|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
8-524 |
0e+00 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 728.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 8 FVTIISAFFAAAIGLVGGYALKHWRDTRKIQNADQIANNIFDQANSEAKGIIRAAEFDAKDLAQKYRDEVDQSLADRHHE 87
Cdd:PRK12704 4 LIIILIALVALVVGAVIGYFVRKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 88 VQQQERRLQDRVDTLDKKDATLNQRDASLIQKEDQVQLRLDDAAERQSRANELLTAQQQKLEEIARLTHEDAHQQVLAET 167
Cdd:PRK12704 84 LQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEILLEKV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 168 KNDLVQERAELIREYETDAKSEAERRARNIVVQAIQRSAADSVSDVTVSVVDLPSEDMKGRIIGREGRNIRTIEALTGID 247
Cdd:PRK12704 164 EEEARHEAAVLIKEIEEEAKEEADKKAKEILAQAIQRCAADHVAETTVSVVNLPNDEMKGRIIGREGRNIRALETLTGVD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 248 LIIDDTPESVVLSGFDPLRRQIAKDALEALIADGRINPARIEEAVEKARRHMDEVVREKGEQAVFELGLRGMHPDLIKMI 327
Cdd:PRK12704 244 LIIDDTPEAVILSGFDPIRREIARLALEKLVQDGRIHPARIEEMVEKARKEVDEEIREEGEQAVFELGIHGLHPELIKLL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 328 GRMNYRTSYGQNVLQHSIEVAKLAGAMAAELKLDVALAKRAGLIHDIGKAVDAEVEGSHVELGVRLAEKFNEKPVIVNAI 407
Cdd:PRK12704 324 GRLKYRTSYGQNVLQHSIEVAHLAGLMAAELGLDVKLAKRAGLLHDIGKALDHEVEGSHVEIGAELAKKYKESPVVINAI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 408 AAHHGDVAASSPIADLIGAADAISAARPGARSESLENYVQRLKDLEQIADNYQGVRNAFAIQAGREVRVIVEPKQVTDIQ 487
Cdd:PRK12704 404 AAHHGDEEPTSIEAVLVAAADAISAARPGARRETLENYIKRLEKLEEIANSFEGVEKAYAIQAGREIRVIVKPDKVDDLQ 483
|
490 500 510
....*....|....*....|....*....|....*..
gi 2467955144 488 ATVLAHDIKSEVEEKLEYPGHVKVTVVRETRAVDYAH 524
Cdd:PRK12704 484 AVRLARDIAKKIEEELQYPGQIKVTVIRETRAVEYAK 520
|
|
| RNase_Y |
TIGR03319 |
ribonuclease Y; Members of this family are RNase Y, an endoribonuclease. The member from ... |
11-523 |
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: 682.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 11 IISAFFAAAIGLVGGYALKHWRDTRKIQNADQIANNIFDQANSEAKGIIRAAEFDAKDLAQKYRDEVDQSLADRHHEVQQ 90
Cdd:TIGR03319 1 ILLALVALIVGLIIGYLLRKRIAEKKLGSAEELAKRIIEEAKKEAETLKKEALLEAKEEVHKLRAELERELKERRNELQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 91 QERRLQDRVDTLDKKDATLNQRDASLIQKEDQVQLRLDDAAERQSRANELLTAQQQKLEEIARLTHEDAHQQVLAETKND 170
Cdd:TIGR03319 81 LERRLLQREETLDRKMESLDKKEENLEKKEKELSNKEKNLDEKEEELEELIAEQREELERISGLTQEEAKEILLEEVEEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 171 LVQERAELIREYETDAKSEAERRARNIVVQAIQRSAADSVSDVTVSVVDLPSEDMKGRIIGREGRNIRTIEALTGIDLII 250
Cdd:TIGR03319 161 ARHEAAKLIKEIEEEAKEEADKKAKEILATAIQRYAGDHVAETTVSVVNLPNDEMKGRIIGREGRNIRALETLTGVDLII 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 251 DDTPESVVLSGFDPLRRQIAKDALEALIADGRINPARIEEAVEKARRHMDEVVREKGEQAVFELGLRGMHPDLIKMIGRM 330
Cdd:TIGR03319 241 DDTPEAVILSGFDPVRREIARMALEKLIQDGRIHPARIEEMVEKATKEVDNAIREEGEQAAFDLGVHGLHPELIKLLGRL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 331 NYRTSYGQNVLQHSIEVAKLAGAMAAELKLDVALAKRAGLIHDIGKAVDAEVEGSHVELGVRLAEKFNEKPVIVNAIAAH 410
Cdd:TIGR03319 321 KFRTSYGQNVLQHSIEVAHLAGIMAAELGEDVKLAKRAGLLHDIGKAVDHEVEGSHVEIGAELAKKYKESPEVVNAIAAH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 411 HGDVAASSPIADLIGAADAISAARPGARSESLENYVQRLKDLEQIADNYQGVRNAFAIQAGREVRVIVEPKQVTDIQATV 490
Cdd:TIGR03319 401 HGDVEPTSIEAVLVAAADALSAARPGARRESLENYIKRLEKLEEIANSFEGVEKSYAIQAGREIRVMVKPEKISDDQAVV 480
|
490 500 510
....*....|....*....|....*....|...
gi 2467955144 491 LAHDIKSEVEEKLEYPGHVKVTVVRETRAVDYA 523
Cdd:TIGR03319 481 LARDIAKKIEEELEYPGQIKVTVIRETRAVEYA 513
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
9-523 |
0e+00 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 532.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 9 VTIISAFFAAAIGLVGGYA-----LKHWRDTRKIQ--NADQIANNIFDQANSEAKGIIRAAE-----------FDAKDLA 70
Cdd:PRK00106 2 INIIILVVSALIGLVIGYVlisikMKSAKEAAELTllNAEQEAVNLRGKAERDAEHIKKTAKreskalkkellLEAKEEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 71 QKYRDEVDQSLADRHHEVQQQERRLQDRVDTLDKKDATLNQRDASLIQKEDQVQLRLDDAAERQSRANELLTAQQQKLEE 150
Cdd:PRK00106 82 RKYREEIEQEFKSERQELKQIESRLTERATSLDRKDENLSSKEKTLESKEQSLTDKSKHIDEREEQVEKLEEQKKAELER 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 151 IARLTHEDAHQQVLAETKNDLVQERAELIREYETDAKSEAERRARNIVVQAIQRSAADSVSDVTVSVVDLPSEDMKGRII 230
Cdd:PRK00106 162 VAALSQAEAREIILAETENKLTHEIATRIREAEREVKDRSDKMAKDLLAQAMQRLAGEYVTEQTITTVHLPDDNMKGRII 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 231 GREGRNIRTIEALTGIDLIIDDTPESVVLSGFDPLRRQIAKDALEALIADGRINPARIEEAVEKARRHMDEVVREKGEQA 310
Cdd:PRK00106 242 GREGRNIRTLESLTGIDVIIDDTPEVVVLSGFDPIRREIARMTLESLIKDGRIHPARIEELVEKNRLEMDNRIREYGEAA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 311 VFELGLRGMHPDLIKMIGRMNYRTSYGQNVLQHSIEVAKLAGAMAAELKLDVALAKRAGLIHDIGKAVDAEVEGSHVELG 390
Cdd:PRK00106 322 AYEIGAPNLHPDLIKIMGRLQFRTSYGQNVLRHSVEVGKLAGILAGELGENVALARRAGFLHDMGKAIDREVEGSHVEIG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 391 VRLAEKFNEKPVIVNAIAAHHGDVAASSPIADLIGAADAISAARPGARSESLENYVQRLKDLEQIADNYQGVRNAFAIQA 470
Cdd:PRK00106 402 MEFARKYKEHPVVVNTIASHHGDVEPESVIAVIVAAADALSSARPGARNESMENYIKRLRDLEEIANSFDGVQNSFALQA 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2467955144 471 GREVRVIVEPKQVTDIQATVLAHDIKSEVEEKLEYPGHVKVTVVRETRAVDYA 523
Cdd:PRK00106 482 GREIRIMVQPEKISDDQVTILAHKVREKIENNLDYPGNIKVTVIRELRAVDYA 534
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
10-523 |
1.09e-168 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 486.91 E-value: 1.09e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 10 TIISAFFAAAIGLVGGYALkhwRDTRKIQNADQIANNIFDQANSEAKGIIRAAEFDAKDLAQKYRDEVDQSLADRHHEVQ 89
Cdd:PRK12705 4 SILLVILLLLIGLLLGVLV---VLLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 90 QQERRLQDRVDTLDKKDATLNQRDASLIQKEDQVQLRLDDAAERQSRANElltaqqqKLEEIARLTHEDAHQQVLAETKN 169
Cdd:PRK12705 81 REEERLVQKEEQLDARAEKLDNLENQLEEREKALSARELELEELEKQLDN-------ELYRVAGLTPEQARKLLLKLLDA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 170 DLVQERAELIREYETDAKSEAERRARNIVVQAIQRSAADSVSDVTVSVVDLPSEDMKGRIIGREGRNIRTIEALTGIDLI 249
Cdd:PRK12705 154 ELEEEKAQRVKKIEEEADLEAERKAQNILAQAMQRIASETASDLSVSVVPIPSDAMKGRIIGREGRNIRAFEGLTGVDLI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 250 IDDTPESVVLSGFDPLRRQIAKDALEALIADGRINPARIEEAVEKARRHMDEVVREKGEQAVFELGLRGMHPDLIKMIGR 329
Cdd:PRK12705 234 IDDTPEAVVISSFNPIRREIARLTLEKLLADGRIHPARIEEYVQKANEEFKQKIYEIGEEVLEELGIFDLKPGLVRLLGR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 330 MNYRTSYGQNVLQHSIEVAKLAGAMAAELKLDVALAKRAGLIHDIGKAVDAEVEGSHVELGVRLAEKFNEKPVIVNAIAA 409
Cdd:PRK12705 314 LYFRTSYGQNVLSHSLEVAHLAGIIAAEIGLDPALAKRAGLLHDIGKSIDRESDGNHVEIGAELARKFNEPDEVINAIAS 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 410 HHGDVAASSPIADLIGAADAISAARPGARSESLENYVQRLKDLEQIADNYQGVRNAFAIQAGREVRVIVEPKQVTDIQAT 489
Cdd:PRK12705 394 HHNKVNPETVYSVLVQIADALSAARPGARRESLDEYVQRLEELEQIAESFPGVEKAYAIQAGRELRVIVEPEKVSDAQAT 473
|
490 500 510
....*....|....*....|....*....|....
gi 2467955144 490 VLAHDIKSEVEEKLEYPGHVKVTVVRETRAVDYA 523
Cdd:PRK12705 474 LLARDIAKKIENDLTYPGPIKVTLIRETRAVEYA 507
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
11-207 |
2.65e-47 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 163.13 E-value: 2.65e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 11 IISAFFAAAIGLVGGYALKHWRDTRKIQNADQIANNIFDQANSEAKGIIRAAEFDAKDLAQKYRDEVDQSLADRHHEVQQ 90
Cdd:pfam12072 3 IILAIIALVVGFVVGYLVRKSIAEAKIGSAEELAKRIIEEAKKEAETKKKEALLEAKEEIHKLRAEAERELKERRNELQR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 91 QERRLQDRVDTLDKKDATLNQRDASLIQKEDQVQLRLDDAAERQSRANELLTAQQQKLEEIARLTHEDAHQQVLAETKND 170
Cdd:pfam12072 83 QERRLLQKEETLDRKDESLEKKEESLEKKEKELEAQQQQLEEKEEELEELIEEQRQELERISGLTSEEAKEILLDEVEEE 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 2467955144 171 LVQERAELIREYETDAKSEAERRARNIVVQAIQRSAA 207
Cdd:pfam12072 163 LRHEAAVMIKEIEEEAKEEADKKAKEIIALAIQRCAA 199
|
|
| KH-I_RNaseY |
cd22431 |
type I K homology (KH) RNA-binding domain found in ribonuclease Y (RNase Y) and similar ... |
220-290 |
6.78e-39 |
|
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: 136.56 E-value: 6.78e-39
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2467955144 220 LPSEDMKGRIIGREGRNIRTIEALTGIDLIIDDTPESVVLSGFDPLRRQIAKDALEALIADGRINPARIEE 290
Cdd:cd22431 9 LPNDEMKGRIIGREGRNIRAFEAATGVDLIIDDTPEAVILSGFDPVRREVARRTLEKLVEDGRIHPARIEE 79
|
|
| RnaY |
COG1418 |
HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal ... |
321-518 |
1.30e-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: 139.65 E-value: 1.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 321 PDLIKMIgrMNYRTSYGQNVLQHSIEVAKLAGAMAAELKLDVALAKRAGLIHDIGKAVDAEVEGSHVELGVRLAEKFN-- 398
Cdd:COG1418 2 PELIKLV--KYLRTSYGQHDLQHSLRVAKLAGLIAAEEGADVEVAKRAALLHDIGKAKDHEVEGSHAEIGAELARKYLes 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 399 ------EKPVIVNAIAAHHGDVA--ASSPIADLIGAADAISAArpGARseslenyvqrlkdleqiadnyqGVRNAFAI-- 468
Cdd:COG1418 80 lgfpeeEIEAVVHAIEAHSFSGGiePESLEAKIVQDADRLDAL--GAI----------------------GVARAFAIgg 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 469 QAGREVRVIVEP---------KQVTDIQATVLAHDIKSEVEEKLE-YPghvkVTVVRETR 518
Cdd:COG1418 136 QAGRELRDPEDTainhfyeklLKLKDLMATELARDIAKKREEFMEeFP----VTVIRETR 191
|
|
| HDIG |
TIGR00277 |
HDIG domain; This domain is found in a few known nucleotidyltransferes and in a large number ... |
336-413 |
8.29e-25 |
|
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: 97.79 E-value: 8.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 336 YGQNVLQHSIEVAKLAGAMAAELKLDVALAKRAGLIHDIGKAVDAE--VEGSHVELGVRLAEKFNEKPVIVNAIAAHHGD 413
Cdd:TIGR00277 1 YGQNVLQHSLEVAKLAEALARELGLDVELARRGALLHDIGKPITREgvIFESHVVVGAEIARKYGEPLEVIDIIAEHHGK 80
|
|
| Krr1 |
COG1094 |
rRNA processing protein Krr1/Pno1, contains KH domain [Translation, ribosomal structure and ... |
223-305 |
1.61e-23 |
|
rRNA processing protein Krr1/Pno1, contains KH domain [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440711 [Multi-domain] Cd Length: 177 Bit Score: 97.59 E-value: 1.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 223 EDMKGRIIGREGRNIRTIEALTGIDLIIDDTPESvVLSGFDPLrrQIAKDALEALIaDGRINPArIEEAVEKARRHMDEV 302
Cdd:COG1094 98 DRIKGRIIGREGRTRRIIEELTGVDISIYGKTVA-IIGDFDQV--EIAREAIEMLI-DGRIHPT-VYEFLEKARRELKRR 172
|
...
gi 2467955144 303 VRE 305
Cdd:COG1094 173 RLE 175
|
|
| HD |
pfam01966 |
HD domain; HD domains are metal dependent phosphohydrolases. |
340-433 |
4.60e-11 |
|
HD domain; HD domains are metal dependent phosphohydrolases.
Pssm-ID: 460398 [Multi-domain] Cd Length: 110 Bit Score: 59.94 E-value: 4.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 340 VLQHSIEVAKLAGAMAAELK-LDVALAKRAGLIHDIGKAV------DAEVEGSHVELGVRLAEKFNEKP---VIVNAIAA 409
Cdd:pfam01966 1 RLEHSLRVALLARELAEELGeLDRELLLLAALLHDIGKGPfgdekpEFEIFLGHAVVGAEILRELEKRLgleDVLKLILE 80
|
90 100 110
....*....|....*....|....*....|
gi 2467955144 410 HHGD------VAASSPIADLIGAADAISAA 433
Cdd:pfam01966 81 HHESwegagyPEEISLEARIVKLADRLDAL 110
|
|
| HDc |
smart00471 |
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ... |
336-439 |
4.65e-11 |
|
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: 60.39 E-value: 4.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 336 YGQNVLQHSIEVAKLAGAMAAELKL-DVALAKRAGLIHDIGKA-------VDAEVEGSHVELGVRLAEKFNEKPVIVN-- 405
Cdd:smart00471 1 SDYHVFEHSLRVAQLAAALAEELGLlDIELLLLAALLHDIGKPgtpdsflVKTSVLEDHHFIGAEILLEEEEPRILEEil 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2467955144 406 --AIAAHHGDVAAS-----SPIADLIGAADAISAARPGARS 439
Cdd:smart00471 81 rtAILSHHERPDGLrgepiTLEARIVKVADRLDALRADRRY 121
|
|
| HDGYP |
COG2206 |
HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal ... |
197-411 |
7.06e-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: 54.21 E-value: 7.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 197 IVVQAIQRSAADSVSDVTVSVVDLPSEDMKGRIIGREGRNIRTIEALTGIDLIIDDTPESVVLSGFDPLRRQIAKDALEA 276
Cdd:COG2206 1 LLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLLLLLLALLALLLLLLLLLALLALLLALLALLLLLLLLLLLLSLLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 277 LIADGRINPARIEEAVEKARRHMDEVVREKGEQAVFEL--GLRGMHPDLIK-MIGRMNYRTSYgqnVLQHSIEVAKLAGA 353
Cdd:COG2206 81 AVALLLAELLLLLAALESLLAELFEELRLGLLEELKKLveELDELLPDALLaLLAALDAKDPY---TYGHSVRVAVLALA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2467955144 354 MAAELKLD---VALAKRAGLIHDIGK-AVDAEV---EG-----------SHVELGVRLAEKFNEKPVIVNAIAAHH 411
Cdd:COG2206 158 LARELGLSeeeLEDLGLAALLHDIGKiGIPDEIlnkPGkltdeefeiikKHPEYGYEILKKLPGLSEVAEIVLQHH 233
|
|
| HDc |
cd00077 |
Metal dependent phosphohydrolases with conserved 'HD' motif |
338-440 |
7.42e-08 |
|
Metal dependent phosphohydrolases with conserved 'HD' motif
Pssm-ID: 238032 [Multi-domain] Cd Length: 145 Bit Score: 51.57 E-value: 7.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 338 QNVLQHSIEVAKLAGAMAAELKL---DVALAKRAGLIHDIGKAVD--------AEVEGSHVELGVRLA------EKFNEK 400
Cdd:cd00077 1 EHRFEHSLRVAQLARRLAEELGLseeDIELLRLAALLHDIGKPGTpdaiteeeSELEKDHAIVGAEILrellleEVIKLI 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2467955144 401 PVIVNAIAAHHGDVA------------ASSPIADLIGAADAISAARPGARSE 440
Cdd:cd00077 81 DELILAVDASHHERLdglgypdglkgeEITLEARIVKLADRLDALRRDSREK 132
|
|
| arCOG04150 |
TIGR03665 |
arCOG04150 universal archaeal KH domain protein; This family of proteins is universal among ... |
226-282 |
3.79e-06 |
|
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: 47.17 E-value: 3.79e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2467955144 226 KGRIIGREGRNIRTIEALTGIDLIIDDtpESVVLSGfDPLRRQIAKDALEALIaDGR 282
Cdd:TIGR03665 100 KGRIIGEGGKTRRIIEELTGVSISVYG--KTVGIIG-DPEQVQIAREAIEMLI-EGA 152
|
|
| PRK13763 |
PRK13763 |
putative RNA-processing protein; Provisional |
225-278 |
7.88e-06 |
|
putative RNA-processing protein; Provisional
Pssm-ID: 237494 [Multi-domain] Cd Length: 180 Bit Score: 46.40 E-value: 7.88e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2467955144 225 MKGRIIGREGRNIRTIEALTGIDLIIDDTpeSVVLSGfDPLRRQIAKDALEALI 278
Cdd:PRK13763 105 IKGRIIGEGGKTRRIIEELTGVDISVYGK--TVAIIG-DPEQVEIAREAIEMLI 155
|
|
| HDOD |
COG1639 |
HD-like signal output (HDOD) domain, no enzymatic activity [Signal transduction mechanisms]; |
338-449 |
1.29e-05 |
|
HD-like signal output (HDOD) domain, no enzymatic activity [Signal transduction mechanisms];
Pssm-ID: 441246 [Multi-domain] Cd Length: 244 Bit Score: 46.50 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 338 QNVLQHSIEVAKLAGAMAAELKL---DVALAkrAGLIHDIGK------------AVDAEVEG---------------SHV 387
Cdd:COG1639 103 RRFWRHSLAVAAAARALARRLGLldpEEAFL--AGLLHDIGKlvllslfpeeyaELLALAEAdglslaeaerevlgtDHA 180
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2467955144 388 ELGVRLAEKFNEKPVIVNAIAAHH--GDVAASSPIADLIGAADAISAARPGARSESLENYVQRL 449
Cdd:COG1639 181 ELGAALARKWGLPEELVEAIRYHHdpEAAGEHRRLAALVHLANRLARALGEEDPALPEAALALL 244
|
|
| KH |
smart00322 |
K homology RNA-binding domain; |
223-278 |
1.62e-05 |
|
K homology RNA-binding domain;
Pssm-ID: 197652 [Multi-domain] Cd Length: 68 Bit Score: 42.67 E-value: 1.62e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2467955144 223 EDMKGRIIGREGRNIRTIEALTG--IDLIIDDTPESVVLSGFDPLRRQIAKDALEALI 278
Cdd:smart00322 11 ADKVGLIIGKGGSTIKKIEEETGvkIDIPGPGSEERVVEITGPPENVEKAAELILEIL 68
|
|
| nadD |
PRK07152 |
nicotinate-nucleotide adenylyltransferase; |
341-381 |
2.44e-05 |
|
nicotinate-nucleotide adenylyltransferase;
Pssm-ID: 235947 [Multi-domain] Cd Length: 342 Bit Score: 46.48 E-value: 2.44e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2467955144 341 LQHSIEVAKLAGAMAAELKLDVALAKRAGLIHDIGKAVDAE 381
Cdd:PRK07152 198 YKHCLRVAQLAAELAKKNNLDPKKAYYAGLYHDITKEWDEE 238
|
|
| HDOD |
pfam08668 |
HDOD domain; |
342-411 |
4.09e-05 |
|
HDOD domain;
Pssm-ID: 430141 [Multi-domain] Cd Length: 196 Bit Score: 44.53 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 342 QHSIEVAKLAGAMAAELKLDVA-LAKRAGLIHDIGK------------------------AVDAE---VEGSHVELGVRL 393
Cdd:pfam08668 97 EHSLACALAARLLARRLGLDDPeEAFLAGLLHDIGKlillsllpdkyeellekaaeegisLLEAErelLGTDHAEVGAAL 176
|
90
....*....|....*...
gi 2467955144 394 AEKFNEKPVIVNAIAAHH 411
Cdd:pfam08668 177 LERWNLPEELVEAIAYHH 194
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
49-301 |
1.19e-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: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 49 DQANSEAKGIIRAAEFDAKDLAQKYRDEVDQSLADRHHEVQQQERRLQDRVDTLDKKDATLNQRDASLIQKEDQVQLRLD 128
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 129 DAAERQSRANELLTAQQQKLEEIARLthEDAHQQVLAETKNDLVQERAELIREYETDAKSEAERRARNIVVQAIQRSAAD 208
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEE--LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 209 SVSDVTVSVVDLpsEDMKGRIIGREGRNIRTIEALTGIDLIIDDTPESVVLSGFDPLRRQIAKDALEALIADGRINPARI 288
Cdd:COG1196 398 LAAQLEELEEAE--EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
250
....*....|...
gi 2467955144 289 EEAVEKARRHMDE 301
Cdd:COG1196 476 EAALAELLEELAE 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
32-298 |
1.55e-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: 44.66 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 32 RDTRKIQN-ADQIANNIFDQANSEAKgiiRAAEFDAKDLAQKYRDEVDQSLADRHHEVQQQERRLQDRVDTLDKKDATLN 110
Cdd:TIGR02168 737 RLEAEVEQlEERIAQLSKELTELEAE---IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 111 QRDASLIQKEDQVQLRLDDAAERQSRANELLTAQQQKLEEIARLTHEDAHQQVLAETKNDlvqERAELIREYETDAKSEA 190
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES---ELEALLNERASLEEALA 890
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 191 ERRARNIVVQAIQRSAADSVSDVTVSVVDLPS--EDMKGRIIGREGRNIRTIEALTG---IDLIIDDTPESVVLSGFDPL 265
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREklAQLELRLEGLEVRIDNLQERLSEeysLTLEEAEALENKIEDDEEEA 970
|
250 260 270
....*....|....*....|....*....|....
gi 2467955144 266 RRQIAKdaLEALIAD-GRINPARIEEAVEKARRH 298
Cdd:TIGR02168 971 RRRLKR--LENKIKElGPVNLAAIEEYEELKERY 1002
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
69-501 |
1.93e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 69 LAQKYRDEVDQSLADRHHEVQQQERRLQDRVDTLDKKDATLNQRDASLIQKEDQVQLRLDDAAERQSRANELLTAQQQKL 148
Cdd:COG1196 229 LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 149 EEIARLTHEDAH-QQVLAETKNDLVQERAELIREYETDAKSEAERRARNIVVQAIQRSAADSVSDVTVSVVDLpsEDMKG 227
Cdd:COG1196 309 ERRRELEERLEElEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL--EELAE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 228 RIIGREGRNIRTIEALTGIDLIIDDtpesvvlsgfdplrRQIAKDALEALIADGRINPARIEEAVEKARRHMDEVVREKG 307
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEAEEA--------------LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 308 EQAVFELGLRGMHPDLikmigrmnyRTSYGQNVLQHSIEVAKLAGAMAAELKLDVALAKRAGLIHDIGKAVD-AEVEGSH 386
Cdd:COG1196 453 ELEEEEEALLELLAEL---------LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLlAGLRGLA 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 387 VELGVRLAEKFNEKPVIVNAIAAHHGDVAASSpIADLIGAADAISAARPGARSESLENyvqRLKDLEQIADNYQGVRNAF 466
Cdd:COG1196 524 GAVAVLIGVEAAYEAALEAALAAALQNIVVED-DEVAAAAIEYLKAAKAGRATFLPLD---KIRARAALAAALARGAIGA 599
|
410 420 430
....*....|....*....|....*....|....*
gi 2467955144 467 AIqAGREVRVIVEPKQVTDIQATVLAHDIKSEVEE 501
Cdd:COG1196 600 AV-DLVASDLREADARYYVLGDTLLGRTLVAARLE 633
|
|
| Cas10_III |
cd09680 |
CRISPR/Cas system-associated protein Cas10; CRISPR (Clustered Regularly Interspaced Short ... |
368-433 |
3.03e-04 |
|
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: 43.47 E-value: 3.03e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2467955144 368 AGLIHDIGKAV----DAEVEGSHVELGVR-LAEKFNEKPVIVNAIAAHH-GDVAASSPIADLIGA-----ADAISAA 433
Cdd:cd09680 4 GALLHDIGKVVqragLGFYSKTHSKFGAEfLKEFSKNKDDLGDCISYHHtKELAKALLENHHPLAyivyiADNIAAS 80
|
|
| KH-I_IGF2BP2_rpt2 |
cd22494 |
second type I K homology (KH) RNA-binding domain found in insulin-like growth factor 2 ... |
220-276 |
3.09e-04 |
|
second type I K homology (KH) RNA-binding domain found in insulin-like growth factor 2 mRNA-binding protein 2 (IGF2BP2) and similar proteins; IGF2BP2, also called IGF2 mRNA-binding protein 2 (IMP-2), or hepatocellular carcinoma autoantigen p62, or IGF-II mRNA-binding protein 2, or VICKZ family member 2 (VICKZ2), is an RNA-binding factor that recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). It functions by binding to the 5' UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulating IGF2 translation. It also binds to beta-actin/ACTB and MYC transcripts. IGF2BP2 can form homooligomers and heterooligomers with IGF2BP1 and IGF2BP3 in an RNA-dependent manner. It contains four K-homology (KH) RNA-binding domains which are important in RNA binding and are known to be involved in RNA synthesis and metabolism. The model corresponds to the second one.
Pssm-ID: 411922 Cd Length: 77 Bit Score: 39.63 E-value: 3.09e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2467955144 220 LPSEDMKGRIIGREGRNIRTIEALTGIDLIIDDTPEsvvLSGFDPLRRQIAKDALEA 276
Cdd:cd22494 5 LAHNSLVGRLIGKEGRNLKKIEQDTGTKITISSLQD---LTIYNPERTITVKGSIEA 58
|
|
| KH-I_Dim2p_like_rpt2 |
cd22390 |
second type I K homology (KH) RNA-binding domain found in Pyrococcus horikoshii Dim2p and ... |
226-278 |
8.81e-04 |
|
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: 38.74 E-value: 8.81e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2467955144 226 KGRIIGREGRNIRTIEALTGIDL-IIDDTpesVVLSGfDPLRRQIAKDALEALI 278
Cdd:cd22390 30 KGRVIGSGGKTRRLIEELTGCYIsVYGKT---VSIIG-DFENLQIAKEAIEMLL 79
|
|
| KH_1 |
pfam00013 |
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ... |
224-276 |
9.30e-04 |
|
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: 37.65 E-value: 9.30e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2467955144 224 DMKGRIIGREGRNIRTIEALTGIDLIIDDTPES-----VVLSGfDPLRRQIAKDALEA 276
Cdd:pfam00013 9 SLVGLIIGKGGSNIKEIREETGAKIQIPPSESEgneriVTITG-TPEAVEAAKALIEE 65
|
|
| YqeK |
COG1713 |
Diadenosine tetraphosphatase YqeK or a related HD superfamily phosphohydrolase [Signal ... |
341-416 |
2.00e-03 |
|
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: 39.33 E-value: 2.00e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2467955144 341 LQHSIEVAKLAGAMAAELKLDVALAKRAGLIHDIGKAVDAEvegshvELgVRLAEKFN--EKPVIVNAIAAHHGDVAA 416
Cdd:COG1713 19 YEHTLGVAETAVELAERYGVDVEKAELAGLLHDYAKELPPE------EL-LELAKEYGldLDELEEYNPELLHGPVGA 89
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
70-383 |
3.30e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 70 AQKYRDEVDQSLADRHHEVQQQERRLQDRVDTLDKKDATLNQRDASLIQKEDQVQLRLDDAAERQSRANELLTAQQQKLE 149
Cdd:COG4372 57 AREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 150 EIARLTHEDAHQQVLAETKNDLVQERAELIREYETDAKSEAERRARNIVVQaiQRSAADSVSDVTVSVVDLPSEDMKGRI 229
Cdd:COG4372 137 QIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDE--LLKEANRNAEKEEELAEAEKLIESLPR 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 230 IGREGRNIRTIEALTGIDLIIDDTPESVVLSGFDPLRRQIAKDALEALIADGRINPARIEEAVEKARRHMDEVVREKGEQ 309
Cdd:COG4372 215 ELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALE 294
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2467955144 310 AVFELGLRGMHPDLIKMIGRMNYRTSYGQNVLQHSIEVAKLAGAMAAELKLDVALAKRAGLIHDIGKAVDAEVE 383
Cdd:COG4372 295 LKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVA 368
|
|
| YhaM |
COG3481 |
3'-5' exoribonuclease YhaM, can participate in 23S rRNA maturation, HD superfamily ... |
341-432 |
3.47e-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: 39.79 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 341 LQHSIEVAKLAGAMAA---ELKLDVALAkrAGLIHDIGK--------AVDAEVEGS---HVELGVRL----AEKFNEKP- 401
Cdd:COG3481 163 LEHTLSVARLAKALADlypELNRDLLIA--GAILHDIGKvrelsgppGTEYTDEGQllgHIVLGVEMieeaAAELGDFPe 240
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2467955144 402 ----VIVNAIAAHHGDVAASSPI------ADLIGAADAISA 432
Cdd:COG3481 241 elllLLKHMILSHHGELEWGSPKrpktpeAEILHYADNLDA 281
|
|
| cas3_HD |
TIGR01596 |
CRISPR-associated endonuclease Cas3-HD; CRISPR/Cas systems are widespread, mobile systems for ... |
341-453 |
3.70e-03 |
|
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: 38.34 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 341 LQHSIEVAKLAGAMAAEL--------KLDVALAKRAGLIHDIGKA----------VDAEVEGS---HVELGVRLAEKFNE 399
Cdd:TIGR01596 2 KEHLLDVAAVAEALPALRprlaeklgLELRELLKLAGLLHDLGKAspafqkklrkAEERGDRGevrHSTLSAALLYDLLE 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2467955144 400 KP--------VIVNAIAAHHGDVAASSPIADLIGAADAISA-ARPGARSESLENYVQRLKDLE 453
Cdd:TIGR01596 82 ELgleeelalLLALAIAGHHGGLIDDDDLEELLELLERELEeALGELLEELEELLDEVLKALP 144
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
60-194 |
4.07e-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: 40.05 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 60 RAAEFDAKdlAQKYRDEVDQ------SLADRHHEVQQQERRLQDRVDTLDKKDATLNQRDASLIQKEDQVQLRLDDAAER 133
Cdd:TIGR02169 372 ELEEVDKE--FAETRDELKDyrekleKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE 449
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2467955144 134 qsranelLTAQQQKLEEIAR-LTHEDAHQQVLAETKNDLVQERAELIREYetdAKSEAERRA 194
Cdd:TIGR02169 450 -------IKKQEWKLEQLAAdLSKYEQELYDLKEEYDRVEKELSKLQREL---AEAEAQARA 501
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
87-195 |
5.68e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 39.29 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 87 EVQQQERRL----------QDRVDTLDKKDATLNQRDASLIQKEDQVQLRLDDAAERQSRANELLTAQQQKLEEIARLTH 156
Cdd:PRK11637 150 ESQRGERILayfgylnqarQETIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESSLQ 229
|
90 100 110
....*....|....*....|....*....|....*....
gi 2467955144 157 EDahQQVLAETKNDLVQERAELIREyETDAKSEAERRAR 195
Cdd:PRK11637 230 KD--QQQLSELRANESRLRDSIARA-EREAKARAEREAR 265
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
81-195 |
8.19e-03 |
|
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: 39.17 E-value: 8.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 81 LADRHHEVQQQERRLQDRVDTLD---KKDATLNQRDASLIQKE-----DQVQLRLDDAAERQSRANELLTAQQQKleeia 152
Cdd:COG3096 939 LQADYLQAKEQQRRLKQQIFALSevvQRRPHFSYEDAVGLLGEnsdlnEKLRARLEQAEEARREAREQLRQAQAQ----- 1013
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2467955144 153 rltHEDAHQqVLA------ETKNDLVQERAELIREYETDAKSEAERRAR 195
Cdd:COG3096 1014 ---YSQYNQ-VLAslkssrDAKQQTLQELEQELEELGVQADAEAEERAR 1058
|
|
| PRK03007 |
PRK03007 |
deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional |
341-375 |
8.29e-03 |
|
deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional
Pssm-ID: 235098 [Multi-domain] Cd Length: 428 Bit Score: 38.77 E-value: 8.29e-03
10 20 30
....*....|....*....|....*....|....*
gi 2467955144 341 LQHSIEVAKLAGAMAAELKLDVALAKRAGLIHDIG 375
Cdd:PRK03007 72 LTHSLEVAQIGRGIAAGLGCDPDLVDLAGLAHDIG 106
|
|
| Cas3''_I |
cd09641 |
CRISPR/Cas system-associated protein Cas3''; CRISPR (Clustered Regularly Interspaced Short ... |
337-413 |
8.94e-03 |
|
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: 37.64 E-value: 8.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955144 337 GQNVLQHSIEVA--------KLAGAMAAELKLDVALAKRAGLIHDIGKA----------------VDAEVEGSHVELGVR 392
Cdd:cd09641 6 WQPLLEHLLDVAawdaelaeEFARKLGLELGLSRELLALAGLLHDLGKAtpafqkylrggkealrEGKRKEVRHSLLGAL 85
|
90 100
....*....|....*....|....*....
gi 2467955144 393 LAEKFNEK--------PVIVNAIAAHHGD 413
Cdd:cd09641 86 LLYELLKElgldeelaLLLAYAIAGHHGG 114
|
|
| KH-I |
cd00105 |
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ... |
223-275 |
9.58e-03 |
|
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found in a wide variety of proteins including ribosomal proteins, transcription factors and post-transcriptional modifiers of mRNA. There are two different KH domains that belong to different protein folds, but they share a single KH motif. The KH motif is folded into a beta alpha alpha beta unit. In addition to the core, type II KH domains (e.g. ribosomal protein S3) include an N-terminal extension and type I KH domains (e.g. hnRNP K) contain a C-terminal extension. Some KH-I superfamily members contain a divergent KH domain that lacks the RNA-binding GXXG motif. Some others have a mutated GXXG motif which may or may not have nucleic acid binding ability.
Pssm-ID: 411802 [Multi-domain] Cd Length: 63 Bit Score: 34.97 E-value: 9.58e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2467955144 223 EDMKGRIIGREGRNIRTIEALTGIDLIIDDTPES-----VVLSGfDPLRRQIAKDALE 275
Cdd:cd00105 7 SELVGLIIGKGGSTIKEIEEETGARIQIPKEGEGsgervVTITG-TPEAVEKAKELIE 63
|
|
| |
