|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
182-495 |
1.50e-152 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 442.44 E-value: 1.50e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 182 QEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWELLQQQTtGSGPSSLEPCFESYISFLCKQLDSLLGERGNLEGELKS 261
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKK-GAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 262 MQDLVEDFKKKYEDEINKRTAAENEFVGLKKDVDAAFMNKVELQAKVDSLTDEVSFLRTLYEMELSQMQSHASDTSVVLS 341
Cdd:pfam00038 80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 342 MDNNRCLDLGSIIAEVRAQYEEIAQRSKSEAEALYQTKLGELQTTAGRHGDDLRNTKSEIMELNRMIQRLRAEIENVKKQ 421
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791670 422 NANLQTAIAEAEQRGEMALKDANAKLQDLQTALQKAKDDLARLLRDYQELMNVKLALDVEIATYRKLLEGEECR 495
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
16-179 |
8.30e-24 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 98.19 E-value: 8.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 16 GFSGRSAVVSGSSRMSCVARSGGAGGGACGFRSGA--GSFGSRSLYNLGSNKSISISVAAGSSRAGG----FGGGRSSCG 89
Cdd:pfam16208 1 GFSSCSAVVPSRSRRSYSSVSSSRRGGGGGGGGGGggGGFGSRSLYNLGGSKSISISVAGGGSRPGSgfgfGGGGGGGFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 90 FAGGYGGGFGGSYGGGFGGGRGVGSGFGGAGGFGGAGGFGGPGVFGGPGSFggpggfgpggfpggIQEVIVNQSLLQPLN 169
Cdd:pfam16208 81 GGFGGGGGGGFGGGGGFGGGFGGGGYGGGGFGGGGFGGRGGFGGPPCPPGG--------------IQEVTVNQSLLQPLN 146
|
170
....*....|
gi 153791670 170 VEIDPQIGQV 179
Cdd:pfam16208 147 LEIDPEIQRV 156
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
181-477 |
2.50e-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: 60.46 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 181 AQEREQ-IKTLNNKFASFIDKVRFLEQQNKVLETKWELLQQQTtgSGPSSLEPCFESYISFLCKQLDSLLGERGNLEGEL 259
Cdd:TIGR02168 672 ILERRReIEELEEKIEELEEKIAELEKALAELRKELEELEEEL--EQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 260 KSMQDLVEDfkkkYEDEINKRTAAENEFVGLKKDVDAafmNKVELQAKVDSLTDEVSFLRTLY---EMELSQMQSHASDT 336
Cdd:TIGR02168 750 AQLSKELTE----LEAEIEELEERLEEAEEELAEAEA---EIEELEAQIEQLKEELKALREALdelRAELTLLNEEAANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 337 SVVLSMDNNRCLDLGSIIAEVRAQYEEIAQRSKSEAEAL--YQTKLGELQTTAGRHG--------------DDLRNTKSE 400
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIeeLEELIEELESELEALLnerasleealallrSELEELSEE 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 401 IMELNRMIQRLRAEIENVKKQNANLQTAIAEAEQR-----------GEMALKDANAKLQDLQTALQKAKDDLARLLRDYQ 469
Cdd:TIGR02168 903 LRELESKRSELRRELEELREKLAQLELRLEGLEVRidnlqerlseeYSLTLEEAEALENKIEDDEEEARRRLKRLENKIK 982
|
....*...
gi 153791670 470 ELMNVKLA 477
Cdd:TIGR02168 983 ELGPVNLA 990
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
299-487 |
1.29e-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: 51.98 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 299 MNKVELQAKV----DSLTDEVSFL-RTLYEMELSQMQSHASDTSVVLSMDNNRCLDLGSIIAEVRAQYEEI--AQRSKSE 371
Cdd:TIGR02168 202 LKSLERQAEKaeryKELKAELRELeLALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELrlEVSELEE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 372 AEALYQTKLGELqttagrhgddlrntKSEIMELNRMIQRLRAEIENVKKQNANLQTAIAEAEQRGEMALKDAN---AKLQ 448
Cdd:TIGR02168 282 EIEELQKELYAL--------------ANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAeleEKLE 347
|
170 180 190
....*....|....*....|....*....|....*....
gi 153791670 449 DLQTALQKAKDDLARLLRDYQELMNVKLALDVEIATYRK 487
Cdd:TIGR02168 348 ELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
251-490 |
1.71e-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: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 251 ERGNLEGELKSMQDLVEDFKKKYEDEINKRTAAENEFVGLKKDVDaafmnkvELQAKVDSLTDEVSFLRTLYEMELSQMQ 330
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE-------ELSRQISALRKDLARLEAEVEQLEERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 331 shasdtsvvlsmdnnrclDLGSIIAEVRAQYEEIAQRSKSEAEALYQT--KLGELQTTAGRHGDDLRNTKSEIMELNRMI 408
Cdd:TIGR02168 751 ------------------QLSKELTELEAEIEELEERLEEAEEELAEAeaEIEELEAQIEQLKEELKALREALDELRAEL 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 409 QRLRAEIENVKKQNANLQTAIAEAEQRGEMA---LKDANAKLQDLQTALQKAKDDLARLLRDYQELMNVKLALDVEIATY 485
Cdd:TIGR02168 813 TLLNEEAANLRERLESLERRIAATERRLEDLeeqIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALL 892
|
....*
gi 153791670 486 RKLLE 490
Cdd:TIGR02168 893 RSELE 897
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
354-493 |
1.12e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 354 IAEVRAQYEEIAQRSKSEAEAL--YQTKLGELQTTAGRHGDDLRNTKSEIMELNRMIQRLRAEIENVKKQNANLQTAIAE 431
Cdd:COG1196 262 LAELEAELEELRLELEELELELeeAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791670 432 AEQRGEMA---LKDANAKLQDLQTALQKAKDDLARLLRDYQELMNVKLALDVEIATYRKLLEGEE 493
Cdd:COG1196 342 LEEELEEAeeeLEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
255-462 |
2.31e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 255 LEGELKSMQDLVEDFKKKYEDEINKRTAAE----------NEFVGLKKDVDAAFMNKVELQAKVDSLTDEVSFLRTLYEm 324
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADevleeheerrEELETLEAEIEDLRETIAETEREREELAEEVRDLRERLE- 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 325 ELSQMQSHASDTSVVLSMDNNRCL----DLGSIIAEVRAQYEEI---AQRSKSEAEAL------YQTKLGELQTTAGRHG 391
Cdd:PRK02224 290 ELEEERDDLLAEAGLDDADAEAVEarreELEDRDEELRDRLEECrvaAQAHNEEAESLredaddLEERAEELREEAAELE 369
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791670 392 DDLRNTKSEIMELNRMIQRLRAEIENVKKQNANLQTAIAEAEQRGEMALK---DANAKLQDLQTALQKAKDDLA 462
Cdd:PRK02224 370 SELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREerdELREREAELEATLRTARERVE 443
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
354-471 |
5.17e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 5.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 354 IAEVRAQYEEI-AQRSKSEAE-ALYQTKLGELQTTAGRHGDDLRNTKSEIMELNRMIQRLRAEIENVKKQNANLQTAIAE 431
Cdd:COG1196 248 LEELEAELEELeAELAELEAElEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 153791670 432 AEQRGEMA---LKDANAKLQDLQTALQKAKDDLARLLRDYQEL 471
Cdd:COG1196 328 LEEELEELeeeLEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
393-474 |
5.74e-05 |
|
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: 45.91 E-value: 5.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 393 DLRNTKSEIMELNRMIQRLRAEIENVKKQNANLQTAIAEAEQR---GEMALKDANAKLQDLQTALQKAKDDLARLLRDYQ 469
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELA 107
|
....*
gi 153791670 470 ELMNV 474
Cdd:COG4942 108 ELLRA 112
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
235-457 |
6.75e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 6.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 235 ESYISFLCKQLDSLLGERGNLEGELKSMQDLVEDFKKKYEDEINKRTAAENEFVGLKKDVDaafmnkvELQAKVDSLTDE 314
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA-------EAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 315 VS-FLRTLYEMELSqmqshASDTSVVLSMDN-----NRCLDLGSIIAEVRAQYEEI--AQRSKSEAEALYQTKLGELQTT 386
Cdd:COG3883 88 LGeRARALYRSGGS-----VSYLDVLLGSESfsdflDRLSALSKIADADADLLEELkaDKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791670 387 AGRHGDDLRNTKSEIMELNRMIQRLRAEIENVKKQNANLQTAIAEAEQRGEMALKDANAKLQDLQTALQKA 457
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
392-471 |
7.01e-05 |
|
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: 45.53 E-value: 7.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 392 DDLRNTKSEIMELNRMIQRLRAEIENVKKQNANLQTAIAEAEQRgemaLKDANAKLQDLQTALQKAKDDLARLLRDYQEL 471
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELAELEKEIAEL 95
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
241-471 |
7.48e-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: 46.21 E-value: 7.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 241 LCKQLDSLLGERGNLEGELKSMQDLVEDFKKKYEDeinkrtaAENEFVGLKKDVDAAFMNKVELQAKVDSLTDEVSFLRT 320
Cdd:TIGR02169 686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGE-------IEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 321 L---YEMELSQMQSHASdtSVVLSMDNNRCLDLGSIIAEVRAQYEEI-AQRSKSEA--EALYQtKLGELQTTAGRHGDDL 394
Cdd:TIGR02169 759 ElkeLEARIEELEEDLH--KLEEALNDLEARLSHSRIPEIQAELSKLeEEVSRIEArlREIEQ-KLNRLTLEKEYLEKEI 835
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791670 395 RNTKSEIMELNRMIQRLRAEIENVKKQNANLQTAIAEAEqrgeMALKDANAKLQDLQTALQKAKDDLARLLRDYQEL 471
Cdd:TIGR02169 836 QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE----AALRDLESRLGDLKKERDELEAQLRELERKIEEL 908
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
354-490 |
7.54e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 7.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 354 IAEVRAQYEEiAQRSKSEAEALY---QTKLGELQTTAGRHGDD--LRNTKSEIMELNRMIQRLRA-------EIENVKKQ 421
Cdd:COG3206 221 LSELESQLAE-ARAELAEAEARLaalRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSArytpnhpDVIALRAQ 299
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791670 422 NANLQTAIAEAEQRG----EMALKDANAKLQDLQTALQKAKDDLARLLRDYQELMNVKLALDVEIATYRKLLE 490
Cdd:COG3206 300 IAALRAQLQQEAQRIlaslEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQ 372
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
354-497 |
2.12e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 354 IAEVRAQYEEIAQ--RSKSEAEALYQTKLGELQTTAGRHGDDLRNTKSEIMELNRMIQRLRAEIENVKKQNANLQTAIAE 431
Cdd:TIGR02168 679 IEELEEKIEELEEkiAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153791670 432 AEQRGE----------MALKDANAKLQDLQTALQKAKDDLARLLRDYQELMNVKLALDVEIATYRKLLEGEECRMS 497
Cdd:TIGR02168 759 LEAEIEeleerleeaeEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
238-490 |
2.19e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 238 ISFLCKQLDSLLGERGNLEGELKSMQDLVEDfkkkYEDEINKRTAAENEFVGLKKDVDAAFmnkVELQAKVDSLTDEVSF 317
Cdd:TIGR02168 227 LALLVLRLEELREELEELQEELKEAEEELEE----LTAELQELEEKLEELRLEVSELEEEI---EELQKELYALANEISR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 318 LRT---LYEMELSQMQSHASDTSVVLSMDNNRCLDLGSIIAEVRAQYEEIAQRSKSEAEAL------------------- 375
Cdd:TIGR02168 300 LEQqkqILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELeeleaeleelesrleelee 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 376 ----YQTKLGELQTTAGRHGDDLRNTKSEIMELNRMIQRLRAEIE--NVKKQNANLQTAIAEAEQRGEMaLKDANAKLQD 449
Cdd:TIGR02168 380 qletLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEelLKKLEEAELKELQAELEELEEE-LEELQEELER 458
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 153791670 450 LQTALQKAKDDLARLLRDYQELMNVKLALDVEIATYRKLLE 490
Cdd:TIGR02168 459 LEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
235-469 |
3.19e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 235 ESYISFLCKQLDSLlgergnlEGELKSMQDLVEDFKKKyedeinkrtaaeNEFVGLKKDVDAAFMNKVELQAKVDSLTDE 314
Cdd:COG3206 174 RKALEFLEEQLPEL-------RKELEEAEAALEEFRQK------------NGLVDLSEEAKLLLQQLSELESQLAEARAE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 315 VSFLRTLYEmELSQMQSHASDTSVVLSMDnnrcldlgSIIAEVRAQYEEIaqrskseaealyQTKLGELQTTAGRHGDDL 394
Cdd:COG3206 235 LAEAEARLA-ALRAQLGSGPDALPELLQS--------PVIQQLRAQLAEL------------EAELAELSARYTPNHPDV 293
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791670 395 RNTKSEIMELNRMIQRLRAEIEnvkkqnANLQTAIAEAEQRgEMALKDANAKLQDLQTALQKAKDDLARLLRDYQ 469
Cdd:COG3206 294 IALRAQIAALRAQLQQEAQRIL------ASLEAELEALQAR-EASLQAQLAQLEARLAELPELEAELRRLEREVE 361
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
182-495 |
4.14e-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: 43.57 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 182 QEREQ-IKTLNNKFASFIDKVRFLEQQNKVLETKWELLQQQTTGSGPSSLEPC-FESYISFLCKQLDS---LLGERGNLE 256
Cdd:pfam15921 506 QEKERaIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAeKDKVIEILRQQIENmtqLVGQHGRTA 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 257 GELksmqdLVEdfKKKYEDEINKRTAAENEFVGLKKDVDAAFMnkvELQAKVDSLTDEVSFLRTLYEMELSQMQSHASDT 336
Cdd:pfam15921 586 GAM-----QVE--KAQLEKEINDRRLELQEFKILKDKKDAKIR---ELEARVSDLELEKVKLVNAGSERLRAVKDIKQER 655
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 337 SVVLSMDNNRCLDLGSIIAEvraqYEEIAQ--RSKSEAEALYQTKLGELQTTAGRHGDDLRNTKSEI-----------ME 403
Cdd:pfam15921 656 DQLLNEVKTSRNELNSLSED----YEVLKRnfRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMegsdghamkvaMG 731
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 404 LNRMIQRLRAEIENVKKQNANLQTAIAEAEQRGEMaLKDANAKLQDLQTALQKAKDDLA---RLLRDYQELMNVKLAlDV 480
Cdd:pfam15921 732 MQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHF-LKEEKNKLSQELSTVATEKNKMAgelEVLRSQERRLKEKVA-NM 809
|
330
....*....|....*
gi 153791670 481 EIATYRKLLEGEECR 495
Cdd:pfam15921 810 EVALDKASLQFAECQ 824
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
234-493 |
6.04e-04 |
|
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: 43.13 E-value: 6.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 234 FESYISFLCKQLDSLLGERGNLEgELKSMQDLVEDFkkkyedeinkrtaaenEFVGLKKDVDAAFMNKVELQAKVDSLTD 313
Cdd:TIGR02169 189 LDLIIDEKRQQLERLRREREKAE-RYQALLKEKREY----------------EGYELLKEKEALERQKEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 314 EVSFLrtlyEMELSQMQSHASDTSVVLSMDNNRCLDLGS-IIAEVRAQYEEI-AQRSKSE-AEALYQTKLGELQTTagrh 390
Cdd:TIGR02169 252 ELEKL----TEEISELEKRLEEIEQLLEELNKKIKDLGEeEQLRVKEKIGELeAEIASLErSIAEKERELEDAEER---- 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 391 gddLRNTKSEIMELNRMIQRLRAEIENVKKQNANLQTAIAEAEQRGEMALKDANA----------KLQDLQTALQKAKDD 460
Cdd:TIGR02169 324 ---LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEvdkefaetrdELKDYREKLEKLKRE 400
|
250 260 270
....*....|....*....|....*....|...
gi 153791670 461 LARLLRDYQELMNVKLALDVEIATYRKLLEGEE 493
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELADLNAAIAGIE 433
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
372-470 |
6.17e-04 |
|
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: 42.41 E-value: 6.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 372 AEALYQTKLGELQTTAGRHGDDLRNTKSEImelnrmiQRLRAEIENVKKQNANLQtaiAEAEQRGEMALKDANAKLQDLQ 451
Cdd:TIGR04320 262 KLATAQADLAAAQTALNTAQAALTSAQTAY-------AAAQAALATAQKELANAQ---AQALQTAQNNLATAQAALANAE 331
|
90
....*....|....*....
gi 153791670 452 TALQKAKDDLARLLRDYQE 470
Cdd:TIGR04320 332 ARLAKAKEALANLNADLAK 350
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
349-492 |
6.87e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 6.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 349 DLGSIIAEVRAQYEEIAQRsKSEAEAL-----YQTKLGELQTTAGRHGD---DLRNTKSEIMELNRMIQRLRAEIENVKK 420
Cdd:COG4913 628 EAEERLEALEAELDALQER-REALQRLaeyswDEIDVASAEREIAELEAeleRLDASSDDLAALEEQLEELEAELEELEE 706
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791670 421 QNANLQTAIAEAEQRgemaLKDANAKLQDLQTALQKAKDDLARLLRDYQELMNVKLALDVEIATYRKLLEGE 492
Cdd:COG4913 707 ELDELKGEIGRLEKE----LEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEER 774
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
243-463 |
8.89e-04 |
|
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: 42.06 E-value: 8.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 243 KQLDSLLGERGNLEGELKSMQDLVEDFKKKYEDEINKRTAAENEFVGLKKDVDAAFMNKVELQAKVDSLTDEVS-FLRTL 321
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAeLLRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 322 YEMelsqmqSHASDTSVVLSMDNnrcldlgSIIAEVRAQY-EEIAQRSKSEAEALyQTKLGELQTTAGRHGDDLRNTKSE 400
Cdd:COG4942 114 YRL------GRQPPLALLLSPED-------FLDAVRRLQYlKYLAPARREQAEEL-RADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791670 401 IMELNRMIQRLRAEIENVKKQNANLQTAIAEAEQRGEmALKDANAKLQDLQTALQKAKDDLAR 463
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELA-ELQQEAEELEALIARLEAEAAAAAE 241
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
354-487 |
1.23e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 354 IAEVRAQYEEIAQRsKSEAEALYQTKLGELQTTAGRHGDDlrntkseimELNRMIQRLRAEIENVKKQNANLQTAIAEAE 433
Cdd:COG4717 390 ALEQAEEYQELKEE-LEELEEQLEELLGELEELLEALDEE---------ELEEELEELEEELEELEEELEELREELAELE 459
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 153791670 434 QRGEMALKDanAKLQDLQTALQKAKDDLARLLRDYQELMNVKLALDVEIATYRK 487
Cdd:COG4717 460 AELEQLEED--GELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
408-469 |
2.39e-03 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 38.84 E-value: 2.39e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791670 408 IQRLRAEIENVKKQNANLQTAIAEAEQRgemaLKDANAKLQDLQTALQKAKDDLARLLRDYQ 469
Cdd:pfam11559 68 IERLQSKIERLKTQLEDLERELALLQAK----ERQLEKKLKTLEQKLKNEKEELQRLKNALQ 125
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
180-429 |
2.46e-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: 41.16 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 180 KAQEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWELLQQQTtgsgpSSLEPCFE---SYISFLCKQLDSLLGERGNLE 256
Cdd:TIGR04523 379 NQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEK-----ELLEKEIErlkETIIKNNSEIKDLTNQDSVKE 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 257 GELKSMQDLVEDFKKK---YEDEINK-RTAAEN---EFVGLKKDVDAAFMNKVELQAKVDSLTDEVSFLRT---LYEMEL 326
Cdd:TIGR04523 454 LIIKNLDNTRESLETQlkvLSRSINKiKQNLEQkqkELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEkieKLESEK 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 327 SQMQSHASD-TSVVLSMDNNrcLDLGSIIAEVRAQYEEIAQrSKSEAEALyQTKLGELQTTAGRHGDDLRNTKSEIMELN 405
Cdd:TIGR04523 534 KEKESKISDlEDELNKDDFE--LKKENLEKEIDEKNKEIEE-LKQTQKSL-KKKQEEKQELIDQKEKEKKDLIKEIEEKE 609
|
250 260
....*....|....*....|....
gi 153791670 406 RMIQRLRAEIENVKKQNANLQTAI 429
Cdd:TIGR04523 610 KKISSLEKELEKAKKENEKLSSII 633
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
171-493 |
2.68e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.04 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 171 EIDPQ-IGQVKAQEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWELLQQQT------TGSGPSSLEPCFESYisflCK 243
Cdd:PRK01156 401 EIDPDaIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSvcpvcgTTLGEEKSNHIINHY----NE 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 244 QLDSLLGERGNLEGELKSMQDLVEDFKKKYE----DEINKRTAAENEFVGLKKDVDAAFMNKVELQAKVDSLTDEVSFLR 319
Cdd:PRK01156 477 KKSRLEEKIREIEIEVKDIDEKIVDLKKRKEylesEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYK 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 320 TLYEMELSQMQSHASDTSVVLS---MDNNRcldlgSIIAEVRAQYEEIAQRSKS------EAEALYQTKLGELQTTAgrh 390
Cdd:PRK01156 557 SLKLEDLDSKRTSWLNALAVISlidIETNR-----SRSNEIKKQLNDLESRLQEieigfpDDKSYIDKSIREIENEA--- 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 391 gDDLRNTKSEIMELNRMIQRLRAEIENVKKQNANLQtAIAEAEQRGEMALKDANAKLQDLQTALQKAKDDLARLLRDYQE 470
Cdd:PRK01156 629 -NNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEID-SIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEI 706
|
330 340
....*....|....*....|...
gi 153791670 471 LMNVKLALDVEIATYRKLLEGEE 493
Cdd:PRK01156 707 LRTRINELSDRINDINETLESMK 729
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
283-487 |
5.19e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 283 AENEFVGLKKDVDAAFMNKVELQAKVDSLTDEVSFLRTLY---EMELSQMQSHASDTSVvlsmdnnrclDLGSIIAEVRA 359
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYnelQAELEALQAEIDKLQA----------EIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 360 QYEEIAQRSKSEAEALYQTKLGELQTTAGRHGDDLRNTK--SEIMELNR-MIQRLRAEIENVKKQNANLQTAIAEAEQrg 436
Cdd:COG3883 84 RREELGERARALYRSGGSVSYLDVLLGSESFSDFLDRLSalSKIADADAdLLEELKADKAELEAKKAELEAKLAELEA-- 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 153791670 437 emALKDANAKLQDLQTALQKAKDDLARLLRDYQELMNVKLALDVEIATYRK 487
Cdd:COG3883 162 --LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
185-490 |
5.21e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 185 EQIKTLNNKFASFIDKVRFLEQQNKVLETKWELLQQQTtgsgpSSLEPCFESyISFLCKQLDSLLGERGNLEGELKSMQD 264
Cdd:PRK03918 193 ELIKEKEKELEEVLREINEISSELPELREELEKLEKEV-----KELEELKEE-IEELEKELESLEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 265 LVEDFKKKYEdEINKRTAAENEfvgLKKDVDaAFMNKVELQAKVDSLTDEVSFLRTLYEMELSQMQSHASDtsvvLSMDN 344
Cdd:PRK03918 267 RIEELKKEIE-ELEEKVKELKE---LKEKAE-EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE----LEEKE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 345 NRCLDLGSIIAEVRAQYEEIAQRSKSEAEALyqTKLGELQTTAGRHG-----------DDLRNTKSEIMElnrMIQRLRA 413
Cdd:PRK03918 338 ERLEELKKKLKELEKRLEELEERHELYEEAK--AKKEELERLKKRLTgltpeklekelEELEKAKEEIEE---EISKITA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 414 EIENVKKQNANLQTAIAE----------------AEQRGEMaLKDANAKLQDLQTALQKAKDDLARLLRDYQELMNVkLA 477
Cdd:PRK03918 413 RIGELKKEIKELKKAIEElkkakgkcpvcgreltEEHRKEL-LEEYTAELKRIEKELKEIEEKERKLRKELRELEKV-LK 490
|
330
....*....|...
gi 153791670 478 LDVEIATYRKLLE 490
Cdd:PRK03918 491 KESELIKLKELAE 503
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
348-493 |
5.66e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.92 E-value: 5.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 348 LDLGSIIAEVRAQYEEIAQRSKSEAEAlyQTKLGELQTTAGRHGDDLRNTKSEIMELNRMIQRLRAEIENVKKQNANLQT 427
Cdd:COG1196 225 LEAELLLLKLRELEAELEELEAELEEL--EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ 302
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153791670 428 AIAEAEQRG---EMALKDANAKLQDLQTALQKAKDDLARLLRDYQELMNVKLALDVEIATYRKLLEGEE 493
Cdd:COG1196 303 DIARLEERRrelEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
349-493 |
6.42e-03 |
|
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: 39.36 E-value: 6.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 349 DLGSIIAEVRAQYEEIAQRSKSEAEALYQtkLGELQTTAGRHGDDLRNTKSEIMELNRMIQRLRAEIENVKKQNANLQTA 428
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQ--LAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153791670 429 IAE-------AEQRGEMAL-------KDANAKLQDLQTALQKAKDDLARLLRDYQELMNVKLALDVEIATYRKLLEGEE 493
Cdd:COG4942 106 LAEllralyrLGRQPPLALllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELE 184
|
|
| GrpE |
COG0576 |
Molecular chaperone GrpE (heat shock protein HSP-70) [Posttranslational modification, protein ... |
398-490 |
6.86e-03 |
|
Molecular chaperone GrpE (heat shock protein HSP-70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440341 [Multi-domain] Cd Length: 147 Bit Score: 37.44 E-value: 6.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 398 KSEIMELNRMIQRLRAEIENVKKQnanlqtaiaeAEQRGEMALKDANAKL-QDLQTALqkakDDLARLLRDYQELMNVK- 475
Cdd:COG0576 5 EAELAELKDRLLRLQAEFENYRKR----------TEREREEARKYALEKLaEDLLPVL----DNLERALAAAEEDEDVKs 70
|
90
....*....|....*
gi 153791670 476 LALDVEiATYRKLLE 490
Cdd:COG0576 71 LLEGVE-MTLKQLLD 84
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
348-493 |
7.86e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.46 E-value: 7.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 348 LDLGSIIAEVraqyeeIAQRSKSEA-EALYQTKLGELQTTAGRHGD----DLRNTKSEIMELNRMIQRLRAEienvkkqN 422
Cdd:COG2433 363 VDRDEVKARV------IRGLSIEEAlEELIEKELPEEEPEAEREKEheerELTEEEEEIRRLEEQVERLEAE-------V 429
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791670 423 ANLQTAIAEAEQRgemalkdanakLQDLQTALQKAKDDLARLLRDYQELMnvklALDVEIATYRKLLEGEE 493
Cdd:COG2433 430 EELEAELEEKDER-----------IERLERELSEARSEERREIRKDREIS----RLDREIERLERELEEER 485
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
355-462 |
7.99e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.51 E-value: 7.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 355 AEVRAQYEEIAQRSKSEAE-ALYQTKLGELQTTAgrhgDDLRNTKSEIMELNRMIQRLRAEIENVKKQNANLQTAIAEA- 432
Cdd:PRK11281 39 ADVQAQLDALNKQKLLEAEdKLVQQDLEQTLALL----DKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEEt 114
|
90 100 110
....*....|....*....|....*....|.
gi 153791670 433 -EQRGEMALKDANAKLQDLQTALQKAKDDLA 462
Cdd:PRK11281 115 rETLSTLSLRQLESRLAQTLDQLQNAQNDLA 145
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
370-493 |
8.56e-03 |
|
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: 38.37 E-value: 8.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 370 SEAEALYQ-----TKLGELQTTAGRHGDDLRNTKSEIMELNRMIQRLRAEIENVKKQNANLQTAIAEAEQRgemaLKDAN 444
Cdd:COG1579 4 EDLRALLDlqeldSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR----IKKYE 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 153791670 445 AKLQDLQT-----ALQKAKDDLARLLRDYQELMnvkLALDVEIATYRKLLEGEE 493
Cdd:COG1579 80 EQLGNVRNnkeyeALQKEIESLKRRISDLEDEI---LELMERIEELEEELAELE 130
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
354-487 |
9.50e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 9.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 354 IAEVRAQYEEIAQRsKSEAEALYQTKLGELQTTAGRH----GDDLRNTKSEIMELNRMIQRLRAEIENVKKQNANLQTAI 429
Cdd:COG4913 297 LEELRAELARLEAE-LERLEARLDALREELDELEAQIrgngGDRLEQLEREIERLERELEERERRRARLEALLAALGLPL 375
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 153791670 430 AEAEQRGEMALKDANAKLQDLQTALQKAKDDLARLLRDYQELMNVKLALDVEIATYRK 487
Cdd:COG4913 376 PASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
345-493 |
9.61e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.15 E-value: 9.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 345 NRCLDlgsIIAEVRAQYE------EIAQR---------------------SKSEAEALYQTKLGELQTTAGRHGDDLRNT 397
Cdd:COG1196 189 ERLED---ILGELERQLEplerqaEKAERyrelkeelkeleaellllklrELEAELEELEAELEELEAELEELEAELAEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791670 398 KSEIMELNRMIQRLRAEIENVKKQNANLQTAIAEAEQRGEMA---LKDANAKLQDLQTALQKAKDDLARLLRDYQELMNV 474
Cdd:COG1196 266 EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLeerRRELEERLEELEEELAELEEELEELEEELEELEEE 345
|
170
....*....|....*....
gi 153791670 475 KLALDVEIATYRKLLEGEE 493
Cdd:COG1196 346 LEEAEEELEEAEAELAEAE 364
|
|
| |
