|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
161-474 |
6.80e-155 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 445.52 E-value: 6.80e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 161 EEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQGTKTVRqNLEPLFEQYINNLRRQLDSIVGERGRLDSELRN 240
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPS-RLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 241 MQDLVEDLKNKYEVEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRALYDAELSQMQTHISDTSVVLS 320
Cdd:pfam00038 80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 321 MDNNRNLDLDSIIAEVKAQYEEIAQRSRAEAESWYQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQ 400
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386849 401 CANLQAAIADAEQRGEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVKLALDVEIATYRKLLEGEECR 474
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
17-158 |
5.03e-33 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 123.61 E-value: 5.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 17 GFSASSARLPGVSRSGFSSISVSRSRGSGGLGGACGGAGFGSRSLYGLGGSKRISI---GGGSCAISG-----------G 82
Cdd:pfam16208 1 GFSSCSAVVPSRSRRSYSSVSSSRRGGGGGGGGGGGGGGFGSRSLYNLGGSKSISIsvaGGGSRPGSGfgfgggggggfG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386849 83 YGSRAGAGYGFGGAGSGFGFGGGAGIGFGLGGGPALLCFGGPGFPVCPPGGIQEVTVNQSLLTPLNLQIDPAIQRI 158
Cdd:pfam16208 81 GGFGGGGGGGFGGGGGFGGGFGGGGYGGGGFGGGGFGGRGGFGGPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
162-456 |
3.61e-12 |
|
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: 69.32 E-value: 3.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 162 EREQ-IKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQGTKTVRQNLEplFEQYINNLRRQLDSIVGERGRLDSELRN 240
Cdd:TIGR02168 674 ERRReIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE--LSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 241 MQDLVEDLKNKYEVEINKRTAAENEFVTLKKdvdaaymNKVELQAKADTLTDEINFLRALYD---AELSQMQTHISDTSV 317
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEA-------EIEELEAQIEQLKEELKALREALDelrAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 318 VLSMDNNR-------NLDLDSIIAEVKAQYEEIAQ----------RSRAEAESWYQtKYEELQVTAGRHGDDLRNTKQEI 380
Cdd:TIGR02168 825 RLESLERRiaaterrLEDLEEQIEELSEDIESLAAeieeleelieELESELEALLN-ERASLEEALALLRSELEELSEEL 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 381 AEINRMIQRLRSEIDHVKKQCANLQAAIADAEQR-----------GEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQE 449
Cdd:TIGR02168 904 RELESKRSELRRELEELREKLAQLELRLEGLEVRidnlqerlseeYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
....*..
gi 386849 450 LMNVKLA 456
Cdd:TIGR02168 984 LGPVNLA 990
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
151-472 |
6.80e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 55.68 E-value: 6.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 151 IDP-AIQRIGAEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQ------GTKTVRQNLEPLFEQYINNLRR- 222
Cdd:PRK01156 402 IDPdAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpvcGTTLGEEKSNHIINHYNEKKSRl 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 223 --QLDSIVGERGRLDSELRNMQDLVEDLKNKyevEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRAL 300
Cdd:PRK01156 482 eeKIREIEIEVKDIDEKIVDLKKRKEYLESE---EINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSL 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 301 YDAELSQMQTHISDTSVVLSmdnnrNLDLDSIIA---EVKAQYEEIAQRSRaEAESWYQTKYEELQVTAGRHGDD---LR 374
Cdd:PRK01156 559 KLEDLDSKRTSWLNALAVIS-----LIDIETNRSrsnEIKKQLNDLESRLQ-EIEIGFPDDKSYIDKSIREIENEannLN 632
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 375 NTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMALkDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVK 454
Cdd:PRK01156 633 NKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRIN-DIEDNLKKSRKALDDAKANRARLESTIEILRTRI 711
|
330
....*....|....*...
gi 386849 455 LALDVEIATYRKLLEGEE 472
Cdd:PRK01156 712 NELSDRINDINETLESMK 729
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
203-450 |
1.29e-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: 54.69 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 203 KTVRQNLEpLFEQYINNLRRQLDSIVGERgrldSELRNMQDLVEDL-KNKYEVEINKRTAAENEFVTLKKDVDAAYMNKV 281
Cdd:TIGR02169 180 EEVEENIE-RLDLIIDEKRQQLERLRRER----EKAERYQALLKEKrEYEGYELLKEKEALERQKEAIERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 282 ELQAKADTLTDEINFLRALydaeLSQMQTHISDtsvvlsMDNNRNLDLDSIIAEVKAqyeEIAQRSRAEAEswYQTKYEE 361
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQL----LEELNKKIKD------LGEEEQLRVKEKIGELEA---EIASLERSIAE--KERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 362 LQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGE----------MALKDAKNKLEGLED 431
Cdd:TIGR02169 320 AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEevdkefaetrDELKDYREKLEKLKR 399
|
250
....*....|....*....
gi 386849 432 ALQKAKQDLARLLKEYQEL 450
Cdd:TIGR02169 400 EINELKRELDRLQEELQRL 418
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
220-469 |
1.48e-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: 54.69 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 220 LRRQLDSIVGERGRLDSELRNMQDLVEDLKNKYEVEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRA 299
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 300 L---YDAELSQMQTHISdtSVVLSMDNNRNLDLDSIIAEVKAQYEEI-AQRSRAEAeswyqtKYEELQVTAGRHGDDLRN 375
Cdd:TIGR02169 759 ElkeLEARIEELEEDLH--KLEEALNDLEARLSHSRIPEIQAELSKLeEEVSRIEA------RLREIEQKLNRLTLEKEY 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 376 TKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRgemaLKDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVKL 455
Cdd:TIGR02169 831 LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE----LEELEAALRDLESRLGDLKKERDELEAQLRELERKIE 906
|
250
....*....|....
gi 386849 456 ALDVEIATYRKLLE 469
Cdd:TIGR02169 907 ELEAQIEKKRKRLS 920
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
163-450 |
1.69e-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: 54.30 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 163 REQIKTLNNKFASF---IDKVRF-LEQQNKVLDTKWTLLQEQGTKtvrqnLEPLFEQYINNLRRQLDSIVGERGRLDSEL 238
Cdd:TIGR02169 236 ERQKEAIERQLASLeeeLEKLTEeISELEKRLEEIEQLLEELNKK-----IKDLGEEEQLRVKEKIGELEAEIASLERSI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 239 RNMQDLVEDLKN---KYEVEINKrTAAENEfvTLKKDVDaaymnkvELQAKADTLTDEINFLRALYDAELSQMQthisdt 315
Cdd:TIGR02169 311 AEKERELEDAEErlaKLEAEIDK-LLAEIE--ELEREIE-------EERKRRDKLTEEYAELKEELEDLRAELE------ 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 316 svvlsmdnnrnldldSIIAEVKAQYEEIAQRSRAEAEswYQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEID 395
Cdd:TIGR02169 375 ---------------EVDKEFAETRDELKDYREKLEK--LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKIN 437
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 386849 396 HVKKQCANLQAAIADAEQrgemalkdaknKLEGLEDALQKAKQDLARLLKEYQEL 450
Cdd:TIGR02169 438 ELEEEKEDKALEIKKQEW-----------KLEQLAADLSKYEQELYDLKEEYDRV 481
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
302-442 |
2.13e-07 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 53.05 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 302 DAELSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEiAQRSRAEAESWYQTKYEELQVTAGRHGD---DLRNTKQ 378
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSA-AEAERSRLQALLAELAGAGAAAEGRAGElaqELDSEKQ 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386849 379 EIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGemalKDAKNKLEG----LEDALQKAKQDLAR 442
Cdd:PRK09039 131 VSARALAQVELLNQQIAALRRQLAALEAALDASEKRD----RESQAKIADlgrrLNVALAQRVQELNR 194
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
164-472 |
3.91e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 164 EQIKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQgtktvRQNLEPLFEQyINNLRRQLDSIVGERGRLDSELRNMQD 243
Cdd:PRK03918 193 ELIKEKEKELEEVLREINEISSELPELREELEKLEKE-----VKELEELKEE-IEELEKELESLEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 244 LVEDLKNKYEvEINKRTAAENEfvtLKKDVDaAYMNKVELQAKADTLTDEINFLRALYDAELSQMQTHISDtsvvLSMDN 323
Cdd:PRK03918 267 RIEELKKEIE-ELEEKVKELKE---LKEKAE-EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE----LEEKE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 324 NRNLDLDSIIAEVKAQYEEIAQRSRAeaeswyqtkYEELQVTAGRhgddLRNTKQEIA-----EINRMIQRLRSEIDHVK 398
Cdd:PRK03918 338 ERLEELKKKLKELEKRLEELEERHEL---------YEEAKAKKEE----LERLKKRLTgltpeKLEKELEELEKAKEEIE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 399 KQCANLQAAIADAEQRGE------MALKDAKNKL---------EGLEDALQKAKQDLARLLKEYQELMNVKLALDVEIAT 463
Cdd:PRK03918 405 EEISKITARIGELKKEIKelkkaiEELKKAKGKCpvcgrelteEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRE 484
|
....*....
gi 386849 464 YRKLLEGEE 472
Cdd:PRK03918 485 LEKVLKKES 493
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
190-450 |
4.76e-07 |
|
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: 52.75 E-value: 4.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 190 LDTKWTLLQEQGTKTVRqnleplFEQYINNLRR-QLDSIVGERGRLDSELRNMQDLVEDLKNKYEVEINKRTAAENEFVT 268
Cdd:TIGR02168 198 LERQLKSLERQAEKAER------YKELKAELRElELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 269 LKKDVDAAYMNKVELQAKADTLTDEINFL---RALYDAELSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIAQ 345
Cdd:TIGR02168 272 LRLEVSELEEEIEELQKELYALANEISRLeqqKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 346 RSRA------EAESWYQ---TKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQR-G 415
Cdd:TIGR02168 352 ELESleaeleELEAELEeleSRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKlE 431
|
250 260 270
....*....|....*....|....*....|....*
gi 386849 416 EMALKDAKNKLEGLEDALQKAKQDLARLLKEYQEL 450
Cdd:TIGR02168 432 EAELKELQAELEELEEELEELQEELERLEEALEEL 466
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
178-446 |
5.69e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 52.32 E-value: 5.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 178 DKVRFLEQQNKVLDTKWTLLQEQgTKTvrqnleplFEQYINNLRRQLDSIVgergrldSELRNMQDLVEDLKNKYEVEIN 257
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQ-IKT--------YNKNIEEQRKKNGENI-------ARKQNKYDELVEEAKTIKAEIE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 258 KRTAAENEFVTLKKDVDAAY----MNKVELQAKADTLTDEINFLRAlYDAELSQMQThISDTsvvlsmdnnrnldlDSII 333
Cdd:PHA02562 238 ELTDELLNLVMDIEDPSAALnklnTAAAKIKSKIEQFQKVIKMYEK-GGVCPTCTQQ-ISEG--------------PDRI 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 334 AEVKAQYEEIAQRSRAEaeswyQTKYEELQVTAGRHgDDLRNTKQE----IAEINRMIQRLRSEIDHVKKQCANLQAAIa 409
Cdd:PHA02562 302 TKIKDKLKELQHSLEKL-----DTAIDELEEIMDEF-NEQSKKLLElknkISTNKQSLITLVDKAKKVKAAIEELQAEF- 374
|
250 260 270
....*....|....*....|....*....|....*..
gi 386849 410 daeqrgemalKDAKNKLEGLEDALQKAKQDLARLLKE 446
Cdd:PHA02562 375 ----------VDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
278-478 |
7.31e-07 |
|
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: 52.37 E-value: 7.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 278 MNKVELQAKADT----LTDEINFL-RALYDAELSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIaQRSRAEAE 352
Cdd:TIGR02168 202 LKSLERQAEKAErykeLKAELRELeLALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL-RLEVSELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 353 SwyqtKYEELQvtagrhgDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMA---LKDAKNKLEGL 429
Cdd:TIGR02168 281 E----EIEELQ-------KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELaeeLAELEEKLEEL 349
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 386849 430 EDALQKAKQDLARLLKEYQELMNVKLALDVEIATYRK---LLEGEECRLNGE 478
Cdd:TIGR02168 350 KEELESLEAELEELEAELEELESRLEELEEQLETLRSkvaQLELQIASLNNE 401
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
214-489 |
1.66e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.79 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 214 EQYIN-NLRRQLDSIVGERGRLDSELRNMQDLVEDLKNKYEveinkRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTD 292
Cdd:COG3206 159 EAYLEqNLELRREEARKALEFLEEQLPELRKELEEAEAALE-----EFRQKNGLVDLSEEAKLLLQQLSELESQLAEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 293 EINFLRALYDAELSQMQTHISDTSVVLSmdnnrnldlDSIIAEVKAQYEEIaqrsraeaeswyQTKYEELQVTAGRHGDD 372
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALPELLQ---------SPVIQQLRAQLAEL------------EAELAELSARYTPNHPD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 373 LRNTKQEIAEINRMIQRLRSEIDhvkkqcANLQAAIADAEQRgemalkdaKNKLEGLEDALQKAKQDLARLLKEYQELMN 452
Cdd:COG3206 293 VIALRAQIAALRAQLQQEAQRIL------ASLEAELEALQAR--------EASLQAQLAQLEARLAELPELEAELRRLER 358
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 386849 453 vklalDVEIA--TYRKLLEG-EECRLNgEGVGQVNISVVQ 489
Cdd:COG3206 359 -----EVEVAreLYESLLQRlEEARLA-EALTVGNVRVID 392
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
198-443 |
4.07e-06 |
|
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: 49.79 E-value: 4.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 198 QEQGTKTVRQNLE-----PLFEQYINNLRRQLDSIVGERGRLDSELRNMQDLVEDLKNKYEVEINKRTAAENEFVTLKKD 272
Cdd:pfam01576 474 QELLQEETRQKLNlstrlRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRE 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 273 VDAAYMNKVELQAKADTLtdeinflralyDAELSQMQTHISDTSVVLsmDNNRNL---------DLDSIIAEVK---AQY 340
Cdd:pfam01576 554 LEALTQQLEEKAAAYDKL-----------EKTKNRLQQELDDLLVDL--DHQRQLvsnlekkqkKFDQMLAEEKaisARY 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 341 EEiaQRSRAEAESwyqTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQ----RLRSEIDHVKKQCANLQAAIADAEQrge 416
Cdd:pfam01576 621 AE--ERDRAEAEA---REKETRALSLARALEEALEAKEELERTNKQLRaemeDLVSSKDDVGKNVHELERSKRALEQ--- 692
|
250 260
....*....|....*....|....*..
gi 386849 417 mALKDAKNKLEGLEDALQKAKQDLARL 443
Cdd:pfam01576 693 -QVEEMKTQLEELEDELQATEDAKLRL 718
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
143-400 |
4.89e-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: 49.68 E-value: 4.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 143 LLTPLNLQIDPAIQRIGAEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQGTKTVRQnleplfeqyINNLRR 222
Cdd:TIGR02169 273 LLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAE---------IEELER 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 223 QLDSIVGERGRLDSELRNMQDLVEDLKNKYEVEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLralyD 302
Cdd:TIGR02169 344 EIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRL----S 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 303 AELSQMQTHISdtsvvlsmdnnrnlDLDSIIAEVKAQYEEIAQRSRAEaeswyQTKYEELQVTAGRHGDDLRNTKQEIAE 382
Cdd:TIGR02169 420 EELADLNAAIA--------------GIEAKINELEEEKEDKALEIKKQ-----EWKLEQLAADLSKYEQELYDLKEEYDR 480
|
250
....*....|....*...
gi 386849 383 INRMIQRLRSEIDHVKKQ 400
Cdd:TIGR02169 481 VEKELSKLQRELAEAEAQ 498
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
217-436 |
2.55e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 217 INNLRRQLDSIVGERGRLDSELRNMQDLVEDLKNKYEVEINKRTAAENEFVTLKKDVDaaymnkvELQAKADTLTDEI-N 295
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA-------EAEAEIEERREELgE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 296 FLRALYDAELSqmqthISDTSVVLSMDN-----NRNLDLDSIIAEVKAQYEEI--AQRSRAEAESWYQTKYEELQVTAGR 368
Cdd:COG3883 91 RARALYRSGGS-----VSYLDVLLGSESfsdflDRLSALSKIADADADLLEELkaDKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386849 369 HGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMALKDAKNKLEGLEDALQKA 436
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
372-453 |
2.76e-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: 46.68 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 372 DLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQR---GEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQ 448
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELA 107
|
....*
gi 386849 449 ELMNV 453
Cdd:COG4942 108 ELLRA 112
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
144-462 |
3.00e-05 |
|
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: 46.97 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 144 LTPLNLQIDPAIQRIgAEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQgTKTVRQNLEpLFEQYINNLRRQ 223
Cdd:TIGR02168 241 LEELQEELKEAEEEL-EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE-ISRLEQQKQ-ILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 224 LDSIVGERGRLDSELRNMQDLVEDLKNKYEVeinkrtaAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRALYDA 303
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEE-------LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 304 ELSQMQTHisdtsvvlsmdNNRNLDLDSIIAEVKAQYEEIAQRSRAEAESWYQTKYEELQVTAGRHGDDLRNTKQEIAEI 383
Cdd:TIGR02168 391 LELQIASL-----------NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERL 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 384 NRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMaLKDAKNKLEGLED---ALQKAKQDLARLLKEYQELMNV--KLALD 458
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELAQLQARLDS-LERLQENLEGFSEgvkALLKNQSGLSGILGVLSELISVdeGYEAA 538
|
....
gi 386849 459 VEIA 462
Cdd:TIGR02168 539 IEAA 542
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
328-469 |
4.40e-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: 44.92 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 328 DLDSIIAEVKAQYEEI-AQRSRAEAE-SWYQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVK--KQCAN 403
Cdd:COG1579 14 ELDSELDRLEHRLKELpAELAELEDElAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnKEYEA 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386849 404 LQAAIADAEQR---GEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQELmnvKLALDVEIATYRKLLE 469
Cdd:COG1579 94 LQKEIESLKRRisdLEDEILELMERIEELEEELAELEAELAELEAELEEK---KAELDEELAELEAELE 159
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
371-450 |
4.79e-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: 4.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 371 DDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRgemaLKDAKNKLEGLEDALQKAKQDLARLLKEYQEL 450
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELAELEKEIAEL 95
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
262-466 |
4.95e-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: 4.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 262 AENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRALYD---AELSQMQTHISDTsvvlsmdnnrNLDLDSIIAEVKA 338
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNelqAELEALQAEIDKL----------QAEIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 339 QYEEIAQRSRAEAESWYQTKYEELQVTAGRHGDDLRNtkqeIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEmA 418
Cdd:COG3883 84 RREELGERARALYRSGGSVSYLDVLLGSESFSDFLDR----LSALSKIADADADLLEELKADKAELEAKKAELEAKLA-E 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 386849 419 LKDAKNKLEGLEDALQKAKQD----LARLLKEYQELMNVKLALDVEIATYRK 466
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEqealLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
230-450 |
6.12e-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: 45.53 E-value: 6.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 230 ERGRLDSELRNMQDLVEDLKNKYEVEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRalydAELSQMQ 309
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR----AELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 310 THISDTSVVLSMDNNRNldldsiIAEVKAQYEEIAQRSRAEAesWYQTKYEELQvtagRHGDDLRNTKQEIAEINRMIQR 389
Cdd:COG4942 104 EELAELLRALYRLGRQP------PLALLLSPEDFLDAVRRLQ--YLKYLAPARR----EQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386849 390 LRSEIDHVKKQCANLQAAIADAEQRGEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQEL 450
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
328-466 |
7.12e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 7.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 328 DLDSIIAEVKAQYEEIAQRsRAEAEswyqTKYEELQVT-AGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQA 406
Cdd:COG4913 299 ELRAELARLEAELERLEAR-LDALR----EELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGL 373
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 407 AIADAEQRGEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVKLALDVEIATYRK 466
Cdd:COG4913 374 PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
282-452 |
1.66e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 282 ELQAKADTLTDEINFLRALY---DAELSQMQTHISDTSVVLSMDNNRnLDLDSI---IAEVKAQYEEI---------AQR 346
Cdd:COG4913 614 ALEAELAELEEELAEAEERLealEAELDALQERREALQRLAEYSWDE-IDVASAereIAELEAELERLdassddlaaLEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 347 SRAEAESWYQTKYEELQVTAGRHGDdlrnTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMALKDAKNKL 426
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGR----LEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELR 768
|
170 180
....*....|....*....|....*.
gi 386849 427 EGLEDALQKAKQDLARLLKEYQELMN 452
Cdd:COG4913 769 ENLEERIDALRARLNRAEEELERAMR 794
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
333-463 |
1.82e-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: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 333 IAEVKAQYEEIAQRSRAEAEswyqtKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAE 412
Cdd:COG1196 262 LAELEAELEELRLELEELEL-----ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 386849 413 QR---GEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVKLALDVEIAT 463
Cdd:COG1196 337 EEleeLEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
217-446 |
2.30e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 217 INNLRRQLDSIVGERGRLDSELRNMQDLVEDLKNKYEVEINKRTaaenEFVTLKKDVDAAYMNKVELQAKADTLTDEINF 296
Cdd:PRK02224 208 LNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE----ELETLEAEIEDLRETIAETEREREELAEEVRD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 297 LRALYDaELSQMQTHISDTSVVLSMDNN----RNLDLDSIIAEVKAQYEEI---AQRSRAEAESW------YQTKYEELQ 363
Cdd:PRK02224 284 LRERLE-ELEEERDDLLAEAGLDDADAEaveaRREELEDRDEELRDRLEECrvaAQAHNEEAESLredaddLEERAEELR 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 364 VTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMALK---DAKNKLEGLEDALQKAKQDL 440
Cdd:PRK02224 363 EEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREerdELREREAELEATLRTARERV 442
|
....*....
gi 386849 441 A---RLLKE 446
Cdd:PRK02224 443 EeaeALLEA 451
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
135-454 |
2.40e-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: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 135 QEVTVNQSLLTPLNLQIdpaiQRIGAEEREQIKTLNNKFASfidkvrfLEQQNKVLDTKWTLLQE-----------QGTK 203
Cdd:pfam05483 370 QRLEKNEDQLKIITMEL----QKKSSELEEMTKFKNNKEVE-------LEELKKILAEDEKLLDEkkqfekiaeelKGKE 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 204 TVRQNLEPLFEQYINNLRRQLDSIVGERGRLDSElrnmqdlVEDLKNKYEVEINKRTAaenefvtLKKDVDAAYMNKVEL 283
Cdd:pfam05483 439 QELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKE-------VEDLKTELEKEKLKNIE-------LTAHCDKLLLENKEL 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 284 QAKADTLTDEINFLRALYDAELSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIAQRSRAEAESWYQTKYEELQ 363
Cdd:pfam05483 505 TQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLK 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 364 VTAGRHGDDLR--NTKQEIAEINRMIQRLRSEIDHVKKQcanlqaaiADAEQRGEMALKDAKNKLEgLEdaLQKAKQDLA 441
Cdd:pfam05483 585 KEKQMKILENKcnNLKKQIENKNKNIEELHQENKALKKK--------GSAENKQLNAYEIKVNKLE-LE--LASAKQKFE 653
|
330
....*....|...
gi 386849 442 RLLKEYQELMNVK 454
Cdd:pfam05483 654 EIIDNYQKEIEDK 666
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
204-450 |
3.33e-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: 42.60 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 204 TVRQNLEPLFEqyINNLRRQLDSIVGERGRLDSELRNMQDLVEDLKNKYEveinkrtAAENEFVTLKKDVDAAYMNKVEL 283
Cdd:COG1579 1 AMPEDLRALLD--LQELDSELDRLEHRLKELPAELAELEDELAALEARLE-------AAKTELEDLEKEIKRLELEIEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 284 QAKADTLTDEINFLRalydaelsqmqthisdtsvvlsmdNNRnlDLDSIIAEVkaqyeEIAQRSRAEAEswyqtkyeelq 363
Cdd:COG1579 72 EARIKKYEEQLGNVR------------------------NNK--EYEALQKEI-----ESLKRRISDLE----------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 364 vtagrhgddlrntkQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMALKDAKNKLEGLEDALQKAKQDL-AR 442
Cdd:COG1579 110 --------------DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIpPE 175
|
....*...
gi 386849 443 LLKEYQEL 450
Cdd:COG1579 176 LLALYERI 183
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
371-477 |
4.33e-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: 4.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 371 DDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANL----------------QAAIADAEQRGEmALKDAKNKLEGLEDALQ 434
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALqrlaeyswdeidvasaEREIAELEAELE-RLDASSDDLAALEEQLE 695
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 386849 435 KAKQDLARLLKEYQELMNVKLALDVEIATYRKLLEGEECRLNG 477
Cdd:COG4913 696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
|
| DUF1351 |
pfam07083 |
Protein of unknown function (DUF1351); This family consists of several bacterial and phage ... |
326-461 |
4.52e-04 |
|
Protein of unknown function (DUF1351); This family consists of several bacterial and phage proteins of around 230 residues in length. The function of this family is unknown.
Pssm-ID: 429283 [Multi-domain] Cd Length: 210 Bit Score: 41.59 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 326 NLDLDSIIAEVKAQYEEIAQRSRAEAEswyqtKYEELQVTAgrhgDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCAnlq 405
Cdd:pfam07083 1 ELSVTQKPAAISFNFEELETYVDGIVA-----KYEGLVVTE----DTVKEAKKERAELNKIAKALDDKRKEVKKQYS--- 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386849 406 AAIADAEQRG---EMALKDAKNKL----EGLEDALQKAKQDLARLLK-EYQELMNVKLAlDVEI 461
Cdd:pfam07083 69 EPYDEFEAKIkelVAKIKEAIDPIdeqiKAFEEKEKDAKRQLVKALIsELAEEYGVPLE-EIEI 131
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
328-475 |
5.31e-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: 5.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 328 DLDSIIAEVKAQYEEIAQRSRA----EAESWYQTKYEELQVTAGRHGD---DLRNTKQEIAEINRMIQRLRSEIDHVKKQ 400
Cdd:COG4913 628 EAEERLEALEAELDALQERREAlqrlAEYSWDEIDVASAEREIAELEAeleRLDASSDDLAALEEQLEELEAELEELEEE 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 401 CANLQAAIADAEQRgemaLKDAKNKLEGLEDALQKA-----KQDLARLLKEYQELM------NVKLALDVEIATYRKLLE 469
Cdd:COG4913 708 LDELKGEIGRLEKE----LEQAEEELDELQDRLEAAedlarLELRALLEERFAAALgdaverELRENLEERIDALRARLN 783
|
....*.
gi 386849 470 GEECRL 475
Cdd:COG4913 784 RAEEEL 789
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
155-449 |
5.64e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.70 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 155 IQRIGAEEREQIKTLNNKF-------ASFIDKVRFLEQQNKVLDTKWTLLQEQgTKTVRQNLEPLfEQYINNLRRQLDSI 227
Cdd:TIGR04523 59 LDKNLNKDEEKINNSNNKIkileqqiKDLNDKLKKNKDKINKLNSDLSKINSE-IKNDKEQKNKL-EVELNKLEKQKKEN 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 228 VGERGRLDSELRNMQDLVEDLKNKYEVEINKRTAAENEFVTLKKDvdaaymnKVELQAKADTLTDEINFLRALydaeLSQ 307
Cdd:TIGR04523 137 KKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKE-------KLNIQKNIDKIKNKLLKLELL----LSN 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 308 MQTHISdtsvvlsmdnnRNLDLDSIIAEVKAQYEEIaqrsraeaeswyQTKYEELQvtagrhgDDLRNTKQEIAEINRMI 387
Cdd:TIGR04523 206 LKKKIQ-----------KNKSLESQISELKKQNNQL------------KDNIEKKQ-------QEINEKTTEISNTQTQL 255
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386849 388 QRLRSEIDHVKKQcanLQAAIADAEQrgemalkdAKNKLEGLEDALQKAKQDLARLLKEYQE 449
Cdd:TIGR04523 256 NQLKDEQNKIKKQ---LSEKQKELEQ--------NNKKIKELEKQLNQLKSEISDLNNQKEQ 306
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
333-466 |
5.90e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 5.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 333 IAEVKAQYEEIAQRsRAEAESWYQTKYEELQVTAGRHgdDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAE 412
Cdd:COG4717 390 ALEQAEEYQELKEE-LEELEEQLEELLGELEELLEAL--DEEELEEELEELEEELEELEEELEELREELAELEAELEQLE 466
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 386849 413 QRGEmalkdaknkLEGLEDALQKAKQDLARLLKEYQELMNVKLALDVEIATYRK 466
Cdd:COG4717 467 EDGE---------LAELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
158-474 |
6.39e-04 |
|
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: 42.65 E-value: 6.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 158 IGAEEREQIKTLNNKFASFIDKVRFLEQQnkvldtkWTLLQEQGTKTvrQNLEPLFEQYINNLRRQLDSIVGERGRLDSE 237
Cdd:TIGR00618 550 QLTSERKQRASLKEQMQEIQQSFSILTQC-------DNRSKEDIPNL--QNITVRLQDLTEKLSEAEDMLACEQHALLRK 620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 238 LR---NMQDLVEDLKNKYEVEINKRTAAENEFVTLKKDvdaaymnKVELQAKADTLTDEINFLRALydAELSQMQTHISD 314
Cdd:TIGR00618 621 LQpeqDLQDVRLHLQQCSQELALKLTALHALQLTLTQE-------RVREHALSIRVLPKELLASRQ--LALQKMQSEKEQ 691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 315 TSVVLSMDNNRNLDLDSI---IAEVKAQYEEIAQRSRA---------EAESWYQTKYEELQVTAGRHG--DDLRNTKQEI 380
Cdd:TIGR00618 692 LTYWKEMLAQCQTLLRELethIEEYDREFNEIENASSSlgsdlaareDALNQSLKELMHQARTVLKARteAHFNNNEEVT 771
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 381 AEINRM--IQRLRSEIDHVKKQCANLQAAIADAEQRGEMALKDAKNKLEGLEDALQKAKQDLARLLKEyqelmnvKLALD 458
Cdd:TIGR00618 772 AALQTGaeLSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEE-------KSATL 844
|
330
....*....|....*.
gi 386849 459 VEIAtyRKLLEGEECR 474
Cdd:TIGR00618 845 GEIT--HQLLKYEECS 858
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
335-472 |
6.99e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 6.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 335 EVKAQYEEIAQRSRAEAESWYQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQR 414
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 386849 415 gemaLKDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVKLALDVEIATYRKLLEGEE 472
Cdd:COG1196 297 ----LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
155-450 |
1.07e-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: 41.93 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 155 IQRIGAEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKwtlLQEQgtktvrQNLEPLFEQYINNLRRQLDSIVGERGRL 234
Cdd:TIGR04523 361 KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESK---IQNQ------EKLNQQKDEQIKKLQQEKELLEKEIERL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 235 DSELRNMQDLVEDLKNK------------------------YEVEINK-RTAAEN---EFVTLKKDVDAAYMNKVELQAK 286
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQdsvkeliiknldntresletqlkvLSRSINKiKQNLEQkqkELKSKEKELKKLNEEKKELEEK 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 287 ADTLTDEINFLRALYD---AELSQMQTHISD-TSVVLSMDNNRNldldsiiaevKAQYEEIAQRSRAEAESWYQT----- 357
Cdd:TIGR04523 512 VKDLTKKISSLKEKIEkleSEKKEKESKISDlEDELNKDDFELK----------KENLEKEIDEKNKEIEELKQTqkslk 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 358 -KYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIadaeqrgeMALKDAKNKL----EGLEDA 432
Cdd:TIGR04523 582 kKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSII--------KNIKSKKNKLkqevKQIKET 653
|
330
....*....|....*...
gi 386849 433 LQKAKQDLARLLKEYQEL 450
Cdd:TIGR04523 654 IKEIRNKWPEIIKKIKES 671
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
232-449 |
1.83e-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: 40.43 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 232 GRLDSELRNMQDLVEDLKNKY---EVEINKRTAaeNEFV-TLKKDVDaaymnkvELQAKADTLTDEIN-FLRAL--YDAE 304
Cdd:cd22656 87 GTIDSYYAEILELIDDLADATddeELEEAKKTI--KALLdDLLKEAK-------KYQDKAAKVVDKLTdFENQTekDQTA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 305 LSQMQTHISDtsvVLSMDNNRNL--DLDSIIAEVKAQYEEIAQRSRA---EAESWYQTKYEELQV------TAGRHGDDL 373
Cdd:cd22656 158 LETLEKALKD---LLTDEGGAIArkEIKDLQKELEKLNEEYAAKLKAkidELKALIADDEAKLAAalrliaDLTAADTDL 234
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386849 374 RNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQrgemALKDAKNKLEGLEDALQKAKqDLARLLKEYQE 449
Cdd:cd22656 235 DNLLALIGPAIPALEKLQGAWQAIATDLDSLKDLLEDDIS----KIPAAILAKLELEKAIEKWN-ELAEKADKFRQ 305
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
210-480 |
2.01e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.04 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 210 EPLFEQYINNLRRQLDSIVGERGRLDSELRNMQDLvEDLKNKYEVEINK---RTAAENEFVTLKKDV---------DAAY 277
Cdd:PRK01156 213 HSITLKEIERLSIEYNNAMDDYNNLKSALNELSSL-EDMKNRYESEIKTaesDLSMELEKNNYYKELeerhmkiinDPVY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 278 MNKVELQAKADTLTDEINFLRAL--YDAELSQMQTHISDTSVVLSMDNN------RNLDLDSIIAEVKaQYEEIAQRSRA 349
Cdd:PRK01156 292 KNRNYINDYFKYKNDIENKKQILsnIDAEINKYHAIIKKLSVLQKDYNDyikkksRYDDLNNQILELE-GYEMDYNSYLK 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 350 EAESwYQTKYEELQVTAGRHGDDLRNT--KQEI--AEINRMIQRLRSEIDHVKKQCANLQAAIaDAEQRGEMALKDAKNK 425
Cdd:PRK01156 371 SIES-LKKKIEEYSKNIERMSAFISEIlkIQEIdpDAIKKELNEINVKLQDISSKVSSLNQRI-RALRENLDELSRNMEM 448
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 426 LEG---------------LEDALQKAKQDLARLLKEYQELMNVKLALDVEIATYRKLLEgeecRLNGEGV 480
Cdd:PRK01156 449 LNGqsvcpvcgttlgeekSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKE----YLESEEI 514
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
222-450 |
2.01e-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: 41.21 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 222 RQLDSIVGERGRLDSELRNMQDLVEDLKNKYEVEINKRTAAENEFVTLKKDVDAAYMNKVELQAKA------------DT 289
Cdd:TIGR02169 716 RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALndlearlshsriPE 795
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 290 LTDEINFLRAlydaELSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIAQR--SRAEAESWYQTKYEELQvtag 367
Cdd:TIGR02169 796 IQAELSKLEE----EVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQikSIEKEIENLNGKKEELE---- 867
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 368 rhgDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAeqrgEMALKDAKNKLEGLEDALQKAKQDLARLLKEY 447
Cdd:TIGR02169 868 ---EELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEL----EAQIEKKRKRLSELKAKLEALEEELSEIEDPK 940
|
...
gi 386849 448 QEL 450
Cdd:TIGR02169 941 GED 943
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
371-475 |
2.35e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.39 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 371 DDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQEL 450
Cdd:smart00787 158 EDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQEL 237
|
90 100 110
....*....|....*....|....*....|..
gi 386849 451 -------MNVKLALDVEIATYRKLLegEECRL 475
Cdd:smart00787 238 eskiedlTNKKSELNTEIAEAEKKL--EQCRG 267
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
371-484 |
2.58e-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: 40.82 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 371 DDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQ-------RGEMALKD---AKNKLEGLEDALQKAKQDL 440
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRkigeiekEIEQLEQEeekLKERLEELEEDLSSLEQEI 753
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 386849 441 ARLLKEYQELMNVKLALDVEIATYRKLLEGEECRLNGEGVGQVN 484
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQ 797
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
333-444 |
2.74e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 40.24 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 333 IAEVKAQYEEIAQRSRAEAESWYQTKYEELQVTAGRHGDDLRNTKQ-EIAEINRMIQRLRSEIDHVKKQCANLQAAIADA 411
Cdd:COG2268 246 LAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREiELQEKEAEREEAELEADVRKPAEAEKQAAEAEA 325
|
90 100 110
....*....|....*....|....*....|....*.
gi 386849 412 EQRGEMALKDAKNKLEGLE---DALQKAKQDLARLL 444
Cdd:COG2268 326 EAEAEAIRAKGLAEAEGKRalaEAWNKLGDAAILLM 361
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
380-475 |
3.14e-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: 40.44 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 380 IAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEmALKDAKNKLEGLeDALQKAKQDLA--RLLKEYQELMNVKLAL 457
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLE-RLRREREKAERY-QALLKEKREYEgyELLKEKEALERQKEAI 242
|
90
....*....|....*...
gi 386849 458 DVEIATYRKLLEGEECRL 475
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEI 260
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
329-466 |
3.14e-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: 39.52 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 329 LDSIIAEVKAQYEEIAQRSRAEAEswYQTKYEELQVTAGRHGDDLRNTKQEIAEI---------NRMIQRLRSEIDHVKK 399
Cdd:COG1579 26 LKELPAELAELEDELAALEARLEA--AKTELEDLEKEIKRLELEIEEVEARIKKYeeqlgnvrnNKEYEALQKEIESLKR 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386849 400 QCANLQAAIADAEQRgemaLKDAKNKLEGLEDALQKAKQDLARLLKEYQELMNvklALDVEIATYRK 466
Cdd:COG1579 104 RISDLEDEILELMER----IEELEEELAELEAELAELEAELEEKKAELDEELA---ELEAELEELEA 163
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
325-472 |
3.26e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 325 RNLDLDSIIAEVKAQYEEIAQRSRAEAESwyQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANL 404
Cdd:COG1196 223 KELEAELLLLKLRELEAELEELEAELEEL--EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386849 405 QAAIADAEQRG---EMALKDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVKLALDVEIATYRKLLEGEE 472
Cdd:COG1196 301 EQDIARLEERRrelEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
357-478 |
3.32e-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: 39.52 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 357 TKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGE------MALKDAKNkLEGLE 430
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKkyeeqlGNVRNNKE-YEALQ 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 386849 431 DALQKAKQDLARLLKEYQELMNVKLALDVEIATYRKLLEGEECRLNGE 478
Cdd:COG1579 96 KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK 143
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
231-469 |
4.19e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.21 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 231 RGRLDSELRNMQDLVEDLKNKYEV-----EINKRTAAENEFVTLKKDVDAAYM-----------NKVELQAKADTLTDEI 294
Cdd:pfam12128 220 RQQVEHWIRDIQAIAGIMKIRPEFtklqqEFNTLESAELRLSHLHFGYKSDETliasrqeerqeTSAELNQLLRTLDDQW 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 295 NFLRALYDAELSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIAQRSRAEAESwyqtKYEELQVTAGRHGDDLR 374
Cdd:pfam12128 300 KEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELEN----LEERLKALTGKHQDVTA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 375 NTKQEIAEI----NRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMALKD--------AKNKLEGLEDALQKAKQDLAR 442
Cdd:pfam12128 376 KYNRRRSKIkeqnNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREqleagkleFNEEEYRLKSRLGELKLRLNQ 455
|
250 260
....*....|....*....|....*..
gi 386849 443 LLKEYQELMNVKlALDVEIATYRKLLE 469
Cdd:pfam12128 456 ATATPELLLQLE-NFDERIERAREEQE 481
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
334-449 |
4.49e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 334 AEVKAQYEEIAQRSRAEAE-----SWYQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAI 408
Cdd:PRK12704 58 ALLEAKEEIHKLRNEFEKElrerrNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELI 137
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 386849 409 ADAEQRGE----MALKDAKNKLegLEDALQKAKQDLARLLKEYQE 449
Cdd:PRK12704 138 EEQLQELErisgLTAEEAKEIL--LEKVEEEARHEAAVLIKEIEE 180
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
160-446 |
9.87e-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: 39.00 E-value: 9.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 160 AEEREQIKTLN---NKFASFI----------DKVRF-LEQQNKVLDTKWTLLQEQgTKTVRQNLEPLFEQyinnLRRQLD 225
Cdd:pfam01576 169 AEEEEKAKSLSklkNKHEAMIsdleerlkkeEKGRQeLEKAKRKLEGESTDLQEQ-IAELQAQIAELRAQ----LAKKEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 226 SIVGERGRLDSE----------LRNMQDLVEDLKNKYEVEINKRTAAENEFVTLKKDVDAAymnKVELQAKADTlTDEIN 295
Cdd:pfam01576 244 ELQAALARLEEEtaqknnalkkIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEAL---KTELEDTLDT-TAAQQ 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 296 FLRALYDAELSQMQTHISDTSVVLsmdnnrnldldsiiaevKAQYEEIAQRSRAE----AESWYQTKYEELQVTAGRHGd 371
Cdd:pfam01576 320 ELRSKREQEVTELKKALEEETRSH-----------------EAQLQEMRQKHTQAleelTEQLEQAKRNKANLEKAKQA- 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386849 372 dLRNTKQEIAEINRMIQRLRSEIDHVKK----QCANLQAAIADAE-QRGEMALKDAK--NKLEGLEDALQKAKQDLARLL 444
Cdd:pfam01576 382 -LESENAELQAELRTLQQAKQDSEHKRKklegQLQELQARLSESErQRAELAEKLSKlqSELESVSSLLNEAEGKNIKLS 460
|
..
gi 386849 445 KE 446
Cdd:pfam01576 461 KD 462
|
|
| |
