|
Name |
Accession |
Description |
Interval |
E-value |
| RNase_Y |
TIGR03319 |
ribonuclease Y; Members of this family are RNase Y, an endoribonuclease. The member from ... |
9-504 |
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: 766.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 9 VVLVTVGLTFGWTIRWLYARFH----LSACEQRAERILQEAQKEAESKKKSILLEAKEYVLRERNQQERDDRDRRAELQR 84
Cdd:TIGR03319 1 ILLALVALIVGLIIGYLLRKRIaekkLGSAEELAKRIIEEAKKEAETLKKEALLEAKEEVHKLRAELERELKERRNELQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 85 AERRLLQKEEALSTRA--------------GELDSRERSLKQRDQSLCQEEARYRQELERVSGLTQNQARDLIIKNLENE 150
Cdd:TIGR03319 81 LERRLLQREETLDRKMesldkkeenlekkeKELSNKEKNLDEKEEELEELIAEQREELERISGLTQEEAKEILLEEVEEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 151 AKHDAQALINKIEEDAALNAERRARDILVTTMQRITADVTGDVTVSTVNLPSEEMKGRIIGREGRNIRALETLTGADVVV 230
Cdd:TIGR03319 161 ARHEAAKLIKEIEEEAKEEADKKAKEILATAIQRYAGDHVAETTVSVVNLPNDEMKGRIIGREGRNIRALETLTGVDLII 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 231 DDTPEAVVISCFDPVRKEIARISLERLVLDGRIHPARIEEIVQKVTQEVSQKIYEEGEKVLFDLGIHDMCPEGVRALGRL 310
Cdd:TIGR03319 241 DDTPEAVILSGFDPVRREIARMALEKLIQDGRIHPARIEEMVEKATKEVDNAIREEGEQAAFDLGVHGLHPELIKLLGRL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 311 YFRTSYGQNVLYHSKEVALLASMLASEIGADVAIAKRGALLHDIGKGVETDSDRNHAEIGMEMARKMNEDPRVVNAVGSH 390
Cdd:TIGR03319 321 KFRTSYGQNVLQHSIEVAHLAGIMAAELGEDVKLAKRAGLLHDIGKAVDHEVEGSHVEIGAELAKKYKESPEVVNAIAAH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 391 HNDIEPCCVESWLVQVADAISAARPGARREMVDHYVKRLENLEAIAEGFSGVEKAYAIQAGRELRVLVNNDKIPDRDVKA 470
Cdd:TIGR03319 401 HGDVEPTSIEAVLVAAADALSAARPGARRESLENYIKRLEKLEEIANSFEGVEKSYAIQAGREIRVMVKPEKISDDQAVV 480
|
490 500 510
....*....|....*....|....*....|....
gi 499184922 471 LGRDIAKKIESDLKYPGRIRVTLIRETRVVEYAR 504
Cdd:TIGR03319 481 LARDIAKKIEEELEYPGQIKVTVIRETRAVEYAK 514
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1-504 |
0e+00 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 701.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 1 MTTSIVIGVVLVTVGLTFGWTIRWLYARFHLSAceqRAERILQEAQKEAESKKKSILLEAKEYVLRERNQQERDDRDRRA 80
Cdd:PRK12705 1 FAMSILLVILLLLIGLLLGVLVVLLKKRQRLAK---EAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRERE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 81 ELQRAERRLLQKEEALSTRAGELD-------SRERSLKQRDQSLCQEEARYRQELERVSGLTQNQARDLIIKNLENEAKH 153
Cdd:PRK12705 78 ELQREEERLVQKEEQLDARAEKLDnlenqleEREKALSARELELEELEKQLDNELYRVAGLTPEQARKLLLKLLDAELEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 154 DAQALINKIEEDAALNAERRARDILVTTMQRITADVTGDVTVSTVNLPSEEMKGRIIGREGRNIRALETLTGADVVVDDT 233
Cdd:PRK12705 158 EKAQRVKKIEEEADLEAERKAQNILAQAMQRIASETASDLSVSVVPIPSDAMKGRIIGREGRNIRAFEGLTGVDLIIDDT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 234 PEAVVISCFDPVRKEIARISLERLVLDGRIHPARIEEIVQKVTQEVSQKIYEEGEKVLFDLGIHDMCPEGVRALGRLYFR 313
Cdd:PRK12705 238 PEAVVISSFNPIRREIARLTLEKLLADGRIHPARIEEYVQKANEEFKQKIYEIGEEVLEELGIFDLKPGLVRLLGRLYFR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 314 TSYGQNVLYHSKEVALLASMLASEIGADVAIAKRGALLHDIGKGVETDSDRNHAEIGMEMARKMNEDPRVVNAVGSHHND 393
Cdd:PRK12705 318 TSYGQNVLSHSLEVAHLAGIIAAEIGLDPALAKRAGLLHDIGKSIDRESDGNHVEIGAELARKFNEPDEVINAIASHHNK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 394 IEPCCVESWLVQVADAISAARPGARREMVDHYVKRLENLEAIAEGFSGVEKAYAIQAGRELRVLVNNDKIPDRDVKALGR 473
Cdd:PRK12705 398 VNPETVYSVLVQIADALSAARPGARRESLDEYVQRLEELEQIAESFPGVEKAYAIQAGRELRVIVEPEKVSDAQATLLAR 477
|
490 500 510
....*....|....*....|....*....|.
gi 499184922 474 DIAKKIESDLKYPGRIRVTLIRETRVVEYAR 504
Cdd:PRK12705 478 DIAKKIENDLTYPGPIKVTLIRETRAVEYAR 508
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1-504 |
0e+00 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 700.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 1 MTTSIVIGVVLVTVGLTFGWTIRWLYARFHLSACEQRAERILQEAQKEAESKKKSILLEAKEYVLRERNQQERDDRDRRA 80
Cdd:PRK12704 3 LLIIILIALVALVVGAVIGYFVRKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 81 ELQRAERRLLQKEEALSTRAGELDSRERSLKQRDQSLCQEE--------------ARYRQELERVSGLTQNQARDLIIKN 146
Cdd:PRK12704 83 ELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQqelekkeeeleeliEEQLQELERISGLTAEEAKEILLEK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 147 LENEAKHDAQALINKIEEDAALNAERRARDILVTTMQRITADVTGDVTVSTVNLPSEEMKGRIIGREGRNIRALETLTGA 226
Cdd:PRK12704 163 VEEEARHEAAVLIKEIEEEAKEEADKKAKEILAQAIQRCAADHVAETTVSVVNLPNDEMKGRIIGREGRNIRALETLTGV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 227 DVVVDDTPEAVVISCFDPVRKEIARISLERLVLDGRIHPARIEEIVQKVTQEVSQKIYEEGEKVLFDLGIHDMCPEGVRA 306
Cdd:PRK12704 243 DLIIDDTPEAVILSGFDPIRREIARLALEKLVQDGRIHPARIEEMVEKARKEVDEEIREEGEQAVFELGIHGLHPELIKL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 307 LGRLYFRTSYGQNVLYHSKEVALLASMLASEIGADVAIAKRGALLHDIGKGVETDSDRNHAEIGMEMARKMNEDPRVVNA 386
Cdd:PRK12704 323 LGRLKYRTSYGQNVLQHSIEVAHLAGLMAAELGLDVKLAKRAGLLHDIGKALDHEVEGSHVEIGAELAKKYKESPVVINA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 387 VGSHHNDIEPCCVESWLVQVADAISAARPGARREMVDHYVKRLENLEAIAEGFSGVEKAYAIQAGRELRVLVNNDKIPDR 466
Cdd:PRK12704 403 IAAHHGDEEPTSIEAVLVAAADAISAARPGARRETLENYIKRLEKLEEIANSFEGVEKAYAIQAGREIRVIVKPDKVDDL 482
|
490 500 510
....*....|....*....|....*....|....*...
gi 499184922 467 DVKALGRDIAKKIESDLKYPGRIRVTLIRETRVVEYAR 504
Cdd:PRK12704 483 QAVRLARDIAKKIEEELQYPGQIKVTVIRETRAVEYAK 520
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
35-504 |
4.08e-156 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 455.10 E-value: 4.08e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 35 EQRAERILQEAQKEAESKKKSILLEAKEYVLRERNQQERDDRDRRAELQRAERRLLQ-------KEEALSTRAGELDSRE 107
Cdd:PRK00106 52 ERDAEHIKKTAKRESKALKKELLLEAKEEARKYREEIEQEFKSERQELKQIESRLTEratsldrKDENLSSKEKTLESKE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 108 RSLK-------QRDQSLCQEEARYRQELERVSGLTQNQARDLIIKNLENEAKHDAQALINKIEEDAALNAERRARDILVT 180
Cdd:PRK00106 132 QSLTdkskhidEREEQVEKLEEQKKAELERVAALSQAEAREIILAETENKLTHEIATRIREAEREVKDRSDKMAKDLLAQ 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 181 TMQRITADVTGDVTVSTVNLPSEEMKGRIIGREGRNIRALETLTGADVVVDDTPEAVVISCFDPVRKEIARISLERLVLD 260
Cdd:PRK00106 212 AMQRLAGEYVTEQTITTVHLPDDNMKGRIIGREGRNIRTLESLTGIDVIIDDTPEVVVLSGFDPIRREIARMTLESLIKD 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 261 GRIHPARIEEIVQKVTQEVSQKIYEEGEKVLFDLGIHDMCPEGVRALGRLYFRTSYGQNVLYHSKEVALLASMLASEIGA 340
Cdd:PRK00106 292 GRIHPARIEELVEKNRLEMDNRIREYGEAAAYEIGAPNLHPDLIKIMGRLQFRTSYGQNVLRHSVEVGKLAGILAGELGE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 341 DVAIAKRGALLHDIGKGVETDSDRNHAEIGMEMARKMNEDPRVVNAVGSHHNDIEPCCVESWLVQVADAISAARPGARRE 420
Cdd:PRK00106 372 NVALARRAGFLHDMGKAIDREVEGSHVEIGMEFARKYKEHPVVVNTIASHHGDVEPESVIAVIVAAADALSSARPGARNE 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 421 MVDHYVKRLENLEAIAEGFSGVEKAYAIQAGRELRVLVNNDKIPDRDVKALGRDIAKKIESDLKYPGRIRVTLIRETRVV 500
Cdd:PRK00106 452 SMENYIKRLRDLEEIANSFDGVQNSFALQAGREIRIMVQPEKISDDQVTILAHKVREKIENNLDYPGNIKVTVIRELRAV 531
|
....
gi 499184922 501 EYAR 504
Cdd:PRK00106 532 DYAK 535
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
3-188 |
4.17e-49 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 167.37 E-value: 4.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 3 TSIVIGVVLVTVGLTFGWTIRWLYARFHLSACEQRAERILQEAQKEAESKKKSILLEAKEYVLRERNQQERDDRDRRAEL 82
Cdd:pfam12072 1 LIIILAIIALVVGFVVGYLVRKSIAEAKIGSAEELAKRIIEEAKKEAETKKKEALLEAKEEIHKLRAEAERELKERRNEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 83 QRAERRLLQKEEALSTRAGELDSRERSLKQRDQSLCQEE--------------ARYRQELERVSGLTQNQARDLIIKNLE 148
Cdd:pfam12072 81 QRQERRLLQKEETLDRKDESLEKKEESLEKKEKELEAQQqqleekeeeleeliEEQRQELERISGLTSEEAKEILLDEVE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499184922 149 NEAKHDAQALINKIEEDAALNAERRARDILVTTMQRITAD 188
Cdd:pfam12072 161 EELRHEAAVMIKEIEEEAKEEADKKAKEIIALAIQRCAAD 200
|
|
| RnaY |
COG1418 |
HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal ... |
311-498 |
1.32e-44 |
|
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: 155.06 E-value: 1.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 311 YFRTSYGQNVLYHSKEVALLASMLASEIGADVAIAKRGALLHDIGKGVETDSDRNHAEIGMEMARKMNED--------PR 382
Cdd:COG1418 10 YLRTSYGQHDLQHSLRVAKLAGLIAAEEGADVEVAKRAALLHDIGKAKDHEVEGSHAEIGAELARKYLESlgfpeeeiEA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 383 VVNAVGSHHND--IEPCCVESWLVQVADAISAArpGARremvdhyvkrlenleaiaegfsGVEKAYAI--QAGRELR--- 455
Cdd:COG1418 90 VVHAIEAHSFSggIEPESLEAKIVQDADRLDAL--GAI----------------------GVARAFAIggQAGRELRdpe 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499184922 456 ------VLVNNDKIPDRDVKALGRDIAKKIESDLK-YPgrirVTLIRETR 498
Cdd:COG1418 146 dtainhFYEKLLKLKDLMATELARDIAKKREEFMEeFP----VTVIRETR 191
|
|
| KH-I_RNaseY |
cd22431 |
type I K homology (KH) RNA-binding domain found in ribonuclease Y (RNase Y) and similar ... |
194-270 |
8.64e-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: 149.27 E-value: 8.64e-44
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499184922 194 TVSTVNLPSEEMKGRIIGREGRNIRALETLTGADVVVDDTPEAVVISCFDPVRKEIARISLERLVLDGRIHPARIEE 270
Cdd:cd22431 3 TVSTVNLPNDEMKGRIIGREGRNIRAFEAATGVDLIIDDTPEAVILSGFDPVRREVARRTLEKLVEDGRIHPARIEE 79
|
|
| HDIG |
TIGR00277 |
HDIG domain; This domain is found in a few known nucleotidyltransferes and in a large number ... |
316-393 |
2.92e-28 |
|
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: 107.42 E-value: 2.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 316 YGQNVLYHSKEVALLASMLASEIGADVAIAKRGALLHDIGKGV--ETDSDRNHAEIGMEMARKMNEDPRVVNAVGSHHND 393
Cdd:TIGR00277 1 YGQNVLQHSLEVAKLAEALARELGLDVELARRGALLHDIGKPItrEGVIFESHVVVGAEIARKYGEPLEVIDIIAEHHGK 80
|
|
| Krr1 |
COG1094 |
rRNA processing protein Krr1/Pno1, contains KH domain [Translation, ribosomal structure and ... |
192-285 |
1.16e-25 |
|
rRNA processing protein Krr1/Pno1, contains KH domain [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440711 [Multi-domain] Cd Length: 177 Bit Score: 103.37 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 192 DVTVSTVNLPS--------EEMKGRIIGREGRNIRALETLTGADVVVDDTPEAvVISCFDPVrkEIARISLERLvLDGRI 263
Cdd:COG1094 79 DYMLEVIDLPDvgkspnalDRIKGRIIGREGRTRRIIEELTGVDISIYGKTVA-IIGDFDQV--EIAREAIEML-IDGRI 154
|
90 100
....*....|....*....|..
gi 499184922 264 HPArIEEIVQKVTQEVSQKIYE 285
Cdd:COG1094 155 HPT-VYEFLEKARRELKRRRLE 175
|
|
| HD |
pfam01966 |
HD domain; HD domains are metal dependent phosphohydrolases. |
320-413 |
2.20e-14 |
|
HD domain; HD domains are metal dependent phosphohydrolases.
Pssm-ID: 460398 [Multi-domain] Cd Length: 110 Bit Score: 69.19 E-value: 2.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 320 VLYHSKEVALLASMLASEIG-ADVAIAKRGALLHDIGKGVETD------SDRNHAEIGMEMARKMNEDPR---VVNAVGS 389
Cdd:pfam01966 1 RLEHSLRVALLARELAEELGeLDRELLLLAALLHDIGKGPFGDekpefeIFLGHAVVGAEILRELEKRLGledVLKLILE 80
|
90 100 110
....*....|....*....|....*....|
gi 499184922 390 HHNDI------EPCCVESWLVQVADAISAA 413
Cdd:pfam01966 81 HHESWegagypEEISLEARIVKLADRLDAL 110
|
|
| HDc |
smart00471 |
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ... |
316-419 |
5.74e-14 |
|
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: 68.48 E-value: 5.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 316 YGQNVLYHSKEVALLASMLASEIGA-DVAIAKRGALLHDIGKGVETDS-------DRNHAEIGMEMARKMNEDPRVVN-- 385
Cdd:smart00471 1 SDYHVFEHSLRVAQLAAALAEELGLlDIELLLLAALLHDIGKPGTPDSflvktsvLEDHHFIGAEILLEEEEPRILEEil 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 499184922 386 --AVGSHH-----NDIEPCCVESWLVQVADAISAARPGARR 419
Cdd:smart00471 81 rtAILSHHerpdgLRGEPITLEARIVKVADRLDALRADRRY 121
|
|
| HDc |
cd00077 |
Metal dependent phosphohydrolases with conserved 'HD' motif |
318-432 |
2.31e-10 |
|
Metal dependent phosphohydrolases with conserved 'HD' motif
Pssm-ID: 238032 [Multi-domain] Cd Length: 145 Bit Score: 58.89 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 318 QNVLYHSKEVALLASMLASEIG---ADVAIAKRGALLHDIGKGVETDSD--------RNHAEIGMEMARKM------NED 380
Cdd:cd00077 1 EHRFEHSLRVAQLARRLAEELGlseEDIELLRLAALLHDIGKPGTPDAIteeeseleKDHAIVGAEILRELlleeviKLI 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499184922 381 PRVVNAVGSHHNDI------------EPCCVESWLVQVADAISAARPGARREMVDHYVKRLENL 432
Cdd:cd00077 81 DELILAVDASHHERldglgypdglkgEEITLEARIVKLADRLDALRRDSREKRRRIAEEDLEEL 144
|
|
| HDGYP |
COG2206 |
HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal ... |
207-391 |
8.33e-10 |
|
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: 59.99 E-value: 8.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 207 GRIIGREGRNIRALETLTGADVVVDDTPEAVVISCFDPVRKEIARISLERLVLDGRIHPARIEEIVQKVTQEVSQKIYEE 286
Cdd:COG2206 42 LLALLLLLLLLLALLALLLALLALLLLLLLLLLLLSLLLAVALLLAELLLLLAALESLLAELFEELRLGLLEELKKLVEE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 287 GEKVLFDLGIHdmcpegvrALGRLYFRTSYgqnVLYHSKEVALLASMLASEIG---ADVAIAKRGALLHDIGK------- 356
Cdd:COG2206 122 LDELLPDALLA--------LLAALDAKDPY---TYGHSVRVAVLALALARELGlseEELEDLGLAALLHDIGKigipdei 190
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499184922 357 ----GVETDSDRN----HAEIGMEMARKMNEDPRVVNAVGSHH 391
Cdd:COG2206 191 lnkpGKLTDEEFEiikkHPEYGYEILKKLPGLSEVAEIVLQHH 233
|
|
| PRK12703 |
PRK12703 |
tRNA 2'-O-methylase; Reviewed |
320-454 |
2.13e-06 |
|
tRNA 2'-O-methylase; Reviewed
Pssm-ID: 237176 [Multi-domain] Cd Length: 339 Bit Score: 49.87 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 320 VLYHSKEVALLASMLASEIGADVAIAKRGALLHDIGKGVETDSDrnHAEIGMEMARKMNEDPRVVNAVGSH--------- 390
Cdd:PRK12703 188 LIRHVKTVYKLAMRIADCINADRRLVAAGALLHDIGRTKTNGID--HAVAGAEILRKENIDDRVVSIVERHigagitsee 265
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499184922 391 -------HNDIEPCCVESWLVQVADAISAARPGAR-REMVDHYVKRleNLEAIAEGFSGVEKAYAIQAGREL 454
Cdd:PRK12703 266 aqklglpVKDYVPETIEEMIVAHADNLFAGDKRLNlKQVMDKYRKK--GLHDAAERIKKLHEELSSICGRDL 335
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
35-175 |
3.50e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 35 EQRAERILQEAQKEAESKKKSILLEAKEyvLRERNQQERDDRDRRAELQRAERRLLQKEEALSTRAGELDSRERSLKQRD 114
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEE--LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499184922 115 QSLCQEEARYRQELERVSgLTQNQARDLIIKNLENEAKHDAQALINKIEEDAALNAERRAR 175
Cdd:COG1196 389 LEALRAAAELAAQLEELE-EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
|
| NhaP |
COG0025 |
NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion transport and metabolism]; |
4-141 |
4.75e-06 |
|
NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion transport and metabolism];
Pssm-ID: 439796 [Multi-domain] Cd Length: 506 Bit Score: 49.19 E-value: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 4 SIVIGVVLVTV---GLTFGWTIRWLYARFHLSACEQRAERILQEAQKEAESKKKSILLEAKEYVLRERNQQERDDRDRRA 80
Cdd:COG0025 366 ALAFGVILLTLvlqGLTLPPLARRLGLREDEPEGEELEAALARAALLELLAAELLADDEEVVLRAARRARRRREAAELLS 445
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499184922 81 ELQRAERRLLQKEEALSTRAGELDSRERSLKQRDQSLCQEEARYRQELERVSGLTQNQARD 141
Cdd:COG0025 446 EEAEEELDEDLLRLLLALLRLRLLNALAAARLERLLLRRRVEELLRLLERLLRERELEELR 506
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
35-176 |
5.96e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 5.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 35 EQRAERILQEAQKEAESKKKSILLEAKEYVLRERNQQERDDRdRRAELQRAERRLLQKEEALSTRAGELDSRERSLKQRD 114
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE-LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499184922 115 QSLCQEEARYRQELERVSGLTQNQARdlIIKNLENEAKHDAQALINKIEEDAALNAERRARD 176
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEE--LEEAEEALLERLERLEEELEELEEALAELEEEEE 438
|
|
| YhaM |
COG3481 |
3'-5' exoribonuclease YhaM, can participate in 23S rRNA maturation, HD superfamily ... |
321-412 |
6.07e-06 |
|
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: 48.27 E-value: 6.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 321 LYHSKEVALLASMLAS---EIGADVAIAkrGALLHDIGKGVETDSDRN-----------HAEIGMEM-ARKMNE----DP 381
Cdd:COG3481 163 LEHTLSVARLAKALADlypELNRDLLIA--GAILHDIGKVRELSGPPGteytdegqllgHIVLGVEMiEEAAAElgdfPE 240
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 499184922 382 RVVNAVG----SHHNDIE------PCCVESWLVQVADAISA 412
Cdd:COG3481 241 ELLLLLKhmilSHHGELEwgspkrPKTPEAEILHYADNLDA 281
|
|
| HDOD |
COG1639 |
HD-like signal output (HDOD) domain, no enzymatic activity [Signal transduction mechanisms]; |
323-429 |
7.27e-06 |
|
HD-like signal output (HDOD) domain, no enzymatic activity [Signal transduction mechanisms];
Pssm-ID: 441246 [Multi-domain] Cd Length: 244 Bit Score: 47.27 E-value: 7.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 323 HSKEVALLASMLASEIG---ADVA-IAkrgALLHDIGK------------GVETDSDR---------------NHAEIGM 371
Cdd:COG1639 108 HSLAVAAAARALARRLGlldPEEAfLA---GLLHDIGKlvllslfpeeyaELLALAEAdglslaeaerevlgtDHAELGA 184
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 372 EMARKMNEDPRVVNAVGSHHN--DIEPCCVESWLVQVADAISAARPGARREMVDHYVKRL 429
Cdd:COG1639 185 ALARKWGLPEELVEAIRYHHDpeAAGEHRRLAALVHLANRLARALGEEDPALPEAALALL 244
|
|
| HDOD |
pfam08668 |
HDOD domain; |
323-392 |
2.16e-05 |
|
HDOD domain;
Pssm-ID: 430141 [Multi-domain] Cd Length: 196 Bit Score: 45.30 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 323 HSKEVALLASMLASEIGADVA-IAKRGALLHDIGK-------------GVETDSDR--------------NHAEIGMEMA 374
Cdd:pfam08668 98 HSLACALAARLLARRLGLDDPeEAFLAGLLHDIGKlillsllpdkyeeLLEKAAEEgislleaerellgtDHAEVGAALL 177
|
90
....*....|....*...
gi 499184922 375 RKMNEDPRVVNAVGSHHN 392
Cdd:pfam08668 178 ERWNLPEELVEAIAYHHN 195
|
|
| PRK13763 |
PRK13763 |
putative RNA-processing protein; Provisional |
205-264 |
2.44e-05 |
|
putative RNA-processing protein; Provisional
Pssm-ID: 237494 [Multi-domain] Cd Length: 180 Bit Score: 44.86 E-value: 2.44e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 205 MKGRIIGREGRNIRALETLTGADVVVDDTPEAvVISCFDPVrkEIARISLERLvLDGRIH 264
Cdd:PRK13763 105 IKGRIIGEGGKTRRIIEELTGVDISVYGKTVA-IIGDPEQV--EIAREAIEML-IEGAPH 160
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
24-175 |
2.64e-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: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 24 WLYARFHLSACEQRAERILQEAQKEAESKKKSI-LLEAKEYVLRERNQQERDDRD-----------RRAELQRAERRLLQ 91
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELaELEAELEELRLELEELELELEeaqaeeyellaELARLEQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 92 KEEALSTRAGELDSRERSLKQRDQSLCQEEARYRQELERVsgLTQNQARDLIIKNLENEAKHDAQALINKIEEDAALNAE 171
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEA--EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
|
....
gi 499184922 172 RRAR 175
Cdd:COG1196 388 LLEA 391
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
35-195 |
3.39e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 35 EQRAERILQEAQKEAESKKKSILLEAKEyVLRERNQQERDDRDRRAELQRAERRLLQKEEALSTRAGELDSRERSLKQRD 114
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRA-AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 115 QSLCQEEARYRQELERVSGLTQNQARDLIIKNLENEAKHDAQALINKIE--EDAALNAERRARDILVTTMQRITADVTGD 192
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLllLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
|
...
gi 499184922 193 VTV 195
Cdd:COG1196 526 VAV 528
|
|
| arCOG04150 |
TIGR03665 |
arCOG04150 universal archaeal KH domain protein; This family of proteins is universal among ... |
203-264 |
4.02e-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: 44.09 E-value: 4.02e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499184922 203 EEMKGRIIGREGRNIRALETLTGADVVVDDTpEAVVISCFDPVrkEIARISLERLvLDGRIH 264
Cdd:TIGR03665 97 RRIKGRIIGEGGKTRRIIEELTGVSISVYGK-TVGIIGDPEQV--QIAREAIEML-IEGAPH 154
|
|
| Cas10_III |
cd09680 |
CRISPR/Cas system-associated protein Cas10; CRISPR (Clustered Regularly Interspaced Short ... |
348-421 |
6.84e-05 |
|
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: 45.39 E-value: 6.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 348 GALLHDIGKGVE----TDSDRNHAEIGMEMARKM-NEDPRVVNAVGSHHND------IEPCCVESWLVQVADAISAArpG 416
Cdd:cd09680 4 GALLHDIGKVVQraglGFYSKTHSKFGAEFLKEFsKNKDDLGDCISYHHTKelakalLENHHPLAYIVYIADNIAAS--V 81
|
....*
gi 499184922 417 ARREM 421
Cdd:cd09680 82 ERREG 86
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
36-176 |
7.93e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 7.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 36 QRAERILQEAQKEAESKKKSILLEAKEYVLR-ERNQQERDDRDRRAELQRAERRLLQKEEAlsTRAGELDSRERSLKQRD 114
Cdd:COG1196 287 QAEEYELLAELARLEQDIARLEERRRELEERlEELEEELAELEEELEELEEELEELEEELE--EAEEELEEAEAELAEAE 364
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499184922 115 QSLCQEEARYRQELERVSGLTQNQARDLI-IKNLENEAKHDAQALINKIEEDAALNAERRARD 176
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRaAAELAAQLEELEEAEEALLERLERLEEELEELE 427
|
|
| KH |
smart00322 |
K homology RNA-binding domain; |
192-252 |
1.39e-04 |
|
K homology RNA-binding domain;
Pssm-ID: 197652 [Multi-domain] Cd Length: 68 Bit Score: 39.97 E-value: 1.39e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499184922 192 DVTVSTVNLPSEEMkGRIIGREGRNIRALETLTGADVVVDDTPEA---VVISC-FDPVRKEIARI 252
Cdd:smart00322 1 DPVTIEVLIPADKV-GLIIGKGGSTIKKIEEETGVKIDIPGPGSEervVEITGpPENVEKAAELI 64
|
|
| YlqC |
COG1837 |
Predicted RNA-binding protein YlqC, contains KH domain, UPF0109 family [General function ... |
184-226 |
2.09e-04 |
|
Predicted RNA-binding protein YlqC, contains KH domain, UPF0109 family [General function prediction only];
Pssm-ID: 441442 Cd Length: 76 Bit Score: 39.65 E-value: 2.09e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 499184922 184 RITADVTGDVTVSTVNLPSEEMkGRIIGREGRNIRALETLTGA 226
Cdd:COG1837 20 SVTEEEGERTVVLELRVAPEDL-GKVIGKQGRTAKAIRTVLSA 61
|
|
| KH_4 |
pfam13083 |
KH domain; |
184-226 |
7.58e-04 |
|
KH domain;
Pssm-ID: 463779 Cd Length: 73 Bit Score: 38.23 E-value: 7.58e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 499184922 184 RITADVTGDVTVSTVNLPSEEMkGRIIGREGRNIRALETLTGA 226
Cdd:pfam13083 19 SVTEEEEEKTVVLELNVAGEDM-GKVIGKQGRTLDALRTLVSA 60
|
|
| KH-I_Dim2p_like_rpt2 |
cd22390 |
second type I K homology (KH) RNA-binding domain found in Pyrococcus horikoshii Dim2p and ... |
203-264 |
8.86e-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: 8.86e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499184922 203 EEMKGRIIGREGRNIRALETLTGADVVVDDTPEAvVISCFDPVRkeIARISLERLvLDGRIH 264
Cdd:cd22390 27 RRVKGRVIGSGGKTRRLIEELTGCYISVYGKTVS-IIGDFENLQ--IAKEAIEML-LNGSPH 84
|
|
| glnD |
PRK00227 |
[protein-PII] uridylyltransferase; |
348-454 |
1.16e-03 |
|
[protein-PII] uridylyltransferase;
Pssm-ID: 178937 [Multi-domain] Cd Length: 693 Bit Score: 41.67 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 348 GALLHDIGKGvetdSDRNHAEIGMEM----ARKMNEDPR---VVNAVGSHHNDIepccveswlVQVADAISAARPGARRE 420
Cdd:PRK00227 408 GALYHDIGKG----YPRPHEQVGAEMvaraARRMGLNLRdraVVQTLVAEHTTL---------ARIAGRLDPTSEEAVDK 474
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 499184922 421 MVD--HY----VKRLENL-EAIAEGFS-GVEKAYAIQAGREL 454
Cdd:PRK00227 475 LLDavRYdlltLNLLEVLtEADAEGTGpGVWTARLEQGLRIV 516
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
35-188 |
1.40e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 35 EQRAERILQEAQKEAESKKKSILLEAKEY---------VLRERNQQERDDRDRRAELQRAERRLLQKEEALSTRAGELDS 105
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELELeeaqaeeyeLLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 106 RERSLKQRDQSLCQEEARYRQELERVSGLTQNQARDL-----IIKNLENEAKHDAQALINKIEEDAALNAERRARDILVT 180
Cdd:COG1196 335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEaelaeAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
|
....*...
gi 499184922 181 TMQRITAD 188
Cdd:COG1196 415 RLERLEEE 422
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
43-176 |
1.45e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 43 QEAQKEAESKKKSILLEAKEyvlRERNQQERDDRDRRAELQRAERrLLQKEEALSTRAGELDSRERSLKQRDQSLCQEEA 122
Cdd:PTZ00121 1610 EEAKKAEEAKIKAEELKKAE---EEKKKVEQLKKKEAEEKKKAEE-LKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEE 1685
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 499184922 123 RYRQELERVSGLTQNQARDLIIKNLENEAKHDAQALiNKIEEDAALNAERRARD 176
Cdd:PTZ00121 1686 DEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL-KKAEEENKIKAEEAKKE 1738
|
|
| KH-I_AKAP1 |
cd22395 |
type I K homology (KH) RNA-binding domain found in mitochondrial A-kinase anchor protein 1 ... |
199-235 |
1.47e-03 |
|
type I K homology (KH) RNA-binding domain found in mitochondrial A-kinase anchor protein 1 (AKAP1) and similar proteins; AKAP1, also called A-kinase anchor protein 149 kDa, or AKAP 149, or dual specificity A-kinase-anchoring protein 1, or D-AKAP-1, or protein kinase A-anchoring protein 1 (PRKA1), or spermatid A-kinase anchor protein 84, or S-AKAP84, is a novel developmentally regulated A kinase anchor protein of male germ cells. It binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane.
Pssm-ID: 411823 [Multi-domain] Cd Length: 68 Bit Score: 37.12 E-value: 1.47e-03
10 20 30
....*....|....*....|....*....|....*..
gi 499184922 199 NLPSEEMkGRIIGREGRNIRALETLTGADVVVDDTPE 235
Cdd:cd22395 5 EVPSELV-GRLIGKQGRNVKQLKQKSGAKIYIKPHPY 40
|
|
| KH_1 |
pfam00013 |
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ... |
197-240 |
1.53e-03 |
|
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause paraneoplastic opsoclonus ataxia.
Pssm-ID: 459630 [Multi-domain] Cd Length: 65 Bit Score: 36.88 E-value: 1.53e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 499184922 197 TVNLPSEEMkGRIIGREGRNIRALETLTGADVVVDD-----TPEAVVIS 240
Cdd:pfam00013 3 EILVPSSLV-GLIIGKGGSNIKEIREETGAKIQIPPsesegNERIVTIT 50
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
61-176 |
1.85e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 61 KEYVLRERNQQERDDRDRRAELQRAERRLLQKEEALSTRAGELDSRERSLKQRDQSLCQEEARYRQELERVSGLTQNQAR 140
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR 299
|
90 100 110
....*....|....*....|....*....|....*.
gi 499184922 141 DLIIKNLENEAKHDAQALINKIEEDAALNAERRARD 176
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEEL 335
|
|
| GlnD |
COG2844 |
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ... |
334-376 |
1.91e-03 |
|
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, chaperones, Signal transduction mechanisms];
Pssm-ID: 442092 [Multi-domain] Cd Length: 864 Bit Score: 40.90 E-value: 1.91e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 499184922 334 LASEIGADvaIAKR-----GALLHDIGKGVETDsdrnHAEIGMEMARK 376
Cdd:COG2844 465 LASELIAE--LPKPellylAALFHDIAKGRGGD----HSELGAEDARR 506
|
|
| PgpH |
COG1480 |
Cyclic di-AMP-specific phosphodiesterase PgpH, HD superfamily [Signal transduction mechanisms]; ... |
323-391 |
2.26e-03 |
|
Cyclic di-AMP-specific phosphodiesterase PgpH, HD superfamily [Signal transduction mechanisms];
Pssm-ID: 441089 [Multi-domain] Cd Length: 692 Bit Score: 40.59 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 323 HSKEVALLASMLASEIGADVAIAKRGALLHDIGKG------VE--TDSD---------------RNHAEIGMEMARKMNE 379
Cdd:COG1480 481 HSLMVANLAEAAAEAIGANPLLARVGAYYHDIGKMkrplyfIEnqMGGEnphdklspslsaliiISHVKDGVELARKYKL 560
|
90
....*....|..
gi 499184922 380 DPRVVNAVGSHH 391
Cdd:COG1480 561 PKEIIDFIRQHH 572
|
|
| KH-I |
cd00105 |
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ... |
197-235 |
2.27e-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: 36.51 E-value: 2.27e-03
10 20 30
....*....|....*....|....*....|....*....
gi 499184922 197 TVNLPSEEMkGRIIGREGRNIRALETLTGADVVVDDTPE 235
Cdd:cd00105 2 EIEVPSELV-GLIIGKGGSTIKEIEEETGARIQIPKEGE 39
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
37-152 |
2.42e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 39.96 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 37 RAERILQEAQKEAESKKKSILLEAKEYVLRERNQQErdDRDRRAELQRAERRLLQKEEALSTRageLDSRERS----LKQ 112
Cdd:pfam02841 173 KAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEA--ERAKAEAAEAEQELLREKQKEEEQM---MEAQERSyqehVKQ 247
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 499184922 113 RDQSLCQEEARYRQELERVSGLTQNQARDLIIKNLENEAK 152
Cdd:pfam02841 248 LIEKMEAEREQLLAEQERMLEHKLQEQEELLKEGFKTEAE 287
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
43-174 |
2.48e-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: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 43 QEAQKEAESKKKSILLEAKEYVLRERNQQERDDRDRRAELQRAERRLLQKEEALST---RAGELDSRERSLKQRDQSLCQ 119
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEElrlELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 120 EEARYRQELERVSGLTQNQARDLI-----IKNLENEAKHDAQALINKIEEDAALNAERRA 174
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEeleeeLAELEEELEELEEELEELEEELEEAEEELEE 355
|
|
| PRK03381 |
PRK03381 |
PII uridylyl-transferase; Provisional |
348-391 |
2.94e-03 |
|
PII uridylyl-transferase; Provisional
Pssm-ID: 235123 [Multi-domain] Cd Length: 774 Bit Score: 40.36 E-value: 2.94e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 499184922 348 GALLHDIGKGVETDsdrnHAEIGMEMARKMN-------EDPRVVNAVGSHH 391
Cdd:PRK03381 448 GALLHDIGKGRGGD----HSVVGAELARQIGarlglspADVALLSALVRHH 494
|
|
| KH-II_YlqC-like |
cd22533 |
type II K-homology (KH) RNA-binding domain found in Bacillus subtilis UPF0109 protein YlqC and ... |
184-226 |
3.52e-03 |
|
type II K-homology (KH) RNA-binding domain found in Bacillus subtilis UPF0109 protein YlqC and similar proteins; The family includes a group of uncharacterized proteins which show sequence similarity to Bacillus subtilis UPF0109 protein YlqC. They are mainly found in bacteria and contain only one canonical type II K-homology (KH) domain that has the signature motif GXXG (where X represents any amino acid).
Pssm-ID: 411790 Cd Length: 75 Bit Score: 36.29 E-value: 3.52e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 499184922 184 RITADVTGDVTVSTVNLPSEEMkGRIIGREGRNIRALETLTGA 226
Cdd:cd22533 20 RVSEIEGEKTTVYELRVAPEDV-GRVIGKQGRTAKAIRTLVSA 61
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
35-183 |
3.54e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.11 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 35 EQRAERILQEAQK-EAES-KKKSILLEAKEYVLRERNQQERDDRDRRA--ELQRAERRLLQKEE-----------ALSTR 99
Cdd:pfam17380 347 ERELERIRQEERKrELERiRQEEIAMEISRMRELERLQMERQQKNERVrqELEAARKVKILEEErqrkiqqqkveMEQIR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 100 AGELDSRERSLKQRDQSLCQEEARYRQE-------LERVSGLTQNQARDLIIKNLENEAKHDAQALINKI------EEDA 166
Cdd:pfam17380 427 AEQEEARQREVRRLEEERAREMERVRLEeqerqqqVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIlekeleERKQ 506
|
170
....*....|....*..
gi 499184922 167 ALNAERRARDILVTTMQ 183
Cdd:pfam17380 507 AMIEEERKRKLLEKEME 523
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
35-165 |
3.69e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 35 EQRAERILQEAQKEAESKKKSILLEAKEYVLRERNQQER----DDRDRRAELQRAERRLLQKEEALSTRAGELDSRERSL 110
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAkkaeEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELK 1708
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 499184922 111 KQRdqslcQEEARYRQELERVSGLTQNQARDLiiKNLENEAKHDAQALinKIEED 165
Cdd:PTZ00121 1709 KKE-----AEEKKKAEELKKAEEENKIKAEEA--KKEAEEDKKKAEEA--KKDEE 1754
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
36-175 |
4.68e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 36 QRAE--RILQEAQKEAESKKKSILLEAKEYV----LRERNQQERDDRDRRAELQRAErRLLQKEEALSTRAGELDSRERS 109
Cdd:PTZ00121 1528 KKAEeaKKADEAKKAEEKKKADELKKAEELKkaeeKKKAEEAKKAEEDKNMALRKAE-EAKKAEEARIEEVMKLYEEEKK 1606
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499184922 110 LKQrDQSLCQEEARYRQelERVSGLTQNQARDLIIKNLENEAKHDAQALiNKIEEDAALNAERRAR 175
Cdd:PTZ00121 1607 MKA-EEAKKAEEAKIKA--EELKKAEEEKKKVEQLKKKEAEEKKKAEEL-KKAEEENKIKAAEEAK 1668
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
35-130 |
5.19e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 35 EQRAE--RILQEAQKEAESKKKsilleAKEYVLRERNQQERDDRDRRAELQRAERRLLQKEEALSTRAGELDSRERSLKQ 112
Cdd:PTZ00121 1437 KKKAEeaKKADEAKKKAEEAKK-----AEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKK 1511
|
90
....*....|....*...
gi 499184922 113 RDQSLCQEEARYRQELER 130
Cdd:PTZ00121 1512 ADEAKKAEEAKKADEAKK 1529
|
|
| KH-I_IGF2BP_rpt4 |
cd22403 |
fourth type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ... |
205-235 |
5.48e-03 |
|
fourth type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 mRNA-binding protein (IGF2BP) family; The IGF2BP family includes three members: IGF2BP1/IMP-1/CRD-BP/VICKZ1, IGF2BP2/IMP-2/VICKZ2, and IGF2BP3/IMP-3/VICKZ3, which are RNA-binding factors that recruit target transcripts to cytoplasmic protein-RNA complexes (mRNPs). They function by binding to the 5' UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulating IGF2 translation. IGF2BP proteins contain 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 fourth one.
Pssm-ID: 411831 [Multi-domain] Cd Length: 66 Bit Score: 35.68 E-value: 5.48e-03
10 20 30
....*....|....*....|....*....|.
gi 499184922 205 MKGRIIGREGRNIRALETLTGADVVVDDTPE 235
Cdd:cd22403 10 MVGRIIGKGGQNVRELQRLTGAIIKLPRDQT 40
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
35-165 |
5.85e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499184922 35 EQRAERILQEAQKEAESKKKSILLEAKEYVLRERNQQ----ERDDRDRRAELQRaerrllqKEEALSTRAGELDSRERSL 110
Cdd:PTZ00121 1615 AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEElkkaEEENKIKAAEEAK-------KAEEDKKKAEEAKKAEEDE 1687
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 499184922 111 KQRDQSLCQ--EEARYRQELERVSGLTQNQARDLiiKNLENEAKHDAQALINKIEED 165
Cdd:PTZ00121 1688 KKAAEALKKeaEEAKKAEELKKKEAEEKKKAEEL--KKAEEENKIKAEEAKKEAEED 1742
|
|
| |
