAEDIVNQAHKEADNIKKEKLLEAKEENQILREQTEAELRERRSELQRQETRLLQKEENLERKSDLLDK 106
Cdd:PRK12705 23 VLLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 107 KDEILEQKESKIEEKQQQVDAKESSVqtlimkhEQELERISGLTQEEAINEQLQRVEEELSQDIAVLVKEKEKEAKEKVD 186
Cdd:PRK12705 103 LENQLEEREKALSARELELEELEKQL-------DNELYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 187 KTAKELLATAVQRLAADHTSESTVSVVNLPNDEMKGRIIGREGRNIRTLETLTGIDLIIDDTPEAVILSGFDPIRREIAR 266
Cdd:PRK12705 176 RKAQNILAQAMQRIASETASDLSVSVVPIPSDAMKGRIIGREGRNIRAFEGLTGVDLIIDDTPEAVVISSFNPIRREIAR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 267 TALVNLVSDGRIHPGRIEDMVEKARKEVDDIIREAGEQATFEVNAHNMHPDLVKIVGRLNYRTSYGQNVLKHSIEVAHLA 346
Cdd:PRK12705 256 LTLEKLLADGRIHPARIEEYVQKANEEFKQKIYEIGEEVLEELGIFDLKPGLVRLLGRLYFRTSYGQNVLSHSLEVAHLA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 347 SMLAAELGEDETLAKRAGLLHDVGKAIDHEVEGSHVEIGVELAKKYGENETVINAIHSHHGDVEPTSIISILVAAADALS 426
Cdd:PRK12705 336 GIIAAEIGLDPALAKRAGLLHDIGKSIDRESDGNHVEIGAELARKFNEPDEVINAIASHHNKVNPETVYSVLVQIADALS 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 427 AARPGARKETLENYIRRLERLETLSESYDGVEKAFAIQAGREIRVIVSPEEIDDLKSYRLARDIKNQIEDELQYPGHIKV 506
Cdd:PRK12705 416 AARPGARRESLDEYVQRLEELEQIAESFPGVEKAYAIQAGRELRVIVEPEKVSDAQATLLARDIAKKIENDLTYPGPIKV 495
|
490
....*....|...
gi 616394879 507 TVVRETRAVEYAK 519
Cdd:PRK12705 496 TLIRETRAVEYAR 508
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
21-204 |
2.47e-60 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 197.42 E-value: 2.47e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 21 YVVARNLLLQKQSQARQTAEDIVNQAHKEADNIKKEKLLEAKEENQILREQTEAELRERRSELQRQETRLLQKEENLERK 100
Cdd:pfam12072 18 YLVRKSIAEAKIGSAEELAKRIIEEAKKEAETKKKEALLEAKEEIHKLRAEAERELKERRNELQRQERRLLQKEETLDRK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 101 SDLLDKKDEILEQKESKIEEKQQQVDAKESSVQTLIMKHEQELERISGLTQEEAINEQLQRVEEELSQDIAVLVKEKEKE 180
Cdd:pfam12072 98 DESLEKKEESLEKKEKELEAQQQQLEEKEEELEELIEEQRQELERISGLTSEEAKEILLDEVEEELRHEAAVMIKEIEEE 177
|
170 180
....*....|....*....|....
gi 616394879 181 AKEKVDKTAKELLATAVQRLAADH 204
Cdd:pfam12072 178 AKEEADKKAKEIIALAIQRCAADH 201
|
|
| KH-I_RNaseY |
cd22431 |
type I K homology (KH) RNA-binding domain found in ribonuclease Y (RNase Y) and similar ... |
207-284 |
7.99e-44 |
|
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: 149.65 E-value: 7.99e-44
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616394879 207 ESTVSVVNLPNDEMKGRIIGREGRNIRTLETLTGIDLIIDDTPEAVILSGFDPIRREIARTALVNLVSDGRIHPGRIE 284
Cdd:cd22431 1 ERTVSTVNLPNDEMKGRIIGREGRNIRAFEAATGVDLIIDDTPEAVILSGFDPVRREVARRTLEKLVEDGRIHPARIE 78
|
|
| RnaY |
COG1418 |
HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal ... |
316-513 |
2.14e-39 |
|
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: 141.57 E-value: 2.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 316 PDLVKIVgrLNYRTSYGQNVLKHSIEVAHLASMLAAELGEDETLAKRAGLLHDVGKAIDHEVEGSHVEIGVELAKKYG-- 393
Cdd:COG1418 2 PELIKLV--KYLRTSYGQHDLQHSLRVAKLAGLIAAEEGADVEVAKRAALLHDIGKAKDHEVEGSHAEIGAELARKYLes 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 394 ------ENETVINAIHSHHGDV--EPTSIISILVAAADalsaarpgarketlenyirRLERLETlsesyDGVEKAFAI-- 463
Cdd:COG1418 80 lgfpeeEIEAVVHAIEAHSFSGgiEPESLEAKIVQDAD-------------------RLDALGA-----IGVARAFAIgg 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 464 QAGREIR---------VIVSPEEIDDLKSYRLARDIKNQIEDELQ-YPghikVTVVRETR 513
Cdd:COG1418 136 QAGRELRdpedtainhFYEKLLKLKDLMATELARDIAKKREEFMEeFP----VTVIRETR 191
|
|
| Krr1 |
COG1094 |
rRNA processing protein Krr1/Pno1, contains KH domain [Translation, ribosomal structure and ... |
207-300 |
1.78e-26 |
|
rRNA processing protein Krr1/Pno1, contains KH domain [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440711 [Multi-domain] Cd Length: 177 Bit Score: 105.68 E-value: 1.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 207 ESTVSVVNLPN--------DEMKGRIIGREGRNIRTLETLTGIDLIIDDTPEAVIlSGFDPIrrEIARTALVNLVsDGRI 278
Cdd:COG1094 79 DYMLEVIDLPDvgkspnalDRIKGRIIGREGRTRRIIEELTGVDISIYGKTVAII-GDFDQV--EIAREAIEMLI-DGRI 154
|
90 100
....*....|....*....|..
gi 616394879 279 HPGrIEDMVEKARKEVDDIIRE 300
Cdd:COG1094 155 HPT-VYEFLEKARRELKRRRLE 175
|
|
| HDIG |
TIGR00277 |
HDIG domain; This domain is found in a few known nucleotidyltransferes and in a large number ... |
331-408 |
6.27e-26 |
|
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: 100.87 E-value: 6.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 331 YGQNVLKHSIEVAHLASMLAAELGEDETLAKRAGLLHDVGKAIDHE--VEGSHVEIGVELAKKYGENETVINAIHSHHGD 408
Cdd:TIGR00277 1 YGQNVLQHSLEVAKLAEALARELGLDVELARRGALLHDIGKPITREgvIFESHVVVGAEIARKYGEPLEVIDIIAEHHGK 80
|
|
| HD |
pfam01966 |
HD domain; HD domains are metal dependent phosphohydrolases. |
335-413 |
1.04e-12 |
|
HD domain; HD domains are metal dependent phosphohydrolases.
Pssm-ID: 460398 [Multi-domain] Cd Length: 110 Bit Score: 64.56 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 335 VLKHSIEVAHLASMLAAELGE-DETLAKRAGLLHDVGK------AIDHEVEGSHVEIGVELAKKYGEN---ETVINAIHS 404
Cdd:pfam01966 1 RLEHSLRVALLARELAEELGElDRELLLLAALLHDIGKgpfgdeKPEFEIFLGHAVVGAEILRELEKRlglEDVLKLILE 80
|
....*....
gi 616394879 405 HHGDVEPTS 413
Cdd:pfam01966 81 HHESWEGAG 89
|
|
| HDc |
smart00471 |
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ... |
331-407 |
5.96e-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: 54.22 E-value: 5.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 331 YGQNVLKHSIEVAHLASMLAAELG-EDETLAKRAGLLHDVGKAIDH-------EVEGSHVEIGVELAKKYGENETVIN-- 400
Cdd:smart00471 1 SDYHVFEHSLRVAQLAAALAEELGlLDIELLLLAALLHDIGKPGTPdsflvktSVLEDHHFIGAEILLEEEEPRILEEil 80
|
....*....
gi 616394879 401 --AIHSHHG 407
Cdd:smart00471 81 rtAILSHHE 89
|
|
| HDGYP |
COG2206 |
HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal ... |
338-406 |
3.19e-08 |
|
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: 55.36 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 338 HSIEVAHLASMLAAELGEDETLAKR---AGLLHDVGK-AIDHEV---EG-----------SHVEIGVELAKKYGENETVI 399
Cdd:COG2206 147 HSVRVAVLALALARELGLSEEELEDlglAALLHDIGKiGIPDEIlnkPGkltdeefeiikKHPEYGYEILKKLPGLSEVA 226
|
....*..
gi 616394879 400 NAIHSHH 406
Cdd:COG2206 227 EIVLQHH 233
|
|
| HDc |
cd00077 |
Metal dependent phosphohydrolases with conserved 'HD' motif |
333-413 |
6.99e-08 |
|
Metal dependent phosphohydrolases with conserved 'HD' motif
Pssm-ID: 238032 [Multi-domain] Cd Length: 145 Bit Score: 51.57 E-value: 6.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 333 QNVLKHSIEVAHLASMLAAELG---EDETLAKRAGLLHDVGKAID--------HEVEGSHVEIGVELA------KKYGEN 395
Cdd:cd00077 1 EHRFEHSLRVAQLARRLAEELGlseEDIELLRLAALLHDIGKPGTpdaiteeeSELEKDHAIVGAEILrellleEVIKLI 80
|
90
....*....|....*...
gi 616394879 396 ETVINAIHSHHGDVEPTS 413
Cdd:cd00077 81 DELILAVDASHHERLDGL 98
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
29-202 |
1.09e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 29 LQKQSQARQTAEDIVNQAHKEADNIKKE--KLLEAKEENQILREQTEAELRERRSELQRQETRLLQKEENLERKSDLLDK 106
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAElaRLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 107 KDEILEQKESKIEEKQQQVDAKESSVQTLIMKHEQELERISGLTQEEAINEQLQRVEEELSQDIAVLVKEKEKEAKEKVD 186
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
170
....*....|....*.
gi 616394879 187 KTAKELLATAVQRLAA 202
Cdd:COG1196 429 ALAELEEEEEEEEEAL 444
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
30-202 |
2.23e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 30 QKQSQARQTAEDIVNQAHKEADNIKKEKLLEAKEENQILREQTEAELRERRSELQRQETRLLQKEENLERKSDLLDKKDE 109
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 110 ILEQKESKIEEKQQQVDAKESSVQtlimkhEQELERISGLTQEEAINEQLQRVEEELSQDIAVLVKEKEKEAKEKVDKTA 189
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEEE------EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA 491
|
170
....*....|...
gi 616394879 190 KELLATAVQRLAA 202
Cdd:COG1196 492 RLLLLLEAEADYE 504
|
|
| PgpH |
COG1480 |
Cyclic di-AMP-specific phosphodiesterase PgpH, HD superfamily [Signal transduction mechanisms]; ... |
338-416 |
5.10e-06 |
|
Cyclic di-AMP-specific phosphodiesterase PgpH, HD superfamily [Signal transduction mechanisms];
Pssm-ID: 441089 [Multi-domain] Cd Length: 692 Bit Score: 49.06 E-value: 5.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 338 HSIEVAHLASMLAAELGEDETLAKRAGLLHDVGKAIDHE--VEG---------------------SHVEIGVELAKKYGE 394
Cdd:COG1480 481 HSLMVANLAEAAAEAIGANPLLARVGAYYHDIGKMKRPLyfIENqmggenphdklspslsaliiiSHVKDGVELARKYKL 560
|
90 100
....*....|....*....|..
gi 616394879 395 NETVINAIHSHHGdvepTSIIS 416
Cdd:COG1480 561 PKEIIDFIRQHHG----TTLVK 578
|
|
| PRK13763 |
PRK13763 |
putative RNA-processing protein; Provisional |
220-294 |
7.36e-06 |
|
putative RNA-processing protein; Provisional
Pssm-ID: 237494 [Multi-domain] Cd Length: 180 Bit Score: 46.40 E-value: 7.36e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616394879 220 MKGRIIGREGRNIRTLETLTGIDLIIDDTPEAVIlsGfDPIRREIARTAlVNLVSDGRIHpGRIEDMVEKARKEV 294
Cdd:PRK13763 105 IKGRIIGEGGKTRRIIEELTGVDISVYGKTVAII--G-DPEQVEIAREA-IEMLIEGAPH-GTVYKFLERKKREL 174
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
54-238 |
8.44e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 8.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 54 KKEKLLEAKEENQILREQTEAELRERRSELQRQETRLLQKEENLERKSDLLDKKDEILEQKESKIEEKQQQVDAKESSVQ 133
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 134 TLIMKHEQELERISGLTQE-EAINEQLQRVEEELSQDIAVLvkEKEKEAKEKVDKTAKELLATAVQRLAADHTSESTVSV 212
Cdd:COG1196 320 ELEEELAELEEELEELEEElEELEEELEEAEEELEEAEAEL--AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
170 180
....*....|....*....|....*.
gi 616394879 213 VNLPNDEMKGRIIGREGRNIRTLETL 238
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEEL 423
|
|
| YqeK |
COG1713 |
Diadenosine tetraphosphatase YqeK or a related HD superfamily phosphohydrolase [Signal ... |
336-405 |
1.13e-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: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 336 LKHSIEVAHLASMLAAELGEDETLAKRAGLLHDVGKAIDHE---------------VEGSHVEI-----GVELAKK-YG- 393
Cdd:COG1713 19 YEHTLGVAETAVELAERYGVDVEKAELAGLLHDYAKELPPEellelakeygldldeLEEYNPELlhgpvGAYLAKEeFGi 98
|
90
....*....|..
gi 616394879 394 ENETVINAIHSH 405
Cdd:COG1713 99 TDEEILNAIRYH 110
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
29-204 |
1.88e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 29 LQKQSQARQTAEDIVNQAHKEADNIKKEKLLEAKEENQILREQTEAE--LRERRSELQRQETRLLQKEENLERKSDLLDK 106
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEeeLEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 107 KDEILEQKESKIEEKQQQVDAKESSVQTLIMKHEQELERISGLTQEEAINEQLQRVEEELSQDIAVLVKEKEKEAKEKVD 186
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
170
....*....|....*...
gi 616394879 187 KTAKELLATAVQRLAADH 204
Cdd:COG1196 464 LLAELLEEAALLEAALAE 481
|
|
| arCOG04150 |
TIGR03665 |
arCOG04150 universal archaeal KH domain protein; This family of proteins is universal among ... |
221-293 |
1.96e-05 |
|
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: 45.25 E-value: 1.96e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616394879 221 KGRIIGREGRNIRTLETLTGIDLIIDDTPEAVIlsGfDPIRREIARTAlVNLVSDGRIHpGRIEDMVEKARKE 293
Cdd:TIGR03665 100 KGRIIGEGGKTRRIIEELTGVSISVYGKTVGII--G-DPEQVQIAREA-IEMLIEGAPH-GTVYKFLERKRRE 167
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
56-143 |
2.24e-05 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 44.83 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 56 EKLLEAKEENQILREQTEAELRERRSELQRQETRLLQKEENLERKSDLLdkKDEILEQKESKIEEKQQQVDAKESSVQTL 135
Cdd:COG2825 32 QRILQESPEGKAAQKKLEKEFKKRQAELQKLEKELQALQEKLQKEAATL--SEEERQKKERELQKKQQELQRKQQEAQQD 109
|
....*...
gi 616394879 136 IMKHEQEL 143
Cdd:COG2825 110 LQKRQQEL 117
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
24-173 |
3.20e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 24 ARNLLLQKQSQARQTAEDIVNQAHKEADNIKKEKLLEAKEENQILREQTEAELRER-RSELQRQETRLLQKEENLERKSD 102
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERlEEELEELEEALAELEEEEEEEEE 442
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616394879 103 LLDKKDEILEQKESKIEEKQQQVDAKESSVQTLIMKHEQELERISGLTQEEAINEQLQRVEEELSQDIAVL 173
Cdd:COG1196 443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA 513
|
|
| nadD |
PRK07152 |
nicotinate-nucleotide adenylyltransferase; |
336-405 |
3.74e-05 |
|
nicotinate-nucleotide adenylyltransferase;
Pssm-ID: 235947 [Multi-domain] Cd Length: 342 Bit Score: 45.71 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 336 LKHSIEVAHLASMLAAELGEDETLAKRAGLLHDVGKAID-----------------------HEVEGSHVeigveLAKKY 392
Cdd:PRK07152 198 YKHCLRVAQLAAELAKKNNLDPKKAYYAGLYHDITKEWDeekhrkflkkylkdvknlpwyvlHQYVGALW-----LKHVY 272
|
90
....*....|....
gi 616394879 393 G-ENETVINAIHSH 405
Cdd:PRK07152 273 GiDDEEILNAIRNH 286
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
26-207 |
4.87e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 4.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 26 NLLLQKQSQARQTAEDIVNQAHKEADNIKKEKLLEAKEENQILREQTE-AELRERRSELQRQETRLLQKEENLERKSDLL 104
Cdd:COG1196 228 ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLElEELELELEEAQAEEYELLAELARLEQDIARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 105 DKK-----DEILEQKESKIEEKQQQVDAKESSVQTLIMKHEQELERISGLTQEEAINEQLQRVEEELSQDIAVLVKEKEK 179
Cdd:COG1196 308 EERrreleERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
|
170 180
....*....|....*....|....*...
gi 616394879 180 EAKEKVDKTAKELLATAVQRLAADHTSE 207
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLER 415
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
30-202 |
7.04e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 7.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 30 QKQSQARQTAEDIVNQAHKEAD-NIKKEKLLEAKEENQILREQ---TEAELRERRSELQRQETRLLQKEENLERKSDLLD 105
Cdd:COG1196 247 ELEELEAELEELEAELAELEAElEELRLELEELELELEEAQAEeyeLLAELARLEQDIARLEERRRELEERLEELEEELA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 106 KKDEILEQKESKIEEKQQQVDAKESSVQTLIMKHEQELERISGLTQE--EAINEQLQRVEEELSQDIAVLVKEKEKEAKE 183
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAElaEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
170
....*....|....*....
gi 616394879 184 KVDKTAKELLATAVQRLAA 202
Cdd:COG1196 407 EAEEALLERLERLEEELEE 425
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
28-173 |
1.61e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.56 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 28 LLQKQSQARQTAEDIVNQAHKE-ADNIKKEKLLEAKEENQILREQTEAELRERRSELQRQETRLLQKEENLERKSDLLDK 106
Cdd:COG3096 527 RLRQQQNAERLLEEFCQRIGQQlDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLA 606
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616394879 107 KDEILEQkeskieeKQQQVDAKESSVQTLIMKHEQELERISGLTQEEainEQLQRVEEELSQDIAVL 173
Cdd:COG3096 607 AQDALER-------LREQSGEALADSQEVTAAMQQLLEREREATVER---DELAARKQALESQIERL 663
|
|
| PRK02292 |
PRK02292 |
V-type ATP synthase subunit E; Provisional |
32-159 |
2.17e-04 |
|
V-type ATP synthase subunit E; Provisional
Pssm-ID: 235026 [Multi-domain] Cd Length: 188 Bit Score: 42.29 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 32 QSQARQTAEDIVNQAHKEADNIkkekLLEAKEENQILREQTEAELRERRSELQRQETrllqKEENLERKSDLLDKKDEIL 111
Cdd:PRK02292 11 RDEARARASEIRAEADEEAEEI----IAEAEADAEEILEDREAEAEREIEQLREQEL----SSAKLEAKRERLNARKEVL 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 616394879 112 EQKESKIEEKQQQVDA--KESSVQTLIMKHEQELERISGLTQEEAINEQL 159
Cdd:PRK02292 83 EDVRNQVEDEIASLDGdkREELTKSLLDAADADGVRVYSRKDDEDLVKSL 132
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
25-165 |
3.12e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 25 RNLLLQKQSQARQTAEDIVNQAHKEADNIKKEKLLEAKEENQilrEQTEAELRERRSELQRQETRLLQKEENLERKSDLL 104
Cdd:PTZ00121 1576 KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE---AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEEL 1652
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616394879 105 DKKDEILEQKESKIEEKQQQVDAKESSVQTLIMKHEQELERISGLTQEEAINEQLQRVEEE 165
Cdd:PTZ00121 1653 KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAE 1713
|
|
| HDOD |
pfam08668 |
HDOD domain; |
338-406 |
3.18e-04 |
|
HDOD domain;
Pssm-ID: 430141 [Multi-domain] Cd Length: 196 Bit Score: 41.83 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 338 HSIEVAHLASMLAAELGEDET-LAKRAGLLHDVGKAI----------------------DHEVE----G-SHVEIGVELA 389
Cdd:pfam08668 98 HSLACALAARLLARRLGLDDPeEAFLAGLLHDIGKLIllsllpdkyeellekaaeegisLLEAErellGtDHAEVGAALL 177
|
90
....*....|....*..
gi 616394879 390 KKYGENETVINAIHSHH 406
Cdd:pfam08668 178 ERWNLPEELVEAIAYHH 194
|
|
| Cas3''_I |
cd09641 |
CRISPR/Cas system-associated protein Cas3''; CRISPR (Clustered Regularly Interspaced Short ... |
332-408 |
4.01e-04 |
|
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: 41.88 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 332 GQNVLKHSIEVA--------HLASMLAAELGEDETLAKRAGLLHDVGKA----------------------IDHEVEGSh 381
Cdd:cd09641 6 WQPLLEHLLDVAawdaelaeEFARKLGLELGLSRELLALAGLLHDLGKAtpafqkylrggkealregkrkeVRHSLLGA- 84
|
90 100 110
....*....|....*....|....*....|.
gi 616394879 382 vEIGVELAKKYGENETVIN----AIHSHHGD 408
Cdd:cd09641 85 -LLLYELLKELGLDEELALllayAIAGHHGG 114
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
28-86 |
4.04e-04 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 40.76 E-value: 4.04e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 616394879 28 LLQKQSQARQTAEDIVNQAHKEADNIKKEKLLEAKEENQILREQTEAELRERRSELQRQ 86
Cdd:PRK07353 62 YEQQLASARKQAQAVIAEAEAEADKLAAEALAEAQAEAQASKEKARREIEQQKQAALAQ 120
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
30-86 |
6.01e-04 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 40.11 E-value: 6.01e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616394879 30 QKQSQARQTAEDIVNQAHKEADNIKKEKLLEAKEENQILREQTEAEL-RER---RSELQRQ 86
Cdd:cd06503 58 EKLAEARAEAQEIIEEARKEAEKIKEEILAEAKEEAERILEQAKAEIeQEKekaLAELRKE 118
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
35-173 |
7.84e-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: 42.35 E-value: 7.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 35 ARQTAEDIVNQAHKEADNIKKEKLLEAKEENQilrEQTEAELRERRSELQRQETRLLQKEENLERKSDLLDKKDEILEQK 114
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEEKIEELEEKIAEL---EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE 741
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616394879 115 ESKIEEKQQQVDAKESSVQTLIMKHEQELERISGLTQE-----EAINEQLQRVEEELSQDIAVL 173
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEaeaeiEELEAQIEQLKEELKALREAL 805
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
56-165 |
9.11e-04 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 39.49 E-value: 9.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 56 EKLLEAKEENQILREQTEAELRERRSELQRQETRLLQKEENLERKSDLLDKKDeiLEQKESKIEEKQQQVDAKESSVQ-T 134
Cdd:smart00935 7 QKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLSEAA--REKKEKELQKKVQEFQRKQQKLQqD 84
|
90 100 110
....*....|....*....|....*....|.
gi 616394879 135 LIMKHEQELERIsgltqEEAINEQLQRVEEE 165
Cdd:smart00935 85 LQKRQQEELQKI-----LDKINKAIKEVAKK 110
|
|
| cas3_HD |
TIGR01596 |
CRISPR-associated endonuclease Cas3-HD; CRISPR/Cas systems are widespread, mobile systems for ... |
336-464 |
9.54e-04 |
|
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: 40.26 E-value: 9.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 336 LKHSIEVAHLASML-------AAELGED-ETLAKRAGLLHDVGKA-------------------IDHEVEGShvEIGVEL 388
Cdd:TIGR01596 2 KEHLLDVAAVAEALpalrprlAEKLGLElRELLKLAGLLHDLGKAspafqkklrkaeergdrgeVRHSTLSA--ALLYDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 389 AKKYGENETVIN----AIHSHHGDVEPT-SIISILVAAADALSAARPGARKE--TLENYIRRLERLETLSESYDGVEKAF 461
Cdd:TIGR01596 80 LEELGLEEELALllalAIAGHHGGLIDDdDLEELLELLERELEEALGELLEEleELLDEVLKALPLRLLLDKEEPIELYL 159
|
...
gi 616394879 462 AIQ 464
Cdd:TIGR01596 160 LAR 162
|
|
| KH-I_Dim2p_like_rpt2 |
cd22390 |
second type I K homology (KH) RNA-binding domain found in Pyrococcus horikoshii Dim2p and ... |
221-292 |
1.30e-03 |
|
second type I K homology (KH) RNA-binding domain found in Pyrococcus horikoshii Dim2p and similar proteins; The family includes a group of conserved KH domain-containing protein mainly from archaea, such as Dim2p homologues from Pyrococcus horikoshii and Aeropyrum pernix. Dim2p acts as a preribosomal RNA processing factor that has been identified as an essential protein for the maturation of 40S ribosomal subunit in Saccharomyces cerevisiae. It is required for the cleavage at processing site A2 to generate the pre-20S rRNA and for the dimethylation of the 18S rRNA by 18S rRNA dimethyltransferase, Dim1p. Dim2p contains two K-homology (KH) RNA-binding domains. The model corresponds to the second one.
Pssm-ID: 411818 Cd Length: 96 Bit Score: 37.97 E-value: 1.30e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616394879 221 KGRIIGREGRNIRTLETLTGIDLIIDDTPEAVIlSGFDPIRreIARTAlVNLVSDGRIHpGRIEDMVEKARK 292
Cdd:cd22390 30 KGRVIGSGGKTRRLIEELTGCYISVYGKTVSII-GDFENLQ--IAKEA-IEMLLNGSPH-SSVYRFLEKKRR 96
|
|
| Cas10_III |
cd09680 |
CRISPR/Cas system-associated protein Cas10; CRISPR (Clustered Regularly Interspaced Short ... |
363-408 |
1.41e-03 |
|
CRISPR/Cas system-associated protein Cas10; 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; Multidomain protein with permuted HD nuclease domain, palm domain and Zn-ribbon; signature gene for type III; also known as Csm1 family
Pssm-ID: 187811 [Multi-domain] Cd Length: 650 Bit Score: 41.15 E-value: 1.41e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 616394879 363 AGLLHDVGKAI----DHEVEGSHVEIGVELAKKYGEN-ETVINAIHSHHGD 408
Cdd:cd09680 4 GALLHDIGKVVqragLGFYSKTHSKFGAEFLKEFSKNkDDLGDCISYHHTK 54
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
28-166 |
1.60e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 28 LLQKQSQARQTAEDIVNQAHKEADNIKKEKLLEAKEENQILREQTEAELRERRSELQRQETRLLQKEENLERKSDLLDKK 107
Cdd:COG1579 43 LEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEEL 122
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 616394879 108 DEILEQKESKIEEKQQQVDAKESSVQTLIMKHEQELERIsgltqEEAINEQLQRVEEEL 166
Cdd:COG1579 123 EEELAELEAELAELEAELEEKKAELDEELAELEAELEEL-----EAEREELAAKIPPEL 176
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
24-170 |
1.97e-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: 40.88 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 24 ARNLLLQKQSQARQTAEDIVNQAHKEADNIKKEkllEAKEENQILREQTEAELRERRSELQRQETRLLQKEENLERKSDL 103
Cdd:pfam17380 324 ARQAEMDRQAAIYAEQERMAMERERELERIRQE---ERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEA 400
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616394879 104 LdKKDEILEqkeskiEEKQQQvdakessvqtlIMKHEQELERISGlTQEEAINEQLQRVEEELSQDI 170
Cdd:pfam17380 401 A-RKVKILE------EERQRK-----------IQQQKVEMEQIRA-EQEEARQREVRRLEEERAREM 448
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
24-167 |
1.99e-03 |
|
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: 41.21 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 24 ARNLLLQKQSQARQTAEDIVN---------QAHKEADNIKKEKLLEAKEENQILREQTEAELRERRSELQRQETRLLQKE 94
Cdd:TIGR02169 823 RLTLEKEYLEKEIQELQEQRIdlkeqiksiEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616394879 95 ENLERKSDLLDKKDEILEQKESKIEEKQQQVDAKESSVQtlimkheQELERISGLTQEEAINEQLQRVEEELS 167
Cdd:TIGR02169 903 RKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKG-------EDEEIPEEELSLEDVQAELQRVEEEIR 968
|
|
| She9_MDM33 |
pfam05546 |
She9 / Mdm33 family; Members of this family are mitochondrial inner membrane proteins with a ... |
45-138 |
2.00e-03 |
|
She9 / Mdm33 family; Members of this family are mitochondrial inner membrane proteins with a role in inner mitochondrial membrane organization and biogenesis.
Pssm-ID: 428516 [Multi-domain] Cd Length: 198 Bit Score: 39.48 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 45 QAHKEADNIKKEKLLEAKEENQILREQTEAELrERRSELQRQETRLLQKEEN-----LERKSDLLdKKDEILEQKESKIE 119
Cdd:pfam05546 33 EKLKKSIEELEAELEAAKEEVREAKLAYKDAI-ARRSASQREVNELLQRKHSwsptdLERFTELY-RNDHANEQEEAEAK 110
|
90
....*....|....*....
gi 616394879 120 EKQQQVDAKESSVQTLIMK 138
Cdd:pfam05546 111 EKLTEAEAKEERLSDELYR 129
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
49-167 |
2.04e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 49 EADNIKKEKLLEAKEENQILREQTEAELrERRSELQRQETRLLQKEENLERKSDLLDKKDEILEQKESKIEEKQQQVD-- 126
Cdd:PRK02224 471 EEDRERVEELEAELEDLEEEVEEVEERL-ERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAel 549
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 616394879 127 -----AKESSVQTLIMKHEQELERISGLTQEEAIN----EQLQRVEEELS 167
Cdd:PRK02224 550 eaeaeEKREAAAEAEEEAEEAREEVAELNSKLAELkeriESLERIRTLLA 599
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
33-106 |
2.15e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 38.99 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 33 SQARQTAEDIVNQAHKEADNIKKEKLLEAKEENQILREQTEAEL-RER---RSELQRQ--------ETRLLQKEENLERK 100
Cdd:PRK05759 66 AEARAEAAEIIEQAKKRAAQIIEEAKAEAEAEAARIKAQAQAEIeQERkraREELRKQvadlavagAEKILGRELDAAAQ 145
|
....*.
gi 616394879 101 SDLLDK 106
Cdd:PRK05759 146 SDLIDK 151
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
45-518 |
2.18e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 40.79 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 45 QAHKEADNIKKEKLLEAKEENQILREQTEAELRERRSELQRQETRLLQKEENLERKSDLLDKKDEILEQKESKIEEKQQQ 124
Cdd:COG3064 13 AAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 125 VDAKESSVQTLIMKHEQElERISGLTQEEAINEQLQRVEEELSQDIAVLVKEKEKEAKEKVDKTAKELLATAVQRLAADH 204
Cdd:COG3064 93 AAAEKAKAAKEAEAAAAA-EKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 205 TSESTVSVVNLPNDEMKGRIIGREGRNIRTLETLTGIDLIIDDTPEAVILSGFDPIRREIARTALVNLVSDGRIHPGRIE 284
Cdd:COG3064 172 ARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 285 DMVEKARKEVDDIIREAGEQATFEVNAHNMHPDLVKIVGRLNYRTSYGQNVLKHSIEVAHLASMLAAELGEDETLAKRAG 364
Cdd:COG3064 252 ADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 365 LLHDVGKAIDHEVEGSHVEIGVELAKKYGENETVINAIHSHHGDVEPTSIISILVAAADALSAARPGARKETLENYIRRL 444
Cdd:COG3064 332 GGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAAL 411
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616394879 445 ERLETLSESYDGVEKAFAIQAGREIRVIVSPEEIDDLKSYRLARDIKNQIEDELQYPGHIKVTVVRETRAVEYA 518
Cdd:COG3064 412 LEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGGAVLADLLLLGG 485
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
40-172 |
2.35e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.84 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 40 EDIVNQAHKEADNIKKEKLLEAKEENQILREQtEAELRERRSELQRQETRLLQKEENLERKSDLLDKKDEILEQKESKIE 119
Cdd:COG0542 417 ERRLEQLEIEKEALKKEQDEASFERLAELRDE-LAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEKELA 495
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616394879 120 EKQQQVDAKESSVQTLIMKHE--QELERISG-----LTQEEAinEQLQRVEEELS-----QDIAV 172
Cdd:COG0542 496 ELEEELAELAPLLREEVTEEDiaEVVSRWTGipvgkLLEGER--EKLLNLEEELHervigQDEAV 558
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
29-165 |
2.53e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 29 LQKQSQARQTAEDI--VNQAHKEADNIKKEKLLEAKEENQILREQTEAELRE----RRSELQRQETRLLQKEENLERKSD 102
Cdd:PTZ00121 1612 AKKAEEAKIKAEELkkAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAaeeaKKAEEDKKKAEEAKKAEEDEKKAA 1691
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616394879 103 lldkkdeilEQKESKIEEKQQqvdakessVQTLIMKHEQELERISGLTQEEAIN----EQLQRVEEE 165
Cdd:PTZ00121 1692 ---------EALKKEAEEAKK--------AEELKKKEAEEKKKAEELKKAEEENkikaEEAKKEAEE 1741
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
22-173 |
2.70e-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: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 22 VVARNLLLQKQSQARQTAEDIVNQAHKEADNIKKEKLLEAKEENQILREQTEAELRERRSELQRQETRLLQKEENLERKS 101
Cdd:COG1196 628 VAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEER 707
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616394879 102 DLLDKKDEILEQKESKIEEKQQQVDAKESSVQTLIMKHEQELERISGLTQEEAINEQLQRVEEELSQDIAVL 173
Cdd:COG1196 708 ELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
26-173 |
3.36e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.00 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 26 NLLLQKQSQARQTaEDIVNQAHKEADNIKKEKLlEAKEENQILREQTEAELRERRSeLQRQETRLLQKEENLE-RKSDL- 103
Cdd:TIGR04523 321 KKLEEIQNQISQN-NKIISQLNEQISQLKKELT-NSESENSEKQRELEEKQNEIEK-LKKENQSYKQEIKNLEsQINDLe 397
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 616394879 104 --LDKKDEILEQKESKIEEKQQQVDAKESSVQTLIMKHEQELERISGLTQEEA----INEQLQRVEEELSQDIAVL 173
Cdd:TIGR04523 398 skIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSvkelIIKNLDNTRESLETQLKVL 473
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
56-143 |
4.13e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 37.56 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 56 EKLLEAKEENQILREQTEAELRERRSELQRQETRLLQKEENLERKSDLLdkkDEILEQKESKIEEKQQQVDAKESSVQTL 135
Cdd:pfam03938 8 QKILEESPEGKAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALL---EEEREEKEQELQKKEQELQQLQQKAQQE 84
|
....*...
gi 616394879 136 IMKHEQEL 143
Cdd:pfam03938 85 LQKKQQEL 92
|
|
| YhaM |
COG3481 |
3'-5' exoribonuclease YhaM, can participate in 23S rRNA maturation, HD superfamily ... |
283-410 |
4.58e-03 |
|
3'-5' exoribonuclease YhaM, can participate in 23S rRNA maturation, HD superfamily [Translation, ribosomal structure and biogenesis]; 3'-5' exoribonuclease YhaM, can participate in 23S rRNA maturation, HD superfamily is part of the Pathway/BioSystem: 23S rRNA modification
Pssm-ID: 442704 [Multi-domain] Cd Length: 316 Bit Score: 39.02 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 283 IEDMVEKARKEVDDIIREAgEQATFEVNahnmHPDLVKIVGRL---NYRTSY-----GQNV--------LKHSIEVAHLA 346
Cdd:COG3481 99 PSDFLPSSPKDIEEMYEEL-LELIDSIE----NPYLKRLLRAIldkEFRERFltapaAKSNhhayigglLEHTLSVARLA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 347 SMLAA---ELGEDETLAkrAGLLHDVGK--------AIDHEVEGS---HVEIGVEL----AKKYG--ENETVINAIH--- 403
Cdd:COG3481 174 KALADlypELNRDLLIA--GAILHDIGKvrelsgppGTEYTDEGQllgHIVLGVEMieeaAAELGdfPEELLLLLKHmil 251
|
....*..
gi 616394879 404 SHHGDVE 410
Cdd:COG3481 252 SHHGELE 258
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
31-168 |
4.65e-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: 39.65 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 31 KQSQARQTAEDIVNQAHKEADNIKKEKLLEAKEENQILREQTEAELRERRSELQRQETRLLQKEENLERKSDLLDKKDEI 110
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 616394879 111 LEQKESKIEEKQQQVDAKESSVQTLIMKHEQELERISgLTQEEAINEQLQRVEEELSQ 168
Cdd:TIGR02168 395 IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE-EAELKELQAELEELEEELEE 451
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
32-168 |
4.98e-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: 39.65 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 32 QSQARQTAEDIVNQAHKEAD-NIKKEKLLEAKEENQILREQTEAELRERRSELQRQETRLLQKEENLERKSDLLDKKDEI 110
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIEElEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 616394879 111 LEQKESKIEEKQQQVDAKEssvQTLIMKHEQELERIsgLTQEEAINEQLQRVEEELSQ 168
Cdd:TIGR02168 924 LAQLELRLEGLEVRIDNLQ---ERLSEEYSLTLEEA--EALENKIEDDEEEARRRLKR 976
|
|
| PRK03007 |
PRK03007 |
deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional |
336-370 |
6.59e-03 |
|
deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional
Pssm-ID: 235098 [Multi-domain] Cd Length: 428 Bit Score: 39.16 E-value: 6.59e-03
10 20 30
....*....|....*....|....*....|....*
gi 616394879 336 LKHSIEVAHLASMLAAELGEDETLAKRAGLLHDVG 370
Cdd:PRK03007 72 LTHSLEVAQIGRGIAAGLGCDPDLVDLAGLAHDIG 106
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
75-203 |
7.07e-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: 39.27 E-value: 7.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 75 ELRERRSELQRQETRLLQKEENLERKSDLLDKKDEILEQKESKIEEKQQQVDAKESSVQTLIMKHEQELERIS-----GL 149
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRerlanLE 315
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 616394879 150 TQEEAINEQLQRVEEELSQDIAVLVKEKEKEAKEKVDKTAKELLATAVQRLAAD 203
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE 369
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
55-166 |
7.24e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 38.90 E-value: 7.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 55 KEKLLEAKEENQILREQTEAELRERRSELQRQETRLLQKEENLERKSDLLDKKDEILEQKESKIEEKQQQVDAKESSVQT 134
Cdd:pfam05622 281 REKLIRLQHENKMLRLGQEGSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKAEDSSL 360
|
90 100 110
....*....|....*....|....*....|..
gi 616394879 135 LIMKHEQELERISGLtqeeaiNEQLQRVEEEL 166
Cdd:pfam05622 361 LKQKLEEHLEKLHEA------QSELQKKKEQI 386
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
29-202 |
7.55e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.15 E-value: 7.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 29 LQKQSQARQTAEDIVNQAHKEADnikkEKLLEAKEENQILREQTEAELRERRS--E--------LQRQETRLLQKEENLE 98
Cdd:COG1196 258 LEAELAELEAELEELRLELEELE----LELEEAQAEEYELLAELARLEQDIARleErrreleerLEELEEELAELEEELE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 99 RKSDLLDKKDEILEQKESKIEEKQQQVDAKESSVQTLIMKHEQELERISGLTQEEAinEQLQRVEEELSQDIAVLVKEKE 178
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL--EALRAAAELAAQLEELEEAEEA 411
|
170 180
....*....|....*....|....
gi 616394879 179 KEAKEKVDKTAKELLATAVQRLAA 202
Cdd:COG1196 412 LLERLERLEEELEELEEALAELEE 435
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
28-311 |
7.60e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 38.73 E-value: 7.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 28 LLQKQSQARQTAEDIVNQAHKEADNIKKE--KLLEAKEENQILREQTEAELRERRSELQRQETRLLQKEENLERKSDLLD 105
Cdd:COG4372 18 LRPKTGILIAALSEQLRKALFELDKLQEEleQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 106 KKDEILEQKESKIEEKQQQVDAKESSVQTLIMKHEQELERI----SGLTQEEAINEQLQRVEEELSQDIAVLVKEKEKEA 181
Cdd:COG4372 98 QAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIaelqSEIAEREEELKELEEQLESLQEELAALEQELQALS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 182 KEKVDKTAKELLATAVQRlaADHTSESTVSVVNLPNDEMKGRIIGREGRNIRTLETLTGIDLIIDDTPEAVILSGFDPIR 261
Cdd:COG4372 178 EAEAEQALDELLKEANRN--AEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEV 255
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 616394879 262 REIARTALVNLVSDGRIHPGRIEDMVEKARKEVDDIIREAGEQATFEVNA 311
Cdd:COG4372 256 ILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLA 305
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
30-86 |
9.00e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 37.07 E-value: 9.00e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 616394879 30 QKQSQARQTAEDIVNQAHKEADNIKKEKLLEAKEENQILREQTEAELRERRSELQRQ 86
Cdd:COG0711 59 EKLAEARAEAAEIIAEARKEAEAIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAE 115
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
30-171 |
9.91e-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: 38.57 E-value: 9.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 30 QKQSQARQTAEDIVNQAHKEADNIKKEKLlEAKEENQILREQTEAELRE-RRSELQRQETRLLQKEENLERKSDLLDKKD 108
Cdd:pfam17380 389 QKNERVRQELEAARKVKILEEERQRKIQQ-QKVEMEQIRAEQEEARQREvRRLEEERAREMERVRLEEQERQQQVERLRQ 467
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616394879 109 EILEQKESKIEEKQQQVDAKESSVQTLIMKHEQELERISGLTQEEAINEQLQRVEEELSQDIA 171
Cdd:pfam17380 468 QEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIY 530
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
51-165 |
9.97e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 38.07 E-value: 9.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616394879 51 DNIKK---EKLLEAKEENQILREQTE------AELRERRSELQRQETRLLQKEENLER-KSDLLDK-KDEILEQKE---- 115
Cdd:smart00787 143 EGLKEgldENLEGLKEDYKLLMKELEllnsikPKLRDRKDALEEELRQLKQLEDELEDcDPTELDRaKEKLKKLLQeimi 222
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616394879 116 --SKIEEKQQQVDAKESSVQTL----------IMKHEQELERISGLTQEEA--INEQLQRVEEE 165
Cdd:smart00787 223 kvKKLEELEEELQELESKIEDLtnkkselnteIAEAEKKLEQCRGFTFKEIekLKEQLKLLQSL 286
|
|
| |
