|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
162-475 |
2.76e-151 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 436.66 E-value: 2.76e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 162 EEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWTLLQEQGTKTVRqNLEPLFEQYINNLRRQLDSIVGERGRLDSELRG 241
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPS-RLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 242 MQDLVEDFKNKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRALYDAELSQMQTHISDTSVVLS 321
Cdd:pfam00038 80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 322 MDNNRNLDLDSIIAEVKAQYEEIAQRSRAEAESWYQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQ 401
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5031839 402 CANLQAAIADAEQRGEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVKLALDVEIATYRKLLEGEECR 475
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
59-159 |
4.30e-19 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 84.32 E-value: 4.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 59 RSLYGLGGSKRISI---GGGSCAISG---GYGSRAGGSYGFGGAGSGFGFGGG-------AGIGFGLGGGAGLAGGFGGP 125
Cdd:pfam16208 43 RSLYNLGGSKSISIsvaGGGSRPGSGfgfGGGGGGGFGGGFGGGGGGGFGGGGgfgggfgGGGYGGGGFGGGGFGGRGGF 122
|
90 100 110
....*....|....*....|....*....|....
gi 5031839 126 GFPVCPPGGIQEVTVNQSLLTPLNLQIDPTIQRV 159
Cdd:pfam16208 123 GGPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
162-457 |
8.05e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.08 E-value: 8.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 162 EEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWTLLQEQGTKTVRQNLEplFEQYINNLRRQLDSIVGERGRLDSELRG 241
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE--LSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 242 MQDLVEDFKNKYEDEINKRTAAENEFVTLKKdvdaaymNKVELQAKADTLTDEINFLRALYD---AELSQMQTHISDTSV 318
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEA-------EIEELEAQIEQLKEELKALREALDelrAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 319 VLSMDNNR-------NLDLDSIIAEVKAQYEEIAQ----------RSRAEAESWYQtKYEELQVTAGRHGDDLRNTKQEI 381
Cdd:TIGR02168 825 RLESLERRiaaterrLEDLEEQIEELSEDIESLAAeieeleelieELESELEALLN-ERASLEEALALLRSELEELSEEL 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 382 AEINRMIQRLRSEIDHVKKQCANLQAAIADAEQR-----------GEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQE 450
Cdd:TIGR02168 904 RELESKRSELRRELEELREKLAQLELRLEGLEVRidnlqerlseeYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
....*..
gi 5031839 451 LMNVKLA 457
Cdd:TIGR02168 984 LGPVNLA 990
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
303-443 |
3.27e-07 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 52.66 E-value: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 303 DAELSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEiAQRSRAEAESWYQTKYEELQVTAGRHGD---DLRNTKQ 379
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSA-AEAERSRLQALLAELAGAGAAAEGRAGElaqELDSEKQ 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5031839 380 EIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGemalKDAKNKLEG----LEDALQKAKQDLAR 443
Cdd:PRK09039 131 VSARALAQVELLNQQIAALRRQLAALEAALDASEKRD----RESQAKIADlgrrLNVALAQRVQELNR 194
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
152-473 |
5.75e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.60 E-value: 5.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 152 IDPT-IQRVRAEEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWTLLQEQ------GTKTVRQNLEPLFEQYINNLRR- 223
Cdd:PRK01156 402 IDPDaIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpvcGTTLGEEKSNHIINHYNEKKSRl 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 224 --QLDSIVGERGRLDSELRGMQDLVEDFKNKyedEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRAL 301
Cdd:PRK01156 482 eeKIREIEIEVKDIDEKIVDLKKRKEYLESE---EINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSL 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 302 YDAELSQMQTHISDTSVVLSmdnnrNLDLDSIIA---EVKAQYEEIAQRSRaEAESWYQTKYEELQVTAGRHGDD---LR 375
Cdd:PRK01156 559 KLEDLDSKRTSWLNALAVIS-----LIDIETNRSrsnEIKKQLNDLESRLQ-EIEIGFPDDKSYIDKSIREIENEannLN 632
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 376 NTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMALkDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVK 455
Cdd:PRK01156 633 NKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRIN-DIEDNLKKSRKALDDAKANRARLESTIEILRTRI 711
|
330
....*....|....*...
gi 5031839 456 LALDVEIATYRKLLEGEE 473
Cdd:PRK01156 712 NELSDRINDINETLESMK 729
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
221-470 |
1.05e-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: 51.99 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 221 LRRQLDSIVGERGRLDSELRGMQDLVEDFKNKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRA 300
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 301 L---YDAELSQMQTHISdtSVVLSMDNNRNLDLDSIIAEVKAQYEEI-AQRSRAEAeswyqtKYEELQVTAGRHGDDLRN 376
Cdd:TIGR02169 759 ElkeLEARIEELEEDLH--KLEEALNDLEARLSHSRIPEIQAELSKLeEEVSRIEA------RLREIEQKLNRLTLEKEY 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 377 TKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRgemaLKDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVKL 456
Cdd:TIGR02169 831 LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE----LEELEAALRDLESRLGDLKKERDELEAQLRELERKIE 906
|
250
....*....|....
gi 5031839 457 ALDVEIATYRKLLE 470
Cdd:TIGR02169 907 ELEAQIEKKRKRLS 920
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
151-451 |
1.71e-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: 51.22 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 151 QIDPTIQRVRaEEREQIKTLNNKFASFIDKVRflEQQNKVLETKWTLLQEQGTKTVRQNLE-PLFEQYINNLRRQLDSIV 229
Cdd:TIGR02169 167 EFDRKKEKAL-EELEEVEENIERLDLIIDEKR--QQLERLRREREKAERYQALLKEKREYEgYELLKEKEALERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 230 GERGRLDSELRGMQDLVEDFKNKYE------DEINKRTAA--ENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFL--- 298
Cdd:TIGR02169 244 RQLASLEEELEKLTEEISELEKRLEeieqllEELNKKIKDlgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAeer 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 299 RALYDAELSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIAQR----------------SRAEAESWYQTKYEE 362
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEleevdkefaetrdelkDYREKLEKLKREINE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 363 LQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQrgemalkdaknKLEGLEDALQKAKQDLA 442
Cdd:TIGR02169 404 LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEW-----------KLEQLAADLSKYEQELY 472
|
....*....
gi 5031839 443 RLLKEYQEL 451
Cdd:TIGR02169 473 DLKEEYDRV 481
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
206-479 |
1.96e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 206 VRQNLEPLFEQ------YiNNLRRQLDsivgergRLDSELRGMQDlvEDFKNKYEDEINKRTAAENEFVTLKKDVDAAYM 279
Cdd:COG1196 198 LERQLEPLERQaekaerY-RELKEELK-------ELEAELLLLKL--RELEAELEELEAELEELEAELEELEAELAELEA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 280 NKVELQAKADTLTDEINFLRALYDAELSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIAQRSRAEAESwyQTK 359
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL--EEE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 360 YEELQvtagrhgDDLRNTKQEIAEINRMIQRLRSEIDHVKKQcanlQAAIADAEQRGEMALKDAKNKLEGLEDALQKAKQ 439
Cdd:COG1196 346 LEEAE-------EELEEAEAELAEAEEALLEAEAELAEAEEE----LEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 5031839 440 DLARLLKEYQELMNVKLALDVEIATYRKLLEGEECRLNGE 479
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
191-451 |
2.12e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 191 LETKWTLLQEQGTKTVRqnleplFEQYINNLRR-QLDSIVGERGRLDSELRGMQDLVEDFKNKYEDEINKRTAAENEFVT 269
Cdd:TIGR02168 198 LERQLKSLERQAEKAER------YKELKAELRElELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 270 LKKDVDAAYMNKVELQAKADTLTDEINFL---RALYDAELSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIAQ 346
Cdd:TIGR02168 272 LRLEVSELEEEIEELQKELYALANEISRLeqqKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 347 RSRA------EAESWYQ---TKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQR-G 416
Cdd:TIGR02168 352 ELESleaeleELEAELEeleSRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKlE 431
|
250 260 270
....*....|....*....|....*....|....*
gi 5031839 417 EMALKDAKNKLEGLEDALQKAKQDLARLLKEYQEL 451
Cdd:TIGR02168 432 EAELKELQAELEELEEELEELQEELERLEEALEEL 466
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
279-479 |
3.04e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 279 MNKVELQAKADT----LTDEINFL-RALYDAELSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIaQRSRAEAE 353
Cdd:TIGR02168 202 LKSLERQAEKAErykeLKAELRELeLALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL-RLEVSELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 354 SwyqtKYEELQvtagrhgDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMA---LKDAKNKLEGL 430
Cdd:TIGR02168 281 E----EIEELQ-------KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELaeeLAELEEKLEEL 349
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 5031839 431 EDALQKAKQDLARLLKEYQELMNVKLALDVEIATYRK---LLEGEECRLNGE 479
Cdd:TIGR02168 350 KEELESLEAELEELEAELEELESRLEELEEQLETLRSkvaQLELQIASLNNE 401
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
165-473 |
7.78e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 7.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 165 EQIKTLNNKFASFIDKVRFLEQQNKVLETKWTLLQEQgtktvRQNLEPLFEQyINNLRRQLDSIVGERGRLDSELRGMQD 244
Cdd:PRK03918 193 ELIKEKEKELEEVLREINEISSELPELREELEKLEKE-----VKELEELKEE-IEELEKELESLEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 245 LVEDFKNKYEdEINKRTAAENEfvtLKKDVDaAYMNKVELQAKADTLTDEINFLRALYDAELSQMQTHISDtsvvLSMDN 324
Cdd:PRK03918 267 RIEELKKEIE-ELEEKVKELKE---LKEKAE-EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE----LEEKE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 325 NRNLDLDSIIAEVKAQYEEIAQRSRAeaeswyqtkYEELQVTAGRhgddLRNTKQEIA-----EINRMIQRLRSEIDHVK 399
Cdd:PRK03918 338 ERLEELKKKLKELEKRLEELEERHEL---------YEEAKAKKEE----LERLKKRLTgltpeKLEKELEELEKAKEEIE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 400 KQCANLQAAIADAEQRGE------MALKDAKNKL---------EGLEDALQKAKQDLARLLKEYQELMNVKLALDVEIAT 464
Cdd:PRK03918 405 EEISKITARIGELKKEIKelkkaiEELKKAKGKCpvcgrelteEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRE 484
|
....*....
gi 5031839 465 YRKLLEGEE 473
Cdd:PRK03918 485 LEKVLKKES 493
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
215-490 |
1.98e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 215 EQYIN-NLRRQLDSIVGERGRLDSELRGMQDLVEDFKNKYEDeinkrTAAENEFVTLKKDVDAAYMNKVELQAKADTLTD 293
Cdd:COG3206 159 EAYLEqNLELRREEARKALEFLEEQLPELRKELEEAEAALEE-----FRQKNGLVDLSEEAKLLLQQLSELESQLAEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 294 EINFLRALYDAELSQMQTHISDTSVVLSmdnnrnldlDSIIAEVKAQYEEIaqrsraeaeswyQTKYEELQVTAGRHGDD 373
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALPELLQ---------SPVIQQLRAQLAEL------------EAELAELSARYTPNHPD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 374 LRNTKQEIAEINRMIQRLRSEIDhvkkqcANLQAAIADAEQRgemalkdaKNKLEGLEDALQKAKQDLARLLKEYQELMN 453
Cdd:COG3206 293 VIALRAQIAALRAQLQQEAQRIL------ASLEAELEALQAR--------EASLQAQLAQLEARLAELPELEAELRRLER 358
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 5031839 454 vklalDVEIA--TYRKLLEG-EECRLNgEGVGQVNISVVQ 490
Cdd:COG3206 359 -----EVEVAreLYESLLQRlEEARLA-EALTVGNVRVID 392
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
263-473 |
2.22e-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: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 263 AENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRALYD---AELSQMQTHISDTsvvlsmdnnrNLDLDSIIAEVKA 339
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNelqAELEALQAEIDKL----------QAEIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 340 QYEEIAQRSRAEAESWYQTKYEELQVTAGRHGDDLRNtkqeIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQrgema 419
Cdd:COG3883 84 RREELGERARALYRSGGSVSYLDVLLGSESFSDFLDR----LSALSKIADADADLLEELKADKAELEAKKAELEA----- 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 5031839 420 lkdAKNKLEGLEDALQKAKQDLARLLKEYQELMNvklALDVEIATYRKLLEGEE 473
Cdd:COG3883 155 ---KLAELEALKAELEAAKAELEAQQAEQEALLA---QLSAEEAAAEAQLAELE 202
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
157-444 |
2.42e-05 |
|
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: 47.48 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 157 QRVRAEEREQIKTLNNKFASFIDKVRFLEQQN-------KVLETKWTLLQEQGTKTVRQNLE-----PLFEQYINNLRRQ 224
Cdd:pfam01576 425 ERQRAELAEKLSKLQSELESVSSLLNEAEGKNiklskdvSSLESQLQDTQELLQEETRQKLNlstrlRQLEDERNSLQEQ 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 225 LDSIVGERGRLDSELRGMQDLVEDFKNKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLtdeinflralyDA 304
Cdd:pfam01576 505 LEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKL-----------EK 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 305 ELSQMQTHISDTSVVLsmDNNRNL---------DLDSIIAEVK---AQYEEiaQRSRAEAESwyqTKYEELQVTAGRHGD 372
Cdd:pfam01576 574 TKNRLQQELDDLLVDL--DHQRQLvsnlekkqkKFDQMLAEEKaisARYAE--ERDRAEAEA---REKETRALSLARALE 646
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5031839 373 DLRNTKQEIAEINRMIQ----RLRSEIDHVKKQCANLQAAIADAEQrgemALKDAKNKLEGLEDALQKAKQDLARL 444
Cdd:pfam01576 647 EALEAKEELERTNKQLRaemeDLVSSKDDVGKNVHELERSKRALEQ----QVEEMKTQLEELEDELQATEDAKLRL 718
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
373-454 |
6.14e-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: 6.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 373 DLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQR---GEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQ 449
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELA 107
|
....*
gi 5031839 450 ELMNV 454
Cdd:COG4942 108 ELLRA 112
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
179-447 |
7.24e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.39 E-value: 7.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 179 DKVRFLEQQNKVLETKWTLLQEQgTKTvrqnleplFEQYINNLRRQLDSIVgergrldSELRGMQD-LVEDFKNkYEDEI 257
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQ-IKT--------YNKNIEEQRKKNGENI-------ARKQNKYDeLVEEAKT-IKAEI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 258 NKRTAAENEFVTLKKDVDAAY----MNKVELQAKADTLTDEINFLRAlYDAELSQMQThISDTsvvlsmdnnrnldlDSI 333
Cdd:PHA02562 237 EELTDELLNLVMDIEDPSAALnklnTAAAKIKSKIEQFQKVIKMYEK-GGVCPTCTQQ-ISEG--------------PDR 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 334 IAEVKAQYEEIAQRSRAEaeswyQTKYEELQVTAGRHgDDLRNTKQE----IAEINRMIQRLRSEIDHVKKQCANLQAAI 409
Cdd:PHA02562 301 ITKIKDKLKELQHSLEKL-----DTAIDELEEIMDEF-NEQSKKLLElknkISTNKQSLITLVDKAKKVKAAIEELQAEF 374
|
250 260 270
....*....|....*....|....*....|....*...
gi 5031839 410 adaeqrgemalKDAKNKLEGLEDALQKAKQDLARLLKE 447
Cdd:PHA02562 375 -----------VDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
372-451 |
1.03e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 372 DDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRgemaLKDAKNKLEGLEDALQKAKQDLARLLKEYQEL 451
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELAELEKEIAEL 95
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
230-453 |
1.54e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 230 GERGRLDSELRGMQDLVEDFKNkyedeINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRAL-----YDA 304
Cdd:COG4913 587 GTRHEKDDRRRIRSRYVLGFDN-----RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLaeyswDEI 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 305 ELSQMQTHISDTSVVLsmdnnRNLDLDS-IIAEVKAQYEEiAQRSRAEAESwyqtKYEELQVTAGRHgddlrntKQEIAE 383
Cdd:COG4913 662 DVASAEREIAELEAEL-----ERLDASSdDLAALEEQLEE-LEAELEELEE----ELDELKGEIGRL-------EKELEQ 724
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 384 INRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQELMN 453
Cdd:COG4913 725 AEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMR 794
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
329-467 |
1.61e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 329 DLDSIIAEVKAQYEEIAQRsRAEAEswyqTKYEELQVT-AGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQA 407
Cdd:COG4913 299 ELRAELARLEAELERLEAR-LDALR----EELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGL 373
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 408 AIADAEQRGEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVKLALDVEIATYRK 467
Cdd:COG4913 374 PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
329-470 |
2.61e-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: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 329 DLDSIIAEVKAQYEEI-AQRSRAEAE-SWYQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVK--KQCAN 404
Cdd:COG1579 14 ELDSELDRLEHRLKELpAELAELEDElAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnKEYEA 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5031839 405 LQAAIADAEQR---GEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQELmnvKLALDVEIATYRKLLE 470
Cdd:COG1579 94 LQKEIESLKRRisdLEDEILELMERIEELEEELAELEAELAELEAELEEK---KAELDEELAELEAELE 159
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
231-451 |
4.55e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 4.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 231 ERGRLDSELRGMQDLVEDFKNKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRalydAELSQMQ 310
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR----AELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 311 THISDTSVVLSMDNNRNldldsiIAEVKAQYEEIAQRSRAEAesWYQTKYEELQvtagRHGDDLRNTKQEIAEINRMIQR 390
Cdd:COG4942 104 EELAELLRALYRLGRQP------PLALLLSPEDFLDAVRRLQ--YLKYLAPARR----EQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5031839 391 LRSEIDHVKKQCANLQAAIADAEQRGEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQEL 451
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
218-437 |
5.04e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 5.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 218 INNLRRQLDSIVGERGRLDSELRGMQDLVEDFKNKYEDEINKRTAAENEFVTLKKDVDaaymnkvELQAKADTLTDEI-N 296
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA-------EAEAEIEERREELgE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 297 FLRALYDAELSqmqthISDTSVVLSMDN-----NRNLDLDSIIAEVKAQYEEI--AQRSRAEAESWYQTKYEELQVTAGR 369
Cdd:COG3883 91 RARALYRSGGS-----VSYLDVLLGSESfsdflDRLSALSKIADADADLLEELkaDKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5031839 370 HGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMALKDAKNKLEGLEDALQKA 437
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
149-463 |
5.71e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 5.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 149 NLQIDPTIQRVRaEEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWTLLQEQgtktvRQNLEPLFEQY----------I 218
Cdd:TIGR02168 224 ELELALLVLRLE-ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLE-----VSELEEEIEELqkelyalaneI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 219 NNLRRQLDSIVGERGRLDSELRGMQDLVEDFKNK---YEDEINKRTA----AENEFVTLKKDVDAAYMNKVELQAKADTL 291
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEAQLEELESKldeLAEELAELEEkleeLKEELESLEAELEELEAELEELESRLEEL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 292 TDEINFLRALYDAELSQMQTHisdtsvvlsmdNNRNLDLDSIIAEVKAQYEEIAQRSRAEAESWYQTKYEELQVTAGRHG 371
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASL-----------NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 372 DDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMaLKDAKNKLEGLED---ALQKAKQDLARLLKEY 448
Cdd:TIGR02168 447 EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS-LERLQENLEGFSEgvkALLKNQSGLSGILGVL 525
|
330
....*....|....*..
gi 5031839 449 QELMNV--KLALDVEIA 463
Cdd:TIGR02168 526 SELISVdeGYEAAIEAA 542
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
136-315 |
6.06e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 6.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 136 QEVTVNQSLLTPLNLQIDptiQRVRAEEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWTLLQEQGTKTVRQNLEPLfE 215
Cdd:COG4913 269 ERLAELEYLRAALRLWFA---QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQL-E 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 216 QYINNLRRQLDSIVGERGRLDSELRGMQ----DLVEDFKNKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTL 291
Cdd:COG4913 345 REIERLERELEERERRRARLEALLAALGlplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREL 424
|
170 180
....*....|....*....|....*..
gi 5031839 292 TDEINFLRA---LYDAELSQMQTHISD 315
Cdd:COG4913 425 EAEIASLERrksNIPARLLALRDALAE 451
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
372-478 |
9.86e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 9.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 372 DDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANL----------------QAAIADAEQRGEmALKDAKNKLEGLEDALQ 435
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALqrlaeyswdeidvasaEREIAELEAELE-RLDASSDDLAALEEQLE 695
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 5031839 436 KAKQDLARLLKEYQELMNVKLALDVEIATYRKLLEGEECRLNG 478
Cdd:COG4913 696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
329-476 |
1.36e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 329 DLDSIIAEVKAQYEEIAQRSRA----EAESWYQTKYEELQVTAGRHGD---DLRNTKQEIAEINRMIQRLRSEIDHVKKQ 401
Cdd:COG4913 628 EAEERLEALEAELDALQERREAlqrlAEYSWDEIDVASAEREIAELEAeleRLDASSDDLAALEEQLEELEAELEELEEE 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 402 CANLQAAIADAEQRgemaLKDAKNKLEGLEDALQKA-----KQDLARLLKEYQELM------NVKLALDVEIATYRKLLE 470
Cdd:COG4913 708 LDELKGEIGRLEKE----LEQAEEELDELQDRLEAAedlarLELRALLEERFAAALgdaverELRENLEERIDALRARLN 783
|
....*.
gi 5031839 471 GEECRL 476
Cdd:COG4913 784 RAEEEL 789
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
155-455 |
2.21e-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: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 155 TIQRVRAEEREQIKTLNNKFASFIDKVRFLEQQNKVLETKwtlLQEQgtktvrQNLEPLFEQYINNLRRQLDSIVGERGR 234
Cdd:TIGR04523 360 EKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESK---IQNQ------EKLNQQKDEQIKKLQQEKELLEKEIER 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 235 LDSElrgmqdlVEDFKNKYEDEINKRTAAENEFVTLKKDVDaaymnkvELQAKADTLTDEINFLRalydAELSQMQTHIS 314
Cdd:TIGR04523 431 LKET-------IIKNNSEIKDLTNQDSVKELIIKNLDNTRE-------SLETQLKVLSRSINKIK----QNLEQKQKELK 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 315 DTSVVLSMDNNRNLDLDSIIAEVKAQYEEIAQRSR------AEAESWYQTKYEELQvtagrhGDDLRNTKQ----EIAEI 384
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEklesekKEKESKISDLEDELN------KDDFELKKEnlekEIDEK 566
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5031839 385 NRMIQRLRSEIDHVKKQCANLQAAIADAEQRgemaLKDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVK 455
Cdd:TIGR04523 567 NKEIEELKQTQKSLKKKQEEKQELIDQKEKE----KKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSII 633
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
334-467 |
2.22e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 334 IAEVKAQYEEIAQRsRAEAESWYQTKYEELQVTAGRHgdDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAE 413
Cdd:COG4717 390 ALEQAEEYQELKEE-LEELEEQLEELLGELEELLEAL--DEEELEEELEELEEELEELEEELEELREELAELEAELEQLE 466
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 5031839 414 QRGEmalkdaknkLEGLEDALQKAKQDLARLLKEYQELMNVKLALDVEIATYRK 467
Cdd:COG4717 467 EDGE---------LAELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
|
|
| DUF1351 |
pfam07083 |
Protein of unknown function (DUF1351); This family consists of several bacterial and phage ... |
327-462 |
2.30e-03 |
|
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: 39.67 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 327 NLDLDSIIAEVKAQYEEIAQRSRAEAEswyqtKYEELQVTAgrhgDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCAnlq 406
Cdd:pfam07083 1 ELSVTQKPAAISFNFEELETYVDGIVA-----KYEGLVVTE----DTVKEAKKERAELNKIAKALDDKRKEVKKQYS--- 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5031839 407 AAIADAEQRG---EMALKDAKNKL----EGLEDALQKAKQDLARLLK-EYQELMNVKLAlDVEI 462
Cdd:pfam07083 69 EPYDEFEAKIkelVAKIKEAIDPIdeqiKAFEEKEKDAKRQLVKALIsELAEEYGVPLE-EIEI 131
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
156-455 |
2.36e-03 |
|
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: 40.86 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 156 IQRVRAEEREQIKTLNNKFASfidkvrfLEQQNKVLETKWTLLQE-----------QGTKTVRQNLEPLFEQYINNLRRQ 224
Cdd:pfam05483 386 LQKKSSELEEMTKFKNNKEVE-------LEELKKILAEDEKLLDEkkqfekiaeelKGKEQELIFLLQAREKEIHDLEIQ 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 225 LDSIVGERGRLDSElrgmqdlVEDFKNKYEDEINKRTAaenefvtLKKDVDAAYMNKVELQAKADTLTDEINFLRALYDA 304
Cdd:pfam05483 459 LTAIKTSEEHYLKE-------VEDLKTELEKEKLKNIE-------LTAHCDKLLLENKELTQEASDMTLELKKHQEDIIN 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 305 ELSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIAQRSRAEAESWYQTKYEELQVTAGRHGDDLR--NTKQEIA 382
Cdd:pfam05483 525 CKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKcnNLKKQIE 604
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5031839 383 EINRMIQRLRSEIDHVKKQcanlqaaiADAEQRGEMALKDAKNKLEgLEdaLQKAKQDLARLLKEYQELMNVK 455
Cdd:pfam05483 605 NKNKNIEELHQENKALKKK--------GSAENKQLNAYEIKVNKLE-LE--LASAKQKFEEIIDNYQKEIEDK 666
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
218-447 |
3.11e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 218 INNLRRQLDSIVGERGRLDSELRGMQDLVEDFKNKYEDEINKRTaaenEFVTLKKDVDAAYMNKVELQAKADTLTDEINF 297
Cdd:PRK02224 208 LNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE----ELETLEAEIEDLRETIAETEREREELAEEVRD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 298 LRALYDaELSQMQTHISDTSVVLSMDNN----RNLDLDSIIAEVKAQYEEI---AQRSRAEAESW------YQTKYEELQ 364
Cdd:PRK02224 284 LRERLE-ELEEERDDLLAEAGLDDADAEaveaRREELEDRDEELRDRLEECrvaAQAHNEEAESLredaddLEERAEELR 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 365 VTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMALK---DAKNKLEGLEDALQKAKQDL 441
Cdd:PRK02224 363 EEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREerdELREREAELEATLRTARERV 442
|
....*....
gi 5031839 442 A---RLLKE 447
Cdd:PRK02224 443 EeaeALLEA 451
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
334-445 |
5.26e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 39.47 E-value: 5.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 334 IAEVKAQYEEIAQRSRAEAESWYQTKYEELQVTAGRHGDDLRNTKQ-EIAEINRMIQRLRSEIDHVKKQCANLQAAIADA 412
Cdd:COG2268 246 LAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREiELQEKEAEREEAELEADVRKPAEAEKQAAEAEA 325
|
90 100 110
....*....|....*....|....*....|....*.
gi 5031839 413 EQRGEMALKDAKNKLEGLE---DALQKAKQDLARLL 445
Cdd:COG2268 326 EAEAEAIRAKGLAEAEGKRalaEAWNKLGDAAILLM 361
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
372-476 |
5.74e-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: 39.23 E-value: 5.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 372 DDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQEL 451
Cdd:smart00787 158 EDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQEL 237
|
90 100 110
....*....|....*....|....*....|..
gi 5031839 452 -------MNVKLALDVEIATYRKLLegEECRL 476
Cdd:smart00787 238 eskiedlTNKKSELNTEIAEAEKKL--EQCRG 267
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
372-485 |
6.67e-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: 6.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 372 DDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQ-------RGEMALKD---AKNKLEGLEDALQKAKQDL 441
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRkigeiekEIEQLEQEeekLKERLEELEEDLSSLEQEI 753
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 5031839 442 ARLLKEYQELMNVKLALDVEIATYRKLLEGEECRLNGEGVGQVN 485
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQ 797
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
335-450 |
7.69e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.99 E-value: 7.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 335 AEVKAQYEEIAQRSRAEAE-----SWYQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAI 409
Cdd:PRK12704 58 ALLEAKEEIHKLRNEFEKElrerrNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELI 137
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 5031839 410 ADAEQRGE----MALKDAKNKLegLEDALQKAKQDLARLLKEYQE 450
Cdd:PRK12704 138 EEQLQELErisgLTAEEAKEIL--LEKVEEEARHEAAVLIKEIEE 180
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
381-476 |
7.92e-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: 39.28 E-value: 7.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 381 IAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEmALKDAKNKLEGLeDALQKAKQDLA--RLLKEYQELMNVKLAL 458
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLE-RLRREREKAERY-QALLKEKREYEgyELLKEKEALERQKEAI 242
|
90
....*....|....*...
gi 5031839 459 DVEIATYRKLLEGEECRL 476
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEI 260
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
334-444 |
8.50e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 8.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 334 IAEVKAQYEEIaQRSRAEAESWY-QTKYEELQvtagrhgDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADA 412
Cdd:COG4913 264 YAAARERLAEL-EYLRAALRLWFaQRRLELLE-------AELEELRAELARLEAELERLEARLDALREELDELEAQIRGN 335
|
90 100 110
....*....|....*....|....*....|..
gi 5031839 413 EQRgemALKDAKNKLEGLEDALQKAKQDLARL 444
Cdd:COG4913 336 GGD---RLEQLEREIERLERELEERERRRARL 364
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
205-451 |
9.55e-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: 37.98 E-value: 9.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 205 TVRQNLEPLFEqyINNLRRQLDSIVGERGRLDSELRGMQDLVEDFKNKYEDEINKRTAAENEFVTLKKDVDaaymnkvEL 284
Cdd:COG1579 1 AMPEDLRALLD--LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE-------EV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 285 QAKADTLTDEINFLRalydaelsqmqthisdtsvvlsmdNNRnlDLDSIIAEVkaqyeEIAQRSRAEAEswyqtkyeelq 364
Cdd:COG1579 72 EARIKKYEEQLGNVR------------------------NNK--EYEALQKEI-----ESLKRRISDLE----------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031839 365 vtagrhgddlrntkQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMALKDAKNKLEGLEDALQKAKQDL-AR 443
Cdd:COG1579 110 --------------DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIpPE 175
|
....*...
gi 5031839 444 LLKEYQEL 451
Cdd:COG1579 176 LLALYERI 183
|
|
| |
