|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1-419 |
0e+00 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 706.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 1 MTRAVKPRRFAIRPIIYASVLSAGVLLCAFSAHA-DERDQLKSIQADIAAKERAVRQKQQQRASLLAQLKKQEEAISEAT 79
Cdd:PRK11637 9 MTRAVKPRRFAIRPILYASVLSAGVLLCAFSAHAsDNRDQLKSIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAISQAS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 80 RKLRETQNTLNQLNKQIDEMNASIAKLEQQKAAQERSLAAQLDAAFRQGEHTGIQLILSGEESQRGQRLQAYFGYLNQAR 159
Cdd:PRK11637 89 RKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQERLLAAQLDAAFRQGEHTGLQLILSGEESQRGERILAYFGYLNQAR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 160 QETIAQLKQTREEVAMQRAELEEKQSEQQTLLYEQRAQQAKLTQALNERKKTLAGLESSIQQGQQQLSELRANESRLRNS 239
Cdd:PRK11637 169 QETIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELRANESRLRDS 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 240 IARAEAAAKARAEREAREAQAVRDRQKEATRKGTTYKPTESEKSLMSRTGGLGAPRGQAFWPVRGPTLHRYGEQLQGELR 319
Cdd:PRK11637 249 IARAEREAKARAEREAREAARVRDKQKQAKRKGSTYKPTESERSLMSRTGGLGRPRGQAFWPVRGPTLHRFGEQLQGELR 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 320 WKGMVIGASEGTEVKAIADGRVILADWLQGYGLVVVVEHGKGDMSLYGYNQSALVSVGSQVRAGQPIALVGSSGGQGRPS 399
Cdd:PRK11637 329 WKGMVIGASEGTEVKAIADGRVLLADWLQGYGLVVVVEHGKGDMSLYGYNQSALVSVGAQVRAGQPIALVGSSGGQGRPS 408
|
410 420
....*....|....*....|
gi 446118401 400 LYFEIRRQGQAVNPQPWLGR 419
Cdd:PRK11637 409 LYFEIRRQGQAVNPQPWLGR 428
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
12-419 |
1.19e-94 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 288.97 E-value: 1.19e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 12 IRPIIYASVLSAGVLLCAFSAHADERDQLKSIQADIAAKERAVRQKQQQRASLLAQLKKQEEAISEATRKLRETQNTLNQ 91
Cdd:COG4942 1 MRKLLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 92 LNKQIDEMNASIAKLEQQKAAQERSLAAQLDAAFRQGEHTGIQLILSGEESQRGQRLQAYFGYLNQARQETIAQLKQTRE 171
Cdd:COG4942 81 LEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 172 EVAMQRAELEEKQSEQQTLLYEQRAQQAKLTQALNERKKTLAGLESSIQQGQQQLSELRANESRLRNSIARAEAAakara 251
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE----- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 252 ereareaqavrdrqkeatrkgttykptESEKSLMSRTGGLGAPRGQAFWPVRGPTLHRYGEQLQGELRWKGMVIGASEGT 331
Cdd:COG4942 236 ---------------------------AAAAAERTPAAGFAALKGKLPWPVSGRVVRRFGERDGGGGRNKGIDIAAPPGA 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 332 EVKAIADGRVILADWLQGYGLVVVVEHGKGDMSLYGYNQSALVSVGSQVRAGQPIALVGSSGGQGRPSLYFEIRRQGQAV 411
Cdd:COG4942 289 PVRAVADGTVVYAGWLRGYGNLVIIDHGGGYLTLYAHLSSLLVKVGQRVKAGQPIGTVGSSGGQGGPTLYFELRKNGKPV 368
|
....*...
gi 446118401 412 NPQPWLGR 419
Cdd:COG4942 369 DPLPWLAK 376
|
|
| NlpD |
COG0739 |
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ... |
230-417 |
3.00e-41 |
|
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440502 [Multi-domain] Cd Length: 196 Bit Score: 144.73 E-value: 3.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 230 RANESRLRNSIARAEAAAKARAEREAREAQAVRDRQKEATRKGTTYKPTESEKSLMSRTGGLGAPRGQAFWPVRGPTLHR 309
Cdd:COG0739 3 LALALAAALLALALLASAAGAAAAVAAAAAAAAAAAALAAAALAAAVSAAASAAAAAAAAAAAIALGSGAWPVKGRITSG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 310 YGEQLQGELRW----KGMVIGASEGTEVKAIADGRVILADWLQGYGLVVVVEHGKGDMSLYGYNQSALVSVGSQVRAGQP 385
Cdd:COG0739 83 FGYRRHPVTGRrrfhKGIDIAAPTGTPVYAAADGTVVFAGWNGGYGNLVIIDHGNGYTTLYAHLSSILVKVGQRVKAGQV 162
|
170 180 190
....*....|....*....|....*....|..
gi 446118401 386 IALVGSSGGQGRPSLYFEIRRQGQAVNPQPWL 417
Cdd:COG0739 163 IGYVGNTGRSTGPHLHFEVRVNGKPVDPLPFL 194
|
|
| Peptidase_M23 |
pfam01551 |
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ... |
320-413 |
2.81e-39 |
|
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins such as Swiss:P33648 for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.
Pssm-ID: 460250 [Multi-domain] Cd Length: 96 Bit Score: 136.14 E-value: 2.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 320 WKGMVIGASEGTEVKAIADGRVILADWLQGYGLVVVVEHGKGDMSLYGYNQSALVSVGSQVRAGQPIALVGSSGGQGRPS 399
Cdd:pfam01551 3 HKGIDIAAPTGTPVYAAADGVVVFAGWLGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRSTGPH 82
|
90
....*....|....
gi 446118401 400 LYFEIRRQGQAVNP 413
Cdd:pfam01551 83 LHFEIRKNGKPVDP 96
|
|
| M23_peptidase |
cd12797 |
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ... |
321-404 |
6.75e-30 |
|
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; This model describes the metallopeptidase M23 family, which includes beta-lytic metallopeptidase and lysostaphin. Members of this family are zinc endopeptidases that lyse bacterial cell wall peptidoglycans; they cleave either the N-acylmuramoyl-Ala bond between the cell wall peptidoglycan and the cross-linking peptide (e.g. beta-lytic endopeptidase) or a bond within the cross-linking peptide (e.g. stapholysin, and lysostaphin). Beta-lytic metallopeptidase, formerly known as beta-lytic protease, has a preference for cleavage of Gly-X bonds and favors hydrophobic or apolar residues on either side. It inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent. Lysostaphin, produced by Staphylococcus genus, cleaves pentaglycine cross-bridges of cell wall peptidoglycan, acting as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Staphylolysin (also known as LasA) is implicated in a range of processes related to Pseudomonas virulence, including stimulating shedding of the ectodomain of cell surface heparan sulphate proteoglycan syndecan-1, and elastin degradation in connective tissue. Its active site is less constricted and contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules, possibly contributing to its activity against a wider range of substrates than those used by related lytic enzymes, consistent with its multiple roles in Pseudomonas virulence. The family includes members that do not appear to have the conserved zinc-binding site and might be lipoproteins lacking proteolytic activity.
Pssm-ID: 410984 [Multi-domain] Cd Length: 85 Bit Score: 110.76 E-value: 6.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 321 KGMVIGASEGTEVKAIADGRVILADWLQGYGLVVVVEHGKGDMSLYGYNQSALVSVGSQVRAGQPIALVGSSGGQGRPSL 400
Cdd:cd12797 2 NGIDIAAPEGTPVYAAADGTVVFAGWDGGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTGPHL 81
|
....
gi 446118401 401 YFEI 404
Cdd:cd12797 82 HFEI 85
|
|
| SpoIIQ2 |
COG5821 |
Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell ... |
266-417 |
1.58e-28 |
|
Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444523 [Multi-domain] Cd Length: 200 Bit Score: 110.89 E-value: 1.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 266 KEATRKGTTYKPTESEKSlmsrTGGLGAPRGQAF-WPVRGPTLHRYGEQLQ-----GELRW-KGMVIGASEGTEVKAIAD 338
Cdd:COG5821 40 NKLEEETVKNKSESNEKS----KSKVTASTSNKFlKPVSGKITREFGEDLVysktlNEWRThTGIDIAAKEGTPVKAAAD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 339 GRVILADWLQGYGLVVVVEHGKGDMSLYGY-NQSALVSVGSQVRAGQPIALVGSSGGQGR---PSLYFEIRRQGQAVNPQ 414
Cdd:COG5821 116 GVVVEVGKDPKYGITVVIDHGNGIKTVYANlDSKIKVKVGQKVKKGQVIGKVGSTALFESsegPHLHFEVLKNGKPVDPM 195
|
...
gi 446118401 415 PWL 417
Cdd:COG5821 196 KYL 198
|
|
| nlpD |
PRK10871 |
murein hydrolase activator NlpD; |
277-417 |
2.31e-18 |
|
murein hydrolase activator NlpD;
Pssm-ID: 236782 [Multi-domain] Cd Length: 319 Bit Score: 85.27 E-value: 2.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 277 PTESEKSLMSRTGGLGAPRGQAFWPVRGPTLHRYGEQLQGElrwKGMVIGASEGTEVKAIADGRVILA-DWLQGYGLVVV 355
Cdd:PRK10871 179 PTASTTEPTASSTSTSTPISTWRWPTDGKVIENFSASEGGN---KGIDIAGSKGQAIIATADGRVVYAgNALRGYGNLII 255
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446118401 356 VEHGKGDMSLYGYNQSALVSVGSQVRAGQPIALVGSSgGQGRPSLYFEIRRQGQAVNPQPWL 417
Cdd:PRK10871 256 IKHNDDYLSAYAHNDTMLVREQQEVKAGQKIATMGST-GTSSTRLHFEIRYKGKSVNPLRYL 316
|
|
| SpoIVFA |
COG5833 |
Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, ... |
285-414 |
1.23e-17 |
|
Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444535 [Multi-domain] Cd Length: 219 Bit Score: 81.19 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 285 MSRTGGLGAPRGQAF-WPVRGPTLHRYGEQLqgelrwKGMVIGASEGTEVKAIADGRVILADWLQGYGLVVVVEHGKGDM 363
Cdd:COG5833 90 PFGKEEETVEQGEAFaLPVSGKVVESFQENG------KGVDIETPGGANVKAVKEGYVIFAGKDEETGKTVIIQHADGSE 163
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 446118401 364 SLYGYNQSALVSVGSQVRAGQPIALVGSSGGQgRPSLYFEIRRQGQAVNPQ 414
Cdd:COG5833 164 SWYGNLSSIDVKLYDFVEAGQKIGTVPATEGE-EGTFYFAIKKGGKFIDPI 213
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
22-408 |
5.60e-17 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 81.80 E-value: 5.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 22 SAGVLLCAFSAHADerdqlksiqADIAAKERAVRQKQQQRASLLAQLKKQEEAISEATRKLRETQNTLNQLNKQIDEMNA 101
Cdd:COG3883 2 LALALAAPTPAFAD---------PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 102 SIAKLEQQKAAQERSLAAQLDAAFRQGEHTG-IQLILSGEESQRGQRLQAYFGYLNQARQETIAQLKQTREEVAMQRAEL 180
Cdd:COG3883 73 EIAEAEAEIEERREELGERARALYRSGGSVSyLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAEL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 181 EEKQSEQQTLLYEQRAQQAKLTQALNERKKTLAGLESSIQQGQQQLSELRANESRLRNSIARAEAAAKARAEREAREAQA 260
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 261 VRDRQKEATRKGTTYKPTESEKSLMSRTGGLGAPRGQAFWPVRGPTLHRYGEQLQGELRWKGMVIGASEGTEVKAIADGR 340
Cdd:COG3883 233 AAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGG 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446118401 341 VILADWlqGYGLVVVVEHGKGDMSLYGYNQSALVSVGSQVRAGQPIALVGSSGGQGRPSLYFEIRRQG 408
Cdd:COG3883 313 VGSGGG--AGAVVGGASAGGGGGSGGGGGSSGGGSGGGGGGGGGGGGSSSGGGGGGVGLSVGGGYVGG 378
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
32-240 |
4.04e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 4.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 32 AHADERDQLKSIQADIAAKERAVRQKQQQRASLLAQLKKQEEAISEATRKLRETQNTLNQLNKQIDEMNASIAKLEQQKA 111
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 112 AQERSLAAQLDAAFR-QGEHTGIQLILSGEESQRGQRLQAYFGYLNQARQ--ETIAQLKQTREEVAMQRAELEEKQSEQQ 188
Cdd:COG1196 355 EAEAELAEAEEALLEaEAELAEAEEELEELAEELLEALRAAAELAAQLEEleEAEEALLERLERLEEELEELEEALAELE 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446118401 189 TLLYEQRAQQAKLTQALNERKKTLAGLESSIQQGQQQLSELRANESRLRNSI 240
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
37-270 |
5.05e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.04 E-value: 5.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 37 RDQLKSI--QADIAAKERAVRQKQQQR--ASLLAQLKKQEEAISEATRKLRETQNTLNQLNKQIDEMNASIAKLEQQKAA 112
Cdd:COG1196 199 ERQLEPLerQAEKAERYRELKEELKELeaELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 113 QERSLAAQLDAafrqgehtgIQLILSGEESQRGQRlqayfgylnQARQETIAQLKQTREEVAMQRAELEEKQSEQQTLLY 192
Cdd:COG1196 279 LELELEEAQAE---------EYELLAELARLEQDI---------ARLEERRRELEERLEELEEELAELEEELEELEEELE 340
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446118401 193 EQRAQQAKLTQALNERKKTLAGLESSIQQGQQQLSELRANESRLRNSIARAEAAAKARAEREAREAQAVRDRQKEATR 270
Cdd:COG1196 341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
34-271 |
8.20e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 8.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 34 ADERDQLKSIQADIAAKERAVRQKQQQRASLLAQLKKQEEAISEATRKLRETQNTLNQLNKQIDEMNASIAKLEQQKA-- 111
Cdd:COG1196 263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEel 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 112 -AQERSLAAQLDAAfrqgehtgiQLILSGEESQRGQRLQAYfgylnQARQETIAQLKQTREEVAMQRAELEEKQSEQQTL 190
Cdd:COG1196 343 eEELEEAEEELEEA---------EAELAEAEEALLEAEAEL-----AEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 191 LYEQRAQQAKLTQALNERKKTLAGLESSIQQGQQQLSELRANESRLRNSIARAEAAAKARAEREAREAQAVRDRQKEATR 270
Cdd:COG1196 409 EEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
.
gi 446118401 271 K 271
Cdd:COG1196 489 A 489
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
36-238 |
4.17e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 4.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 36 ERDQLKSIQADIAAKERAVRQKQQQRASLLAQLKKQEEAISEATRKLRETQNTLNQLNKQIDEMNASIAKLEQQKAAQER 115
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 116 SLAAQLDAAFRQGEHtgiQLILSGEESQRGQRLQAYfgyLNQARQETIAQLKQTREEVAMQRAELEEKQSEQqtllyEQR 195
Cdd:COG1196 387 ELLEALRAAAELAAQ---LEELEEAEEALLERLERL---EEELEELEEALAELEEEEEEEEEALEEAAEEEA-----ELE 455
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446118401 196 AQQAKLTQALNERKKTLAGLESSIQQGQQQLSELRANESRLRN 238
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
33-240 |
9.22e-11 |
|
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: 63.92 E-value: 9.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 33 HADERDQLKSIQADIAAKERAVRQKQQQRASLLAQLKKQEEAISEATRKLRETQNTLNQLNKQIDEMNASIAKLEQQKAA 112
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 113 QERSLAAQLDAAFR-QGEHTGIQLILSGEESQRGQR------LQAYFGYLNQARQETIAQLKQTREEVAMQRAELEEKQS 185
Cdd:TIGR02168 335 LAEELAELEEKLEElKEELESLEAELEELEAELEELesrleeLEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446118401 186 EQQTLLYEQRAQQAKLT-QALNERKKTLAGLESSIQQGQQQLSELRANESRLRNSI 240
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEeAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
37-271 |
9.63e-11 |
|
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: 63.92 E-value: 9.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 37 RDQLKSIQADIAAKEraVRQKQQQRASLLAQLKKQEEAISEATRKLRETQNTLNQLNKQIDEMNASIAklEQQKAAQErs 116
Cdd:TIGR02168 219 KAELRELELALLVLR--LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIE--ELQKELYA-- 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 117 LAAQLDAAFRQGEHTgiqlilsgeeSQRGQRLQAYfgylNQARQETIAQLKQTREEVAMQRAELEEKQSEQQTLLYEQRA 196
Cdd:TIGR02168 293 LANEISRLEQQKQIL----------RERLANLERQ----LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEA 358
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446118401 197 QQAKLTQALNERKKTLAGLESSIQQGQQQLSELRANESRLRNSIARAEAAAKARAEREAREAQAVRDRQKEATRK 271
Cdd:TIGR02168 359 ELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
35-237 |
3.24e-09 |
|
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: 58.91 E-value: 3.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 35 DERDQLKSIQADIAAKERAVRQKQQQRASLLAQLKKQEEAISEATRKLRETQNTLNQLNKQIDEMNASIAKLEQQKAAQE 114
Cdd:TIGR02168 723 ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR 802
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 115 RSLAAQLDAAFRQGEHtgiqlilSGEESQRGQRLQAYFGYLNQARQETIAQLKQTREEVAMQRAELEEKQseqqtllYEQ 194
Cdd:TIGR02168 803 EALDELRAELTLLNEE-------AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE-------ELI 868
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446118401 195 RAQQAKLTQALNERKKTLAGLESSIQQGQQQLSELRANESRLR 237
Cdd:TIGR02168 869 EELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911
|
|
| PRK11649 |
PRK11649 |
putative peptidase; Provisional |
330-413 |
3.33e-09 |
|
putative peptidase; Provisional
Pssm-ID: 236946 [Multi-domain] Cd Length: 439 Bit Score: 58.52 E-value: 3.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 330 GTEVKAIADGRVILADWLQGYGLVVVVEHGKGDMSLYGYNQSALVSVGSQVRAGQPIALVGSSGGQGRPSLYFEIRRQGQ 409
Cdd:PRK11649 323 GTPVLAVGDGEVVVAKRSGAAGNYVAIRHGRQYTTRYMHLRKLLVKPGQKVKRGDRIALSGNTGRSTGPHLHYEVWINQQ 402
|
....
gi 446118401 410 AVNP 413
Cdd:PRK11649 403 AVNP 406
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
34-237 |
4.93e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 4.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 34 ADERDQLKSiQADIAAKERAVRQKQQQRASLLAQLKKQEEAISEATRKLRETQNTLNQLNKQIDEM-NASIAKLEQQKAA 112
Cdd:COG4913 271 LAELEYLRA-ALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIER 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 113 QERSLAAQldaafrqgehtgiqlilsgeeSQRGQRLQAYFGYLNQARQETIAQLKQTREEVAMQRAELEEKQSEQQTLLY 192
Cdd:COG4913 350 LERELEER---------------------ERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALA 408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446118401 193 EQRAQQAKLTQALNERKKTLAGLE---SSIQQGQQQL-----SELRANESRLR 237
Cdd:COG4913 409 EAEAALRDLRRELRELEAEIASLErrkSNIPARLLALrdalaEALGLDEAELP 461
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
77-271 |
8.35e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 8.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 77 EATRKLRETQNTLNQLNKQIDEMNASIAKLEQQKAAQERSLAAQLDAAFRQGEHTGIQLILSGEESQRGQRLQAYFGYLN 156
Cdd:COG1196 176 EAERKLEATEENLERLEDILGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 157 QARQETIAQLKQTREEVAMQRAELEEKQSEQQTLLYEQRAQQAKLTQALNERKKTLAGLESSIQQGQQQLSELRANESRL 236
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335
|
170 180 190
....*....|....*....|....*....|....*
gi 446118401 237 RNSIARAEAAAKARAEREAREAQAVRDRQKEATRK 271
Cdd:COG1196 336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
6-236 |
1.23e-08 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 57.23 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 6 KPRRFAIRPIIYASVLSAGVLLCAFSAHADERDQL--KSIQADIA---------AKERAVRQKQQQRASLLAQLKKQEEA 74
Cdd:PRK11281 2 KRSRHFVFRAFIAFLFLLLCLSSAFARAASNGDLPteADVQAQLDalnkqklleAEDKLVQQDLEQTLALLDKIDRQKEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 75 -------ISEATRKLRETQNTLNQLNKQIDEM------NASIAKLEQQKAAQERSLA-AQLDAAfrqgeHTGIQLIlsge 140
Cdd:PRK11281 82 teqlkqqLAQAPAKLRQAQAELEALKDDNDEEtretlsTLSLRQLESRLAQTLDQLQnAQNDLA-----EYNSQLV---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 141 eSQRGQ--RLQAYFgYLNQAR-QETIAQLKQTREEVAMQRAeleekqsEQQTLLyeqRAQQAKLTQALNERKKTLAGLES 217
Cdd:PRK11281 153 -SLQTQpeRAQAAL-YANSQRlQQIRNLLKGGKVGGKALRP-------SQRVLL---QAEQALLNAQNDLQRKSLEGNTQ 220
|
250
....*....|....*....
gi 446118401 218 SIQQGQQQLSELRANESRL 236
Cdd:PRK11281 221 LQDLLQKQRDYLTARIQRL 239
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
38-240 |
5.71e-08 |
|
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: 55.03 E-value: 5.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 38 DQLKSIQADIAAKERAVRQKQQQRASLLAQLKKQEEAISEATRKLRETQNTLNQLNKQIDEMNASIAKLEQQKAAQ-ERS 116
Cdd:TIGR04523 232 DNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDwNKE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 117 LAAQLDAafRQGEHTGIQLILSGEESQRGQrlqayfgyLNQarqeTIAQLKQTR-----EEVAMQRaELEEKQSEQQTLL 191
Cdd:TIGR04523 312 LKSELKN--QEKKLEEIQNQISQNNKIISQ--------LNE----QISQLKKELtnsesENSEKQR-ELEEKQNEIEKLK 376
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446118401 192 YEQRA----------QQAKLTQALNERKKTLAGLESSIQQGQQQLSELRANESRLRNSI 240
Cdd:TIGR04523 377 KENQSykqeiknlesQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETI 435
|
|
| SpoIIQ |
COG5820 |
Stage II sporulation protein SpoIIQ, required for engulfement [Cell cycle control, cell ... |
321-413 |
1.68e-07 |
|
Stage II sporulation protein SpoIIQ, required for engulfement [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444522 [Multi-domain] Cd Length: 224 Bit Score: 51.85 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 321 KGMVIGASEGT--EVKAIADGRVILA--DWLQGYglVVVVEHGKGDMSLYGYNQSALVSVGSQVRAGQPIA-----LVGS 391
Cdd:COG5820 121 TGIDIAAKDGEsfDVLAALSGTVTEVeeDPLLGY--VVEIKHDNGVSTVYQSLSDVKVKAGDEVKQGQVIGtagrnLFNK 198
|
90 100
....*....|....*....|..
gi 446118401 392 SGGQgrpSLYFEIRRQGQAVNP 413
Cdd:COG5820 199 DAGV---HLHFEVRKDGKAVNP 217
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
33-236 |
6.30e-07 |
|
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: 51.99 E-value: 6.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 33 HADE-RDQLKSIQADIAAKERAVRQKQQQRASLLAQLKKQEEAISEATRKLRETQNTLNQLNKQIDEMNASIAKLEQQKA 111
Cdd:TIGR02169 703 RLDElSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALN 782
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 112 AQERSLA----AQLDAAFR--QGEHTGIQLILSGEEsQRGQRLQAYFGYLNQARQETIAQL-------KQTREEVAMQRA 178
Cdd:TIGR02169 783 DLEARLShsriPEIQAELSklEEEVSRIEARLREIE-QKLNRLTLEKEYLEKEIQELQEQRidlkeqiKSIEKEIENLNG 861
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446118401 179 ELEEKQS---EQQTLLYEQRAQQAKLTQALNERKKTLAGLESSIQQGQQQLSELRANESRL 236
Cdd:TIGR02169 862 KKEELEEeleELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL 922
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
77-236 |
1.07e-06 |
|
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: 51.21 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 77 EATRKLRETQNTLNQLNKQIDEMNASIAKLEQQ--KAAQERSLAAQLDAafrqgehtgIQLILSgeesqrGQRLQAYFGY 154
Cdd:TIGR02168 176 ETERKLERTRENLDRLEDILNELERQLKSLERQaeKAERYKELKAELRE---------LELALL------VLRLEELREE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 155 LNQARQEtIAQLKQTREEVAMQRAELEEKQSEQQTLLYEQRAQQAKLTQALNERKKTLAGLESSIQQGQQQLSELRANES 234
Cdd:TIGR02168 241 LEELQEE-LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLE 319
|
..
gi 446118401 235 RL 236
Cdd:TIGR02168 320 EL 321
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
40-271 |
2.44e-06 |
|
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: 50.06 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 40 LKSIQADIAAKERAVRQKQQQRASLLAQLKKQEEAISEATRKLRETQNTLNQLNKQIDEMNASIAKLEQQKAAQERSLAA 119
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 120 QLDAAFRQGEHTGIQLILSGEESQRGQRLQAYFGYLNQARQETIAQLKQTREEVAMQRAELEEKQSEQQTLLYEQRAQQA 199
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446118401 200 KLTQALNERKKT---LAGLESSIQQGQQQLSELRAN---ESRLRNSIARAEAAAKARAEREAREAQAVRDRQKEATRK 271
Cdd:TIGR02168 839 RLEDLEEQIEELsedIESLAAEIEELEELIEELESEleaLLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
32-205 |
2.89e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 32 AHADERDQLKSIQADIAAKERAVRQKQQQRASL--LAQLKKQEEAISEATRKLRETQNTLNQLNKQIDEMNASIAKLEQQ 109
Cdd:COG4717 89 EYAELQEELEELEEELEELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEEL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 110 KAAQERsLAAQLDAAFRQgehtgiqliLSGEESQRGQRLQAYFGYLNQARQETIAQLKQTREEVAMQRAELEEKQSEQQT 189
Cdd:COG4717 169 EAELAE-LQEELEELLEQ---------LSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238
|
170
....*....|....*.
gi 446118401 190 LLYEQRAQQAKLTQAL 205
Cdd:COG4717 239 AALEERLKEARLLLLI 254
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
32-240 |
4.92e-06 |
|
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: 48.91 E-value: 4.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 32 AHADERDQLKSIQADIAAKERA------VRQKQQ---QRASLLAQLKKQEEAISEATRKLRETQNTLNQLNKQIDEMN-- 100
Cdd:TIGR02169 208 EKAERYQALLKEKREYEGYELLkekealERQKEAierQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGee 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 101 -------------ASIAKLE--------QQKAAQERSLAAQLDAAFRQGEHTGIqlilsgEESQRGQRLQayfgylnqaR 159
Cdd:TIGR02169 288 eqlrvkekigeleAEIASLErsiaekerELEDAEERLAKLEAEIDKLLAEIEEL------EREIEEERKR---------R 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 160 QETIAQLKQTREEVAMQRAELEEKQSEQQTLLYEQRAQQAKLTQA---LNERKKTLAGLESSIQQGQQQLSELRANESRL 236
Cdd:TIGR02169 353 DKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLkreINELKRELDRLQEELQRLSEELADLNAAIAGI 432
|
....
gi 446118401 237 RNSI 240
Cdd:TIGR02169 433 EAKI 436
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
35-238 |
6.59e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 6.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 35 DERDQLKSIQADIA-AKERA-----VRQKQQQRASLLAQLKKQEEAISEATRKLRETQntLNQLNKQIDEMNASIAKLEQ 108
Cdd:COG4913 232 EHFDDLERAHEALEdAREQIellepIRELAERYAAARERLAELEYLRAALRLWFAQRR--LELLEAELEELRAELARLEA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 109 QKAAqersLAAQLDAAfrQGEHTGIQLILSGEESQRGQRLQAyfgyLNQARQETIAQLKQTREEVAMQRAELEEKQSEQQ 188
Cdd:COG4913 310 ELER----LEARLDAL--REELDELEAQIRGNGGDRLEQLER----EIERLERELEERERRRARLEALLAALGLPLPASA 379
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446118401 189 TLLYEQRAQQAKLTQALNERKKTL----AGLESSIQQGQQQLSELRANESRLRN 238
Cdd:COG4913 380 EEFAALRAEAAALLEALEEELEALeealAEAEAALRDLRRELRELEAEIASLER 433
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
37-230 |
8.22e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 8.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 37 RDQLKSIQADIAAKERAVRQKQQ---------QRASLLAQLKKQEEAISEATRKLRETQNTLNQLNKQIDEMNASIAKLE 107
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQknglvdlseEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 108 QQKAAQErsLAAQLDAAfrqgehtgiqlilsgeESQRgQRLQAYFGYLNQARQETIAQLKQTREEVamqRAELEEKQSEQ 187
Cdd:COG3206 261 QSPVIQQ--LRAQLAEL----------------EAEL-AELSARYTPNHPDVIALRAQIAALRAQL---QQEAQRILASL 318
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446118401 188 QTLLYEQRAQQAKLTQALNERKKTLAGLessiQQGQQQLSELR 230
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLAEL----PELEAELRRLE 357
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
62-189 |
1.07e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.90 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 62 ASLLAQLKKQEEAISEATRKLRETQNTLNQLNKQIDEMNASIAKL--EQQKAAQERSLAAQLDAAfrqgehtgiQLILSG 139
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLleEAEKEAQQAIKEAKKEAD---------EIIKEL 593
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 446118401 140 EESQRGQrlqayfgYLNQARQETIAQLKQTREevAMQraELEEKQSEQQT 189
Cdd:PRK00409 594 RQLQKGG-------YASVKAHELIEARKRLNK--ANE--KKEKKKKKQKE 632
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
34-240 |
1.21e-05 |
|
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: 47.76 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 34 ADERDQLKSIQADIAAKERAVRQKQQQRASLLAQLKKQEEAISEATRKLRETQNTLNQLNKQIDEMNASIAKLEQQKAAQ 113
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 114 ERSLAAqldaafrqgehtgiqlilsgeESQRGQRLQAYFGYLnqarQETIAQLKQTREEV----AMQR-AELEEKQSEQQ 188
Cdd:TIGR02169 750 EQEIEN---------------------VKSELKELEARIEEL----EEDLHKLEEALNDLearlSHSRiPEIQAELSKLE 804
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446118401 189 TLLYEQRAQQAKLTQALNERKKTLAGLESSIQQGQQQLSELRANESRLRNSI 240
Cdd:TIGR02169 805 EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI 856
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
10-206 |
1.41e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 47.01 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 10 FAIRPIIYASVLSAGVLLCAFSAHADERDQLKSIQADI--AAKERAVRQKQQQRASLLAQLKKQEEAISEATRKLRETQN 87
Cdd:PRK12705 1 FAMSILLVILLLLIGLLLGVLVVLLKKRQRLAKEAERIlqEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 88 T----LNQLNKQIDEMNASIAKLEQQKAAQERSLAAQldaafrqgehtgiQLILSGEESQRGQRLQAYFGYL-NQARQET 162
Cdd:PRK12705 81 ReeerLVQKEEQLDARAEKLDNLENQLEEREKALSAR-------------ELELEELEKQLDNELYRVAGLTpEQARKLL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446118401 163 IAQLKQTREEvamQRAELEEKQSEQQTLLYEQRAQQAkLTQALN 206
Cdd:PRK12705 148 LKLLDAELEE---EKAQRVKKIEEEADLEAERKAQNI-LAQAMQ 187
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
38-231 |
2.63e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.50 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 38 DQLKSIQADIAAKERAVRQKQQQRASLLAQLKKQEEAISEATRKlretQNTLNQLNKQIDEMNASIAKLE-QQKAAQERS 116
Cdd:TIGR00618 215 DTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKK----QQLLKQLRARIEELRAQEAVLEeTQERINRAR 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 117 LAAQLDAAFRQGEHTG--IQLILSGEESQRGQRLQAYFGYLNQARQETIAQLKQTREEVAMQRAELEEKQSEQQTLLYEQ 194
Cdd:TIGR00618 291 KAAPLAAHIKAVTQIEqqAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREI 370
|
170 180 190
....*....|....*....|....*....|....*..
gi 446118401 195 RAQQAKLTQALNERKKTLAGLESSIQQGQQQLSELRA 231
Cdd:TIGR00618 371 SCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQR 407
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
42-240 |
2.75e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 42 SIQADIAAKERAVRQKQQQRASLLAQLKKQEEAISE--ATRKLRETQNTLNQLNKQIDEMNASIAKLEQQKAAQErSLAA 119
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAE-ARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 120 QLDAAFRQGEHTGIQLILSgeesqrgqrlqayfgylnqarqETIAQLKQTREEVAMQRAELEEKQSEQQTLLYEQRAQQA 199
Cdd:COG3206 244 ALRAQLGSGPDALPELLQS----------------------PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIA 301
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446118401 200 KLTQALN-ERKKTLAGLESSIQQGQQQLSELRANESRLRNSI 240
Cdd:COG3206 302 ALRAQLQqEAQRILASLEAELEALQAREASLQAQLAQLEARL 343
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
37-230 |
3.16e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 37 RDQLKSIQADIAAKERAVRQKQQQRASL---LAQLKKQEEAI------SEATRKLRETQNTLNQLNKQIDEMNASIAKLE 107
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALeaeLDALQERREALqrlaeySWDEIDVASAEREIAELEAELERLDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 108 QQKAAQERsLAAQLDAAfrqgehtgiqlilsgeESQRGQRLQAYfgylnQARQETIAQLKQTREEVAMQRAELEEKQSEQ 187
Cdd:COG4913 689 ALEEQLEE-LEAELEEL----------------EEELDELKGEI-----GRLEKELEQAEEELDELQDRLEAAEDLARLE 746
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446118401 188 QTLLYEQRAQQAKLTQAlneRKKTLAGLESSIQQGQQQLSELR 230
Cdd:COG4913 747 LRALLEERFAAALGDAV---ERELRENLEERIDALRARLNRAE 786
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
44-230 |
4.83e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.71 E-value: 4.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 44 QADIAAKERAVRQKQQQRASLLAQLKKQEEAISEATRKLRETQNTLNQLNKQ------------IDEMNASIAKLEQQKA 111
Cdd:COG3096 831 APDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQanlladetladrLEELREELDAAQEAQA 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 112 --AQERSLAAQLD---AAFRQGEHTGIQLILSGEE-SQRGQRLQA-------------YFGYlnqarQETIAQLKQTREE 172
Cdd:COG3096 911 fiQQHGKALAQLEplvAVLQSDPEQFEQLQADYLQaKEQQRRLKQqifalsevvqrrpHFSY-----EDAVGLLGENSDL 985
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446118401 173 VAMQRAELEEKQSEQQTLLYEQRAQQAKLTQALnerkKTLAGLESSIQQGQQQLSELR 230
Cdd:COG3096 986 NEKLRARLEQAEEARREAREQLRQAQAQYSQYN----QVLASLKSSRDAKQQTLQELE 1039
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
53-281 |
5.12e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 5.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 53 AVRQKQQQRASLLAQLKKQEEAISEAtrklrETQNTLNQLNKQIDEMNASIAKLEQQKAAQerslAAQLDAAfrqgehtg 132
Cdd:PRK02224 177 GVERVLSDQRGSLDQLKAQIEEKEEK-----DLHERLNGLESELAELDEEIERYEEQREQA----RETRDEA-------- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 133 iQLILSGEESqrgqrlqayfgylnqaRQETIAQLKQTREEVAMQRAELEEKQSEQQTLLYEQRAQQAKLTQALNERKKTL 212
Cdd:PRK02224 240 -DEVLEEHEE----------------RREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA 302
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446118401 213 AGLESSIQQGQQQLSELRANESRLRNSIARAEAAAKARAEREAREAQAVRDRQKEATRKGTTYKPTESE 281
Cdd:PRK02224 303 GLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESE 371
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
38-240 |
5.57e-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: 45.40 E-value: 5.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 38 DQLKSIQADIAAKERAVRQKQQQRASLLAQLKKQEEAISEATRKLRETQNTLNQLNKQIDEMNASIAKLEQQKAAQERSL 117
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKI 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 118 ------AAQLDAAFRQGEHTGIQLilsgeeSQRGQRLQAyfgyLNQARQETIAQLKQTREEVAMQRAELEEKQSEQQT-- 189
Cdd:TIGR04523 401 qnqeklNQQKDEQIKKLQQEKELL------EKEIERLKE----TIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETql 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446118401 190 --LLYEQRAQQAKL---TQALNERKKTLAGLESSIQQGQQQLSELRANESRLRNSI 240
Cdd:TIGR04523 471 kvLSRSINKIKQNLeqkQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKI 526
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
34-230 |
6.95e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.43 E-value: 6.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 34 ADERDQLKSIQADIAAKE-------------RAVRQKQQQR------ASLLAQLKKQEeaiSEATRKLRETQNTLNQLNK 94
Cdd:PRK10929 89 NNERDEPRSVPPNMSTDAleqeilqvssqllEKSRQAQQEQdrareiSDSLSQLPQQQ---TEARRQLNEIERRLQTLGT 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 95 QIDEMNASIAKLEQQKAAQERSLA-----AQLDAAFRQgEHTGIQLILSgeeSQRGQRLQAYFgylnQARQETIAQLKQT 169
Cdd:PRK10929 166 PNTPLAQAQLTALQAESAALKALVdelelAQLSANNRQ-ELARLRSELA---KKRSQQLDAYL----QALRNQLNSQRQR 237
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446118401 170 REEVAMQRAELEEKQSEQ-QTLLYEQRAQQAKLTQALNERKKTLAGLES-------SIQQGQQQLSELR 230
Cdd:PRK10929 238 EAERALESTELLAEQSGDlPKSIVAQFKINRELSQALNQQAQRMDLIASqqrqaasQTLQVRQALNTLR 306
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
44-197 |
7.24e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 7.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 44 QADIAAKERAVRQKQQQraslLAQLKKQEEAISEATRKLRETQNTLNQLNKQIDEMNASIAKLEQQKAAQERSLAAQLDA 123
Cdd:COG4913 660 EIDVASAEREIAELEAE----LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446118401 124 AfrqgehtgiQLILSGEESQRGQRLQAYFGYLNQARQEtiaqlKQTREEVAMQRAELEEKQSEQQTLLYEQRAQ 197
Cdd:COG4913 736 L---------EAAEDLARLELRALLEERFAAALGDAVE-----RELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
49-284 |
8.91e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 8.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 49 AKERAVRQKQQQRASLLAQLKKQEEAISEATRKLRETQNTLNQLNKQIDEMNAS-IAKLEQQKAAQERSLAAQLDAA-FR 126
Cdd:PTZ00121 1508 AKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEeKKKAEEAKKAEEDKNMALRKAEeAK 1587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 127 QGEHTGIQLILSGEESQRGQRLQayfgylnQARQETIAQLKQtrEEVamQRAELEEKQSEQQTLLYEQRAQQA-KLTQAL 205
Cdd:PTZ00121 1588 KAEEARIEEVMKLYEEEKKMKAE-------EAKKAEEAKIKA--EEL--KKAEEEKKKVEQLKKKEAEEKKKAeELKKAE 1656
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446118401 206 NERKKTLAGLESSIQQGQQQLSELRANESRLRNSiaraeAAAKARAEREAREAQAVRDRQKEATRKGTTYKPTESEKSL 284
Cdd:PTZ00121 1657 EENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKA-----AEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKI 1730
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
51-229 |
1.22e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 51 ERAVRQKQQQRASLLAQLKKQEEAISEATRKLRETQNTLNQLNKQIDEMN---------------ASIAKLEQQKA--AQ 113
Cdd:PRK04863 836 EAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNlladetladrveeirEQLDEAEEAKRfvQQ 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 114 ERSLAAQLD---AAFRQGEHTGIQL---ILSGEESQRGQRLQAY-FGYLNQAR-----QETIAQLKQTREEVAMQRAELE 181
Cdd:PRK04863 916 HGNALAQLEpivSVLQSDPEQFEQLkqdYQQAQQTQRDAKQQAFaLTEVVQRRahfsyEDAAEMLAKNSDLNEKLRQRLE 995
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446118401 182 EKQSEQQTLLYEQRAQQAKLTQAlnerKKTLAGLESSIQQGQQQLSEL 229
Cdd:PRK04863 996 QAEQERTRAREQLRQAQAQLAQY----NQVLASLKSSYDAKRQMLQEL 1039
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
39-239 |
1.27e-04 |
|
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: 44.24 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 39 QLKSIQADIAAKERAVRQKQQQrasllaqLKKQEEAISEATRKLRETQNTLNQLNKQIDEMNASIAKLEQQKAAQERSLa 118
Cdd:TIGR04523 469 QLKVLSRSINKIKQNLEQKQKE-------LKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI- 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 119 AQLDAAFRQGEHTGIQLILSGEEsqrgqrlqayfgylnQARQETIAQLKQTREevamqraELEEKQSEQQTLLYEQRAQQ 198
Cdd:TIGR04523 541 SDLEDELNKDDFELKKENLEKEI---------------DEKNKEIEELKQTQK-------SLKKKQEEKQELIDQKEKEK 598
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446118401 199 AKLTQALNERKKTLAGLESSIQQGQQQLSELRANESRLRNS 239
Cdd:TIGR04523 599 KDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSK 639
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
39-219 |
3.28e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 39 QLKSIQADIAAKERAVRQKQQQRASLLAQLKKQEEAISEATRKLRETQNTLNQLNKQIDEMNASIAKLEQqkaaqersla 118
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 119 aQLDAAFRQGEHTGIQLILSGEESQRGQRLQAYFGyLNQARQETIAQLKQTREEVAMQRAELEEKQSEQQTLLYEQRAQQ 198
Cdd:COG1579 81 -QLGNVRNNKEYEALQKEIESLKRRISDLEDEILE-LMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
170 180
....*....|....*....|.
gi 446118401 199 AKLTQalnERKKTLAGLESSI 219
Cdd:COG1579 159 EELEA---EREELAAKIPPEL 176
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
38-228 |
4.31e-04 |
|
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: 42.70 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 38 DQLKSIQADIAAKERAVRQKQQQRASL---LAQLKKQEEAISEATRKLRETQNTLNQLNKQIDEMNASIAKLEQQ-KAAQ 113
Cdd:TIGR04523 173 NELNLLEKEKLNIQKNIDKIKNKLLKLellLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEiSNTQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 114 ERSLAA---------QLDAAFRQGEHTGIQLIlsgEESQRGQRLQAYFGYLNQARQETIaqLKQTREEVAMQRAELEEKQ 184
Cdd:TIGR04523 253 TQLNQLkdeqnkikkQLSEKQKELEQNNKKIK---ELEKQLNQLKSEISDLNNQKEQDW--NKELKSELKNQEKKLEEIQ 327
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446118401 185 SEqqtlLYEQRAQQAKLTQALNERKKTLAGLESSIQQGQQQLSE 228
Cdd:TIGR04523 328 NQ----ISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE 367
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
37-239 |
4.52e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.80 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 37 RDQLKSIQADIaakERAVRQKQQQRASLLAQLKKQEEAISEATRKLRETQNT----LNQLNKQIDEMNASI--AKLEQQK 110
Cdd:pfam15921 291 RSQANSIQSQL---EIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMyedkIEELEKQLVLANSELteARTERDQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 111 AAQER-SLAAQLDAAFRQGEHTGIQLILSGEESQR-GQRLQAYFGYLNQARQEtiaqLKQTREEVAMQRAELEEKQSEQQ 188
Cdd:pfam15921 368 FSQESgNLDDQLQKLLADLHKREKELSLEKEQNKRlWDRDTGNSITIDHLRRE----LDDRNMEVQRLEALLKAMKSECQ 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446118401 189 TLLYEQRAQQAKLTQALNERKKTLAGLESSIQQGQQQLSELRANESRLRNS 239
Cdd:pfam15921 444 GQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESS 494
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
36-240 |
5.10e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.41 E-value: 5.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 36 ERDQLksiqadiaAKERAVRQKQQQRasLLAQLKKQEEAIS---EATRKL--RETQN--TLNQLNKQIDEMNASIAKLEQ 108
Cdd:pfam15921 364 ERDQF--------SQESGNLDDQLQK--LLADLHKREKELSlekEQNKRLwdRDTGNsiTIDHLRRELDDRNMEVQRLEA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 109 QKAAQERSLAAQLD--AAFRQGEHTGIQLILSgeesqrgqrlqayfgylnqarqeTIAQLKQTREevaMQRAELEEKQSE 186
Cdd:pfam15921 434 LLKAMKSECQGQMErqMAAIQGKNESLEKVSS-----------------------LTAQLESTKE---MLRKVVEELTAK 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446118401 187 QQTLLYEQRAQqAKLTQALNERKKTLAG-------LESSIQQGQQQLSELRANESRLRNSI 240
Cdd:pfam15921 488 KMTLESSERTV-SDLTASLQEKERAIEAtnaeitkLRSRVDLKLQELQHLKNEGDHLRNVQ 547
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
32-124 |
5.54e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 42.17 E-value: 5.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 32 AHADERDQLKSIQADIAAKeRAVRQKQQQRASLLAQLKKQEEAISEATRKLRETQNTLnqLNKQIDEMNASIAKLEQQKA 111
Cdd:PRK12472 192 AETLAREAEDAARAADEAK-TAAAAAAREAAPLKASLRKLERAKARADAELKRADKAL--AAAKTDEAKARAEERQQKAA 268
|
90
....*....|...
gi 446118401 112 AQERSLAAQLDAA 124
Cdd:PRK12472 269 QQAAEAATQLDTA 281
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
39-231 |
5.54e-04 |
|
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: 42.31 E-value: 5.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 39 QLKSIQADIAAKERAVR-------QKQQQRASLLAQLKKQEEAISEATRKLRETQNTLNQLNKQIDEMNASIAKLEQQKA 111
Cdd:TIGR04523 41 KLKTIKNELKNKEKELKnldknlnKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 112 AQErslaAQLDAAFRQGEHTGIQLILSGEESqrgQRLQAYFGYLNQARQETIAQLKQTREEVAMQRAELEEKQSEQQTLL 191
Cdd:TIGR04523 121 KLE----VELNKLEKQKKENKKNIDKFLTEI---KKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIK 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446118401 192 YEQRAQQAKLT--QALNERKKTLAG-----------LESSIQQGQQQLSELRA 231
Cdd:TIGR04523 194 NKLLKLELLLSnlKKKIQKNKSLESqiselkkqnnqLKDNIEKKQQEINEKTT 246
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
52-237 |
6.36e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 6.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 52 RAVRQKQQQRASLLAQLKKQEEAISEATRKLRETQNTLNQLNKQIDEMNASIAKLEQQKAAQERslaaqldaafRQGEHT 131
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE----------LKEEIE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 132 GIQLILSGEEsQRGQRLQAYFGYLNQARQETIAQLKQTREEVAmQRAELEEKQSEQQTLlyeqRAQQAKLTQALNERKKT 211
Cdd:PRK03918 242 ELEKELESLE-GSKRKLEEKIRELEERIEELKKEIEELEEKVK-ELKELKEKAEEYIKL----SEFYEEYLDELREIEKR 315
|
170 180
....*....|....*....|....*.
gi 446118401 212 LAGLESSIQQGQQQLSELRANESRLR 237
Cdd:PRK03918 316 LSRLEEEINGIEERIKELEEKEERLE 341
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
58-231 |
7.39e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.08 E-value: 7.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 58 QQQRASLLAQLKKQEEAISEATRKLRETQNTLNQLNKQIDEMNASIAKLeQQKAAQERSLAAQLDAAFRQgehtgiqlil 137
Cdd:pfam01576 228 QAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISEL-QEDLESERAARNKAEKQRRD---------- 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 138 sgeesqRGQRLQAYFGYLNQARQETIAQ--LKQTRE-EVAMQRAELEE--KQSEQQTLLYEQRAQQA--KLTQALNERKK 210
Cdd:pfam01576 297 ------LGEELEALKTELEDTLDTTAAQqeLRSKREqEVTELKKALEEetRSHEAQLQEMRQKHTQAleELTEQLEQAKR 370
|
170 180
....*....|....*....|.
gi 446118401 211 TLAGLESSIQQGQQQLSELRA 231
Cdd:pfam01576 371 NKANLEKAKQALESENAELQA 391
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
62-231 |
1.33e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 62 ASLLAQLKKQEEAISEATRKLRETQNTLNQ-------LNKQIDEMNASIAKLEQQ----KAAQERSLAAQLDAafRQGEH 130
Cdd:PRK04863 445 EEFQAKEQEATEELLSLEQKLSVAQAAHSQfeqayqlVRKIAGEVSRSEAWDVARellrRLREQRHLAEQLQQ--LRMRL 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 131 TGIQLILsgEESQRGQRLQAYFGYLNQARQETIAQLKQTREEVAMQRAELEEKQSEQQTLLYEQRAQQakltQALNERKK 210
Cdd:PRK04863 523 SELEQRL--RQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQL----EQLQARIQ 596
|
170 180
....*....|....*....|.
gi 446118401 211 TLAGLESSIQQGQQQLSELRA 231
Cdd:PRK04863 597 RLAARAPAWLAAQDALARLRE 617
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
61-239 |
1.47e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 61 RASLLAQLKKQEEAISEAT--------RKLRETQNTLNQLNKQIDEMNASIAKLEQQKAAQE--RSLAAQLDAAFRQGEH 130
Cdd:COG4717 44 RAMLLERLEKEADELFKPQgrkpelnlKELKELEEELKEAEEKEEEYAELQEELEELEEELEelEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 131 TGIQLILSGEESQRGQRLQAYFGYLNQARQEtIAQLKQTREEVAMQRAELEEKQSEQQTLL----YEQRAQQAKLTQALN 206
Cdd:COG4717 124 LLQLLPLYQELEALEAELAELPERLEELEER-LEELRELEEELEELEAELAELQEELEELLeqlsLATEEELQDLAEELE 202
|
170 180 190
....*....|....*....|....*....|...
gi 446118401 207 ERKKTLAGLESSIQQGQQQLSELRANESRLRNS 239
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
34-240 |
1.59e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 34 ADERDQLKSIQADIAAKERA-----VRQKQQQRASLLAQLKKQEEAISEATRKLRETQNTLN---QLNKQIDEMNASIAK 105
Cdd:PRK02224 183 SDQRGSLDQLKAQIEEKEEKdlherLNGLESELAELDEEIERYEEQREQARETRDEADEVLEeheERREELETLEAEIED 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 106 LEQQKAAQERSLAAQLDAAfrqgehtgiqlilsgeESQRGQRLQayfgyLNQARQETIAQLKQTR---EEVAMQRAELEE 182
Cdd:PRK02224 263 LRETIAETEREREELAEEV----------------RDLRERLEE-----LEEERDDLLAEAGLDDadaEAVEARREELED 321
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446118401 183 KQSEQQTLLYEQR-AQQAKLTQA---------LNERKKTL----AGLESSIQQGQQQLSELRANESRLRNSI 240
Cdd:PRK02224 322 RDEELRDRLEECRvAAQAHNEEAeslredaddLEERAEELreeaAELESELEEAREAVEDRREEIEELEEEI 393
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
35-231 |
1.66e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 35 DERDQLKSIQADIAAKERAVRQKQQQRASLLAQLKKQEEAISEATRKLR---------ETQNTLNQLNKQIDEMNASIAK 105
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEklekllqllPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 106 LEQQkAAQERSLAAQLDAafrqgehtgiqliLSGEESQRGQRLQAYFGYLNQARQETIAQLKQTREEVAMQRAELEEKQS 185
Cdd:COG4717 151 LEER-LEELRELEEELEE-------------LEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE 216
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446118401 186 EQQTLLYEQRAQQAKLTQALNerkktlaglessIQQGQQQLSELRA 231
Cdd:COG4717 217 EAQEELEELEEELEQLENELE------------AAALEERLKEARL 250
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
54-201 |
1.88e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 54 VRQKQQQRASLLAQLKKQEEAISEATRKLRETQNTLNQLNKQIDEMNASIAKLEQQKaaqeRSLAAQLDAAFRQGEhtgi 133
Cdd:pfam01576 491 LRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGK----KRLQRELEALTQQLE---- 562
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446118401 134 qlilsgEESQRGQRLQAYFGYLNQARQETIAQLKQTREEVamqrAELEEKQSEQQTLLYEQRAQQAKL 201
Cdd:pfam01576 563 ------EKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLV----SNLEKKQKKFDQMLAEEKAISARY 620
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
31-118 |
1.94e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.00 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 31 SAHADERDQLKSIQADIAAKERAVRQKQQQRASLLAQ----LKKQEEAISEATRKLRETQNTLNQLNKQIDEMNASIAKL 106
Cdd:smart00787 172 SIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRakekLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSEL 251
|
90
....*....|..
gi 446118401 107 EQQKAAQERSLA 118
Cdd:smart00787 252 NTEIAEAEKKLE 263
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
40-239 |
1.96e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 40.37 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 40 LKSIQADIAAKERAVRQKQ-QQRASLLAQLKKQEEAISEATRKLRETQNTLNQLNKQIDEMNASIAKLEQQKAAQERSla 118
Cdd:pfam05262 203 LKERESQEDAKRAQQLKEElDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQK-- 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 119 aqldaafRQGEHTGIQLILSGEESQRGQRLQAYfgylnQARQETIAQLKQTREEVAMQRAELEEKQSEQQTLLYEQRAQQ 198
Cdd:pfam05262 281 -------REIEKAQIEIKKNDEEALKAKDHKAF-----DLKQESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQP 348
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446118401 199 AKLTQALNERKKTLAGLEssIQQGQQQLSELR----ANESRLRNS 239
Cdd:pfam05262 349 TSLNEDAIDSSNPVYGLK--VVDPITNLSELVlidlKTEVRLRES 391
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
29-113 |
2.24e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 40.10 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 29 AFSAHADERDQLKSIQADIAAKERAVRQKQQQRASLLAQ-LKKQEEAISEATRKLRETQNTLNQLNKQIDEMNASIAKle 107
Cdd:TIGR04320 273 AQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQaLQTAQNNLATAQAALANAEARLAKAKEALANLNADLAK-- 350
|
....*.
gi 446118401 108 QQKAAQ 113
Cdd:TIGR04320 351 KQAALD 356
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
36-207 |
2.57e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.56 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 36 ERDQLKSIQADIAAKERAVRQKQQQRASLLAQLKKQEEAISEATRKLRETQNTLNQLNKQIDEMNASIAKLEQQKAAQER 115
Cdd:PRK09039 72 ERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQIAALRR 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 116 SLAA---QLDAAFRQGEHTGIQLilsgeeSQRGQRlqayfgyLNQARQETIAQLKQTREEVAMQ-RAELEEK-------- 183
Cdd:PRK09039 152 QLAAleaALDASEKRDRESQAKI------ADLGRR-------LNVALAQRVQELNRYRSEFFGRlREILGDRegirivgd 218
|
170 180 190
....*....|....*....|....*....|....
gi 446118401 184 ----QSE------QQTLLYEQRAQQAKLTQALNE 207
Cdd:PRK09039 219 rfvfQSEvlfptgSAELNPEGQAEIAKLAAALIE 252
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
34-284 |
2.76e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 34 ADERDQLKSIQADIAAKERAVRQKQQQRASLLAQLKKQEEAiseatRKLRETQNTLNQLNKQiDEMNASIAKLeQQKAAQ 113
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA-----KKAEEAKIKAEELKKA-EEEKKKVEQL-KKKEAE 1644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 114 ERSLAAQLDAAFRQGEHTGIQLILSGEESQRgqrlqayfgylnQARQETIAQLKQTREEVAMQRAELEEKQSEQQTLLYE 193
Cdd:PTZ00121 1645 EKKKAEELKKAEEENKIKAAEEAKKAEEDKK------------KAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEA 1712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 194 QRAQQA-KLTQALNERKKTLAGLESSIQQGQQQLSELRANESRlRNSIARAEAAAKARAEREAREAQAVrdrQKEATRKG 272
Cdd:PTZ00121 1713 EEKKKAeELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE-KKKIAHLKKEEEKKAEEIRKEKEAV---IEEELDEE 1788
|
250
....*....|..
gi 446118401 273 TTYKPTESEKSL 284
Cdd:PTZ00121 1789 DEKRRMEVDKKI 1800
|
|
| ClyA_MakA-like |
cd22655 |
Vibrio cholerae cytotoxin MakA (motility associated killing factor A), and similar proteins; ... |
30-119 |
2.91e-03 |
|
Vibrio cholerae cytotoxin MakA (motility associated killing factor A), and similar proteins; This model includes Vibrio cholerae motility associated killing factor A (MakA) cytotoxin, a member of the cytolysin A (ClyA) family of alpha pore-forming toxins (alpha-PFTs). The MakA protein is encoded by the mak operon. Transport of the MakA protein from the bacteria is shown to occur by flagellum-dependent secretion, highlighting a non-conventional and direct role of flagella in pathogenesis of V. cholerae; a conserved N-terminal FTPP motif is essential for MakA secretion via the flagellum channel in a proton motive force-dependent manner. Structure of MakA shows an elongated, almost entirely alpha-helical protein, with the head domain consisting of two helices and three beta-strands that together with the short beta-strand of the tail domain forms a four-stranded sheet. MakA has been demonstrated to cause toxicity in both Caenorhabditis elegans and zebrafish.
Pssm-ID: 439153 [Multi-domain] Cd Length: 342 Bit Score: 39.57 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 30 FSAHADERD--QLKSIQADIAAKERAVRQKQQQRASLLAQLKKQEEAISEATRKLRET----QNTLNQLNKQIDEMNASI 103
Cdd:cd22655 84 FKALPTAPDdaQVEQIIALLQALQKPVQEIISNIAAYQGKLKAWGDKMQAAHDNLTTGaaqiQAAETDLQADIDKINNAI 163
|
90
....*....|....*.
gi 446118401 104 AKLEQQKAAQERSLAA 119
Cdd:cd22655 164 ANLNAEIAKDNKAIAA 179
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
72-240 |
3.17e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 72 EEAISEATRKLRETQNTLNQLNKQIDEMNASIAKLEQQKAAQERSLAAQLDAAFRQgehtgiqlilsgeesQRGQRLQAY 151
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELE---------------YLRAALRLW 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 152 FgylnqaRQETIAQLKQTREEVAMQRAELEEKQSEQQTLLYEQRAQQAKLTQALNERK-KTLAGLESSIQQGQQQLSELR 230
Cdd:COG4913 285 F------AQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERE 358
|
170
....*....|
gi 446118401 231 ANESRLRNSI 240
Cdd:COG4913 359 RRRARLEALL 368
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
103-236 |
3.97e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 103 IAKLEQQKAAQERSLAaQLDAAFRQgehtgiqliLSGEESQRGQRLQAYFGYLNQARQET-IAQLKQTREEVAMQRAELE 181
Cdd:COG4913 612 LAALEAELAELEEELA-EAEERLEA---------LEAELDALQERREALQRLAEYSWDEIdVASAEREIAELEAELERLD 681
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 446118401 182 EKQSEQQTL---LYEQRAQQAKLTQALNERKKTLAGLESSIQQGQQQLSELRANESRL 236
Cdd:COG4913 682 ASSDDLAALeeqLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
33-166 |
4.32e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 39.31 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 33 HADERDQLKSIQADIAAKERAVRQKQQQRASLlAQLKKQEEAISEATRKLRETQNTLNQLNKQIDEMNASIAKLEQQKAA 112
Cdd:PRK12705 66 NQQRQEARREREELQREEERLVQKEEQLDARA-EKLDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEQAR 144
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 446118401 113 QErsLAAQLDAAFRQGEHTGIQLILsgEESQRGQRLQA---YFGYLNQARQETIAQL 166
Cdd:PRK12705 145 KL--LLKLLDAELEEEKAQRVKKIE--EEADLEAERKAqniLAQAMQRIASETASDL 197
|
|
| PRK10920 |
PRK10920 |
putative uroporphyrinogen III C-methyltransferase; Provisional |
143-218 |
4.34e-03 |
|
putative uroporphyrinogen III C-methyltransferase; Provisional
Pssm-ID: 236795 Cd Length: 390 Bit Score: 38.92 E-value: 4.34e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446118401 143 QRGQRLQAYfgylNQARQETIAQLKQTREEvamQRAELEEKQSEQQTLLYEQRAQQAKLTQALNERKKTLAGLESS 218
Cdd:PRK10920 60 QQAQNQTAT----NDALANQLTALQKAQES---QKQELEGILKQQAKALDQANRQQAALAKQLDELQQKVATISGS 128
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
31-240 |
4.84e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.25 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 31 SAHADERDQLKSIQADIAAKERAVRQKQQQRasllaqlkkqeEAISEATRKLRETQNTLNqlnkqiDEMNASIAKLEQQK 110
Cdd:PRK02224 244 EEHEERREELETLEAEIEDLRETIAETERER-----------EELAEEVRDLRERLEELE------EERDDLLAEAGLDD 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 111 AAQErSLAAQLDAAFRQGEHTgiqlilsgEESQRGQRLQAYfGYLNQAR--QETIAQLKQTREEVAMQRAELEEKQSEQQ 188
Cdd:PRK02224 307 ADAE-AVEARREELEDRDEEL--------RDRLEECRVAAQ-AHNEEAEslREDADDLEERAEELREEAAELESELEEAR 376
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446118401 189 TLLYEQRAQQAKLTQALNERKKTLAGLESSIQQGQQQLSELRANESRLRNSI 240
Cdd:PRK02224 377 EAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE 428
|
|
| COG5325 |
COG5325 |
t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion]; |
43-232 |
4.90e-03 |
|
t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion];
Pssm-ID: 227635 [Multi-domain] Cd Length: 283 Bit Score: 38.67 E-value: 4.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 43 IQADIAAKERAVRQKQQQRAslLAQLKKQEEAISEATRKLRETQNTLNQLNKQIDEMNASIAKLEQQKAAQERSLAAQLD 122
Cdd:COG5325 39 SAASVDQELTAVRRSISRLG--KVYAKHTEPSFSDKSEKEDEIDELSKKVNQDLQRCEKILKTKYKNLQSSFLQSKLLRD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 123 AAFRQGEHTGIQLILSGEESQRGQRLQAYFGYLNQ----ARQETIAQLKQTREEVAMQRAELEEKQSEQQTLLYEQRAQQ 198
Cdd:COG5325 117 LNTECMEGQRIQQKSAQFRKYQVLQAKFLRNKNNDqhplEEEEDEESLSSLGSQQTLQQQGLSNEELEYQQILITERDEE 196
|
170 180 190
....*....|....*....|....*....|....*
gi 446118401 199 -AKLTQALNERKKTLAGLESSIQQGQQQLSELRAN 232
Cdd:COG5325 197 iKNLARGIYELNEIFRDLGSLVGEQGELVDRIDFN 231
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
51-241 |
6.77e-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: 6.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 51 ERAVRQKQQQRASLLAQLKKQEEAISEATRKLRE--TQNTLNQLNKQIDEMNASIAKLEQQKAAqerslaAQLDAAFRQG 128
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAE------ARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 129 EHTGIQLILSGEESQRGQRLQayfgylnqarQETIAQLKQTREEVAMQRAELEEKQSEQQTLLYEQRAQQAKLTQALNER 208
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQ----------SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQE 310
|
170 180 190
....*....|....*....|....*....|...
gi 446118401 209 kktlagLESSIQQGQQQLSELRANESRLRNSIA 241
Cdd:COG3206 311 ------AQRILASLEAELEALQAREASLQAQLA 337
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
11-229 |
6.83e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.60 E-value: 6.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 11 AIRPIIYASVLSAGVLLCAFSAHADERDQLKSIQADIAAKERAVRQKQQQRASLLAQLKKQEEAISEATRKLRETQNTLN 90
Cdd:COG4717 271 LILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 91 QLNKQIDEMNASIAKLEQQKAAQErsLAAQLDAAFRQgehtgiQLILSGEESQRGQRLQAYF----GYLNQARQETIAQL 166
Cdd:COG4717 351 ELLREAEELEEELQLEELEQEIAA--LLAEAGVEDEE------ELRAALEQAEEYQELKEELeeleEQLEELLGELEELL 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446118401 167 KQ-TREEVAMQRAELEEKQSEQQTLLYEQRAQQAKLTQALN--ERKKTLAGLESSIQQGQQQLSEL 229
Cdd:COG4717 423 EAlDEEELEEELEELEEELEELEEELEELREELAELEAELEqlEEDGELAELLQELEELKAELREL 488
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
143-237 |
7.32e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 38.74 E-value: 7.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 143 QRGQRLQAYFGYLNQARQETI-AQLKQTREEVAMQRAELEEKQSEQQTLlyEQRAQQAKLTQALNERKKTLAGLESSIQQ 221
Cdd:COG4913 595 RRRIRSRYVLGFDNRAKLAALeAELAELEEELAEAEERLEALEAELDAL--QERREALQRLAEYSWDEIDVASAEREIAE 672
|
90
....*....|....*.
gi 446118401 222 GQQQLSELRANESRLR 237
Cdd:COG4913 673 LEAELERLDASSDDLA 688
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
38-120 |
7.67e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 38.17 E-value: 7.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 38 DQLKSIQADIAAKERAVRQKQQQRASLLAQLKKQEEAISEATRKLRETQNTLNQLNKQIDEM-NASIAKLEQQKA-AQER 115
Cdd:TIGR04320 254 NSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTaQNNLATAQAALAnAEAR 333
|
....*
gi 446118401 116 SLAAQ 120
Cdd:TIGR04320 334 LAKAK 338
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
38-239 |
8.10e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 38.46 E-value: 8.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 38 DQLKSIQADIAAKERAVRQKQQQRASLLAQLKKQEEAISEATRKLRETQNTLNQLNKQIDEM-------NASIAKLEQQK 110
Cdd:TIGR04523 370 NEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLketiiknNSEIKDLTNQD 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118401 111 AAQERSLaAQLDaAFRQGEHTGIQlILSGEESQRGQRLQAYFGYLNQARQEtIAQLKQTREEVAMQRAELEEKQSE---- 186
Cdd:TIGR04523 450 SVKELII-KNLD-NTRESLETQLK-VLSRSINKIKQNLEQKQKELKSKEKE-LKKLNEEKKELEEKVKDLTKKISSlkek 525
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446118401 187 QQTLLYEQRAQQAKLTQALNERKK-----TLAGLESSIQQGQQQLSELRANESRLRNS 239
Cdd:TIGR04523 526 IEKLESEKKEKESKISDLEDELNKddfelKKENLEKEIDEKNKEIEELKQTQKSLKKK 583
|
|
| |
