|
Name |
Accession |
Description |
Interval |
E-value |
| RNase_Y |
TIGR03319 |
ribonuclease Y; Members of this family are RNase Y, an endoribonuclease. The member from ... |
11-524 |
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: 802.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 11 ILLAIIGLIVGLGLGVYVTKSRHEKEINGAQNSAAGIIESAKKEAETLKKEALLEAKEENQKYRSEIESELKESKLDLKS 90
Cdd:TIGR03319 1 ILLALVALIVGLIIGYLLRKRIAEKKLGSAEELAKRIIEEAKKEAETLKKEALLEAKEEVHKLRAELERELKERRNELQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 91 QENRLLQREQVLDRKDDSLEKRERSLEDKEGRLSEKQQLIDEREKEVENLIDGQQKELERIAALSRDEAKELIMKSTEEE 170
Cdd:TIGR03319 81 LERRLLQREETLDRKMESLDKKEENLEKKEKELSNKEKNLDEKEEELEELIAEQREELERISGLTQEEAKEILLEEVEEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 171 LNHELTIMVKESEQRAKEEADRKAKNLLSLAIQRCAADQVSETTVSVVSLPNDEMKGRIIGREGRNIRTLETLTGIDLII 250
Cdd:TIGR03319 161 ARHEAAKLIKEIEEEAKEEADKKAKEILATAIQRYAGDHVAETTVSVVNLPNDEMKGRIIGREGRNIRALETLTGVDLII 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 251 DDTPEAVVLSGFDPIRREIARMTLEKLIQDGRIHPARIEEMVEKSRKEMDEHIREYGEQAAFEVGAHTLHPDLIKILGRL 330
Cdd:TIGR03319 241 DDTPEAVILSGFDPVRREIARMALEKLIQDGRIHPARIEEMVEKATKEVDNAIREEGEQAAFDLGVHGLHPELIKLLGRL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 331 RFRTSYGQNVLNHSIEVAKLTGVLAAELGEDIQLAKRAGLLHDIGKALDHEIEGSHVEIGAELAAKYKENGVVINAIASH 410
Cdd:TIGR03319 321 KFRTSYGQNVLQHSIEVAHLAGIMAAELGEDVKLAKRAGLLHDIGKAVDHEVEGSHVEIGAELAKKYKESPEVVNAIAAH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 411 HGDVEATSVISVLVAAADALSAARPGARSESLENYIRRLQNLENIANGFKGVDSSFAVQAGREVRVMVKPEEISDLDAVR 490
Cdd:TIGR03319 401 HGDVEPTSIEAVLVAAADALSAARPGARRESLENYIKRLEKLEEIANSFEGVEKSYAIQAGREIRVMVKPEKISDDQAVV 480
|
490 500 510
....*....|....*....|....*....|....
gi 491374999 491 LVRDIRKKIEDDLDYPGHIKVTVIRETRATDYAK 524
Cdd:TIGR03319 481 LARDIAKKIEEELEYPGQIKVTVIRETRAVEYAK 514
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
8-524 |
0e+00 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 798.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 8 LLYILLAIIGLIVGLGLGVYVTKSRHEKEINGAQNSAAGIIESAKKEAETLKKEALLEAKEENQKYRSEIESELKESKLD 87
Cdd:PRK12704 4 LIIILIALVALVVGAVIGYFVRKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 88 LKSQENRLLQREQVLDRKDDSLEKRERSLEDKEGRLSEKQQLIDEREKEVENLIDGQQKELERIAALSRDEAKELIMKST 167
Cdd:PRK12704 84 LQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEILLEKV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 168 EEELNHELTIMVKESEQRAKEEADRKAKNLLSLAIQRCAADQVSETTVSVVSLPNDEMKGRIIGREGRNIRTLETLTGID 247
Cdd:PRK12704 164 EEEARHEAAVLIKEIEEEAKEEADKKAKEILAQAIQRCAADHVAETTVSVVNLPNDEMKGRIIGREGRNIRALETLTGVD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 248 LIIDDTPEAVVLSGFDPIRREIARMTLEKLIQDGRIHPARIEEMVEKSRKEMDEHIREYGEQAAFEVGAHTLHPDLIKIL 327
Cdd:PRK12704 244 LIIDDTPEAVILSGFDPIRREIARLALEKLVQDGRIHPARIEEMVEKARKEVDEEIREEGEQAVFELGIHGLHPELIKLL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 328 GRLRFRTSYGQNVLNHSIEVAKLTGVLAAELGEDIQLAKRAGLLHDIGKALDHEIEGSHVEIGAELAAKYKENGVVINAI 407
Cdd:PRK12704 324 GRLKYRTSYGQNVLQHSIEVAHLAGLMAAELGLDVKLAKRAGLLHDIGKALDHEVEGSHVEIGAELAKKYKESPVVINAI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 408 ASHHGDVEATSVISVLVAAADALSAARPGARSESLENYIRRLQNLENIANGFKGVDSSFAVQAGREVRVMVKPEEISDLD 487
Cdd:PRK12704 404 AAHHGDEEPTSIEAVLVAAADAISAARPGARRETLENYIKRLEKLEEIANSFEGVEKAYAIQAGREIRVIVKPDKVDDLQ 483
|
490 500 510
....*....|....*....|....*....|....*..
gi 491374999 488 AVRLVRDIRKKIEDDLDYPGHIKVTVIRETRATDYAK 524
Cdd:PRK12704 484 AVRLARDIAKKIEEELQYPGQIKVTVIRETRAVEYAK 520
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
8-524 |
0e+00 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 628.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 8 LLYILLAIIGLIVG-LGLGVYVTKSRHEKEI-------------NGAQNSAAGIIESAKKEAETLKKEALLEAKEENQKY 73
Cdd:PRK00106 5 IILVVSALIGLVIGyVLISIKMKSAKEAAELtllnaeqeavnlrGKAERDAEHIKKTAKRESKALKKELLLEAKEEARKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 74 RSEIESELKESKLDLKSQENRLLQREQVLDRKDDSLEKRERSLEDKEGRLSEKQQLIDEREKEVENLIDGQQKELERIAA 153
Cdd:PRK00106 85 REEIEQEFKSERQELKQIESRLTERATSLDRKDENLSSKEKTLESKEQSLTDKSKHIDEREEQVEKLEEQKKAELERVAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 154 LSRDEAKELIMKSTEEELNHELTIMVKESEQRAKEEADRKAKNLLSLAIQRCAADQVSETTVSVVSLPNDEMKGRIIGRE 233
Cdd:PRK00106 165 LSQAEAREIILAETENKLTHEIATRIREAEREVKDRSDKMAKDLLAQAMQRLAGEYVTEQTITTVHLPDDNMKGRIIGRE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 234 GRNIRTLETLTGIDLIIDDTPEAVVLSGFDPIRREIARMTLEKLIQDGRIHPARIEEMVEKSRKEMDEHIREYGEQAAFE 313
Cdd:PRK00106 245 GRNIRTLESLTGIDVIIDDTPEVVVLSGFDPIRREIARMTLESLIKDGRIHPARIEELVEKNRLEMDNRIREYGEAAAYE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 314 VGAHTLHPDLIKILGRLRFRTSYGQNVLNHSIEVAKLTGVLAAELGEDIQLAKRAGLLHDIGKALDHEIEGSHVEIGAEL 393
Cdd:PRK00106 325 IGAPNLHPDLIKIMGRLQFRTSYGQNVLRHSVEVGKLAGILAGELGENVALARRAGFLHDMGKAIDREVEGSHVEIGMEF 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 394 AAKYKENGVVINAIASHHGDVEATSVISVLVAAADALSAARPGARSESLENYIRRLQNLENIANGFKGVDSSFAVQAGRE 473
Cdd:PRK00106 405 ARKYKEHPVVVNTIASHHGDVEPESVIAVIVAAADALSSARPGARNESMENYIKRLRDLEEIANSFDGVQNSFALQAGRE 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 491374999 474 VRVMVKPEEISDLDAVRLVRDIRKKIEDDLDYPGHIKVTVIRETRATDYAK 524
Cdd:PRK00106 485 IRIMVQPEKISDDQVTILAHKVREKIENNLDYPGNIKVTVIRELRAVDYAK 535
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
5-524 |
0e+00 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 531.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 5 SLELLYILLAIIGLIVGLGLGVYVTKSRHEKEingaqnSAAGIIESAKKEAETLKKEALLEAKEENQKYRSEIESELKES 84
Cdd:PRK12705 2 AMSILLVILLLLIGLLLGVLVVLLKKRQRLAK------EAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 85 KLDLKSQENRLLQREQVLDRKDDSLEKRERSLEDKEGRLSEKQQLIDEREKEVENlidgqqkELERIAALSRDEAKELIM 164
Cdd:PRK12705 76 REELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSARELELEELEKQLDN-------ELYRVAGLTPEQARKLLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 165 KSTEEELNHELTIMVKESEQRAKEEADRKAKNLLSLAIQRCAADQVSETTVSVVSLPNDEMKGRIIGREGRNIRTLETLT 244
Cdd:PRK12705 149 KLLDAELEEEKAQRVKKIEEEADLEAERKAQNILAQAMQRIASETASDLSVSVVPIPSDAMKGRIIGREGRNIRAFEGLT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 245 GIDLIIDDTPEAVVLSGFDPIRREIARMTLEKLIQDGRIHPARIEEMVEKSRKEMDEHIREYGEQAAFEVGAHTLHPDLI 324
Cdd:PRK12705 229 GVDLIIDDTPEAVVISSFNPIRREIARLTLEKLLADGRIHPARIEEYVQKANEEFKQKIYEIGEEVLEELGIFDLKPGLV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 325 KILGRLRFRTSYGQNVLNHSIEVAKLTGVLAAELGEDIQLAKRAGLLHDIGKALDHEIEGSHVEIGAELAAKYKENGVVI 404
Cdd:PRK12705 309 RLLGRLYFRTSYGQNVLSHSLEVAHLAGIIAAEIGLDPALAKRAGLLHDIGKSIDRESDGNHVEIGAELARKFNEPDEVI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 405 NAIASHHGDVEATSVISVLVAAADALSAARPGARSESLENYIRRLQNLENIANGFKGVDSSFAVQAGREVRVMVKPEEIS 484
Cdd:PRK12705 389 NAIASHHNKVNPETVYSVLVQIADALSAARPGARRESLDEYVQRLEELEQIAESFPGVEKAYAIQAGRELRVIVEPEKVS 468
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 491374999 485 DLDAVRLVRDIRKKIEDDLDYPGHIKVTVIRETRATDYAK 524
Cdd:PRK12705 469 DAQATLLARDIAKKIENDLTYPGPIKVTLIRETRAVEYAR 508
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
9-209 |
1.11e-79 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 247.49 E-value: 1.11e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 9 LYILLAIIGLIVGLGLGVYVTKSRHEKEINGAQNSAAGIIESAKKEAETLKKEALLEAKEENQKYRSEIESELKESKLDL 88
Cdd:pfam12072 1 LIIILAIIALVVGFVVGYLVRKSIAEAKIGSAEELAKRIIEEAKKEAETKKKEALLEAKEEIHKLRAEAERELKERRNEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 89 KSQENRLLQREQVLDRKDDSLEKRERSLEDKEGRLSEKQQLIDEREKEVENLIDGQQKELERIAALSRDEAKELIMKSTE 168
Cdd:pfam12072 81 QRQERRLLQKEETLDRKDESLEKKEESLEKKEKELEAQQQQLEEKEEELEELIEEQRQELERISGLTSEEAKEILLDEVE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491374999 169 EELNHELTIMVKESEQRAKEEADRKAKNLLSLAIQRCAADQ 209
Cdd:pfam12072 161 EELRHEAAVMIKEIEEEAKEEADKKAKEIIALAIQRCAADH 201
|
|
| KH-I_RNaseY |
cd22431 |
type I K homology (KH) RNA-binding domain found in ribonuclease Y (RNase Y) and similar ... |
212-290 |
1.09e-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: 157.36 E-value: 1.09e-46
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491374999 212 ETTVSVVSLPNDEMKGRIIGREGRNIRTLETLTGIDLIIDDTPEAVVLSGFDPIRREIARMTLEKLIQDGRIHPARIEE 290
Cdd:cd22431 1 ERTVSTVNLPNDEMKGRIIGREGRNIRAFEAATGVDLIIDDTPEAVILSGFDPVRREVARRTLEKLVEDGRIHPARIEE 79
|
|
| RnaY |
COG1418 |
HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal ... |
321-518 |
3.11e-37 |
|
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: 135.80 E-value: 3.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 321 PDLIKILgrLRFRTSYGQNVLNHSIEVAKLTGVLAAELGEDIQLAKRAGLLHDIGKALDHEIEGSHVEIGAELAAKYK-- 398
Cdd:COG1418 2 PELIKLV--KYLRTSYGQHDLQHSLRVAKLAGLIAAEEGADVEVAKRAALLHDIGKAKDHEVEGSHAEIGAELARKYLes 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 399 ------ENGVVINAIASHHGDV--EATSVISVLVaaadalsaarpgarseslenyirrlQ---NLENIanGFKGVDSSFA 467
Cdd:COG1418 80 lgfpeeEIEAVVHAIEAHSFSGgiEPESLEAKIV-------------------------QdadRLDAL--GAIGVARAFA 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491374999 468 V--QAGREVR---------VMVKPEEISDLDAVRLVRDIRKKIEDDL-DYPghikVTVIRETR 518
Cdd:COG1418 133 IggQAGRELRdpedtainhFYEKLLKLKDLMATELARDIAKKREEFMeEFP----VTVIRETR 191
|
|
| Krr1 |
COG1094 |
rRNA processing protein Krr1/Pno1, contains KH domain [Translation, ribosomal structure and ... |
149-306 |
8.33e-32 |
|
rRNA processing protein Krr1/Pno1, contains KH domain [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440711 [Multi-domain] Cd Length: 177 Bit Score: 120.70 E-value: 8.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 149 ERIAALSRDEAKelIMKSTEEELNHELTIMVKESEQRAKEEADR----KAKNLLSLAIQRCAADQVS-----ETTVSVVS 219
Cdd:COG1094 9 DRIGVLIGKGGE--TKKEIEEKTGVKLDIDSETGEVTIEPGEDPlaalKARDIVKAIGRGFSPEKALrllddDYMLEVID 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 220 LPN--------DEMKGRIIGREGRNIRTLETLTGIDLIIDDTPEAvVLSGFDPIrrEIARMTLEKLIqDGRIHPArIEEM 291
Cdd:COG1094 87 LPDvgkspnalDRIKGRIIGREGRTRRIIEELTGVDISIYGKTVA-IIGDFDQV--EIAREAIEMLI-DGRIHPT-VYEF 161
|
170
....*....|....*
gi 491374999 292 VEKSRKEMDEHIREY 306
Cdd:COG1094 162 LEKARRELKRRRLEL 176
|
|
| HDIG |
TIGR00277 |
HDIG domain; This domain is found in a few known nucleotidyltransferes and in a large number ... |
336-413 |
2.99e-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: 98.95 E-value: 2.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 336 YGQNVLNHSIEVAKLTGVLAAELGEDIQLAKRAGLLHDIGKALDHE--IEGSHVEIGAELAAKYKENGVVINAIASHHGD 413
Cdd:TIGR00277 1 YGQNVLQHSLEVAKLAEALARELGLDVELARRGALLHDIGKPITREgvIFESHVVVGAEIARKYGEPLEVIDIIAEHHGK 80
|
|
| HD |
pfam01966 |
HD domain; HD domains are metal dependent phosphohydrolases. |
340-413 |
3.37e-12 |
|
HD domain; HD domains are metal dependent phosphohydrolases.
Pssm-ID: 460398 [Multi-domain] Cd Length: 110 Bit Score: 63.02 E-value: 3.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 340 VLNHSIEVAKLTGVLAAELGE-DIQLAKRAGLLHDIGKAL------DHEIEGSHVEIGAELAAKYKEN---GVVINAIAS 409
Cdd:pfam01966 1 RLEHSLRVALLARELAEELGElDRELLLLAALLHDIGKGPfgdekpEFEIFLGHAVVGAEILRELEKRlglEDVLKLILE 80
|
....
gi 491374999 410 HHGD 413
Cdd:pfam01966 81 HHES 84
|
|
| HDc |
smart00471 |
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ... |
336-412 |
4.76e-10 |
|
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: 57.31 E-value: 4.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 336 YGQNVLNHSIEVAKLTGVLAAELG-EDIQLAKRAGLLHDIGKALDH-------EIEGSHVEIGAELAAKYKENGVVIN-- 405
Cdd:smart00471 1 SDYHVFEHSLRVAQLAAALAEELGlLDIELLLLAALLHDIGKPGTPdsflvktSVLEDHHFIGAEILLEEEEPRILEEil 80
|
....*....
gi 491374999 406 --AIASHHG 412
Cdd:smart00471 81 rtAILSHHE 89
|
|
| HDGYP |
COG2206 |
HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal ... |
200-411 |
1.93e-09 |
|
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: 59.22 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 200 LAIQRCAADQVSETTVSVVSLPNDEMKGRIIGREGRNIRTLETLTGIDLIIDDTPEAVVLSGFDPIRREIARMTLEKLIQ 279
Cdd:COG2206 4 LLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLLLLLLALLALLLLLLLLLALLALLLALLALLLLLLLLLLLLSLLLAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 280 DGRIHPARIEEMVEKSRKEMDEHIREYGEQAAFEV--GAHTLHPDLIK-ILGRLRFRTSYgqnVLNHSIEVAKLTGVLAA 356
Cdd:COG2206 84 LLLAELLLLLAALESLLAELFEELRLGLLEELKKLveELDELLPDALLaLLAALDAKDPY---TYGHSVRVAVLALALAR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491374999 357 ELG---EDIQLAKRAGLLHDIGK-ALDHEI---EG-----------SHVEIGAELAAKYKENGVVINAIASHH 411
Cdd:COG2206 161 ELGlseEELEDLGLAALLHDIGKiGIPDEIlnkPGkltdeefeiikKHPEYGYEILKKLPGLSEVAEIVLQHH 233
|
|
| HDc |
cd00077 |
Metal dependent phosphohydrolases with conserved 'HD' motif |
338-412 |
6.30e-08 |
|
Metal dependent phosphohydrolases with conserved 'HD' motif
Pssm-ID: 238032 [Multi-domain] Cd Length: 145 Bit Score: 51.96 E-value: 6.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 338 QNVLNHSIEVAKLTGVLAAELG---EDIQLAKRAGLLHDIGKALD--------HEIEGSHVEIGAELAAKYKENG----- 401
Cdd:cd00077 1 EHRFEHSLRVAQLARRLAEELGlseEDIELLRLAALLHDIGKPGTpdaiteeeSELEKDHAIVGAEILRELLLEEvikli 80
|
90
....*....|...
gi 491374999 402 --VVINAIASHHG 412
Cdd:cd00077 81 deLILAVDASHHE 93
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
49-204 |
1.03e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 49 ESAKKEAETLKKEALLEAKEENQKYRSEIESELKESKLDLKSQENRLLQREQVLDRKDDSLEKRERSLEDKEGRLSEKQQ 128
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491374999 129 LIDEREKEVENLIDGQQKELERIAALSRDEAKELimKSTEEELNHELTIMVKESEQRAKEEADRKAKNLLSLAIQR 204
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEEL--EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
52-209 |
6.29e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 6.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 52 KKEAETLKKEALLEAKEENQKYRSEIESELKESKLDLKSQENRLLQREQVLDRKDDSLEKRERSLEDKEGRLSEKQQLID 131
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 132 EREKEVENLIDGQQKELERIAAL--SRDEAKELIMKSTEEELNHELTIMVKESEQRAKEEADRKAKNLLSLAIQRCAADQ 209
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELeeELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
|
| PgpH |
COG1480 |
Cyclic di-AMP-specific phosphodiesterase PgpH, HD superfamily [Signal transduction mechanisms]; ... |
342-421 |
1.47e-05 |
|
Cyclic di-AMP-specific phosphodiesterase PgpH, HD superfamily [Signal transduction mechanisms];
Pssm-ID: 441089 [Multi-domain] Cd Length: 692 Bit Score: 47.91 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 342 NHSIEVAKLTGVLAAELGEDIQLAKRAGLLHDIGKALD--------------HE---------IEGSHVEIGAELAAKYK 398
Cdd:COG1480 480 HHSLMVANLAEAAAEAIGANPLLARVGAYYHDIGKMKRplyfienqmggenpHDklspslsalIIISHVKDGVELARKYK 559
|
90 100
....*....|....*....|...
gi 491374999 399 ENGVVINAIASHHGdveaTSVIS 421
Cdd:COG1480 560 LPKEIIDFIRQHHG----TTLVK 578
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
42-203 |
5.73e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.78 E-value: 5.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 42 NSAAGIIESAKKEAETLKKEALLEAKEENQKYRSEIESELKESKLDLKSQENRLLQREQVLDRKDDSLEKRERSLEDKEG 121
Cdd:TIGR04523 277 EQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 122 RLSEKQQLIDEREKEVENLIDGQQKELERIAAL--SRDEAKELIMKSTEEELNHELTIMVKESEqraKEEADRKAKNLLS 199
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLesQINDLESKIQNQEKLNQQKDEQIKKLQQE---KELLEKEIERLKE 433
|
....
gi 491374999 200 LAIQ 203
Cdd:TIGR04523 434 TIIK 437
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
30-91 |
6.73e-05 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 42.81 E-value: 6.73e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491374999 30 KSRHEKEINGAQNSAAGIIESAKKEAETLKKEALLEAKEENQKY----RSEIESELKESKLDLKSQ 91
Cdd:cd06503 53 LAEYEEKLAEARAEAQEIIEEARKEAEKIKEEILAEAKEEAERIleqaKAEIEQEKEKALAELRKE 118
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
30-257 |
7.03e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 45.81 E-value: 7.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 30 KSRHEKEINGAQNSAAGIIESAKKEAETlKKEALLEAKEENQKY-RSEIESELKESKLDLKSQENRLLQREQVLDRKDDS 108
Cdd:TIGR01612 702 KSKIDKEYDKIQNMETATVELHLSNIEN-KKNELLDIIVEIKKHiHGEINKDLNKILEDFKNKEKELSNKINDYAKEKDE 780
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 109 LEKRERSLEDKEGRLSEKQQLIDEREKEVENLIDgQQKELERIAALSRDEAKELI--MKSTEEELNHELTIMVKeSEQRA 186
Cdd:TIGR01612 781 LNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYD-KSKEYIKTISIKEDEIFKIIneMKFMKDDFLNKVDKFIN-FENNC 858
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491374999 187 KEEADRKAKNLLSLAIQrcAADQVSETTVSVVSLPNDEMKGRI------IGREGRNIRTLETLTGIDLIIDDTPEAV 257
Cdd:TIGR01612 859 KEKIDSEHEQFAELTNK--IKAEISDDKLNDYEKKFNDSKSLIneinksIEEEYQNINTLKKVDEYIKICENTKESI 933
|
|
| Cas3''_I |
cd09641 |
CRISPR/Cas system-associated protein Cas3''; CRISPR (Clustered Regularly Interspaced Short ... |
343-413 |
1.06e-04 |
|
CRISPR/Cas system-associated protein Cas3''; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; HD-like nuclease, specifically digesting double-stranded oligonucleotides and preferably cleaving at G:C pairs; signature gene for Type I
Pssm-ID: 193608 [Multi-domain] Cd Length: 200 Bit Score: 43.42 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 343 HSIEVAKLTGVLAAELGEDI--------QLAKRAGLLHDIGKA----------------------LDHEIEGSHV--EIG 390
Cdd:cd09641 12 HLLDVAAWDAELAEEFARKLglelglsrELLALAGLLHDLGKAtpafqkylrggkealregkrkeVRHSLLGALLlyELL 91
|
90 100
....*....|....*....|...
gi 491374999 391 AELAAKYKENGVVINAIASHHGD 413
Cdd:cd09641 92 KELGLDEELALLLAYAIAGHHGG 114
|
|
| PRK13763 |
PRK13763 |
putative RNA-processing protein; Provisional |
225-299 |
1.16e-04 |
|
putative RNA-processing protein; Provisional
Pssm-ID: 237494 [Multi-domain] Cd Length: 180 Bit Score: 42.93 E-value: 1.16e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491374999 225 MKGRIIGREGRNIRTLETLTGIDLIIDDTpeAVVLSGfDPIRREIARMTLEKLIqDGRIHpARIEEMVEKSRKEM 299
Cdd:PRK13763 105 IKGRIIGEGGKTRRIIEELTGVDISVYGK--TVAIIG-DPEQVEIAREAIEMLI-EGAPH-GTVYKFLERKKREL 174
|
|
| nadD |
PRK07152 |
nicotinate-nucleotide adenylyltransferase; |
341-410 |
1.78e-04 |
|
nicotinate-nucleotide adenylyltransferase;
Pssm-ID: 235947 [Multi-domain] Cd Length: 342 Bit Score: 43.78 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 341 LNHSIEVAKLTGVLAAELGEDIQLAKRAGLLHDIGKALD-----------------------HEIEGSHVeigaeLAAKY 397
Cdd:PRK07152 198 YKHCLRVAQLAAELAKKNNLDPKKAYYAGLYHDITKEWDeekhrkflkkylkdvknlpwyvlHQYVGALW-----LKHVY 272
|
90
....*....|....
gi 491374999 398 K-ENGVVINAIASH 410
Cdd:PRK07152 273 GiDDEEILNAIRNH 286
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
48-383 |
1.97e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 48 IESAKKEAETLKKE--ALLEAKEENQKYRSEIESELKESKLDLKSQENRLLQREQVLDRKDDSLEKRERSLEDKEGRLSE 125
Cdd:COG4372 33 LRKALFELDKLQEEleQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 126 KQQLIDEREKEVENLIDGQQKELERIAALSRD----EAKELIMKSTEEELNHELTIMVKESEQRAKEEADRKAKNLLSla 201
Cdd:COG4372 113 LQEELEELQKERQDLEQQRKQLEAQIAELQSEiaerEEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLK-- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 202 iqrcAADQVSETTVSVVSLPNDEMKGRIIGREGRNIRTLETLTGIDLIIDDTPEAVVLSGFDPIRREIARMTLEKLIQDG 281
Cdd:COG4372 191 ----EANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 282 RIHPARIEEMVEKSRKEMDEHIREYGEQAAFEVGAHTLHPDLIKILGRLRFRTSYGQNVLNHSIEVAKLTGVLAAELGED 361
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLL 346
|
330 340
....*....|....*....|..
gi 491374999 362 IQLAKRAGLLHDIGKALDHEIE 383
Cdd:COG4372 347 LVGLLDNDVLELLSKGAEAGVA 368
|
|
| arCOG04150 |
TIGR03665 |
arCOG04150 universal archaeal KH domain protein; This family of proteins is universal among ... |
226-284 |
3.51e-04 |
|
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: 41.40 E-value: 3.51e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 491374999 226 KGRIIGREGRNIRTLETLTGIDLIIDDtpEAVVLSGfDPIRREIARMTLEKLIqDGRIH 284
Cdd:TIGR03665 100 KGRIIGEGGKTRRIIEELTGVSISVYG--KTVGIIG-DPEQVQIAREAIEMLI-EGAPH 154
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
26-188 |
3.86e-04 |
|
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: 43.19 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 26 VYVTKSRHEKEiNGAQNSAAGIIESAKKEAETLKKEAL--------LEAKEENQKyRSEIESELKESKLDLKSQENRLLQ 97
Cdd:pfam17380 420 VEMEQIRAEQE-EARQREVRRLEEERAREMERVRLEEQerqqqverLRQQEEERK-RKKLELEKEKRDRKRAEEQRRKIL 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 98 REQVLDRKDDSLE-KRERSLEDKEgrLSEKQQLI-DEREKEVENLIDGQQKELERiaalsRDEAKELIMKSTEE------ 169
Cdd:pfam17380 498 EKELEERKQAMIEeERKRKLLEKE--MEERQKAIyEEERRREAEEERRKQQEMEE-----RRRIQEQMRKATEErsrlea 570
|
170 180
....*....|....*....|
gi 491374999 170 -ELNHELTIMVKESEQRAKE 188
Cdd:pfam17380 571 mEREREMMRQIVESEKARAE 590
|
|
| YqeK |
COG1713 |
Diadenosine tetraphosphatase YqeK or a related HD superfamily phosphohydrolase [Signal ... |
341-410 |
3.99e-04 |
|
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: 41.26 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 341 LNHSIEVAKLTGVLAAELGEDIQLAKRAGLLHDIGKALDHE-----IEGSHVEI---------------GAELAAkyKEN 400
Cdd:COG1713 19 YEHTLGVAETAVELAERYGVDVEKAELAGLLHDYAKELPPEellelAKEYGLDLdeleeynpellhgpvGAYLAK--EEF 96
|
90
....*....|....
gi 491374999 401 GV----VINAIASH 410
Cdd:COG1713 97 GItdeeILNAIRYH 110
|
|
| cas3_HD |
TIGR01596 |
CRISPR-associated endonuclease Cas3-HD; CRISPR/Cas systems are widespread, mobile systems for ... |
343-412 |
4.12e-04 |
|
CRISPR-associated endonuclease Cas3-HD; CRISPR/Cas systems are widespread, mobile systems for host defense against invasive elements such as phage. In these systems, Cas3 designates one of the core proteins shared widely by multiple types of CRISPR/Cas system. This model represents an HD-like endonuclease that occurs either separately or as the N-terminal region of Cas3, the helicase-containing CRISPR-associated protein.
Pssm-ID: 273711 [Multi-domain] Cd Length: 176 Bit Score: 41.42 E-value: 4.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 343 HSIEVAKLTGVL-------AAELGEDI-QLAKRAGLLHDIGKA-------------------LDHEIEGSHV--EIGAEL 393
Cdd:TIGR01596 4 HLLDVAAVAEALpalrprlAEKLGLELrELLKLAGLLHDLGKAspafqkklrkaeergdrgeVRHSTLSAALlyDLLEEL 83
|
90
....*....|....*....
gi 491374999 394 AAKYKENGVVINAIASHHG 412
Cdd:TIGR01596 84 GLEEELALLLALAIAGHHG 102
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
49-212 |
4.57e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 49 ESAKKEAETLKKEALlEAKEENQKYRSEIESELKESKLDLKSQENRLLQREQVlDRKDDSLEKRersledkegrlSEKQQ 128
Cdd:PTZ00121 1325 EEAKKKADAAKKKAE-EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA-KKKADAAKKK-----------AEEKK 1391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 129 LIDEREKEVENliDGQQKELERIAALSRDEAKELIMKSTE----EELNHELTIMVKESEQRAKEEADRKAKNLLSLAIQR 204
Cdd:PTZ00121 1392 KADEAKKKAEE--DKKKADELKKAAAAKKKADEAKKKAEEkkkaDEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA 1469
|
....*...
gi 491374999 205 CAADQVSE 212
Cdd:PTZ00121 1470 KKADEAKK 1477
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
49-193 |
5.08e-04 |
|
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: 42.80 E-value: 5.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 49 ESAKKEAETLKKEAL--------------LEAKEENQKYRSEIESELKEskldlksqenRLLQREQVLDRKDDSLEKRER 114
Cdd:pfam17380 356 EERKRELERIRQEEIameisrmrelerlqMERQQKNERVRQELEAARKV----------KILEEERQRKIQQQKVEMEQI 425
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491374999 115 SLEDKEGRLSEKQQLIDEREKEVENLidgQQKELERIAALSRdeakeliMKSTEEELNHELTIMVKESEQRAKEEADRK 193
Cdd:pfam17380 426 RAEQEEARQREVRRLEEERAREMERV---RLEEQERQQQVER-------LRQQEEERKRKKLELEKEKRDRKRAEEQRR 494
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
32-199 |
5.29e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 5.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 32 RHEKEINGAQNSAAGIIESAKKEAETLKKE--------ALLEAKEENQKYRSE----IESELKESKLDLKSQENRLLQRE 99
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEEKKKAEELKKAeeenkikaAEEAKKAEEDKKKAEeakkAEEDEKKAAEALKKEAEEAKKAE 1705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 100 QVLDRKDDSLEKRERSLEDKEGRLSEKQQLIDEREKEVENLIDGQQKELE--RIAALSRDEAK--ELIMKSTEEELNHEl 175
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEkkKIAHLKKEEEKkaEEIRKEKEAVIEEE- 1784
|
170 180
....*....|....*....|....
gi 491374999 176 timVKESEQRAKEEADRKAKNLLS 199
Cdd:PTZ00121 1785 ---LDEEDEKRRMEVDKKIKDIFD 1805
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
35-193 |
6.22e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 6.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 35 KEINGAQNSAAGIIESAKKEAETLKKEALLEAKEENQKYRSEIES----ELKESKLDLKSQENRLLQREQVLDRKDDSLE 110
Cdd:PTZ00121 1623 EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAkkaeEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 111 KRE--RSLEDKEGRLSEK-QQLIDEREKEVENLIDGQQKELERIAALSRDEAKELIMKSTEEELNHELTIMVKESEQRAK 187
Cdd:PTZ00121 1703 KAEelKKKEAEEKKKAEElKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
|
....*.
gi 491374999 188 EEADRK 193
Cdd:PTZ00121 1783 EELDEE 1788
|
|
| HDOD |
COG1639 |
HD-like signal output (HDOD) domain, no enzymatic activity [Signal transduction mechanisms]; |
338-411 |
7.33e-04 |
|
HD-like signal output (HDOD) domain, no enzymatic activity [Signal transduction mechanisms];
Pssm-ID: 441246 [Multi-domain] Cd Length: 244 Bit Score: 41.49 E-value: 7.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 338 QNVLNHSIEVAKLTGVLAAELG----EDIQLAkraGLLHDIGK---------------------------ALDHEIEGSH 386
Cdd:COG1639 103 RRFWRHSLAVAAAARALARRLGlldpEEAFLA---GLLHDIGKlvllslfpeeyaellalaeadglslaeAEREVLGTDH 179
|
90 100
....*....|....*....|....*
gi 491374999 387 VEIGAELAAKYKENGVVINAIASHH 411
Cdd:COG1639 180 AELGAALARKWGLPEELVEAIRYHH 204
|
|
| HDOD |
pfam08668 |
HDOD domain; |
342-411 |
8.28e-04 |
|
HDOD domain;
Pssm-ID: 430141 [Multi-domain] Cd Length: 196 Bit Score: 40.67 E-value: 8.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 342 NHSIEVAKLTGVLAAELG-EDIQLAKRAGLLHDIGK---------------------------ALDHEIEGSHVEIGAEL 393
Cdd:pfam08668 97 EHSLACALAARLLARRLGlDDPEEAFLAGLLHDIGKlillsllpdkyeellekaaeegislleAERELLGTDHAEVGAAL 176
|
90
....*....|....*...
gi 491374999 394 AAKYKENGVVINAIASHH 411
Cdd:pfam08668 177 LERWNLPEELVEAIAYHH 194
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
34-197 |
8.84e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 42.27 E-value: 8.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 34 EKEINGAQNSAAGIIESAKKEAETLKKEALLEAKEENQKYRSEIESELKESKLDLKSQENRLLQREQVLDRKDDSLEKRE 113
Cdd:pfam02463 243 QELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 114 RSLEDKEgrLSEKQQLIDEREKEVENLIDGQQKELERIAALSRDEAKELIMKSTEEELNHELTIMVKESEQRAKEEADRK 193
Cdd:pfam02463 323 KKKAEKE--LKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELK 400
|
....
gi 491374999 194 AKNL 197
Cdd:pfam02463 401 SEEE 404
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
28-193 |
1.55e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 28 VTKSRHEKEINGAQNSAAGIIESAKKEAET-LKKEALLEAKEENQK---YRSEIESELKESKLDLKSQENRLLQREQVLD 103
Cdd:PTZ00121 1589 AEEARIEEVMKLYEEEKKMKAEEAKKAEEAkIKAEELKKAEEEKKKveqLKKKEAEEKKKAEELKKAEEENKIKAAEEAK 1668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 104 RKDDSLEKRE--RSLEDKEGRLSEKQQLIDEREKEVENLIDGQQKELERIAALSRDEAKElimKSTEEELNHELTIMVKE 181
Cdd:PTZ00121 1669 KAEEDKKKAEeaKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEN---KIKAEEAKKEAEEDKKK 1745
|
170
....*....|..
gi 491374999 182 SEQRAKEEADRK 193
Cdd:PTZ00121 1746 AEEAKKDEEEKK 1757
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
48-195 |
1.69e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 48 IESAKKEAETLKKEALLEAKEENQKYRSEIESELKESKLDLKSQENRllqreqvldrKDDSLEKRERSLEDKEGRLSEKQ 127
Cdd:PTZ00121 1232 AEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEAR----------KADELKKAEEKKKADEAKKAEEK 1301
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491374999 128 QLIDEREKEVENliDGQQKELERIAALSRDEAKELIMKSTEEELNHELTIMVKESEQRAKEEADRKAK 195
Cdd:PTZ00121 1302 KKADEAKKKAEE--AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAE 1367
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
49-195 |
1.75e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 49 ESAKKEAETLKKEAllEAKEENQKYRSEIESELKESKLDLKSQENRLLQREQvldrkddslEKRErslEDKEGRLSEKQQ 128
Cdd:PTZ00121 1616 EEAKIKAEELKKAE--EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE---------EAKK---AEEDKKKAEEAK 1681
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491374999 129 LIDEREKEVENLIDGQQKELERIAALSRDEAKElimKSTEEELNHELTIMVKESEQRAKEEADRKAK 195
Cdd:PTZ00121 1682 KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEE---KKKAEELKKAEEENKIKAEEAKKEAEEDKKK 1745
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
48-195 |
1.94e-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: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 48 IESAKKEAETLKKEAlleAKEENQKY-----RSEIESELKESKLDLKSQENRLLQREQVLDRKDDSLEKRERSLEDKEGR 122
Cdd:COG1196 283 LEEAQAEEYELLAEL---ARLEQDIArleerRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491374999 123 LSEKQQLIDEREKEVENLIDGQQKELERIAALSRDEAKElimKSTEEELNHELTIMVKESEQRAKEEADRKAK 195
Cdd:COG1196 360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL---AAQLEELEEAEEALLERLERLEEELEELEEA 429
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
32-197 |
2.25e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.88 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 32 RHEKEINGAQNSAagiiESAKKEAETLKKEALLEAKEENQKYRSEIESELKESKLD-----------LKSQENRLLQREQ 100
Cdd:pfam17380 279 QHQKAVSERQQQE----KFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDrqaaiyaeqerMAMERERELERIR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 101 VLDRKDDSLEKRERSLEDKEGRLSEKQQLIDER--------------------EKEVENLIDGQQKELERIAAlSRDEAK 160
Cdd:pfam17380 355 QEERKRELERIRQEEIAMEISRMRELERLQMERqqknervrqeleaarkvkilEEERQRKIQQQKVEMEQIRA-EQEEAR 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491374999 161 ELIMKSTEEELNHELTIMVKESEQRA-------KEEADRKAKNL 197
Cdd:pfam17380 434 QREVRRLEEERAREMERVRLEEQERQqqverlrQQEEERKRKKL 477
|
|
| Cas10_III |
cd09680 |
CRISPR/Cas system-associated protein Cas10; CRISPR (Clustered Regularly Interspaced Short ... |
368-413 |
2.64e-03 |
|
CRISPR/Cas system-associated protein Cas10; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Multidomain protein with permuted HD nuclease domain, palm domain and Zn-ribbon; signature gene for type III; also known as Csm1 family
Pssm-ID: 187811 [Multi-domain] Cd Length: 650 Bit Score: 40.38 E-value: 2.64e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 491374999 368 AGLLHDIGK----ALDHEIEGSHVEIGAE-LAAKYKENGVVINAIASHHGD 413
Cdd:cd09680 4 GALLHDIGKvvqrAGLGFYSKTHSKFGAEfLKEFSKNKDDLGDCISYHHTK 54
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
34-91 |
2.65e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 38.60 E-value: 2.65e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491374999 34 EKEINGAQNSAAGIIESAKKEAETLKKEALLEAKEENQKY----RSEIESELKESKLDLKSQ 91
Cdd:PRK05759 62 EAQLAEARAEAAEIIEQAKKRAAQIIEEAKAEAEAEAARIkaqaQAEIEQERKRAREELRKQ 123
|
|
| PRK02292 |
PRK02292 |
V-type ATP synthase subunit E; Provisional |
40-174 |
2.68e-03 |
|
V-type ATP synthase subunit E; Provisional
Pssm-ID: 235026 [Multi-domain] Cd Length: 188 Bit Score: 39.21 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 40 AQNSAAGIIESAKKEAETLKKEALLEAKEENQKYRseiESELKESKLDLKsqENRLLQREQVLDRKDDSLEKRERSLEdk 119
Cdd:PRK02292 25 ADEEAEEIIAEAEADAEEILEDREAEAEREIEQLR---EQELSSAKLEAK--RERLNARKEVLEDVRNQVEDEIASLD-- 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 491374999 120 egrlsekqqlIDEREKEVENLIDGQqkELERIAALSRDEAKELIMKSTEEELNHE 174
Cdd:PRK02292 98 ----------GDKREELTKSLLDAA--DADGVRVYSRKDDEDLVKSLLSDYDGLE 140
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
52-290 |
3.15e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 52 KKEAETLKKEALLEAKEENQ--KYRSEIESELKESKLDLKSQENRLLQREQVLD---RKDDSLEKRERSLEDKEGRlsEK 126
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKaeEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAeelKKAEEEKKKVEQLKKKEAE--EK 1646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 127 QQLIDEREKEVENLIdgQQKELERIAALSRDEAKELiMKSTEEELNHELTIMVKESEQRAKEEADRKAKNLLSLAIQRCA 206
Cdd:PTZ00121 1647 KKAEELKKAEEENKI--KAAEEAKKAEEDKKKAEEA-KKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKK 1723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 207 ADQVSETTVSVVSLPNDEMK-----GRIIGREGRNIRTLETLTGIDL-IIDDTPEAVVLSGFDPiRREIARMTLEKLIQD 280
Cdd:PTZ00121 1724 AEEENKIKAEEAKKEAEEDKkkaeeAKKDEEEKKKIAHLKKEEEKKAeEIRKEKEAVIEEELDE-EDEKRRMEVDKKIKD 1802
|
250
....*....|
gi 491374999 281 GRIHPARIEE 290
Cdd:PTZ00121 1803 IFDNFANIIE 1812
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
49-195 |
4.17e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 49 ESAKKEAETLKKEALLEAKEENQKYRSEIESELKESKLdlKSQENRLLQREQvldRKDDSLEKRERSLEDKEGRLSEKQQ 128
Cdd:PTZ00121 1460 EEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKK--KADEAKKAAEAK---KKADEAKKAEEAKKADEAKKAEEAK 1534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 129 LIDEREK--------------------EVENLIDGQQKELERIAALSRDEA--------KELIMKSTEEELNHELTIMVK 180
Cdd:PTZ00121 1535 KADEAKKaeekkkadelkkaeelkkaeEKKKAEEAKKAEEDKNMALRKAEEakkaeearIEEVMKLYEEEKKMKAEEAKK 1614
|
170
....*....|....*
gi 491374999 181 ESEQRAKEEADRKAK 195
Cdd:PTZ00121 1615 AEEAKIKAEELKKAE 1629
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
48-212 |
5.25e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 48 IESAKKEAETLKKEALLEAKEENQKYRSEiesELKESKLDLKSQENRLLQREQvldRKDDSLEKRERSLEDKEGRLSEKQ 127
Cdd:PTZ00121 1304 ADEAKKKAEEAKKADEAKKKAEEAKKKAD---AAKKKAEEAKKAAEAAKAEAE---AAADEAEAAEEKAEAAEKKKEEAK 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 128 QLIDEREKEVENLidGQQKELERIAALSRDEAKELIMKSTEEElnheltimvKESEQRAKEEADRKAKNLLSLAIQRCAA 207
Cdd:PTZ00121 1378 KKADAAKKKAEEK--KKADEAKKKAEEDKKKADELKKAAAAKK---------KADEAKKKAEEKKKADEAKKKAEEAKKA 1446
|
....*
gi 491374999 208 DQVSE 212
Cdd:PTZ00121 1447 DEAKK 1451
|
|
| PRK03007 |
PRK03007 |
deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional |
341-379 |
6.91e-03 |
|
deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional
Pssm-ID: 235098 [Multi-domain] Cd Length: 428 Bit Score: 38.77 E-value: 6.91e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 491374999 341 LNHSIEVAKLTGVLAAELGEDIQLAKRAGLLHDIG---------KALD 379
Cdd:PRK03007 72 LTHSLEVAQIGRGIAAGLGCDPDLVDLAGLAHDIGhppyghngeRALD 119
|
|
| Fibrinogen_BP |
pfam08017 |
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ... |
34-198 |
7.96e-03 |
|
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family includes the fibrinogen receptor, FbsA, which mediates platelet aggregation.
Pssm-ID: 311808 [Multi-domain] Cd Length: 393 Bit Score: 38.69 E-value: 7.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 34 EKEINGAQNSAAG-IIESAKKEAETLKKEALLEAKEENQKYRSEIES-ELKESKLDLKSQENRLLQREQVLDRKD--DSL 109
Cdd:pfam08017 80 ERRQRDAENRSQGnVLERRQRDAENRSQGNVLERRQRDAENKSQGNVlERRQRDAENRSQGNVLERRQRDAENRSqgNVL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 110 EKRERSLEDK-EGRLSEKQQ----------LIDEREKEVENLIDGQQKELERIAALSRDEAKELIMKSTEEELNHELTIM 178
Cdd:pfam08017 160 ERRQRDAENRsQGNVLERRQrdaenksqgnVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVL 239
|
170 180
....*....|....*....|
gi 491374999 179 vkesEQRAKEEADRKAKNLL 198
Cdd:pfam08017 240 ----ERRQRDAENKSQGNVL 255
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
47-199 |
8.65e-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: 38.90 E-value: 8.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 47 IIESAKKEAETLKKEalleaKEENQKYRsEIESELKESKLDLKSQENRLLQREqvldrkddsLEKRERSLEDKEGRLSEK 126
Cdd:TIGR02169 192 IIDEKRQQLERLRRE-----REKAERYQ-ALLKEKREYEGYELLKEKEALERQ---------KEAIERQLASLEEELEKL 256
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491374999 127 QQLIDEREKEVENLIDGQQKELERIAALSRDEA---KELIMKSTEEELNHELTIMVKESEQRAKEEADRKAKNLLS 199
Cdd:TIGR02169 257 TEEISELEKRLEEIEQLLEELNKKIKDLGEEEQlrvKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEID 332
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
47-197 |
8.65e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 38.88 E-value: 8.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 47 IIESAKKEAETLKKEAllEAKEENQKYRSEIES-ELKESKLDLKSQENRLLQREQVLDRKDDSLEKRERSLEDKEGRLSE 125
Cdd:TIGR02168 194 ILNELERQLKSLERQA--EKAERYKELKAELRElELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEE 271
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491374999 126 KQQLIDEREKEvenlIDGQQKELERIAALSRDEAKELIMKSTEEELNHELTIMVKESEQRAKEEADRKAKNL 197
Cdd:TIGR02168 272 LRLEVSELEEE----IEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL 339
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
49-197 |
9.46e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.97 E-value: 9.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491374999 49 ESAKKEAETLKKEALLEAKEENQKYRSEiesELKESKLDLKSQENRLLQREQVldRKDDSLEKRErsledKEGRLSEKQQ 128
Cdd:PTZ00121 1381 DAAKKKAEEKKKADEAKKKAEEDKKKAD---ELKKAAAAKKKADEAKKKAEEK--KKADEAKKKA-----EEAKKADEAK 1450
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491374999 129 LIDEREKEVENLidGQQKELERIAALSRDEAKEliMKSTEEELNHELTIMVKESEQRAKEEADRKAKNL 197
Cdd:PTZ00121 1451 KKAEEAKKAEEA--KKKAEEAKKADEAKKKAEE--AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEA 1515
|
|
| KH |
smart00322 |
K homology RNA-binding domain; |
217-278 |
9.53e-03 |
|
K homology RNA-binding domain;
Pssm-ID: 197652 [Multi-domain] Cd Length: 68 Bit Score: 34.96 E-value: 9.53e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491374999 217 VVSLPNDEMkGRIIGREGRNIRTLETLTG--IDLIIDDTPEAVVLSGFDPIRREIARMTLEKLI 278
Cdd:smart00322 6 EVLIPADKV-GLIIGKGGSTIKKIEEETGvkIDIPGPGSEERVVEITGPPENVEKAAELILEIL 68
|
|
| |
