|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
90-401 |
8.41e-154 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 439.74 E-value: 8.41e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 90 QEKEQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTSR-SNMDNMFESYINNLRRQLEALGQEKLKLEVELGNM 168
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEpSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 169 QGLVEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQIHEEEIRELQSQISDTSVVLSM 248
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 249 DNSRSLDMDSIIAEVRAQYEEIANRSRAEAETMYQIKYEELQTLAGKHGDDLRRSKTEISEMNRNISRLQAEIDALKGQR 328
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 40786432 329 ATLEAAIADAEQRGELAVKDANAKLEDLKNALQKAKQDMARQLREYQELMNVKLALDIEIATYRKLLEGEESR 401
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
85-409 |
2.50e-13 |
|
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: 72.78 E-value: 2.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 85 QAVRTQEKEQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTSRSNMDNMFESYINNLRRQLEALGQEKLKLEVE 164
Cdd:TIGR02168 669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 165 LGNMQGLVEDFKNKYEDEINKRTEMENEFVlikkdvdEAYMNKVELESRLEGLTDEINFLRqiheEEIRELQSQISDTSV 244
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELA-------EAEAEIEELEAQIEQLKEELKALR----EALDELRAELTLLNE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 245 VLSMDNSRSLDMDSIIAEVRAQYEEIANRSRAEAETMYQIK--YEELQTLAGKHGDDLRRSKTEISEMNRNISRLQAEID 322
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAaeIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 323 ALKGQRATLEAAIADAEQrgelAVKDANAKLEDLKNALQKAKQDMARQLR----EYQELMNVKLALDIEIATYRKLLEGE 398
Cdd:TIGR02168 898 ELSEELRELESKRSELRR----ELEELREKLAQLELRLEGLEVRIDNLQErlseEYSLTLEEAEALENKIEDDEEEARRR 973
|
330
....*....|.
gi 40786432 399 ESRLESGMQNM 409
Cdd:TIGR02168 974 LKRLENKIKEL 984
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
229-374 |
7.23e-10 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 60.36 E-value: 7.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 229 EEEIRELQSQISDTSVVLSMDNSRSLDMDSIIAEVRAQYEEI-ANRSRAEA-ETMYQIKYEELQTLAGKHGDDLRRSKTE 306
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAeAERSRLQAlLAELAGAGAAAEGRAGELAQELDSEKQV 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 40786432 307 ISEMNRNISRLQAEIDALKGQRATLEAAIADAEQRGelavKDANAKLEDLKNALQKAKQDMARQLREY 374
Cdd:PRK09039 132 SARALAQVELLNQQIAALRRQLAALEAALDASEKRD----RESQAKIADLGRRLNVALAQRVQELNRY 195
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
63-87 |
5.85e-09 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 55.05 E-value: 5.85e-09
10 20
....*....|....*....|....*
gi 40786432 63 ITAVTVNQSLLNPLKLEVDPNIQAV 87
Cdd:pfam16208 132 IQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
147-404 |
1.64e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 147 LRRQLEALGQEKLKLEVELGNMQGLVEDFKNKYEDEINKRTEMENEFVLIKKDVDEaymnkveLESRLEGLTDEINFLrq 226
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR-------LEQDIARLEERRREL-- 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 227 ihEEEIRELQSQISDTSVVLSMDNSRSLDMDSIIAEVRAQYEEIAN--RSRAEAETMYQIKYEELQTLAGKHGDDLRRSK 304
Cdd:COG1196 315 --EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAelAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 305 TEISEMNRNISRLQAEIDALKGQRATLEAAIADAEQrgelAVKDANAKLEDLKNALQKAKQDMARQLREYQELMNVKLAL 384
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEE----ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
250 260
....*....|....*....|
gi 40786432 385 DIEIATYRKLLEGEESRLES 404
Cdd:COG1196 469 LEEAALLEAALAELLEELAE 488
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
92-396 |
9.58e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 9.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 92 KEQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKtsrSNMDNMFESyINNLRRQLEALGQEKLKLEVELGNMQGL 171
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEV---KELEELKEE-IEELEKELESLEGSKRKLEEKIRELEER 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 172 VEDFKNKYED------EINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFL-RQIHE--------EEIRELQ 236
Cdd:PRK03918 268 IEELKKEIEEleekvkELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIeERIKEleekeerlEELKKKL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 237 SQISDTSVVLSMDNSRSLDMDSIIAEVRAQYEEIANRSRAEAETmyqiKYEELQTLAGKHGDDLRRSKTEISEMNRNISR 316
Cdd:PRK03918 348 KELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEK----ELEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 317 LQAEIDALKGQRAT--LEAAIADAEQRGELaVKDANAKLEDLKNALQKAKqDMARQLREYQELMNVKLALDIEIATYRKL 394
Cdd:PRK03918 424 LKKAIEELKKAKGKcpVCGRELTEEHRKEL-LEEYTAELKRIEKELKEIE-EKERKLRKELRELEKVLKKESELIKLKEL 501
|
..
gi 40786432 395 LE 396
Cdd:PRK03918 502 AE 503
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
92-410 |
1.51e-07 |
|
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: 53.87 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 92 KEQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTSRSNMDNMFESYINNLRRQLEALGQEKLKLEVELGNMQGL 171
Cdd:TIGR04523 130 EKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKK 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 172 VEDFKnKYEDEINkrtEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQIHEEEIRELQSQISDtsvvLSMDNS 251
Cdd:TIGR04523 210 IQKNK-SLESQIS---ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE----LEQNNK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 252 RSLDMDSIIAEVRAQYEEIANRsrAEAETMYQIKyEELQtlagKHGDDLRRSKTEISEMNRNISRLQAEIDALKGQRATL 331
Cdd:TIGR04523 282 KIKELEKQLNQLKSEISDLNNQ--KEQDWNKELK-SELK----NQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNS 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 332 EA-------AIADAEQRGELAVKDANAKLEDLKNaLQKAKQDMARQLREYQELMNVKlalDIEIatyrKLLEGEESRLES 404
Cdd:TIGR04523 355 ESensekqrELEEKQNEIEKLKKENQSYKQEIKN-LESQINDLESKIQNQEKLNQQK---DEQI----KKLQQEKELLEK 426
|
....*.
gi 40786432 405 GMQNMS 410
Cdd:TIGR04523 427 EIERLK 432
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
150-373 |
2.93e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 150 QLEALGQEKLKLEVELGNMQGLVEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQihe 229
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 230 eEIRELQSQISDTSVVLSMDNSRSLDM------DSIIAEVRAQYEEIANRSRAEAETMYQIKYEELQTLAgkhgDDLRRS 303
Cdd:COG4942 98 -ELEAQKEELAELLRALYRLGRQPPLAlllspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR----AELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 304 KTEISEMNRNISRLQAEIDALKGQRATLEAAIADAEQRGELAVKDANAKLEDLKNALQKAKQDMARQLRE 373
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
252-403 |
3.75e-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: 3.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 252 RSLDMDSIIAEVRAQYEEIANRSRAEAEtmYQIKYEELQTLAGKHGDDLRRSKTEISEMNRNISRLQAEIDALKGQRATL 331
Cdd:TIGR02168 223 RELELALLVLRLEELREELEELQEELKE--AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40786432 332 EAAIADAEQRGELAVKD---ANAKLEDLKNALQKAKQDMARQLREYQELMNVKLALDIEIATYRKLLEGEESRLE 403
Cdd:TIGR02168 301 EQQKQILRERLANLERQleeLEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
209-407 |
8.68e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 8.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 209 ELESRLEGLTDEINFLrqihEEEIRELQSQISDtsvvlsmdnsrsldmdsiIAEVRAQYEEIANRSRAEAETMYQIkyEE 288
Cdd:COG4913 614 ALEAELAELEEELAEA----EERLEALEAELDA------------------LQERREALQRLAEYSWDEIDVASAE--RE 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 289 LQTLAGKHgDDLRRSKTEISEMNRNISRLQAEIDALKGQRATLEAAIADAEQRgelaVKDANAKLEDLKNALQKAKQDMA 368
Cdd:COG4913 670 IAELEAEL-ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE----LEQAEEELDELQDRLEAAEDLAR 744
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 40786432 369 RQLRE-----YQELM------NVKLALDIEIATYRKLLEGEESRLESGMQ 407
Cdd:COG4913 745 LELRAlleerFAAALgdaverELRENLEERIDALRARLNRAEEELERAMR 794
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
93-409 |
1.65e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.84 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 93 EQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTSRSNMDNMFESYINNLRRQLEALGQEKLKLEVELGNmqglV 172
Cdd:TIGR02169 681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN----V 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 173 EDFKNKYEDEINkrtEMENEFVLIKKDVDEAYMNkvELESRLEGLTDEINFLrqihEEEIRELQSQISDTSVVLSMDNSR 252
Cdd:TIGR02169 757 KSELKELEARIE---ELEEDLHKLEEALNDLEAR--LSHSRIPEIQAELSKL----EEEVSRIEARLREIEQKLNRLTLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 253 SLDMDSIIAEVRAQYEEIANRSRAEAETMyqikyEELQTLAGKHGDDLRRSKTEISEMNRNISRLQAEIDALKGQRATLE 332
Cdd:TIGR02169 828 KEYLEKEIQELQEQRIDLKEQIKSIEKEI-----ENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40786432 333 AAIADAeqrgELAVKDANAKLEDLKNALQKAKQdmarQLREYQELMNVKLALDIEIATYRKLLEgEESRLESGMQNM 409
Cdd:TIGR02169 903 RKIEEL----EAQIEKKRKRLSELKAKLEALEE----ELSEIEDPKGEDEEIPEEELSLEDVQA-ELQRVEEEIRAL 970
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
72-332 |
1.81e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.84 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 72 LLNPLKLEVDPNIQAVRTQEKEQIKTLNNKFASFIDKVRFLEQQNKMLETkwsllQQQKTsrsnmdnmfESYINNLRRQL 151
Cdd:TIGR02169 273 LLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEE-----RLAKL---------EAEIDKLLAEI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 152 EalgqeklKLEVELGNMQGLVEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINflrqiheeE 231
Cdd:TIGR02169 339 E-------ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREIN--------E 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 232 IRELQSQISDTSVVLSMdnsRSLDMDSIIAEVRAQYEEIANRSRAEAETMYQI--KYEELQTLAGKHGDDLRRSKTEISE 309
Cdd:TIGR02169 404 LKRELDRLQEELQRLSE---ELADLNAAIAGIEAKINELEEEKEDKALEIKKQewKLEQLAADLSKYEQELYDLKEEYDR 480
|
250 260
....*....|....*....|...
gi 40786432 310 MNRNISRLQAEIDALKGQRATLE 332
Cdd:TIGR02169 481 VEKELSKLQRELAEAEAQARASE 503
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
110-404 |
2.53e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 110 RFLEQQNKMLETKWSLLQQQKTSrsnmdnmFESYINNLRRQLEALGQEKLKLEVELGNMQGLVEDFKNKyedeinkRTEM 189
Cdd:TIGR02168 214 RYKELKAELRELELALLVLRLEE-------LREELEELQEELKEAEEELEELTAELQELEEKLEELRLE-------VSEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 190 ENEFVLIKKDVDEAYMNKVELESRLegltdeinflrQIHEEEIRELQSQISDTSVVLSMDNSRSLDMDSIIAEVRAQYEE 269
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQK-----------QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 270 IANRSRAEAETM--YQIKYEELQTLAGKHGDDLRRSKTEISEMNRNISRLQAEIDALKGQRATLEAAIADAEQRG----- 342
Cdd:TIGR02168 349 LKEELESLEAELeeLEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIeellk 428
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40786432 343 ---ELAVKDANAKLEDLKNALQKAKQDMARQLREYQELMNVKLALDIEIATYRKLLEGEESRLES 404
Cdd:TIGR02168 429 kleEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
147-403 |
2.54e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 147 LRRQLEALGQEK------LKLEVELGNMQGLV-----EDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLE 215
Cdd:COG1196 198 LERQLEPLERQAekaeryRELKEELKELEAELlllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 216 GLTDEINFLRQIHEEEIRELQSQISDTSVVLSMDNSRSLDMDSIIAEVRAQYEEIANRS--RAEAETMYQIKYEELQTLA 293
Cdd:COG1196 278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEeeLEELEEELEEAEEELEEAE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 294 gkhgDDLRRSKTEISEMNRNISRLQAEIDALKGQRATLEAAIADAEQRgelavkdanakLEDLKNALQKAKQDMARQLRE 373
Cdd:COG1196 358 ----AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ-----------LEELEEAEEALLERLERLEEE 422
|
250 260 270
....*....|....*....|....*....|
gi 40786432 374 YQELMNVKLALDIEIATYRKLLEGEESRLE 403
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
210-407 |
4.36e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 4.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 210 LESRLEGLTDEinfLRQIhEEEIRELQSQ--ISDTSVVLSMDNSRSLDMDSIIAEVRAQYEEIANRsRAEAETMYQIKYE 287
Cdd:COG3206 180 LEEQLPELRKE---LEEA-EAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR-LAALRAQLGSGPD 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 288 ELQTLAGkhGDDLRRSKTEISEMNRNISRLQA-------EIDALKGQRATLEAAIADAEQRG----ELAVKDANAKLEDL 356
Cdd:COG3206 255 ALPELLQ--SPVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQEAQRIlaslEAELEALQAREASL 332
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 40786432 357 KNALQKAKQDMARQLREYQELMNVKLALDIEIATYRKLLEG-EESRLESGMQ 407
Cdd:COG3206 333 QAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRlEEARLAEALT 384
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
299-380 |
3.25e-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: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 299 DLRRSKTEISEMNRNISRLQAEIDALKGQRATLEAAIADAEQR---GELAVKDANAKLEDLKNALQKAKQDMARQLREYQ 375
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELA 107
|
....*
gi 40786432 376 ELMNV 380
Cdd:COG4942 108 ELLRA 112
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
83-340 |
3.61e-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: 46.59 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 83 NIQAVRTQEKEQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTSRSNMDNMFESYINNLRRQLEALGQEKLKLE 162
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 163 VELGNMQGLVEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEinflRQIHEEEIRELQSQISDT 242
Cdd:TIGR02168 824 ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE----RASLEEALALLRSELEEL 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 243 SVVLSMDNSRSLDMDSIIAEVRAQYEEIANR-SRAEAETM---------YQIKYEELQTLAGKHGDDLRRSKTEISEMNR 312
Cdd:TIGR02168 900 SEELRELESKRSELRRELEELREKLAQLELRlEGLEVRIDnlqerlseeYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
|
250 260 270
....*....|....*....|....*....|....*
gi 40786432 313 NISRL-------QAEIDALKGQRATLEAAIADAEQ 340
Cdd:TIGR02168 980 KIKELgpvnlaaIEEYEELKERYDFLTAQKEDLTE 1014
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
148-396 |
4.43e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 148 RRQLEALGQEKLKLEVELGNMQGLVEDFKNKYEDEINKRtemenefvlikkdvdeaymnkvELESRLEGLTDEINFLRQi 227
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERR----------------------EALQRLAEYSWDEIDVAS- 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 228 HEEEIRELQSQISDtsvvlsMDNSrsldmDSIIAEVRAQYEEiANRSRAEAETmyqiKYEELQTLAGKHGDDLRRSKTEI 307
Cdd:COG4913 666 AEREIAELEAELER------LDAS-----SDDLAALEEQLEE-LEAELEELEE----ELDELKGEIGRLEKELEQAEEEL 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 308 SEMNRNISRlqAEIDALKGQRATLEAAIADA--EQRGELAVKDANAKLEDLKNALQKAKQDMARQLREYQEL-MNVKLAL 384
Cdd:COG4913 730 DELQDRLEA--AEDLARLELRALLEERFAAAlgDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREwPAETADL 807
|
250
....*....|....*
gi 40786432 385 DIEIAT---YRKLLE 396
Cdd:COG4913 808 DADLESlpeYLALLD 822
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
107-366 |
7.93e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.01 E-value: 7.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 107 DKVRFLEQQNKMLETKWSLLQQQKtsrsnmdNMFESYINNLRRQLEALGQEKLKLEVELGNmqgLVEDFKNkyedEINKR 186
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQI-------KTYNKNIEEQRKKNGENIARKQNKYDELVE---EAKTIKA----EIEEL 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 187 TEMENEFVLIKKDVDEAY----MNKVELESRLEGLTDEINFLRQIHeeEIRELQSQISDTSVVLSmdnsrslDMDSIIAE 262
Cdd:PHA02562 240 TDELLNLVMDIEDPSAALnklnTAAAKIKSKIEQFQKVIKMYEKGG--VCPTCTQQISEGPDRIT-------KIKDKLKE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 263 VRAQYEEIANRSRAEAETMyqIKYEELQTLAGKHGDDLRRSKTEISEMNRNISRLQAEIDALKGQRATLEAAIAdaeqrg 342
Cdd:PHA02562 311 LQHSLEKLDTAIDELEEIM--DEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELA------ 382
|
250 260
....*....|....*....|....
gi 40786432 343 ELavkdaNAKLEDLKNALQKAKQD 366
Cdd:PHA02562 383 KL-----QDELDKIVKTKSELVKE 401
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
209-371 |
1.80e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 209 ELESRLEGLTDEINFLRQIHEE-EIRELQSQISDtsvVLSMDNSRSLDMDSIIAEVRAQYEEIANRSRAEAETMYQIKYE 287
Cdd:COG4717 341 ELLDRIEELQELLREAEELEEElQLEELEQEIAA---LLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGE 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 288 ELQTLAGKHGDDLrrsKTEISEMNRNISRLQAEIDALKGQRATLEAAIADAEQRGELAvkDANAKLEDLKNALQ-KAKQD 366
Cdd:COG4717 418 LEELLEALDEEEL---EEELEELEEELEELEEELEELREELAELEAELEQLEEDGELA--ELLQELEELKAELReLAEEW 492
|
....*
gi 40786432 367 MARQL 371
Cdd:COG4717 493 AALKL 497
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
112-376 |
2.88e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.63 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 112 LEQQNKMLETKWSLLQQQKTSRSNMDNMFESyinnLRRQLEALGQEklkLEVELGNMQGLVEDFKNKYEDEINKRTEMEN 191
Cdd:pfam01576 31 LEKKHQQLCEEKNALQEQLQAETELCAEAEE----MRARLAARKQE---LEEILHELESRLEEEEERSQQLQNEKKKMQQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 192 EFVLIKKDVDEA-------YMNKVELESRLEGLTDEINFL----------RQIHEEEIRELQSQISDTSVVLSMDNSRSL 254
Cdd:pfam01576 104 HIQDLEEQLDEEeaarqklQLEKVTTEAKIKKLEEDILLLedqnsklskeRKLLEERISEFTSNLAEEEEKAKSLSKLKN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 255 DMDSIIA--EVRAQYEEianRSRAEAETMYqikyeelqtlagkhgddlRRSKTEISEMNRNISRLQAEIDALKGQRATLE 332
Cdd:pfam01576 184 KHEAMISdlEERLKKEE---KGRQELEKAK------------------RKLEGESTDLQEQIAELQAQIAELRAQLAKKE 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 40786432 333 AAIADAEQRGElavKDANAkledlKNALQKAKQDMARQLREYQE 376
Cdd:pfam01576 243 EELQAALARLE---EETAQ-----KNNALKKIRELEAQISELQE 278
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
92-362 |
4.15e-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: 43.09 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 92 KEQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTSRSNMDNMFESYINNLRRQLEALGQEKLKLEVELGNMQGL 171
Cdd:TIGR04523 383 KQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNT 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 172 VEDFKNK---YEDEINK-RTEMEN---EFVLIKKDVDEAYMNKVELESRLEGLTDEINFLR---QIHEEEIRELQSQISD 241
Cdd:TIGR04523 463 RESLETQlkvLSRSINKiKQNLEQkqkELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKekiEKLESEKKEKESKISD 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 242 TSVVLSMDNSRsLDMDSIIAEVRAQYEEIANRSraEAETMYQIKYEELQTLAGKHGDDLRRSKTEISEMNRNISRLQAEI 321
Cdd:TIGR04523 543 LEDELNKDDFE-LKKENLEKEIDEKNKEIEELK--QTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKEL 619
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 40786432 322 DALKGQRATLEAAIADAEQRGELAVKDANAKLEDLKNALQK 362
Cdd:TIGR04523 620 EKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNK 660
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
192-393 |
5.74e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 192 EFVLIKKDVDEA-------YMNKVELESRLEGLTDEINFLRQI--HEEEIRELQSQISDTSVVLSM----DNSRSLD-MD 257
Cdd:COG4913 215 EYMLEEPDTFEAadalvehFDDLERAHEALEDAREQIELLEPIreLAERYAAARERLAELEYLRAAlrlwFAQRRLElLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 258 SIIAEVRAQYEEIANRsRAEAETMYQIKYEELQTLAGKH----GDDLRRSKTEISEMNRNISRLQAEIDALKGQRATLEA 333
Cdd:COG4913 295 AELEELRAELARLEAE-LERLEARLDALREELDELEAQIrgngGDRLEQLEREIERLERELEERERRRARLEALLAALGL 373
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 334 AIADAEQRGELAVKDANAKLEDLKNALQKAKQDMARQLREYQELMNVKLALDIEIATYRK 393
Cdd:COG4913 374 PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
209-404 |
6.48e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 6.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 209 ELESRLEGLTDEinflRQIhEEEIRELQSQISDTSVVLSMDNSRSLDMDsiIAEVRAQYEEIANRsRAEAETMYQIKYEE 288
Cdd:COG1196 197 ELERQLEPLERQ----AEK-AERYRELKEELKELEAELLLLKLRELEAE--LEELEAELEELEAE-LEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 289 LQTLAgkhgDDLRRSKTEISEMNRNISRLQAEIDALKGQRATLEAAIADAEQRGElavkDANAKLEDLKNALQKAKQDMA 368
Cdd:COG1196 269 LEELR----LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE----ELEEELAELEEELEELEEELE 340
|
170 180 190
....*....|....*....|....*....|....*.
gi 40786432 369 RQLREYQELMNVKLALDIEIATYRKLLEGEESRLES 404
Cdd:COG1196 341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
85-314 |
6.52e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 42.73 E-value: 6.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 85 QAVRTQEKEQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTSRSNMDNMFESYINNLRRQ-LEALGQEKLKLEV 163
Cdd:TIGR01612 1161 KAISNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKGINLSYGKNLGKLfLEKIDEEKKKSEH 1240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 164 ELGNMQGLVEDFknkyeDEINKRTEMENEFVLIKKDVDeAYMNKVELESRLEgltDEINFLRQIHEEEIrelqSQISDTS 243
Cdd:TIGR01612 1241 MIKAMEAYIEDL-----DEIKEKSPEIENEMGIEMDIK-AEMETFNISHDDD---KDHHIISKKHDENI----SDIREKS 1307
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 40786432 244 VVLSMDNSRSLDMDSI-------IAEVRAQYEEIaNRSRAEAETMYQI-KYEELQTLAgkhgDDLRRSKTEISEMNRNI 314
Cdd:TIGR01612 1308 LKIIEDFSEESDINDIkkelqknLLDAQKHNSDI-NLYLNEIANIYNIlKLNKIKKII----DEVKEYTKEIEENNKNI 1381
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
305-402 |
7.19e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 7.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 305 TEISEMNRNISRLQAEIDALKGQRATLEAAIADAEQR---GELAVKDANAKLEDLKNALQK--AKQDMARQLREYQelmn 379
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTEledLEKEIKRLELEIEEVEARIKKyeEQLGNVRNNKEYE---- 92
|
90 100
....*....|....*....|...
gi 40786432 380 vklALDIEIATYRKLLEGEESRL 402
Cdd:COG1579 93 ---ALQKEIESLKRRISDLEDEI 112
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
120-415 |
7.74e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.03 E-value: 7.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 120 ETKWSLLQQQKTSRSNMDNMFESYINNLRRQLEALGQEKLKLEVELGNM----QGLVE------DFKNKYEDEINKRT-E 188
Cdd:pfam15921 390 EKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMksecQGQMErqmaaiQGKNESLEKVSSLTaQ 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 189 MENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQIHE------EEIRELQSQISDTSVVLSMDNSRSLDMDSIIAE 262
Cdd:pfam15921 470 LESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERaieatnAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTE 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 263 VRAQYEEIANRSRAEAETMYQIkyEELQTLAGKHGDDLRRSKTEISEMNRNISRLQAEIDALKGQRATLEAAIADAEQRG 342
Cdd:pfam15921 550 CEALKLQMAEKDKVIEILRQQI--ENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARV 627
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40786432 343 ---EL-AVKDANAKLEDLKnALQKAKQDMARQLREYQELMNVKLALDIEIATYRKLLEGEESRLESGMQNMSIHTKT 415
Cdd:pfam15921 628 sdlELeKVKLVNAGSERLR-AVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKS 703
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
83-403 |
1.17e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 83 NIQAVRTQEKE--QIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTSRSNMDNMFESYI--NNLRRQLEALGQEK 158
Cdd:COG4717 69 NLKELKELEEElkEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQelEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 159 LKLEVELGNMQGLVEDFKNKYEDEINKRTEMENEFVL-----------IKKDVDEAYMNKVELESRLEGLTDEINFLRQ- 226
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQEELEELLEQlslateeelqdLAEELEELQQRLAELEEELEEAQEELEELEEe 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 227 -----------IHEEEIRELQSQISDTSVVLSMDNSRSLDMDSI------------------IAEVRAQYEEIANRSRAE 277
Cdd:COG4717 229 leqleneleaaALEERLKEARLLLLIAAALLALLGLGGSLLSLIltiagvlflvlgllallfLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 278 A-ETMYQIKYEELQTLAGKHGDDLRRSKTEISEMNRNISRLQAEIDALKGQRATLEA-----------AIADAEQRGELA 345
Cdd:COG4717 309 AlPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLeeleqeiaallAEAGVEDEEELR 388
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40786432 346 VK-DANAKLEDLKNALQKAKQDMARQLREYQELMNV--KLALDIEIATYRKLLEGEESRLE 403
Cdd:COG4717 389 AAlEQAEEYQELKEELEELEEQLEELLGELEELLEAldEEELEEELEELEEELEELEEELE 449
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
85-345 |
1.40e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 85 QAVRTQEK----EQIKTLNNKFASFIDKVRFLEQQNKML-----ETKWSLLQQQktsrsnmdnmfesyINNLRRQLEALG 155
Cdd:COG4913 243 ALEDAREQiellEPIRELAERYAAARERLAELEYLRAALrlwfaQRRLELLEAE--------------LEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 156 QEKLKLEVELGNMQGLVEDFKNKYEDEINKRTEmenefvlikkdvdeaymnkvELESRLEGLTDEinflRQIHEEEIREL 235
Cdd:COG4913 309 AELERLEARLDALREELDELEAQIRGNGGDRLE--------------------QLEREIERLERE----LEERERRRARL 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 236 QSQIsdtsvvlsmdnsRSLDMDsiIAEVRAQYEEIANRSRAEAEtmyqikyeELQTLAGKHGDDLRRSKTEISEMNRNIS 315
Cdd:COG4913 365 EALL------------AALGLP--LPASAEEFAALRAEAAALLE--------ALEEELEALEEALAEAEAALRDLRRELR 422
|
250 260 270
....*....|....*....|....*....|
gi 40786432 316 RLQAEIDALKGQRATLEAAIADAeqRGELA 345
Cdd:COG4913 423 ELEAEIASLERRKSNIPARLLAL--RDALA 450
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
288-404 |
1.60e-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: 39.91 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 288 ELQTLAGKHGDDLRRSKTEISEMNRNISRLQAEIDALKGQRATLEAAIADAEQRgelaVKDANAKLEDLKN-----ALQK 362
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR----IKKYEEQLGNVRNnkeyeALQK 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 40786432 363 AKQDMARQLR----EYQELMNVKLALDIEIATYRKLLEGEESRLES 404
Cdd:COG1579 97 EIESLKRRISdledEILELMERIEELEEELAELEAELAELEAELEE 142
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
92-377 |
1.94e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 92 KEQIKTLNNKFASFIDKVRFLEQQNKMLETKwsLLQQQKTSRsnMDNMFESyINNLRRQLEALGQEKL--------KLEV 163
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELRELEKV--LKKESELIK--LKELAEQ-LKELEEKLKKYNLEELekkaeeyeKLKE 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 164 ELGNMQGLVEDFKnkyeDEINKRTEMENEFVLIKKDVDEAYMNKVELESRL--------EGLTDEINFLRQIHEE----- 230
Cdd:PRK03918 533 KLIKLKGEIKSLK----KELEKLEELKKKLAELEKKLDELEEELAELLKELeelgfesvEELEERLKELEPFYNEylelk 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 231 ----EIRELQSQISDTSVVLSMDNSRSLDMDSIIAEVRAQYEEIanrsraeaetmyQIKYEElqtlagkhgDDLRRSKTE 306
Cdd:PRK03918 609 daekELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEEL------------EKKYSE---------EEYEELREE 667
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40786432 307 ISEMNRNISRLQAEIDALKGQRATLEAAIADAEQRGElAVKDANAKLEDLKNALQKAkQDMARQLREYQEL 377
Cdd:PRK03918 668 YLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE-EREKAKKELEKLEKALERV-EELREKVKKYKAL 736
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
105-378 |
2.36e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.58 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 105 FIDKVRFLEQQNKMLETKWSLLQQQKTSRsnmdnmfESYINNLRRQLEALGQEKLKLEVELGNMQGLVEDFK---NKYED 181
Cdd:pfam10174 466 RLEELESLKKENKDLKEKVSALQPELTEK-------ESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKeecSKLEN 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 182 EINKRTEMEN------EFV----LIKKDV----DEAYMNKVELEsRLEGLTDEINFLRQIHEEEIRELQS----QISDTS 243
Cdd:pfam10174 539 QLKKAHNAEEavrtnpEINdrirLLEQEVarykEESGKAQAEVE-RLLGILREVENEKNDKDKKIAELESltlrQMKEQN 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 244 VVLSMDNSRSLDMDSIIAEvraQYEEIANRSRAEAETMYQIKYEELQTLAGKHGDDLRRSKTEISEMNRNISRLQAEIDA 323
Cdd:pfam10174 618 KKVANIKHGQQEMKKKGAQ---LLEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTN 694
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 40786432 324 LKGQRATLEAAIADAEQRGELAV---KDANAKLEDLKNALQKAKQDMARQL-REYQELM 378
Cdd:pfam10174 695 LRAERRKQLEEILEMKQEALLAAiseKDANIALLELSSSKKKKTQEEVMALkREKDRLV 753
|
|
| Tht1 |
pfam04163 |
Tht1-like nuclear fusion protein; |
177-382 |
3.24e-03 |
|
Tht1-like nuclear fusion protein;
Pssm-ID: 282073 Cd Length: 595 Bit Score: 40.20 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 177 NKYEDEINKRTE-----MENEFVLIKKDVDEAYMNKVELESrlegltdeinflrqiHEEEIRELQSQISDTSVVLSmdnS 251
Cdd:pfam04163 209 DKFDGEFNNATEsnriiIENDFKDFNFKVNDEIMGLVELEN---------------HEQEGMVLEKEIIEKIKQLK---N 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 252 RSLDMDSIIAEVraqYEEIANRSRAEAETMYQIKYEELQTLAGKHGDDLRRSKTEISEMNrnisrlqaeidaLKGQRATL 331
Cdd:pfam04163 271 EIDDIHHFFADF---ADELAGYKNDIIEKINDLKDDSENAIALSAIGKYTSEFSAFMEKN------------IKDLIEMS 335
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 40786432 332 EAAIADAEQRGELAVKDANAKLEDLKNALQKAKQDMARQLREYQELMNVKL 382
Cdd:pfam04163 336 EDSLKESVQRNIDFVNSGFQELEDFSIGLKEELGGLKKDLSEQQNLEAEEI 386
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
93-362 |
3.95e-03 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 39.17 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 93 EQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQK-TSRSNMDNMfesyiNNLRRQLEALGQEKLKlevelgNMQGL 171
Cdd:pfam09728 18 EKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKdQLQSELSKA-----ILAKSKLEKLCRELQK------QNKKL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 172 VEDFKNKYEDEINKRTEMENEFVLIKKDVdEAYMNK------------VELESRLEGLTDEINfLRQIHEEEI---RELQ 236
Cdd:pfam09728 87 KEESKKLAKEEEEKRKELSEKFQSTLKDI-QDKMEEkseknnklreenEELREKLKSLIEQYE-LRELHFEKLlktKELE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 237 SQISDTSVVLSMDNSRSLDMDSIIAEVRAQYEEIANRSRAEAE-----TMYQIKYEELQTLAGKHGDDLRRSKTEISEMN 311
Cdd:pfam09728 165 VQLAEAKLQQATEEEEKKAQEKEVAKARELKAQVQTLSETEKElreqlNLYVEKFEEFQDTLNKSNEVFTTFKKEMEKMS 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 40786432 312 RNISRLQAEIDALK-----GQRATLEAAIADAEQRGELAVKDA-NAKLEDLKNALQK 362
Cdd:pfam09728 245 KKIKKLEKENLTWKrkwekSNKALLEMAEERQKLKEELEKLQKkLEKLENLCRALQA 301
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
255-393 |
5.36e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 38.37 E-value: 5.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 255 DMDSIIAEVRAQYEEIANRsRAEAETMYQIKYEELQTLAGKhgddLRRSKTEISEM--NRNISRLQAEIDALKGQRATLE 332
Cdd:COG1579 35 ELEDELAALEARLEAAKTE-LEDLEKEIKRLELEIEEVEAR----IKKYEEQLGNVrnNKEYEALQKEIESLKRRISDLE 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40786432 333 AAIADAEQRgelaVKDANAKLEDLKNALQKAKQDMARQLREYQELMNvklALDIEIATYRK 393
Cdd:COG1579 110 DEILELMER----IEELEEELAELEAELAELEAELEEKKAELDEELA---ELEAELEELEA 163
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
89-400 |
5.56e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 39.17 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 89 TQEKEQIKTLNNKFASFIdKVRFLEQQNKMLETKwsLLQQQKTSRSNMDNMFESYINNLRrqleaLGQEKLKLEVELGNM 168
Cdd:COG5185 164 IFGKLTQELNQNLKKLEI-FGLTLGLLKGISELK--KAEPSGTVNSIKESETGNLGSEST-----LLEKAKEIINIEEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 169 QGLvEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQIHEEEIRELQSQISDTSVVLSM 248
Cdd:COG5185 236 KGF-QDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 249 DNSRSLdmdsiiAEVRAQYEEianrSRAEAETMYQIKYEELQTLAGKHGDDLRRSKTEISEM--NRNISRLQAEIDALKG 326
Cdd:COG5185 315 EEQLAA------AEAEQELEE----SKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIvgEVELSKSSEELDSFKD 384
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 40786432 327 QRATLEAAIADAEQRGELAVKDANAKLED-LKNALQKAKQ---DMARQLREYQELMNVKLALDIEIATYRKLLEGEES 400
Cdd:COG5185 385 TIESTKESLDEIPQNQRGYAQEILATLEDtLKAADRQIEElqrQIEQATSSNEEVSKLLNELISELNKVMREADEESQ 462
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
138-365 |
5.62e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.25 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 138 NMFESYINNLRRQLEALGQEKLKLEVELGNMQGLVEDfknkYEDeinKRTEMENefvlIKKDVDEAYMNKVELESRLEGL 217
Cdd:PRK02224 209 NGLESELAELDEEIERYEEQREQARETRDEADEVLEE----HEE---RREELET----LEAEIEDLRETIAETEREREEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 218 TDEINFLRQIHEE---EIRELQSQI-----SDTSVVLSMD--NSRSLDMDSIIAEVRAQ---YEEIANRSRAEAETMyQI 284
Cdd:PRK02224 278 AEEVRDLRERLEEleeERDDLLAEAglddaDAEAVEARREelEDRDEELRDRLEECRVAaqaHNEEAESLREDADDL-EE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 285 KYEELQTLAGKHGDDLRRSKTEISEMNRNISRLQAEIDALKGQRATLEAAIADAEQRGELA----------VKDANAKLE 354
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELreerdelrerEAELEATLR 436
|
250
....*....|.
gi 40786432 355 DLKNALQKAKQ 365
Cdd:PRK02224 437 TARERVEEAEA 447
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
298-376 |
6.62e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 38.66 E-value: 6.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 298 DDLRRSKTEISEMNRNISRLQAEIDALKGQRATLEAAIADAEQRGELA---VKDANAKLEDLKNALQKAKQDMARQLREY 374
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALqaeIDKLQAEIAEAEAEIEERREELGERARAL 95
|
..
gi 40786432 375 QE 376
Cdd:COG3883 96 YR 97
|
|
| PRK11929 |
PRK11929 |
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ... |
244-295 |
8.76e-03 |
|
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE/UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase MurF;
Pssm-ID: 237025 [Multi-domain] Cd Length: 958 Bit Score: 38.92 E-value: 8.76e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 40786432 244 VVLSMDNSRSLDMDSIIAEVRA------QYEEIANRSRAEAETMYQIKYEELQTLAGK 295
Cdd:PRK11929 415 VVVTSDNPRSEAPEAIIDQILAgipagaRVFVISDRAEAIRQAIWMAAPGDVILIAGK 472
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
138-363 |
9.09e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 38.76 E-value: 9.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 138 NMFEsyINNLRRQLEAL-GQEKLKLEVELGNMQGLVEDFKNKYEdeINKRTEMENEFVLIKKDVDEAYMNKVELESRLEG 216
Cdd:PRK05771 29 GVVH--IEDLKEELSNErLRKLRSLLTKLSEALDKLRSYLPKLN--PLREEKKKVSVKSLEELIKDVEEELEKIEKEIKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 217 LTDEINFLrqihEEEIRELQSQISD-------------------TSVVLSMDNSRSLDMDSIIAEVRAQYEE-------- 269
Cdd:PRK05771 105 LEEEISEL----ENEIKELEQEIERlepwgnfdldlslllgfkyVSVFVGTVPEDKLEELKLESDVENVEYIstdkgyvy 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40786432 270 --IANRSRAEAETMYQIK---YEELQTLAGKHGDD-LRRSKTEISEMNRNISRLQAEIDALKGQRATLEAAIADA----E 339
Cdd:PRK05771 181 vvVVVLKELSDEVEEELKklgFERLELEEEGTPSElIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEYleieL 260
|
250 260 270
....*....|....*....|....*....|....*..
gi 40786432 340 QRGELAVKDANA-------------KLEDLKNALQKA 363
Cdd:PRK05771 261 ERAEALSKFLKTdktfaiegwvpedRVKKLKELIDKA 297
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