|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
3-540 |
0e+00 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 762.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 3 NTILVPVAVAIVSVLVGGCAGYSIRKNKWETQAQNAAHDAKHILADAESKAKAVEADlasqkeamkkaaadakkeKILEA 82
Cdd:PRK12704 1 MMLLIIILIALVALVVGAVIGYFVRKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKE------------------ALLEA 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 83 QEEIHHYRERVDNELNERRQEVSRQENRLLQREDAIDHKDSLLDQKDSQLTQKENQIKKLQAQVLEKENRADQLVTEREK 162
Cdd:PRK12704 63 KEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 163 KLYEVAELNQEDAKKIVLDKLSDQLVKERAEMIEESNQLAKAKADHFARKVIVDAIQSSAADTVSEKTVSVVNLPSDDMK 242
Cdd:PRK12704 143 ELERISGLTAEEAKEILLEKVEEEARHEAAVLIKEIEEEAKEEADKKAKEILAQAIQRCAADHVAETTVSVVNLPNDEMK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 243 GRIIGREGRNIRSFEALTGVDVIIDDTPDVVVLSGFDPIRREIAKRALERLIKDGRIHPARIEEMVDRARKEVNDDIYEA 322
Cdd:PRK12704 223 GRIIGREGRNIRALETLTGVDLIIDDTPEAVILSGFDPIRREIARLALEKLVQDGRIHPARIEEMVEKARKEVDEEIREE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 323 GESALMELGIHKMHPELVKILGRLKYRTSYGQNVLSHSIEVGKLTGVMAAELGLDEKIAVRAGLLHDIGKSIDHEIEGSH 402
Cdd:PRK12704 303 GEQAVFELGIHGLHPELIKLLGRLKYRTSYGQNVLQHSIEVAHLAGLMAAELGLDVKLAKRAGLLHDIGKALDHEVEGSH 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 403 VEIGVELARKYHEPDLVVNAIAAHHDDVPKLSFIAELVVAADTISSARPGARSESLENYIRRLEQLETIAKGHIGVKQAY 482
Cdd:PRK12704 383 VEIGAELAKKYKESPVVINAIAAHHGDEEPTSIEAVLVAAADAISAARPGARRETLENYIKRLEKLEEIANSFEGVEKAY 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 491036056 483 AIQAGREIRVMVEPDKISDARTTILAHDIRNQIEQDMEYPGNIKVTVIREKRAVAIAK 540
Cdd:PRK12704 463 AIQAGREIRVIVKPDKVDDLQAVRLARDIAKKIEEELQYPGQIKVTVIRETRAVEYAK 520
|
|
| RNase_Y |
TIGR03319 |
ribonuclease Y; Members of this family are RNase Y, an endoribonuclease. The member from ... |
9-540 |
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: 712.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 9 VAVAIVSVLVGGCAGYSIRKNKWETQAQNAAHDAKHILADAESKAKAVEADlasqkeamkkaaadakkeKILEAQEEIHH 88
Cdd:TIGR03319 1 ILLALVALIVGLIIGYLLRKRIAEKKLGSAEELAKRIIEEAKKEAETLKKE------------------ALLEAKEEVHK 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 89 YRERVDNELNERRQEVSRQENRLLQREDAIDHKDSLLDQKDSQLTQKENQIKKLQAQVLEKENRADQLVTEREKKLYEVA 168
Cdd:TIGR03319 63 LRAELERELKERRNELQRLERRLLQREETLDRKMESLDKKEENLEKKEKELSNKEKNLDEKEEELEELIAEQREELERIS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 169 ELNQEDAKKIVLDKLSDQLVKERAEMIEESNQLAKAKADHFARKVIVDAIQSSAADTVSEKTVSVVNLPSDDMKGRIIGR 248
Cdd:TIGR03319 143 GLTQEEAKEILLEEVEEEARHEAAKLIKEIEEEAKEEADKKAKEILATAIQRYAGDHVAETTVSVVNLPNDEMKGRIIGR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 249 EGRNIRSFEALTGVDVIIDDTPDVVVLSGFDPIRREIAKRALERLIKDGRIHPARIEEMVDRARKEVNDDIYEAGESALM 328
Cdd:TIGR03319 223 EGRNIRALETLTGVDLIIDDTPEAVILSGFDPVRREIARMALEKLIQDGRIHPARIEEMVEKATKEVDNAIREEGEQAAF 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 329 ELGIHKMHPELVKILGRLKYRTSYGQNVLSHSIEVGKLTGVMAAELGLDEKIAVRAGLLHDIGKSIDHEIEGSHVEIGVE 408
Cdd:TIGR03319 303 DLGVHGLHPELIKLLGRLKFRTSYGQNVLQHSIEVAHLAGIMAAELGEDVKLAKRAGLLHDIGKAVDHEVEGSHVEIGAE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 409 LARKYHEPDLVVNAIAAHHDDVPKLSFIAELVVAADTISSARPGARSESLENYIRRLEQLETIAKGHIGVKQAYAIQAGR 488
Cdd:TIGR03319 383 LAKKYKESPEVVNAIAAHHGDVEPTSIEAVLVAAADALSAARPGARRESLENYIKRLEKLEEIANSFEGVEKSYAIQAGR 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 491036056 489 EIRVMVEPDKISDARTTILAHDIRNQIEQDMEYPGNIKVTVIREKRAVAIAK 540
Cdd:TIGR03319 463 EIRVMVKPEKISDDQAVVLARDIAKKIEEELEYPGQIKVTVIRETRAVEYAK 514
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
6-540 |
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 491036056 6 LVPVAVAIVSVLVGGCAGY---SIRKNKWETQAQ---------------NAAHDAKHILADAESKAKAVEADLasqkeam 67
Cdd:PRK00106 1 MINIIILVVSALIGLVIGYvliSIKMKSAKEAAEltllnaeqeavnlrgKAERDAEHIKKTAKRESKALKKEL------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 68 kkaaadakkekILEAQEEIHHYRERVDNELNERRQEVSRQENRLLQREDAIDHKDSLLDQKDSQLTQKENQIKKLQAQVL 147
Cdd:PRK00106 74 -----------LLEAKEEARKYREEIEQEFKSERQELKQIESRLTERATSLDRKDENLSSKEKTLESKEQSLTDKSKHID 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 148 EKENRADQLVTEREKKLYEVAELNQEDAKKIVLDKLSDQLVKERAEMIEESNQLAKAKADHFARKVIVDAIQSSAADTVS 227
Cdd:PRK00106 143 EREEQVEKLEEQKKAELERVAALSQAEAREIILAETENKLTHEIATRIREAEREVKDRSDKMAKDLLAQAMQRLAGEYVT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 228 EKTVSVVNLPSDDMKGRIIGREGRNIRSFEALTGVDVIIDDTPDVVVLSGFDPIRREIAKRALERLIKDGRIHPARIEEM 307
Cdd:PRK00106 223 EQTITTVHLPDDNMKGRIIGREGRNIRTLESLTGIDVIIDDTPEVVVLSGFDPIRREIARMTLESLIKDGRIHPARIEEL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 308 VDRARKEVNDDIYEAGESALMELGIHKMHPELVKILGRLKYRTSYGQNVLSHSIEVGKLTGVMAAELGLDEKIAVRAGLL 387
Cdd:PRK00106 303 VEKNRLEMDNRIREYGEAAAYEIGAPNLHPDLIKIMGRLQFRTSYGQNVLRHSVEVGKLAGILAGELGENVALARRAGFL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 388 HDIGKSIDHEIEGSHVEIGVELARKYHEPDLVVNAIAAHHDDVPKLSFIAELVVAADTISSARPGARSESLENYIRRLEQ 467
Cdd:PRK00106 383 HDMGKAIDREVEGSHVEIGMEFARKYKEHPVVVNTIASHHGDVEPESVIAVIVAAADALSSARPGARNESMENYIKRLRD 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491036056 468 LETIAKGHIGVKQAYAIQAGREIRVMVEPDKISDARTTILAHDIRNQIEQDMEYPGNIKVTVIREKRAVAIAK 540
Cdd:PRK00106 463 LEEIANSFDGVQNSFALQAGREIRIMVQPEKISDDQVTILAHKVREKIENNLDYPGNIKVTVIRELRAVDYAK 535
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2-540 |
0e+00 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 518.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 2 VNTILVPVAVAIVSVLVGGCAGYsirknkWETQAQNAAHDAKHILADAESKAKAVeadlasqkeamkkaaadaKKEKILE 81
Cdd:PRK12705 1 FAMSILLVILLLLIGLLLGVLVV------LLKKRQRLAKEAERILQEAQKEAEEK------------------LEAALLE 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 82 AQEEIHHYRERVDNELNERRQEVSRQENRLLQREDAIDHKDSLLDQKDSQLTQKENQIKKLQAQVLEKENRADQlvtere 161
Cdd:PRK12705 57 AKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSARELELEELEKQLDN------ 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 162 kKLYEVAELNQEDAKKIVLDKLSDQLVKERAEMIEESNQLAKAKADHFARKVIVDAIQSSAADTVSEKTVSVVNLPSDDM 241
Cdd:PRK12705 131 -ELYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKAQNILAQAMQRIASETASDLSVSVVPIPSDAM 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 242 KGRIIGREGRNIRSFEALTGVDVIIDDTPDVVVLSGFDPIRREIAKRALERLIKDGRIHPARIEEMVDRARKEVNDDIYE 321
Cdd:PRK12705 210 KGRIIGREGRNIRAFEGLTGVDLIIDDTPEAVVISSFNPIRREIARLTLEKLLADGRIHPARIEEYVQKANEEFKQKIYE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 322 AGESALMELGIHKMHPELVKILGRLKYRTSYGQNVLSHSIEVGKLTGVMAAELGLDEKIAVRAGLLHDIGKSIDHEIEGS 401
Cdd:PRK12705 290 IGEEVLEELGIFDLKPGLVRLLGRLYFRTSYGQNVLSHSLEVAHLAGIIAAEIGLDPALAKRAGLLHDIGKSIDRESDGN 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 402 HVEIGVELARKYHEPDLVVNAIAAHHDDVPKLSFIAELVVAADTISSARPGARSESLENYIRRLEQLETIAKGHIGVKQA 481
Cdd:PRK12705 370 HVEIGAELARKFNEPDEVINAIASHHNKVNPETVYSVLVQIADALSAARPGARRESLDEYVQRLEELEQIAESFPGVEKA 449
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 491036056 482 YAIQAGREIRVMVEPDKISDARTTILAHDIRNQIEQDMEYPGNIKVTVIREKRAVAIAK 540
Cdd:PRK12705 450 YAIQAGRELRVIVEPEKVSDAQATLLARDIAKKIENDLTYPGPIKVTLIRETRAVEYAR 508
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
7-224 |
2.54e-52 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 176.62 E-value: 2.54e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 7 VPVAVAIVSVLVGGCAGYSIRKNKWETQAQNAAHDAKHILADAESKAKAV--EAdlasqkeamkkaaadakkekILEAQE 84
Cdd:pfam12072 1 LIIILAIIALVVGFVVGYLVRKSIAEAKIGSAEELAKRIIEEAKKEAETKkkEA--------------------LLEAKE 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 85 EIHHYRERVDNELNERRQEVSRQENRLLQREDAIDHKDSLLDQKDSQLTQKENQIKKLQAQVLEKENRADQLVTEREKKL 164
Cdd:pfam12072 61 EIHKLRAEAERELKERRNELQRQERRLLQKEETLDRKDESLEKKEESLEKKEKELEAQQQQLEEKEEELEELIEEQRQEL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 165 YEVAELNQEDAKKIVLDKLSDQLVKERAEMIEESNQLAKAKADHFARKVIVDAIQSSAAD 224
Cdd:pfam12072 141 ERISGLTSEEAKEILLDEVEEELRHEAAVMIKEIEEEAKEEADKKAKEIIALAIQRCAAD 200
|
|
| KH-I_RNaseY |
cd22431 |
type I K homology (KH) RNA-binding domain found in ribonuclease Y (RNase Y) and similar ... |
228-306 |
1.98e-46 |
|
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: 156.97 E-value: 1.98e-46
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491036056 228 EKTVSVVNLPSDDMKGRIIGREGRNIRSFEALTGVDVIIDDTPDVVVLSGFDPIRREIAKRALERLIKDGRIHPARIEE 306
Cdd:cd22431 1 ERTVSTVNLPNDEMKGRIIGREGRNIRAFEAATGVDLIIDDTPEAVILSGFDPVRREVARRTLEKLVEDGRIHPARIEE 79
|
|
| RnaY |
COG1418 |
HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal ... |
337-534 |
1.71e-42 |
|
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: 150.43 E-value: 1.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 337 PELVKILgrLKYRTSYGQNVLSHSIEVGKLTGVMAAELGLDEKIAVRAGLLHDIGKSIDHEIEGSHVEIGVELARKY--- 413
Cdd:COG1418 2 PELIKLV--KYLRTSYGQHDLQHSLRVAKLAGLIAAEEGADVEVAKRAALLHDIGKAKDHEVEGSHAEIGAELARKYles 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 414 -----HEPDLVVNAIAAHHDDV--PKLSFIAELVVAADTISSArpgarseslenyirrleqletiakGHIGVKQAYAI-- 484
Cdd:COG1418 80 lgfpeEEIEAVVHAIEAHSFSGgiEPESLEAKIVQDADRLDAL------------------------GAIGVARAFAIgg 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 485 QAGREIR---------VMVEPDKISDARTTILAHDIRNQIEQDME-YPgnikVTVIREKR 534
Cdd:COG1418 136 QAGRELRdpedtainhFYEKLLKLKDLMATELARDIAKKREEFMEeFP----VTVIRETR 191
|
|
| Krr1 |
COG1094 |
rRNA processing protein Krr1/Pno1, contains KH domain [Translation, ribosomal structure and ... |
228-321 |
1.35e-26 |
|
rRNA processing protein Krr1/Pno1, contains KH domain [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440711 [Multi-domain] Cd Length: 177 Bit Score: 106.06 E-value: 1.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 228 EKTVSVVNLPS--------DDMKGRIIGREGRNIRSFEALTGVDVIIDDTPdVVVLSGFDPIrrEIAKRALERLIkDGRI 299
Cdd:COG1094 79 DYMLEVIDLPDvgkspnalDRIKGRIIGREGRTRRIIEELTGVDISIYGKT-VAIIGDFDQV--EIAREAIEMLI-DGRI 154
|
90 100
....*....|....*....|..
gi 491036056 300 HPArIEEMVDRARKEVNDDIYE 321
Cdd:COG1094 155 HPT-VYEFLEKARRELKRRRLE 175
|
|
| HDIG |
TIGR00277 |
HDIG domain; This domain is found in a few known nucleotidyltransferes and in a large number ... |
352-429 |
2.75e-24 |
|
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: 96.25 E-value: 2.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 352 YGQNVLSHSIEVGKLTGVMAAELGLDEKIAVRAGLLHDIGKSIDHE--IEGSHVEIGVELARKYHEPDLVVNAIAAHHDD 429
Cdd:TIGR00277 1 YGQNVLQHSLEVAKLAEALARELGLDVELARRGALLHDIGKPITREgvIFESHVVVGAEIARKYGEPLEVIDIIAEHHGK 80
|
|
| HD |
pfam01966 |
HD domain; HD domains are metal dependent phosphohydrolases. |
356-443 |
1.08e-11 |
|
HD domain; HD domains are metal dependent phosphohydrolases.
Pssm-ID: 460398 [Multi-domain] Cd Length: 110 Bit Score: 61.87 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 356 VLSHSIEVGKLTGVMAAELG-LDEKIAVRAGLLHDIGKS------IDHEIEGSHVEIGVELARKYHEP---DLVVNAIAA 425
Cdd:pfam01966 1 RLEHSLRVALLARELAEELGeLDRELLLLAALLHDIGKGpfgdekPEFEIFLGHAVVGAEILRELEKRlglEDVLKLILE 80
|
90
....*....|....*...
gi 491036056 426 HHDDVPKLSFIAELVVAA 443
Cdd:pfam01966 81 HHESWEGAGYPEEISLEA 98
|
|
| HDc |
smart00471 |
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ... |
352-455 |
2.13e-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: 61.16 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 352 YGQNVLSHSIEVGKLTGVMAAELGLDEKIAVR-AGLLHDIGKSIDH-------EIEGSHVEIGVELARKYHEPDLVVN-- 421
Cdd:smart00471 1 SDYHVFEHSLRVAQLAAALAEELGLLDIELLLlAALLHDIGKPGTPdsflvktSVLEDHHFIGAEILLEEEEPRILEEil 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 491036056 422 --AIAAHHD-----DVPKLSFIAELVVAADTISSARPGARS 455
Cdd:smart00471 81 rtAILSHHErpdglRGEPITLEARIVKVADRLDALRADRRY 121
|
|
| HDGYP |
COG2206 |
HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal ... |
213-466 |
4.50e-11 |
|
HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal transduction mechanisms];
Pssm-ID: 441808 [Multi-domain] Cd Length: 316 Bit Score: 64.22 E-value: 4.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 213 VIVDAIQSSAADTVSEKTVSVVNLPSDDMKGRIIGREGRNIRSFEALTGVDVIIDDTPDVVVLSGFDPIRREIAKRALER 292
Cdd:COG2206 1 LLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLLLLLLALLALLLLLLLLLALLALLLALLALLLLLLLLLLLLSLLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 293 LIKDGRIHPARIEEMVDRARKEVNDDIYEAGESALMEL--GIHKMHPELVK-ILGRLKYRTSYgqnVLSHSIEVGKLTGV 369
Cdd:COG2206 81 AVALLLAELLLLLAALESLLAELFEELRLGLLEELKKLveELDELLPDALLaLLAALDAKDPY---TYGHSVRVAVLALA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 370 MAAELGLDE---KIAVRAGLLHDIGK-SIDHEI---EG-----------SHVEIGVELARKYHEPDLVVNAIAAHH---- 427
Cdd:COG2206 158 LARELGLSEeelEDLGLAALLHDIGKiGIPDEIlnkPGkltdeefeiikKHPEYGYEILKKLPGLSEVAEIVLQHHerld 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 491036056 428 ----------DDVPKLSFIAELVVAADTISSARPGARSESLENYIRRLE 466
Cdd:COG2206 238 gsgyprglkgEEIPLLARILAVADVYDALTSDRPYRKALSPEEALEELR 286
|
|
| HDc |
cd00077 |
Metal dependent phosphohydrolases with conserved 'HD' motif |
354-456 |
3.54e-07 |
|
Metal dependent phosphohydrolases with conserved 'HD' motif
Pssm-ID: 238032 [Multi-domain] Cd Length: 145 Bit Score: 49.65 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 354 QNVLSHSIEVGKLTGVMAAELGL---DEKIAVRAGLLHDIGK--------SIDHEIEGSHVEIGVELARKYHE------- 415
Cdd:cd00077 1 EHRFEHSLRVAQLARRLAEELGLseeDIELLRLAALLHDIGKpgtpdaitEEESELEKDHAIVGAEILRELLLeevikli 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 491036056 416 PDLVVNAIAAHHD-----------DVPKLSFIAELVVAADTISSARPGARSE 456
Cdd:cd00077 81 DELILAVDASHHErldglgypdglKGEEITLEARIVKLADRLDALRRDSREK 132
|
|
| arCOG04150 |
TIGR03665 |
arCOG04150 universal archaeal KH domain protein; This family of proteins is universal among ... |
242-300 |
1.58e-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: 48.33 E-value: 1.58e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 491036056 242 KGRIIGREGRNIRSFEALTGVDVIIDDtpDVVVLSGfDPIRREIAKRALERLIkDGRIH 300
Cdd:TIGR03665 100 KGRIIGEGGKTRRIIEELTGVSISVYG--KTVGIIG-DPEQVQIAREAIEMLI-EGAPH 154
|
|
| HDOD |
pfam08668 |
HDOD domain; |
359-428 |
2.91e-06 |
|
HDOD domain;
Pssm-ID: 430141 [Multi-domain] Cd Length: 196 Bit Score: 47.99 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 359 HSIEVGKLTGVMAAELGLDE-KIAVRAGLLHDIGKSI----------------------DHEIE----G-SHVEIGVELA 410
Cdd:pfam08668 98 HSLACALAARLLARRLGLDDpEEAFLAGLLHDIGKLIllsllpdkyeellekaaeegisLLEAErellGtDHAEVGAALL 177
|
90
....*....|....*...
gi 491036056 411 RKYHEPDLVVNAIAAHHD 428
Cdd:pfam08668 178 ERWNLPEELVEAIAYHHN 195
|
|
| PRK13763 |
PRK13763 |
putative RNA-processing protein; Provisional |
241-315 |
3.34e-06 |
|
putative RNA-processing protein; Provisional
Pssm-ID: 237494 [Multi-domain] Cd Length: 180 Bit Score: 47.56 E-value: 3.34e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491036056 241 MKGRIIGREGRNIRSFEALTGVDVIIDDtpDVVVLSGfDPIRREIAKRALERLIkDGRIHpARIEEMVDRARKEV 315
Cdd:PRK13763 105 IKGRIIGEGGKTRRIIEELTGVDISVYG--KTVAIIG-DPEQVEIAREAIEMLI-EGAPH-GTVYKFLERKKREL 174
|
|
| HDOD |
COG1639 |
HD-like signal output (HDOD) domain, no enzymatic activity [Signal transduction mechanisms]; |
354-465 |
5.90e-06 |
|
HD-like signal output (HDOD) domain, no enzymatic activity [Signal transduction mechanisms];
Pssm-ID: 441246 [Multi-domain] Cd Length: 244 Bit Score: 47.65 E-value: 5.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 354 QNVLSHSIEVGKLTGVMAAELG-LDEKIAVRAGLLHDIGKSI---------------------------DHEIEGSHVEI 405
Cdd:COG1639 103 RRFWRHSLAVAAAARALARRLGlLDPEEAFLAGLLHDIGKLVllslfpeeyaellalaeadglslaeaeREVLGTDHAEL 182
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491036056 406 GVELARKYHEPDLVVNAIAAHHD--DVPKLSFIAELVVAADTISSARPGARSESLENYIRRL 465
Cdd:COG1639 183 GAALARKWGLPEELVEAIRYHHDpeAAGEHRRLAALVHLANRLARALGEEDPALPEAALALL 244
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
46-211 |
1.01e-04 |
|
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: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 46 LADAESKAKAVEADLASQKEAMKKAAADAKKEKILEAQEEIHHYRERvdNELNERRQEVSRQENRLLQREDAIDHKDSLL 125
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE--LELEEAQAEEYELLAELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 126 DQKDSQLTQKENQIKKLQAQVLEKENRADQLVTEREKKLYEVAELNQEdakkivLDKLSDQLVKERAEMIEESNQLAKAK 205
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE------LAEAEEALLEAEAELAEAEEELEELA 385
|
....*.
gi 491036056 206 ADHFAR 211
Cdd:COG1196 386 EELLEA 391
|
|
| KH |
smart00322 |
K homology RNA-binding domain; |
228-294 |
1.54e-04 |
|
K homology RNA-binding domain;
Pssm-ID: 197652 [Multi-domain] Cd Length: 68 Bit Score: 39.97 E-value: 1.54e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 228 EKTVSVVNLPSDDMkGRIIGREGRNIRSFEALTGVDVIIDDTP---DVVVLSGfDPIRREIAKRALERLI 294
Cdd:smart00322 1 DPVTIEVLIPADKV-GLIIGKGGSTIKKIEEETGVKIDIPGPGseeRVVEITG-PPENVEKAAELILEIL 68
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
79-224 |
1.89e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 79 ILEAQEEIHHYRERvDNELNERRQEVSRQENRLLQREDAIDHKDSLLDQKDSQLTQKENQIKKLQAQVLEKENRADQLVT 158
Cdd:COG1196 224 ELEAELLLLKLREL-EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ 302
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491036056 159 EREKKLYEVAELNQEdakkivLDKLSDQLVKERAEMIEESNQLAKAKADHFARKVIVDAIQSSAAD 224
Cdd:COG1196 303 DIARLEERRRELEER------LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
|
| KH_1 |
pfam00013 |
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ... |
240-291 |
2.33e-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: 39.57 E-value: 2.33e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 491036056 240 DMKGRIIGREGRNIRSFEALTGVDVIIDD-----TPDVVVLSGfDPIRREIAKRALE 291
Cdd:pfam00013 9 SLVGLIIGKGGSNIKEIREETGAKIQIPPsesegNERIVTITG-TPEAVEAAKALIE 64
|
|
| KH-I_Dim2p_like_rpt2 |
cd22390 |
second type I K homology (KH) RNA-binding domain found in Pyrococcus horikoshii Dim2p and ... |
242-313 |
6.10e-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: 39.13 E-value: 6.10e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491036056 242 KGRIIGREGRNIRSFEALTGVDV-IIDDTpdVVVLSGFDPIRreIAKRALERLIKdGRIHpARIEEMVDRARK 313
Cdd:cd22390 30 KGRVIGSGGKTRRLIEELTGCYIsVYGKT--VSIIGDFENLQ--IAKEAIEMLLN-GSPH-SSVYRFLEKKRR 96
|
|
| Cas10_III |
cd09680 |
CRISPR/Cas system-associated protein Cas10; CRISPR (Clustered Regularly Interspaced Short ... |
384-449 |
6.88e-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: 42.31 E-value: 6.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 384 AGLLHDIGKSI----DHEIEGSHVEIGVEL--------------ARKYHEPDLVVNAIAAHHddvPKLSFIAElvvaADT 445
Cdd:cd09680 4 GALLHDIGKVVqragLGFYSKTHSKFGAEFlkefsknkddlgdcISYHHTKELAKALLENHH---PLAYIVYI----ADN 76
|
....
gi 491036056 446 ISSA 449
Cdd:cd09680 77 IAAS 80
|
|
| nadD |
PRK07152 |
nicotinate-nucleotide adenylyltransferase; |
359-450 |
7.24e-04 |
|
nicotinate-nucleotide adenylyltransferase;
Pssm-ID: 235947 [Multi-domain] Cd Length: 342 Bit Score: 41.86 E-value: 7.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 359 HSIEVGKLTGVMAAELGLDEKIAVRAGLLHDIGKSID-----------------------HEIEGSHVeigveLARKYHE 415
Cdd:PRK07152 200 HCLRVAQLAAELAKKNNLDPKKAYYAGLYHDITKEWDeekhrkflkkylkdvknlpwyvlHQYVGALW-----LKHVYGI 274
|
90 100 110
....*....|....*....|....*....|....*.
gi 491036056 416 PD-LVVNAIAAHHDDVPKLSFIAELVVAADTISSAR 450
Cdd:PRK07152 275 DDeEILNAIRNHTSLAEEMSTLDKIVYVADKIEPGR 310
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
32-206 |
1.03e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 32 ETQAQNAAHDAKHILADAESKAKAVEADLASQKEAMKKAAADAKKEKILEAQEEIHHYRERVDNELNER-RQEVSRQEN- 109
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIaRLEERRRELe 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 110 -RLLQREDAIDHKDSLLDQKDSQLTQKENQIKKLQAQVLEKENRADQLVTEREKKLYEVAELNQEdakkivLDKLSDQLV 188
Cdd:COG1196 316 eRLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE------LEELAEELL 389
|
170
....*....|....*...
gi 491036056 189 KERAEMIEESNQLAKAKA 206
Cdd:COG1196 390 EALRAAAELAAQLEELEE 407
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
81-409 |
1.40e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 81 EAQEEIHHYRErvdnELNERRQEVSRQENRLLQREDAIDHKDSLLDQKDSQLTQKENQIKKLQAQVLEKENRADQLVTER 160
Cdd:COG4372 42 KLQEELEQLRE----ELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 161 EKKLYEVAELNQEDAK-KIVLDKLSDQLVKERAEMIEESNQLAKAKADHFARKVIVDAIQSSAADTVSEKTVSVVN---L 236
Cdd:COG4372 118 EELQKERQDLEQQRKQlEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANrnaE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 237 PSDDMKGRIIGREGRNIRSFEALTGVDVIIDDTPDVVVLSGFDPIRREIAKRALERLIKDGRIHPARIEEMVDRARKEVN 316
Cdd:COG4372 198 KEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 317 DDIYEAGESALMELGIHKMHPELVKILGRLKYRTSYGQNVLSHSIEVGKLTGVMAAELGLDEKIAVRAGLLHDIGKSIDH 396
Cdd:COG4372 278 LEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLE 357
|
330
....*....|...
gi 491036056 397 EIEGSHVEIGVEL 409
Cdd:COG4372 358 LLSKGAEAGVADG 370
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
51-228 |
1.50e-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: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 51 SKAKAVEADLASQKEAMKKAAADAKKEKILEAQEEIhhyrERVDNELNERRQEVSRQENRLLQREDAIDHKDSLLDQKDS 130
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAEL----EELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 131 QLTQKENQIKKLQAQVLEKENRADQLVTEREKKLYEVAELNQE--------DAKKIVLDKLSDQLVKERAEMIEESNQLA 202
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEleeleeelEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180
....*....|....*....|....*.
gi 491036056 203 KAKADHFARKVIVDAIQSSAADTVSE 228
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQ 401
|
|
| KH-I_IGF2BP2_rpt2 |
cd22494 |
second type I K homology (KH) RNA-binding domain found in insulin-like growth factor 2 ... |
236-291 |
1.92e-03 |
|
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: 37.31 E-value: 1.92e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 491036056 236 LPSDDMKGRIIGREGRNIRSFEALTGVDVIIDDTPDvvvLSGFDPIRREIAKRALE 291
Cdd:cd22494 5 LAHNSLVGRLIGKEGRNLKKIEQDTGTKITISSLQD---LTIYNPERTITVKGSIE 57
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
34-212 |
1.95e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 34 QAQNAAHDAKHILADAESKAKAVEADLASQKEAMKKAAADAKKEKILEAQEEIHHYRERvdNELNERRQEVSRQENRLLQ 113
Cdd:PTZ00121 1259 EARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKA--DEAKKKAEEAKKKADAAKK 1336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 114 REDAIDHKDslldqkdsQLTQKENQIKKLQAQVLEKENRADQLVTEREKKLYEVAELNQEDAKKIVLDKLSDQLVKERAE 193
Cdd:PTZ00121 1337 KAEEAKKAA--------EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD 1408
|
170
....*....|....*....
gi 491036056 194 MIEESNQlAKAKADHFARK 212
Cdd:PTZ00121 1409 ELKKAAA-AKKKADEAKKK 1426
|
|
| KH-I_PNPase |
cd02393 |
type I K homology (KH) RNA-binding domain found in polyribonucleotide nucleotidyltransferase ... |
240-296 |
2.39e-03 |
|
type I K homology (KH) RNA-binding domain found in polyribonucleotide nucleotidyltransferase (PNPase) and similar proteins; PNPase, also called polynucleotide phosphorylase, is a polyribonucleotide nucleotidyl transferase that degrades mRNA in prokaryotes and plant chloroplasts. It catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction. It is also involved, along with RNase II, in tRNA processing. The C-terminal region of PNPase contains domains homologous to those in other RNA binding proteins: a KH domain and an S1 domain. The model corresponds to the KH domain.
Pssm-ID: 411803 [Multi-domain] Cd Length: 70 Bit Score: 36.69 E-value: 2.39e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 491036056 240 DMKGRIIGREGRNIRSFEALTGVDVIIDDTpDVVVLSGFDPIRREIAKRALERLIKD 296
Cdd:cd02393 13 DKIGDVIGPGGKTIRAIIEETGAKIDIEDD-GTVTIFATDKESAEAAKAMIEDIVAE 68
|
|
| KH-I |
cd00105 |
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ... |
233-291 |
2.61e-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: 2.61e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491036056 233 VVNLPSDDMkGRIIGREGRNIRSFEALTGVDVIIDD-----TPDVVVLSGfDPIRREIAKRALE 291
Cdd:cd00105 2 EIEVPSELV-GLIIGKGGSTIKEIEEETGARIQIPKegegsGERVVTITG-TPEAVEKAKELIE 63
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
32-207 |
5.71e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.53 E-value: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 32 ETQAQNAAHDAKHILADAESKAKAVEADLAsQKEAMKKAAADAKKEKILEAQEEIhhyRERVDNELNERRQEVSRQENRL 111
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELELEEA-QAEEYELLAELARLEQDIARLEER---RRELEERLEELEEELAELEEEL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 112 LQREDAIDHKDSLLDQKDSQLTQKENQIKKLQAQVLEKENRADQLVTEREKKLYEVAELNQEDAKK----IVLDKLSDQL 187
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELaaqlEELEEAEEAL 412
|
170 180
....*....|....*....|
gi 491036056 188 VKERAEMIEESNQLAKAKAD 207
Cdd:COG1196 413 LERLERLEEELEELEEALAE 432
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
81-208 |
6.78e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 39.32 E-value: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 81 EAQEEIHHYRERVDNELNERRQEVSRQENRLLQREDAIDHKDSLLDQKDSQLTQKENQiKKLQAQVLEKEN-RADQLVTE 159
Cdd:pfam05483 219 EDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEK-TKLQDENLKELIeKKDHLTKE 297
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 491036056 160 RE------KKLYEVAELNQEDAKkiVLDKLSDQLVKERAEMIEESNqlaKAKADH 208
Cdd:pfam05483 298 LEdikmslQRSMSTQKALEEDLQ--IATKTICQLTEEKEAQMEELN---KAKAAH 347
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
122-205 |
7.61e-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: 38.42 E-value: 7.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 122 DSLLdQKDSQLTQKENQIKKLQ--AQVLEKENradQLVTEREKKLYEVAElNQEDAKKIVLDKLSDQLVKERAEMIEESN 199
Cdd:pfam02841 190 EAIL-QTDQALTAKEKAIEAERakAEAAEAEQ---ELLREKQKEEEQMME-AQERSYQEHVKQLIEKMEAEREQLLAEQE 264
|
....*.
gi 491036056 200 QLAKAK 205
Cdd:pfam02841 265 RMLEHK 270
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
34-193 |
8.02e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.98 E-value: 8.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 34 QAQNAAHDAKHILADAESKAKAVEADLASQKEAMKKAAADAKKEkilEAQEEIHHYRERVDnELNERRQEVSRQENRLLQ 113
Cdd:COG4717 92 ELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELE---ALEAELAELPERLE-ELEERLEELRELEEELEE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 114 REDAIDHKDSLLDQKDSQLT-QKENQIKKLQAQVLEKENRADQLVTEREKKLYEVAELNQEdakkivLDKLSDQLVKERA 192
Cdd:COG4717 168 LEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE------LEQLENELEAAAL 241
|
.
gi 491036056 193 E 193
Cdd:COG4717 242 E 242
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
83-201 |
9.13e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 38.84 E-value: 9.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491036056 83 QEEIHHYRERVDNELNERRQEVSRQENRL--LQREDAIDHKDSLLDQKDSQLTQKENQIKKLQAQVLEKENRADQLVTER 160
Cdd:COG3206 170 REEARKALEFLEEQLPELRKELEEAEAALeeFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 491036056 161 EKKLYEVAELNQEDakkiVLDKLSDQLVKERAEMIEESNQL 201
Cdd:COG3206 250 GSGPDALPELLQSP----VIQQLRAQLAELEAELAELSARY 286
|
|
| |
