|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
130-443 |
5.80e-140 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 406.23 E-value: 5.80e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 130 QEREQIKALNNKFASFIDKVRFLEQQNQVLETKWELLQQLDLNNcKNNLEPILEGYISNMRKQLETLSGDRVRLDSELRN 209
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAE-PSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 210 VRDVVEDYKKKYEEEINRRTAAENEFVLLKKDVDAAYANKVELQAKVDTMDQDIKFFKCLFEAEMAQIQSHISDMSVILS 289
Cdd:pfam00038 80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 290 MDNNRNLDLDSIIDEVRAQYEEIALKSKAEAEALYQTKFQELQLAAGRHGDDLKNTKNEITELTRFIQRLRSEIENAKKQ 369
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958791358 370 ASNLETAIADAEQRGDSALKDARAKLDELEGALHQAKEELARMLREYQELMSLKLALDMEIATYRKLLESEECR 443
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
15-127 |
2.00e-30 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 115.91 E-value: 2.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 15 GFSGCSAVLSGGSSSSYRAGGKGLSGGFG------------SRSLYSLGGPRSITLNMAS-------------------- 62
Cdd:pfam16208 1 GFSSCSAVVPSRSRRSYSSVSSSRRGGGGggggggggggfgSRSLYNLGGSKSISISVAGggsrpgsgfgfgggggggfg 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958791358 63 -------------GSGKNGGFGFGRNRASGFAGSIFGSvALGPVCPtVCPPGGIHQVTVNESLLAPLNVELDPEIQKV 127
Cdd:pfam16208 81 ggfgggggggfggGGGFGGGFGGGGYGGGGFGGGGFGG-RGGFGGP-PCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
119-419 |
3.01e-10 |
|
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: 63.16 E-value: 3.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 119 ELDPEIQKVRAqEREQIKALNNKFASFIDKVRfleQQNQVLET-KWELLQQLDLNNCKNNLE-PILEGYISNMRKQLETL 196
Cdd:TIGR02169 167 EFDRKKEKALE-ELEEVEENIERLDLIIDEKR---QQLERLRReREKAERYQALLKEKREYEgYELLKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 197 SGDRVRLDSELRNVRDVVEDYKKKYEE------EINRRTAA--ENEFVLLKKDVDaayankvELQAKVDTMDQDIKFFKC 268
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLEEieqlleELNKKIKDlgEEEQLRVKEKIG-------ELEAEIASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 269 LFEAEMAQIQSHISDMSVILSmdnnRNLDLDSIIDEVRAQYEEI--ALKSKAEAEALYQTKFQELQLAAGRHGDDLKN-- 344
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLA----EIEELEREIEEERKRRDKLteEYAELKEELEDLRAELEEVDKEFAETRDELKDyr 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 345 -----TKNEITELTRFIQRLRSEIENAKKQASNLETAIADAEQRG---DSALKDARAKLDELEGALHQAKEELARMLREY 416
Cdd:TIGR02169 392 eklekLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKInelEEEKEDKALEIKKQEWKLEQLAADLSKYEQEL 471
|
...
gi 1958791358 417 QEL 419
Cdd:TIGR02169 472 YDL 474
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
153-448 |
7.73e-10 |
|
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: 61.61 E-value: 7.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 153 EQQNQVLETKWELLqqldlnNCKNNLEpILEGYISNMRKQLETLSGDRVRLDSELRNVRDVVEDYKKKYEEEINRRTAAE 232
Cdd:TIGR02168 667 KTNSSILERRREIE------ELEEKIE-ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 233 NEFVLLKKDVDAAYANKVELQAKVDTMDQDIKFFKCLF---EAEMAQIQSHISDMsvilsmdNNRNLDLDSIIDEVRAQY 309
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELaeaEAEIEELEAQIEQL-------KEELKALREALDELRAEL 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 310 EEIalkskaeaealyQTKFQELQLAAGRHGDDLKNTKNEITELTRFIQRLRSEIENAKKQASNLETAIADAEQRGDSALK 389
Cdd:TIGR02168 813 TLL------------NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLN 880
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958791358 390 D----------ARAKLDELEGALHQAKEELARMLREYQELMSLKLALDMEIATYRKLLESEECRMSGEY 448
Cdd:TIGR02168 881 ErasleealalLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEY 949
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
117-409 |
2.29e-09 |
|
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: 60.03 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 117 NVELDPEIQkvraQEREQIKALNNKFASFIDKVRFLEQQNQVLETKweLLQQLDLNNCKNNLEPILEGYISNMRKQLETL 196
Cdd:TIGR04523 358 NSEKQRELE----EKQNEIEKLKKENQSYKQEIKNLESQINDLESK--IQNQEKLNQQKDEQIKKLQQEKELLEKEIERL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 197 SGDRVRLDSELRNVRDVVEDYKKKYEEEINRRTAAEN---------------------EFVLLKKDVDAAYANKVELQAK 255
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETqlkvlsrsinkikqnleqkqkELKSKEKELKKLNEEKKELEEK 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 256 VDTMDQDIKFFKC---LFEAEMAQIQSHISDM-SVILSMDNNrnLDLDSIIDEVRAQYEEIAlKSKAEAEALYQTKFqEL 331
Cdd:TIGR04523 512 VKDLTKKISSLKEkieKLESEKKEKESKISDLeDELNKDDFE--LKKENLEKEIDEKNKEIE-ELKQTQKSLKKKQE-EK 587
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958791358 332 QLAAGRHGDDLKNTKNEITELTRFIQRLRSEIENAKKQASNLETAIadaeqrgdsalKDARAKLDELEGALHQAKEEL 409
Cdd:TIGR04523 588 QELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSII-----------KNIKSKKNKLKQEVKQIKETI 654
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
147-433 |
3.91e-09 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 58.87 E-value: 3.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 147 DKVRFLEQQNQVLETKWELL-QQLDLNNcknnlepileGYISNMRKQletlSGDRVrldSELRNVRDVVEDYKKKYEEEI 225
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIqQQIKTYN----------KNIEEQRKK----NGENI---ARKQNKYDELVEEAKTIKAEI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 226 NRRTAAENEFVLLKKDVDAAYAN----KVELQAKVDTMDQDIKFFK-------ClfeaeMAQIQSHisdmsvilsmdnnr 294
Cdd:PHA02562 237 EELTDELLNLVMDIEDPSAALNKlntaAAKIKSKIEQFQKVIKMYEkggvcptC-----TQQISEG-------------- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 295 nldlDSIIDEVRAQYEEIalkskaeaealyQTKFQELQlaagRHGDDLKNTKNEITELTRFIQRLRSEIENAKKQASNLE 374
Cdd:PHA02562 298 ----PDRITKIKDKLKEL------------QHSLEKLD----TAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLV 357
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958791358 375 TAIadaeqrgdsalKDARAKLDELEGALHQAKEELARMLREYQELMSLKLALDMEIATY 433
Cdd:PHA02562 358 DKA-----------KKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHR 405
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
191-419 |
1.30e-08 |
|
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: 57.76 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 191 KQLETLSGDRVRLDSELRNVRDVVEDYKKKYEE---EINRRTAAENEFVL----LKKDVDAAYANKVELQAKVDTMDQDI 263
Cdd:TIGR02168 225 LELALLVLRLEELREELEELQEELKEAEEELEEltaELQELEEKLEELRLevseLEEEIEELQKELYALANEISRLEQQK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 264 KFFKclfeAEMAQIQSHISDMSVILSMDNNRNLDLDSIIDEVRAQYEEIALKSKAEAEAL--YQTKFQELQLAAGRHGDD 341
Cdd:TIGR02168 305 QILR----ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELeeLEAELEELESRLEELEEQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 342 LKNTKNEITELTRFIQRLRSEIENAKKQASNLETAIADAEQRG--------DSALKDARAKLDELEGALHQAKEELARML 413
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIeellkkleEAELKELQAELEELEEELEELQEELERLE 460
|
....*.
gi 1958791358 414 REYQEL 419
Cdd:TIGR02168 461 EALEEL 466
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
119-438 |
2.57e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 119 ELDPEIQKVRAQER-----EQIKALNNKFASFIDKVRFLEQQNQVLETKWELLQQL---------DLNNCKNNLEPILEG 184
Cdd:COG4717 113 ELREELEKLEKLLQllplyQELEALEAELAELPERLEELEERLEELRELEEELEELeaelaelqeELEELLEQLSLATEE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 185 YISNMRKQLETLSGDRVRLDSELRNVRDVVEDYKKKYEEEINRRTAAENE---------------FVLLKKDVDAAYANK 249
Cdd:COG4717 193 ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEerlkearlllliaaaLLALLGLGGSLLSLI 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 250 VEL---------------------QAKVDTMDQDIKFFKCLFEAEMAQIQSHISDMSVILSMDNNRNLDLDSIIDEVRAQ 308
Cdd:COG4717 273 LTIagvlflvlgllallflllareKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEL 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 309 YEEIA-LKSKAEAEALYQTKFQELQLA----------AGRHGDDLKNTKNEITELTRFIQRLRSEI---------ENAKK 368
Cdd:COG4717 353 LREAEeLEEELQLEELEQEIAALLAEAgvedeeelraALEQAEEYQELKEELEELEEQLEELLGELeellealdeEELEE 432
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958791358 369 QASNLETAIADAEQRgdsaLKDARAKLDELEGALHQAKE--ELARMLREYQELMSLKLALDMEIATYRKLLE 438
Cdd:COG4717 433 ELEELEEELEELEEE----LEELREELAELEAELEQLEEdgELAELLQELEELKAELRELAEEWAALKLALE 500
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
217-435 |
6.07e-08 |
|
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: 55.83 E-value: 6.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 217 YKKKYEEEINR-RTAAEN----EFVL--LKKDVdaayaNKVELQAKVDTMDQDIKffkclfeAEMAQIQSHISDMSVils 289
Cdd:TIGR02168 170 YKERRKETERKlERTRENldrlEDILneLERQL-----KSLERQAEKAERYKELK-------AELRELELALLVLRL--- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 290 MDNNRNLD-LDSIIDEVRAQYEEIALKSKAEAEALYQTK--FQELQLAAGRHGDDLKNTKNEITELTRFIQRLRSEIENA 366
Cdd:TIGR02168 235 EELREELEeLQEELKEAEEELEELTAELQELEEKLEELRleVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL 314
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958791358 367 KKQASNLETAIADAEQRGDSA---LKDARAKLDELEGALHQAKEELARMLREYQELMSLKLALDMEIATYRK 435
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELaeeLAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
131-441 |
2.14e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.48 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 131 EREQIKALNNKFASFIDKVRFLEQQNQVLETK---WELLQQLDLNNCKNNLEPILEGYISNMRKQLETLSGDRVRL---- 203
Cdd:COG3206 62 EPQSSDVLLSGLSSLSASDSPLETQIEILKSRpvlERVVDKLNLDEDPLGEEASREAAIERLRKNLTVEPVKGSNVieis 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 204 ----DSEL--RNVRDVVEDYKKKYEEEINRRTAAENEFV-----LLKKDVDAAYANKVELQAKVDTMDqdikffkclFEA 272
Cdd:COG3206 142 ytspDPELaaAVANALAEAYLEQNLELRREEARKALEFLeeqlpELRKELEEAEAALEEFRQKNGLVD---------LSE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 273 EMAQIQSHISDMSVILSMDNNRNLDLDSIIDEVRAQyeeIALKSKAEAEALYQTKFQELQlaagrhgDDLKNTKNEITEL 352
Cdd:COG3206 213 EAKLLLQQLSELESQLAEARAELAEAEARLAALRAQ---LGSGPDALPELLQSPVIQQLR-------AQLAELEAELAEL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 353 -TRF------IQRLRSEIENAKKQasnLETAIADAEQRGDSALKDARAKLDELEGALHQAKEELARMLREYQELMSLKLA 425
Cdd:COG3206 283 sARYtpnhpdVIALRAQIAALRAQ---LQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLERE 359
|
330
....*....|....*.
gi 1958791358 426 LDMEIATYRKLLESEE 441
Cdd:COG3206 360 VEVARELYESLLQRLE 375
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
313-417 |
2.39e-07 |
|
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: 52.84 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 313 ALKSKAEAEALYQTKFQELQLAAGRHGDDLKNTKNEITELTRFIQRLRSEIENAKKQASNLETAIADAEQRgdsaLKDAR 392
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE----LAELE 89
|
90 100
....*....|....*....|....*
gi 1958791358 393 AKLDELEGALHQAKEELARMLREYQ 417
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRALY 114
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
189-419 |
3.32e-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: 53.15 E-value: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 189 MRKQLETLSGDRVRLDSELRNVRDVVEDYKKKYEEEINRRTAAENEFVLLKKDVDAAYANKVELQAKVDTMDQDIKFFKc 268
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK- 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 269 lfeAEMAQIQSHISDMSVILS-----MDNNRNLDLDSIIDEVRAQYEEIA------LKSKAEAEALYQTKFQELQLAAgr 337
Cdd:TIGR02169 758 ---SELKELEARIEELEEDLHkleeaLNDLEARLSHSRIPEIQAELSKLEeevsriEARLREIEQKLNRLTLEKEYLE-- 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 338 hgDDLKNTKNEITELTRFIQRLRSEIENAKKQASNLETAIADAEqrgdSALKDARAKLDELEGALHQAKEELARMLREYQ 417
Cdd:TIGR02169 833 --KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE----AALRDLESRLGDLKKERDELEAQLRELERKIE 906
|
..
gi 1958791358 418 EL 419
Cdd:TIGR02169 907 EL 908
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
302-441 |
7.79e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 7.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 302 IDEVRAQYEEIALKSKAEAEAL--YQTKFQELQLAAGRHGDDLKNTKNEITELTRFIQRLRSEIENAKKQASNLETAIAD 379
Cdd:COG1196 262 LAELEAELEELRLELEELELELeeAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958791358 380 AEQRGDSA---LKDARAKLDELEGALHQAKEELARMLREYQELMSLKLALDMEIATYRKLLESEE 441
Cdd:COG1196 342 LEEELEEAeeeLEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
170-428 |
2.70e-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: 50.45 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 170 DLNNCKNNLEpILEGYISNMRKQLETLSGDRVRLdselrnvrdvvEDYKKKYEEEInrrtaaENEFVLLKKDVDAAYANK 249
Cdd:TIGR02169 178 ELEEVEENIE-RLDLIIDEKRQQLERLRREREKA-----------ERYQALLKEKR------EYEGYELLKEKEALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 250 VELQAKVDTMdqdikffkclfEAEMAQIQSHISDmsvilsmdnnRNLDLDSIIDEVRAQYEEIALKSKAEAEALyQTKFQ 329
Cdd:TIGR02169 240 EAIERQLASL-----------EEELEKLTEEISE----------LEKRLEEIEQLLEELNKKIKDLGEEEQLRV-KEKIG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 330 ELQLAAGRHGDDLKNTKNEITELTRFIQRLRSEIENAKKQASNLETAIADAEQRGDS---ALKDARAKLDELEGALhQAK 406
Cdd:TIGR02169 298 ELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKlteEYAELKEELEDLRAEL-EEV 376
|
250 260
....*....|....*....|..
gi 1958791358 407 EELARMLREyqELMSLKLALDM 428
Cdd:TIGR02169 377 DKEFAETRD--ELKDYREKLEK 396
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
271-411 |
4.38e-06 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 48.81 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 271 EAEMAQIQSHISDMSVILSMDNNRNLDLDSIIDEVRAQYEEiALKSKAEAEALYQTKFQELQLAAGRHGD---DLKNTKN 347
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSA-AEAERSRLQALLAELAGAGAAAEGRAGElaqELDSEKQ 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958791358 348 EITELTRFIQRLRSEIENAKKQASNLETAIADAEQRGdsalKDARAKLD----ELEGALHQAKEELAR 411
Cdd:PRK09039 131 VSARALAQVELLNQQIAALRRQLAALEAALDASEKRD----RESQAKIAdlgrRLNVALAQRVQELNR 194
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
190-418 |
6.04e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 6.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 190 RKQLETLSGDRVRLDSELRNVRDVVEDYKKKYEEEINRRTAAENEFVLLKKDVDAAYAnkvelqakvdtmdqdikffkcl 269
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASA---------------------- 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 270 fEAEMAQIQSHIsdmsvilsmdnnRNLDLDSiiDEVRAQYEEIAlkskaEAEALYQTKFQELQLAAGRHGDdlknTKNEI 349
Cdd:COG4913 667 -EREIAELEAEL------------ERLDASS--DDLAALEEQLE-----ELEAELEELEEELDELKGEIGR----LEKEL 722
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958791358 350 TELTRFIQRLRSEIENAKKQASNLETAIADA-------EQRGDSALKDARAKLDELEGALHQAKEELARMLREYQE 418
Cdd:COG4913 723 EQAEEELDELQDRLEAAEDLARLELRALLEErfaaalgDAVERELRENLEERIDALRARLNRAEEELERAMRAFNR 798
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
191-439 |
1.12e-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: 47.84 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 191 KQLETLSGDRVRLDSELRNVRDVVEDYKKKYEEEINRRTAAENEFVLLKKDVDAAYANKVELQAKVDTMDQDIKffkcLF 270
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA----EL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 271 EAEMAQIQSHISDMSVILSMDNNRNldldsiidevraqYEEIALKSKAEAEALYQTK-FQELQLAAGRHGDDLKNTKNEI 349
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQP-------------PLALLLSPEDFLDAVRRLQyLKYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 350 teltrfiQRLRSEIENAKKQASNLETAIADAEQRGDSALKDARAKLDELEGALHQAKEELARMLREYQELMSLKLALDME 429
Cdd:COG4942 163 -------AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
250
....*....|
gi 1958791358 430 IATYRKLLES 439
Cdd:COG4942 236 AAAAAERTPA 245
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
188-419 |
1.35e-05 |
|
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: 46.46 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 188 NMRKQLETLSgDRVRLDSELRNVRDVVEDYKKKYEEEINRRTAAENEFVLLKKDVDAAYANKVELQAKVDTMDQDIKffK 267
Cdd:COG1579 1 AMPEDLRALL-DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK--K 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 268 clFEAEMAQIQshisdmsvilsmdNNRnlDLDSIIDEVRAQYEEIALKSKAEAEALYQtkfqelqlaagrhgddlkntkn 347
Cdd:COG1579 78 --YEEQLGNVR-------------NNK--EYEALQKEIESLKRRISDLEDEILELMER---------------------- 118
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958791358 348 eiteltrfIQRLRSEIENAKKQASNLETAIADAEQRGDSALKDARAKLDELEGALHQAKEEL-ARMLREYQEL 419
Cdd:COG1579 119 --------IEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIpPELLALYERI 183
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
130-443 |
1.35e-05 |
|
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: 48.19 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 130 QEREQ-IKALNNKFASFIDKVRFLEQQNQVLETKWELLQQLDlNNC---------KNNLEPILEGYISNMRKqletLSGD 199
Cdd:pfam15921 506 QEKERaIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQ-TECealklqmaeKDKVIEILRQQIENMTQ----LVGQ 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 200 RVRLDSELRnvrdvVEdyKKKYEEEINRRTAAENEFVLLKKDVDAAYAnkvELQAKVDTMD-QDIKFFKCLFEAEMAQIQ 278
Cdd:pfam15921 581 HGRTAGAMQ-----VE--KAQLEKEINDRRLELQEFKILKDKKDAKIR---ELEARVSDLElEKVKLVNAGSERLRAVKD 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 279 SHISDMSVILSMDNNRNlDLDSIIDEvraqYEEIALKSKAEAEALyQTKFQELQLAAGRHGDDLKNTKNEITE------- 351
Cdd:pfam15921 651 IKQERDQLLNEVKTSRN-ELNSLSED----YEVLKRNFRNKSEEM-ETTTNKLKMQLKSAQSELEQTRNTLKSmegsdgh 724
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 352 -------LTRFIQRLRSEIENAKKQASNLETAIADAEQRgDSALKDARAKLDELEGALHQAKEELA---RMLREYQELMS 421
Cdd:pfam15921 725 amkvamgMQKQITAKRGQIDALQSKIQFLEEAMTNANKE-KHFLKEEKNKLSQELSTVATEKNKMAgelEVLRSQERRLK 803
|
330 340
....*....|....*....|..
gi 1958791358 422 LKLAlDMEIATYRKLLESEECR 443
Cdd:pfam15921 804 EKVA-NMEVALDKASLQFAECQ 824
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
133-438 |
2.63e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 133 EQIKALNNKFASFIDKVRFLEQQNQVLETKWELLQQLdlnncKNNLEPILEgYISNMRKQLETLSGDRVRLDSELRNVRD 212
Cdd:PRK03918 193 ELIKEKEKELEEVLREINEISSELPELREELEKLEKE-----VKELEELKE-EIEELEKELESLEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 213 VVEDYKKKYEE-EINRRTAAEnefvlLKKDVDaAYANKVELQAKVDTMDQDIKFFKCLFEAEMAQIQSHISDmsviLSMD 291
Cdd:PRK03918 267 RIEELKKEIEElEEKVKELKE-----LKEKAE-EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE----LEEK 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 292 NNRNLDLDSIIDEVRAQYEEIALKSKAEAEAL--------YQTKFQELQLA-AGRHGDDLKNTKNEITE----LTRFIQR 358
Cdd:PRK03918 337 EERLEELKKKLKELEKRLEELEERHELYEEAKakkeelerLKKRLTGLTPEkLEKELEELEKAKEEIEEeiskITARIGE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 359 LRSEIENAKKQASNLETAIA---------DAEQRGDsALKDARAKLDELEGALHQAKEELARMLREYQELMSlKLALDME 429
Cdd:PRK03918 417 LKKEIKELKKAIEELKKAKGkcpvcgrelTEEHRKE-LLEEYTAELKRIEKELKEIEEKERKLRKELRELEK-VLKKESE 494
|
....*....
gi 1958791358 430 IATYRKLLE 438
Cdd:PRK03918 495 LIKLKELAE 503
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
119-441 |
2.69e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.20 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 119 ELDPE-IQKVRAQEREQIKALNNKFASFIDKVRFLEQQNQVLETKWELLQ-QLDLNNCKNNL-EPILEGYISNMRKQLET 195
Cdd:PRK01156 401 EIDPDaIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNgQSVCPVCGTTLgEEKSNHIINHYNEKKSR 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 196 LSGDRVRLDSELRNVRDVVEDYKKKYE----EEINRRTAAENEFVLLKKDVDAAYANKVELQAKVDTMDQDIKFFKCLfe 271
Cdd:PRK01156 481 LEEKIREIEIEVKDIDEKIVDLKKRKEylesEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSL-- 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 272 aemaqiqsHISDMSVILSMDNNRNLDLDSI-IDEVRAQYEEI------ALKSKAEAEALYQTKFQELQLAAGRHGDD--- 341
Cdd:PRK01156 559 --------KLEDLDSKRTSWLNALAVISLIdIETNRSRSNEIkkqlndLESRLQEIEIGFPDDKSYIDKSIREIENEann 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 342 LKNTKNEITELTRFIQRLRSEIENAKKQASNLEtAIADAEQRGDSALKDARAKLDELEGALHQAKEELARMLREYQELMS 421
Cdd:PRK01156 631 LNNKYNEIQENKILIEKLRGKIDNYKKQIAEID-SIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRT 709
|
330 340
....*....|....*....|
gi 1958791358 422 LKLALDMEIATYRKLLESEE 441
Cdd:PRK01156 710 RINELSDRINDINETLESMK 729
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
132-432 |
2.86e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 132 REQIKALNNKFASFIDKVRFLEQQNQVLETKWELLQqldlnncknnlepilegyisnmrkQLETLSGDRVRLDSELRNVR 211
Cdd:COG4913 616 EAELAELEEELAEAEERLEALEAELDALQERREALQ------------------------RLAEYSWDEIDVASAEREIA 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 212 DVvedykkkyEEEINRRTAAENEFVLLKKDVDAAYANKVELQAKVDTMDQDIKffkcLFEAEMAQIQSHisdmsvilsmd 291
Cdd:COG4913 672 EL--------EAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIG----RLEKELEQAEEE----------- 728
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 292 nnrnldldsiIDEVRAQYEEIALKSKAEAEALYQTKFQELqLAAGRHGDDLKNTKNEITELTRFIQRLRSEIENAKKQ-- 369
Cdd:COG4913 729 ----------LDELQDRLEAAEDLARLELRALLEERFAAA-LGDAVERELRENLEERIDALRARLNRAEEELERAMRAfn 797
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958791358 370 ------ASNLETAIADAEqrgdsalkDARAKLDELEG-ALHQAKEELARMLRE--YQELMSLKLALDMEIAT 432
Cdd:COG4913 798 rewpaeTADLDADLESLP--------EYLALLDRLEEdGLPEYEERFKELLNEnsIEFVADLLSKLRRAIRE 861
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
298-440 |
3.60e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 298 LDSIIDEVRAQYEEIALKsKAEAEALYQTKFQELQLAAGRH----GDDLKNTKNEITELTRFIQRLRSEIENAKKQASNL 373
Cdd:COG4913 293 LEAELEELRAELARLEAE-LERLEARLDALREELDELEAQIrgngGDRLEQLEREIERLERELEERERRRARLEALLAAL 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 374 E--------------TAIADAEQRGDSALKDARAKLDELEGALHQAKEELARMLREYQELMSLKLALDMEIATYRKLLES 439
Cdd:COG4913 372 GlplpasaeefaalrAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAE 451
|
.
gi 1958791358 440 E 440
Cdd:COG4913 452 A 452
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
186-411 |
4.06e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 186 ISNMRKQLETLSGDRVRLDSELRNVRDVVEDYKKKYEEEINRRTAAENEFVLLKKDVDAAyanKVELQAKVDTMDQDIkf 265
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA---EAEIEERREELGERA-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 266 fkclfeAEMAQIQSHISDMSVILSMDN-----NRNLDLDSIIDEVRAQYEEI--ALKSKAEAEALYQTKFQELQLAAGRH 338
Cdd:COG3883 93 ------RALYRSGGSVSYLDVLLGSESfsdflDRLSALSKIADADADLLEELkaDKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958791358 339 GDDLKNTKNEITELTRFIQRLRSEIENAKKQASNLETAIADAEQRGDSALKDARAKLDELEGALHQAKEELAR 411
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
297-435 |
5.42e-05 |
|
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: 44.53 E-value: 5.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 297 DLDSIIDEVRAQYEEI--ALKSKAEAEALYQTKFQELQLAAGRHGDDLKNTKNEITELTRFIQRLRS------------- 361
Cdd:COG1579 14 ELDSELDRLEHRLKELpaELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkeyea 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958791358 362 ---EIENAKKQASNLETAIADAEQRgdsaLKDARAKLDELEGALHQAKEELARMLREYQELMSlklALDMEIATYRK 435
Cdd:COG1579 94 lqkEIESLKRRISDLEDEILELMER----IEELEEELAELEAELAELEAELEEKKAELDEELA---ELEAELEELEA 163
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
90-443 |
7.06e-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: 45.73 E-value: 7.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 90 LGPVCPTVCppGGIHQVTvnesllaplnvELDPEIQKVRAQ---EREQIKALNNKFASFIDKVRFLEQQNQVLETKWELL 166
Cdd:TIGR00618 523 PGPLTRRMQ--RGEQTYA-----------QLETSEEDVYHQltsERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNL 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 167 QQLDlnnckNNLEPILEGYISNMRKQLETLSGDRVRLDSELRNVRDVVEDYKKKYEEEINRRTAAENEFVLLKKDVDAAY 246
Cdd:TIGR00618 590 QNIT-----VRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHA 664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 247 ANKVELQAKVDTMDQdikffkclfeAEMAQIQSHISDMSVILSMDNNRNLDLDSI---IDEVRAQYEEIALKSKA----- 318
Cdd:TIGR00618 665 LSIRVLPKELLASRQ----------LALQKMQSEKEQLTYWKEMLAQCQTLLRELethIEEYDREFNEIENASSSlgsdl 734
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 319 ------------EAEALYQTKFQELQLaagrhgDDLKNTKNEITELTRF--IQRLRSEIENAKKQASNLETAIADAEQrg 384
Cdd:TIGR00618 735 aaredalnqslkELMHQARTVLKARTE------AHFNNNEEVTAALQTGaeLSHLAAEIQFFNRLREEDTHLLKTLEA-- 806
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958791358 385 dsalkDARAKLDELEGALHQAKEELARMLREYQELMSLKLALDMEIAtyRKLLESEECR 443
Cdd:TIGR00618 807 -----EIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEIT--HQLLKYEECS 858
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
133-423 |
8.01e-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: 8.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 133 EQIKALNNKFASFIDKVRFLEQQNQVLETKWEllqqlDLNNCKNNLEP---ILEGYISNMRKQLETLSGDRVRLDSELRN 209
Cdd:TIGR04523 131 KQKKENKKNIDKFLTEIKKKEKELEKLNNKYN-----DLKKQKEELENelnLLEKEKLNIQKNIDKIKNKLLKLELLLSN 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 210 VRDVVEDYKKkYEEEINRrtaAENEFVLLKKDVDAAYANKVELQAKVDTMDQDIKFFKCLFEAEMAQIQSHISDmsviLS 289
Cdd:TIGR04523 206 LKKKIQKNKS-LESQISE---LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE----LE 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 290 MDNNRNLDLDSIIDEVRAQYEEiaLKSKAEAEALYQTKfQELQlaagRHGDDLKNTKNEITELTRFIQRLRSEIENAKKQ 369
Cdd:TIGR04523 278 QNNKKIKELEKQLNQLKSEISD--LNNQKEQDWNKELK-SELK----NQEKKLEEIQNQISQNNKIISQLNEQISQLKKE 350
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958791358 370 ASNLET-------AIADAEQRGDSALKDARAKLDELEgALHQAKEELARMLREYQELMSLK 423
Cdd:TIGR04523 351 LTNSESensekqrELEEKQNEIEKLKKENQSYKQEIK-NLESQINDLESKIQNQEKLNQQK 410
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
331-419 |
8.88e-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: 44.75 E-value: 8.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 331 LQLAAGRHGDDLKNTKNEITELTRFIQRLRSEIENAKKQASNLETAIADAEQRgdsaLKDARAKLDELEGALHQAKEELA 410
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELA 86
|
....*....
gi 1958791358 411 RMLREYQEL 419
Cdd:COG4942 87 ELEKEIAEL 95
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
296-441 |
1.48e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 296 LDLDSIIDEVRAQYEEIALKSKAEAEALYQTKFQELQLAAGRHGDDLKNTKNEITELTRFIQRLRSEIENAKKQASNLET 375
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958791358 376 AIADAEQRGDSA---LKDARAKLDELEGALHQAKEELARMLREYQELMSLKLALDMEIATYRKLLESEE 441
Cdd:COG1196 296 ELARLEQDIARLeerRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
103-370 |
2.08e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.94 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 103 IHQVTVNESLLAPLNVELDPEIQKVRAQ-EREQIKalNNKFASFIDKVrFLEQQNQVLETKWELL----QQLDLNNCKNN 177
Cdd:pfam05483 452 IHDLEIQLTAIKTSEEHYLKEVEDLKTElEKEKLK--NIELTAHCDKL-LLENKELTQEASDMTLelkkHQEDIINCKKQ 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 178 LEPIL------EGYISNMRKQLETL------SGDRVR--LDSELRNVRDVVEDYKKKYEEEI-------NRRTAAEN--- 233
Cdd:pfam05483 529 EERMLkqienlEEKEMNLRDELESVreefiqKGDEVKckLDKSEENARSIEYEVLKKEKQMKilenkcnNLKKQIENknk 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 234 -------EFVLLKKDVDA------AY---ANKVELQAK---------VDTMDQDIKFFKCLFEAEMAQIQSH--ISDMSV 286
Cdd:pfam05483 609 nieelhqENKALKKKGSAenkqlnAYeikVNKLELELAsakqkfeeiIDNYQKEIEDKKISEEKLLEEVEKAkaIADEAV 688
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 287 ILSMD-----NNRNLDLDSIIDEVRAQYEEIALKSKAEAeALYQTKFQELQLAAGRHGDDLKNTKNEITELTRFIQRLRS 361
Cdd:pfam05483 689 KLQKEidkrcQHKIAEMVALMEKHKHQYDKIIEERDSEL-GLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKE 767
|
....*....
gi 1958791358 362 EIENAKKQA 370
Cdd:pfam05483 768 EKEKLKMEA 776
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
297-415 |
3.35e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 297 DLDSIIDEVRAQYEEIALKSKA---EAEAL------YQTKFQELQLAAGRHGDDLKNTKNEITELTRFIQRLRSEIENAK 367
Cdd:PRK02224 318 ELEDRDEELRDRLEECRVAAQAhneEAESLredaddLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELR 397
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1958791358 368 KQASNLETAIADAEQRGD---SALKDARAKLDELEGALHQAKEEL--ARMLRE 415
Cdd:PRK02224 398 ERFGDAPVDLGNAEDFLEelrEERDELREREAELEATLRTARERVeeAEALLE 450
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
123-411 |
3.80e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 42.92 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 123 EIQKVRAQE---REQIKALNNKFASFIDKVrfLEQQNQVLETKWELLQQLDlnncknNLEPILEGYISNM--------RK 191
Cdd:pfam06160 108 ELDELLESEeknREEVEELKDKYRELRKTL--LANRFSYGPAIDELEKQLA------EIEEEFSQFEELTesgdyleaRE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 192 QLETLSGDRVRLDSELRNVRDVVEDYKKKYEEEIN------RRTAAEN----------EFVLLKKDVDAAYANKVEL--- 252
Cdd:pfam06160 180 VLEKLEEETDALEELMEDIPPLYEELKTELPDQLEelkegyREMEEEGyalehlnvdkEIQQLEEQLEENLALLENLeld 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 253 --QAKVDTMDQDIKFFKCLFEAEM---AQIQSHISDMSVILS--MDNNRNLDLDsiIDEVRAQY----EEIalkskaEAE 321
Cdd:pfam06160 260 eaEEALEEIEERIDQLYDLLEKEVdakKYVEKNLPEIEDYLEhaEEQNKELKEE--LERVQQSYtlneNEL------ERV 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 322 ALYQTKFQELQlaaGRHGDDLKNTKNE---ITELTRFIQRLRSEIENAKKQASNLETAIADAEQrgdsALKDARAKLDEL 398
Cdd:pfam06160 332 RGLEKQLEELE---KRYDEIVERLEEKevaYSELQEELEEILEQLEEIEEEQEEFKESLQSLRK----DELEAREKLDEF 404
|
330
....*....|...
gi 1958791358 399 EGALHQAKEELAR 411
Cdd:pfam06160 405 KLELREIKRLVEK 417
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
270-440 |
3.90e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 270 FEAEMAQIQSHISDmsvilsmdnnrnldLDSIIDEVRAQYEEIAlKSKAEAEALYQTKFQELQLAAGRHG--------DD 341
Cdd:COG4913 615 LEAELAELEEELAE--------------AEERLEALEAELDALQ-ERREALQRLAEYSWDEIDVASAEREiaeleaelER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 342 LKNTKNEITELTRFIQRLRSEIENAKKQASNLETAIADAEQRgdsaLKDARAKLDELEGALHQAKEELARMLREYQELMS 421
Cdd:COG4913 680 LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE----LEQAEEELDELQDRLEAAEDLARLELRALLEERF 755
|
170
....*....|....*....
gi 1958791358 422 LKLALDMEIATYRKLLESE 440
Cdd:COG4913 756 AAALGDAVERELRENLEER 774
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
181-426 |
6.07e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 6.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 181 ILEGYISNMRKQLETLSGDRVRLDSELRnvrdvvedykKKYEEEINRRTAAENEFVLLKKDVDAAYANKVELQAKVDTMD 260
Cdd:COG4717 46 MLLERLEKEADELFKPQGRKPELNLKEL----------KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 261 QDIKFFKCLFEA-----EMAQIQSHISdmsvilsmdnnrnlDLDSIIDEVRAQYEEIalkskaeaealyqtkfQELQLAA 335
Cdd:COG4717 116 EELEKLEKLLQLlplyqELEALEAELA--------------ELPERLEELEERLEEL----------------RELEEEL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 336 GRHGDDLKNTKNEITELTRFI-QRLRSEIENAKKQASNLETAIADAEQrgdsALKDARAKLDELEGALHQAKEEL--ARM 412
Cdd:COG4717 166 EELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEE----ELEEAQEELEELEEELEQLENELeaAAL 241
|
250
....*....|....
gi 1958791358 413 LREYQELMSLKLAL 426
Cdd:COG4717 242 EERLKEARLLLLIA 255
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
318-441 |
6.38e-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: 41.45 E-value: 6.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 318 AEAEALYQ-----TKFQELQLAAGRHGDDLKNTKNEITELTRFIQRLRSEIENAKKQASNLETAIADAEQRgdsaLKDAR 392
Cdd:COG1579 4 EDLRALLDlqeldSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR----IKKYE 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1958791358 393 AKLDELEGA--LHQAKEELARMLREYQELMSLKLALDMEIATYRKLLESEE 441
Cdd:COG1579 80 EQLGNVRNNkeYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELE 130
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
329-409 |
8.77e-04 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 40.14 E-value: 8.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 329 QELQLAAGRHGDDLKNTKNEITELtrfiqrlrseIENAKKQASN-LETAIADAEQRGDSALKDARAkldELEGALHQAKE 407
Cdd:PRK05759 52 KELELAQAKYEAQLAEARAEAAEI----------IEQAKKRAAQiIEEAKAEAEAEAARIKAQAQA---EIEQERKRARE 118
|
..
gi 1958791358 408 EL 409
Cdd:PRK05759 119 EL 120
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
126-409 |
1.12e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.96 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 126 KVRAQEREQIKALNNKFASFIDKVRFLEQQNQVLETKWELLqqLDLNNCKNNLEPILEGYISNMRKQLETLSGDRVRLDS 205
Cdd:TIGR00606 688 QTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEM--LGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKN 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 206 ELRNVRDVVEDY--KKKYEEEINRRTAAENEFVLLKKDVDAAYANKVelqAKVDTMDQDIKFFKCLFEAEMAQiqsHISD 283
Cdd:TIGR00606 766 DIEEQETLLGTImpEEESAKVCLTDVTIMERFQMELKDVERKIAQQA---AKLQGSDLDRTVQQVNQEKQEKQ---HELD 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 284 mSVILSMDNNRNLDLDSiidevraQYEEIALKSKaeaeaLYQTKFQELQL--AAGRHGDDLKNTKNEITEltrfIQRLRS 361
Cdd:TIGR00606 840 -TVVSKIELNRKLIQDQ-------QEQIQHLKSK-----TNELKSEKLQIgtNLQRRQQFEEQLVELSTE----VQSLIR 902
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1958791358 362 EIENAKKQASNLETAIADAEQRGDSALKDARAKLDELEGALHQAKEEL 409
Cdd:TIGR00606 903 EIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKV 950
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
155-447 |
1.33e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.42 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 155 QNQVLETKWELLQQLDLNNCKNNLEPILEGYISNMRKQLE----TLSGDRVRLDSELRNVRDVVEDYKKKYEEEINRRTA 230
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWErqrrELESRVAELKEELRQSREKHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 231 AENEFVLLKKDVDAAYANKVELQAKVDTMDQDikffKCLFEAEMAQIQSHISDMSVILSMDNNRNLDLDSIIDEVRAQYE 310
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIRELEEDIKTLTQR----VLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 311 EIALKSKAEAEALYQTKFQELQlaagrhgddLKNTKNEITELTRFIQRLRSEIENAKKQASNLETAIADAEQRGD---SA 387
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDTQVLQ---------LQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEglgEE 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 388 LKDARAKLDELEGALHQAKEELARMlreYQELMSLKLALDMEIATYRKllESEECRMSGE 447
Cdd:pfam07888 260 LSSMAAQRDRTQAELHQARLQAAQL---TLQLADASLALREGRARWAQ--ERETLQQSAE 314
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
287-432 |
1.63e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 287 ILSMDNNRNLD-------LD-----SIIDEVRAQYEEI------ALKSKAEAEAL-----YQTKFQELQLAAGRHgDDLK 343
Cdd:COG4913 200 TQSFKPIGDLDdfvreymLEepdtfEAADALVEHFDDLeraheaLEDAREQIELLepireLAERYAAARERLAEL-EYLR 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 344 NTkNEITELTRFIQRLRSEIENAKKQASNLETAIADAEQRgdsaLKDARAKLDELEGA---------------LHQAKEE 408
Cdd:COG4913 279 AA-LRLWFAQRRLELLEAELEELRAELARLEAELERLEAR----LDALREELDELEAQirgnggdrleqlereIERLERE 353
|
170 180
....*....|....*....|....
gi 1958791358 409 LARMLREYQELMSLKLALDMEIAT 432
Cdd:COG4913 354 LEERERRRARLEALLAALGLPLPA 377
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
116-423 |
1.66e-03 |
|
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: 41.48 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 116 LNVELDPEIQKVRAQEREQIKALNNKFASFIDKVRFLEQQNQVLETKWELLQQLdLNNCKNNLEPILEGYISNMRKQLET 195
Cdd:COG3096 826 LAVAFAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKL-LPQANLLADETLADRLEELREELDA 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 196 LSGDRVRLD------SELRNVRDVVEDYKKKYEEEINRRTAAENEFVLLKKDVDA-----------AYANKVELQAKVDT 258
Cdd:COG3096 905 AQEAQAFIQqhgkalAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFAlsevvqrrphfSYEDAVGLLGENSD 984
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 259 MDQDIKffKCLFEAEMA---------QIQSHISDMSVILSmdnnrnlDLDS-------IIDEVRAQYEEIALKSKAEAEA 322
Cdd:COG3096 985 LNEKLR--ARLEQAEEArreareqlrQAQAQYSQYNQVLA-------SLKSsrdakqqTLQELEQELEELGVQADAEAEE 1055
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 323 LYQTKFQELQlaagrhgDDLKNTKNEITELTRFIQRLRSEIENAKKQASNLETAIADAEQRGDSALKD-----ARAKLDE 397
Cdd:COG3096 1056 RARIRRDELH-------EELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQAKAGwcavlRLARDND 1128
|
330 340
....*....|....*....|....*.
gi 1958791358 398 LEGALHqaKEELARMLREYQELMSLK 423
Cdd:COG3096 1129 VERRLH--RRELAYLSADELRSMSDK 1152
|
|
| SEC6 |
COG5173 |
Exocyst complex subunit SEC6 [Intracellular trafficking and secretion]; |
189-424 |
2.00e-03 |
|
Exocyst complex subunit SEC6 [Intracellular trafficking and secretion];
Pssm-ID: 227500 [Multi-domain] Cd Length: 742 Bit Score: 41.08 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 189 MRKQLETLSgDRVRLDSELRNVRDVVEDYKK--KYEEEINRRTAAENEFV-LLKKDVDAAYANKVELQAKVDTMDQDIKF 265
Cdd:COG5173 1 MDKALTQLS-ETLRHDSDLQTVLDIIEQSTKfeALEHHDGNLSAEISKCLnNILNISKRIYGLEEELKSLVEGKRRNVRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 266 FKCLFEaeMAQIQSHISDMSVILSMDNNRNLDLDSIIDEVRAQYEEIA----------LKSKAE---AEALYQTKfqELQ 332
Cdd:COG5173 80 LKGFFR--LVKDYRSVKMTCLAHSNLCNVVEFSDRIEDILGTVLTEDIdmpnllayhtKLYDARdfgEQLDMYAT--EIS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 333 LAAGRHGDDLKNTKNEIT-ELTRFIQRLRSEI-ENAKkqASNLETA-----IADAEQRGDSALKDARAKLDELEGAlhQA 405
Cdd:COG5173 156 HDDYVTVNKAFSTLEKNSlDFDALVLEISEEIiENVK--SGHIEAMdkifkIVEKEEARDELTRKIRDAKSELPKS--QD 231
|
250
....*....|....*....
gi 1958791358 406 KEELARMLREYQELMSLKL 424
Cdd:COG5173 232 NPVLKEFYGMYRMYATRKT 250
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
276-419 |
2.31e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 276 QIQSHISDMSVILSMDNNRNLDLDSIIDEVRAQYEEIAlKSKAEAEAL------YQTKFQELQLAAGRHGDDLKNTKNEI 349
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELE-QARSELEQLeeeleeLNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 350 TELTRFIQRLRSEIENAKKQASNLETAIADAEQrgdsALKDARAKLDELEGALHQAKEELARMLREYQEL 419
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQS----EIAEREEELKELEEQLESLQEELAALEQELQAL 176
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
251-418 |
2.33e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 40.05 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 251 ELQAKVDTMDQDIKFFKCLFEAEMAQIQSHISDMSVILSMDNNRNL--DLDSIIDEVRAQYEEIALKSKA---EAEALYQ 325
Cdd:cd22656 132 KYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTDEGGAIArkEIKDLQKELEKLNEEYAAKLKAkidELKALIA 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 326 TKFQELQLA------AGRHGDDLKNTKNEITELTRFIQRLRSEIENAKKQASNLETAIADAEQRGDSALKdARAKLDELE 399
Cdd:cd22656 212 DDEAKLAAAlrliadLTAADTDLDNLLALIGPAIPALEKLQGAWQAIATDLDSLKDLLEDDISKIPAAIL-AKLELEKAI 290
|
170
....*....|....*....
gi 1958791358 400 galhQAKEELARMLREYQE 418
Cdd:cd22656 291 ----EKWNELAEKADKFRQ 305
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
135-423 |
2.37e-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: 40.77 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 135 IKALNNKFASFIDKVRFLEQQNQVLETKWELLQQ------LDLNNCKNNLEPILEGYI------SNMRKQLETLSGDRVR 202
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQeinektTEISNTQTQLNQLKDEQNkikkqlSEKQKELEQNNKKIKE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 203 LDSELRNVRDVVEDYKKKYEEEINRRtaaenefvlLKKDVDAAYANKVELQAKVDTMDQDIkffkclfeaemAQIQSHIS 282
Cdd:TIGR04523 286 LEKQLNQLKSEISDLNNQKEQDWNKE---------LKSELKNQEKKLEEIQNQISQNNKII-----------SQLNEQIS 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 283 DMSVILSMDNNRNLDLDSIIDEVRAQYEEIALKSKAEAEALYQ---------TKFQELQLAAGRHGDDLKNTKNEITELT 353
Cdd:TIGR04523 346 QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNlesqindleSKIQNQEKLNQQKDEQIKKLQQEKELLE 425
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958791358 354 RFIQRLRSEIENAKKQASNLETAIADAE---QRGDSALKDARAKLDELEGALHQAKEELARMLREY----QELMSLK 423
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIKDLTNQDSVKEliiKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELkskeKELKKLN 502
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
340-447 |
2.89e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 340 DDLKNTKNEITELTRFIQRLRSEIENAKKQASNLETAIADAEQRGDSALKdaraKLDELEGALHQAKEELARMLREYQEL 419
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLR----EINEISSELPELREELEKLEKEVKEL 233
|
90 100
....*....|....*....|....*...
gi 1958791358 420 MSLKlaldMEIATYRKLLESEECRMSGE 447
Cdd:PRK03918 234 EELK----EEIEELEKELESLEGSKRKL 257
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
231-441 |
3.34e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 231 AENEFVLLKKDVDAAYANKVELQAKVDTMDQDIkffkclfEAEMAQIQSHISDMSvilsmDNNRNLD-LDSIIDEVRAQY 309
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAEL-------EELNEEYNELQAELE-----ALQAEIDkLQAEIAEAEAEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 310 EEIALKSKAEAEALYQTKFQ----ELQLAAGRHGDDLKNTKNeITELTRFIQRLRSEIENAKKQASNLETAIADAEQRGD 385
Cdd:COG3883 82 EERREELGERARALYRSGGSvsylDVLLGSESFSDFLDRLSA-LSKIADADADLLEELKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958791358 386 SALKDARAKLDELEGALHQAKEELARMLREYQELMSLKLALDMEIATYRKLLESEE 441
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
119-371 |
4.52e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.12 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 119 ELDPEIQKVRaQEREQIKALNNKFASFIDKVRFL-EQQNQVLETKWELLQQLDLNNCKNNLEPILEGYISNMRKQLETLs 197
Cdd:COG1340 44 KRDELNAQVK-ELREEAQELREKRDELNEKVKELkEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERL- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 198 gdRVRLDSE---LRNVRDVVEDYKKkYEEEINRRTAAENEfvllKKDVDAAYANKVELQAKVDTMDQDIKffkclfeaEM 274
Cdd:COG1340 122 --EWRQQTEvlsPEEEKELVEKIKE-LEKELEKAKKALEK----NEKLKELRAELKELRKEAEEIHKKIK--------EL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 275 AQIQSHISDmsvilsmdnnrnldldsIIDEVRAQYEEIalksKAEAEALYQtKFQELQLAAGRHGDDLKNTKNEITELTR 354
Cdd:COG1340 187 AEEAQELHE-----------------EMIELYKEADEL----RKEADELHK-EIVEAQEKADELHEEIIELQKELRELRK 244
|
250
....*....|....*..
gi 1958791358 355 FIQRLRSEIENAKKQAS 371
Cdd:COG1340 245 ELKKLRKKQRALKREKE 261
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
245-439 |
4.67e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.67 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 245 AYANKVELQAKVDTMDQDIKFFKCLFE---AEMAQIQSHISDMSVILSmdnnrnlDLDSIIDEVRAQYEEIALKSKAEAE 321
Cdd:TIGR02169 665 GILFSRSEPAELQRLRERLEGLKRELSslqSELRRIENRLDELSQELS-------DASRKIGEIEKEIEQLEQEEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 322 ALYQTKfqelqlaagrhgDDLKNTKNEITELTRFIQRLRSEIENAKKQASNLETAIADAEQRGD-----------SALKD 390
Cdd:TIGR02169 738 RLEELE------------EDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLShsripeiqaelSKLEE 805
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958791358 391 ARAK----LDELEGALHQAKEELARMLREYQELMSLKLALDMEIATYRKLLES 439
Cdd:TIGR02169 806 EVSRiearLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN 858
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
340-441 |
5.37e-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: 5.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 340 DDLKNTKNEITELTRFIQRLRSEIENAKKQASNL----------------ETAIADAEQRGDsALKDARAKLDELEGALH 403
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALqrlaeyswdeidvasaEREIAELEAELE-RLDASSDDLAALEEQLE 695
|
90 100 110
....*....|....*....|....*....|....*...
gi 1958791358 404 QAKEELARMLREYQELMSLKLALDMEIATYRKLLESEE 441
Cdd:COG4913 696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
356-412 |
5.54e-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: 37.68 E-value: 5.54e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958791358 356 IQRLRSEIENAKKQASNLETAIADAEQRgdsaLKDARAKLDELEGALHQAKEELARM 412
Cdd:pfam11559 68 IERLQSKIERLKTQLEDLERELALLQAK----ERQLEKKLKTLEQKLKNEKEELQRL 120
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
182-408 |
5.59e-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: 39.77 E-value: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 182 LEGYISNMRKQLETLSGDRVRLDSELRNVRDVVEDYKKKYEEEINRRTAAENEFVLLKKDVDAAyanKVELQAKVDTMDQ 261
Cdd:pfam01576 494 LEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEAL---TQQLEEKAAAYDK 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 262 dikffkclFEAEMAQIQSHISDMSVILsmDNNRNL---------DLDSIIDE---VRAQYEEiaLKSKAEAEAL-YQTKF 328
Cdd:pfam01576 571 --------LEKTKNRLQQELDDLLVDL--DHQRQLvsnlekkqkKFDQMLAEekaISARYAE--ERDRAEAEAReKETRA 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 329 qelqLAAGRHGDDLKNTKNeitELTRFIQRLRSEIE-------NAKKQASNLETAIADAEQrgdsALKDARAKLDELEGA 401
Cdd:pfam01576 639 ----LSLARALEEALEAKE---ELERTNKQLRAEMEdlvsskdDVGKNVHELERSKRALEQ----QVEEMKTQLEELEDE 707
|
....*..
gi 1958791358 402 LhQAKEE 408
Cdd:pfam01576 708 L-QATED 713
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
181-336 |
8.32e-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: 38.46 E-value: 8.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 181 ILEGYISNMRKQLETLSGDRVRLDSELRNVRDVVEDYKKKY---EEEINRRTAAENEFVLLKKDVDAAYANKVELQakvd 257
Cdd:smart00787 141 LLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKdalEEELRQLKQLEDELEDCDPTELDRAKEKLKKL---- 216
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958791358 258 tmDQDIKFFKclfeAEMAQIQSHISDMSVILSMDNNRNLDLDSIIDEVRAQYEEIALKSKAEAEaLYQTKFQELQLAAG 336
Cdd:smart00787 217 --LQEIMIKV----KKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKEIE-KLKEQLKLLQSLTG 288
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
202-435 |
8.65e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 38.87 E-value: 8.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 202 RLDSELRNVRDVVEDYKKKYEEEINRRTAAEnefvllkkDVDAAYAnkvELQAKVDTMDQDIKffkcLFEAEMAQIQSHI 281
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEAD--------EVLEEHE---ERREELETLEAEIE----DLRETIAETERER 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791358 282 SDMSVILSMDNNRNLDLDSIIDEVRAqyeEIALKSkAEAEALYQtkfqelqlaagrHGDDLKNtknEITELTRFIQRLRS 361
Cdd:PRK02224 275 EELAEEVRDLRERLEELEEERDDLLA---EAGLDD-ADAEAVEA------------RREELED---RDEELRDRLEECRV 335
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958791358 362 EIENAKKQASNLETAIADAEQRGdsalKDARAKLDELEGALHQAKEElarmLREYQELMSlklALDMEIATYRK 435
Cdd:PRK02224 336 AAQAHNEEAESLREDADDLEERA----EELREEAAELESELEEAREA----VEDRREEIE---ELEEEIEELRE 398
|
|
| |
