|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
90-401 |
1.16e-150 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 431.65 E-value: 1.16e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 90 QEKEQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTAR-SNMDNMFESYINNLRRQLETLGQEKLKLEAELGNM 168
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEpSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 169 QGLVEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQLYEEEIRELQSQISDTSVVLSM 248
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 249 DNSRSLDMDSIIAEVKAQYEDIANRSRAEAESMYQIKYEELQSLAGKHGDDLRRTKTEISEMNRNISRLQAEIEGLKGQR 328
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 400416 329 ASLEAAIADAEQRGELAIKDANAKLSELEAALQRAKQDMARQLREYQELMNVKLALDIEIATYRKLLEGEESR 401
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
85-403 |
4.66e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.54 E-value: 4.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 85 QAVRTQEKEQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTARSNMDNMFESYINNLRRQLETLGQEKLKLEAE 164
Cdd:TIGR02168 669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 165 LGNMQGLVEDFKNKYEDEINKRTEMENEFVlikkdvdEAYMNKVELESRLEGLTDEINFLRqlyeEEIRELQSQISDTSV 244
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELA-------EAEAEIEELEAQIEQLKEELKALR----EALDELRAELTLLNE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 245 VLSMDNSRSLDMDSIIAEVKAQYEDIANRSRAEAESMYQIK--YEELQSLAGKHGDDLRRTKTEISEMNRNISRLQAEIE 322
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAaeIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 323 GLKGQRASLEAAIADAEQrgelAIKDANAKLSELEAALQRAKQDMARQLR----EYQELMNVKLALDIEIATYRKLLEGE 398
Cdd:TIGR02168 898 ELSEELRELESKRSELRR----ELEELREKLAQLELRLEGLEVRIDNLQErlseEYSLTLEEAEALENKIEDDEEEARRR 973
|
....*
gi 400416 399 ESRLE 403
Cdd:TIGR02168 974 LKRLE 978
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
156-404 |
3.39e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.30 E-value: 3.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 156 QEKLKLEAELGNMQGLVEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQLYEEEIREL 235
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 236 QSQISDTSVVLSMDNSRSLDMDSIIAEVKAQYEDIANRSRAEAESMYQIK-----YEELQSLAGKHGDDLRRTKTEISEM 310
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDelraeLTLLNEEAANLRERLESLERRIAAT 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 311 NRNISRLQAEIEGLKGQRASLEAAIADAEQRGElaikDANAKLSELEAALQRAKQDMARQLREYQELMNVKLALDIEIAT 390
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIE----ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
250
....*....|....
gi 400416 391 YRKLLEGEESRLES 404
Cdd:TIGR02168 913 LRRELEELREKLAQ 926
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
143-407 |
4.44e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 4.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 143 YINNLRRQLETLGQ-------EKLKLEAELGNMQGLVEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLE 215
Cdd:COG1196 233 KLRELEAELEELEAeleeleaELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 216 GLTDEInflrQLYEEEIRELQSQISDTSVVLSMDNSRSLDMDSIIAEVKAQYEDIANRSRAEAESMyqikyEELQSLAGK 295
Cdd:COG1196 313 ELEERL----EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL-----AEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 296 HGDDLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAI---ADAEQRGELAIKDANAKLSELEAALQRAKQDMARQLR 372
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELeelEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260 270
....*....|....*....|....*....|....*
gi 400416 373 EYQELMNVKLALDIEIATYRKLLEGEESRLESGMQ 407
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
63-87 |
1.57e-08 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 53.51 E-value: 1.57e-08
10 20
....*....|....*....|....*
gi 400416 63 ITAVTVNQSLLSPLVLEVDPNIQAV 87
Cdd:pfam16208 132 IQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
229-373 |
1.91e-08 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 56.13 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 229 EEEIRELQSQISDTSVVLSMDNSRSLDMDSIIAEVKAQYEDI-ANRSRAEAesMYQIKYEELQSLAGKHGD---DLRRTK 304
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAeAERSRLQA--LLAELAGAGAAAEGRAGElaqELDSEK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 305 TEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQRGelaiKDANAKL----SELEAALQRAKQDMAR-------QLRE 373
Cdd:PRK09039 130 QVSARALAQVELLNQQIAALRRQLAALEAALDASEKRD----RESQAKIadlgRRLNVALAQRVQELNRyrseffgRLRE 205
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
147-389 |
8.03e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.02 E-value: 8.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 147 LRRQLETLGQEKLKLEAELgnmqglvEDFKNKyedeinkrtemeNEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQ 226
Cdd:COG3206 180 LEEQLPELRKELEEAEAAL-------EEFRQK------------NGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 227 LYEeeirELQSQISDTSVVLSmdnsrSLDMDSIIAEVKAQYEDiANRSRAEAESMYQIKYEELQSLAGKhgddLRRTKTE 306
Cdd:COG3206 241 RLA----ALRAQLGSGPDALP-----ELLQSPVIQQLRAQLAE-LEAELAELSARYTPNHPDVIALRAQ----IAALRAQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 307 I-SEMNRNISRLQAEIEGLKGQRASLEAAIADAEQRgelaikdaNAKLSELEAALQRAKQDMARQLREYQELMNVKLALD 385
Cdd:COG3206 307 LqQEAQRILASLEAELEALQAREASLQAQLAQLEAR--------LAELPELEAELRRLEREVEVARELYESLLQRLEEAR 378
|
....
gi 400416 386 IEIA 389
Cdd:COG3206 379 LAEA 382
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
209-404 |
2.01e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 209 ELESRLEGLTDEINFLR-QLYEEEIRELQSQISDTSVVLSMDNSRSLDMDSIIAEVKAQYEDIANRSRAEAESMYQIKyE 287
Cdd:COG1196 217 ELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL-A 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 288 ELQSLAGkhgdDLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQRGELA---IKDANAKLSELEAALQRAK 364
Cdd:COG1196 296 ELARLEQ----DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAeeeLEEAEAELAEAEEALLEAE 371
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 400416 365 QDMARQLREYQELMNVKLALDIEIATYRKLLEGEESRLES 404
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
92-396 |
4.35e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 4.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 92 KEQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKtarSNMDNMFESyINNLRRQLETLGQEKLKLEAELGNMQGL 171
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEV---KELEELKEE-IEELEKELESLEGSKRKLEEKIRELEER 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 172 VEDFKNKYEDEINKRTEMENefvlIKKDVDEaYMNKVELESRLEGLTDEINFLRQLYEEEIRELQSQISDtsvvLSMDNS 251
Cdd:PRK03918 268 IEELKKEIEELEEKVKELKE----LKEKAEE-YIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE----LEEKEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 252 RSLDMDSIIAEVKAQYEDIanRSRAEAESMYQIKYEELQSLAGKHG-----------DDLRRTKTEISEmnrNISRLQAE 320
Cdd:PRK03918 339 RLEELKKKLKELEKRLEEL--EERHELYEEAKAKKEELERLKKRLTgltpeklekelEELEKAKEEIEE---EISKITAR 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 321 IEGLKGQRASLEAAIA----------------DAEQRGELaIKDANAKLSELEAALQRAKqDMARQLREYQELMNVKLAL 384
Cdd:PRK03918 414 IGELKKEIKELKKAIEelkkakgkcpvcgrelTEEHRKEL-LEEYTAELKRIEKELKEIE-EKERKLRKELRELEKVLKK 491
|
330
....*....|..
gi 400416 385 DIEIATYRKLLE 396
Cdd:PRK03918 492 ESELIKLKELAE 503
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
91-396 |
6.11e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.38 E-value: 6.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 91 EKEQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTarsnmdnmfesyinNLRRQLETLGQEKLKLEAELGNMQG 170
Cdd:TIGR02169 714 ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE--------------NVKSELKELEARIEELEEDLHKLEE 779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 171 LVEDFKNKYEDEINKrtEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQLYEE---EIRELQSQISDTSVVLS 247
Cdd:TIGR02169 780 ALNDLEARLSHSRIP--EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQElqeQRIDLKEQIKSIEKEIE 857
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 248 MDNSRSLDMDSIIAEVKAQYEDI--------ANRSRAEAE-SMYQIKYEELqslagkhgddlrrtKTEISEMNRNISRLQ 318
Cdd:TIGR02169 858 NLNGKKEELEEELEELEAALRDLesrlgdlkKERDELEAQlRELERKIEEL--------------EAQIEKKRKRLSELK 923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 319 AEIEGLKGQRASLEAAIADAEQ--RGELAIKDANAKLSELEAALQ-------RAKQDMARQLREYQELMNVKLALDIEIA 389
Cdd:TIGR02169 924 AKLEALEEELSEIEDPKGEDEEipEEELSLEDVQAELQRVEEEIRalepvnmLAIQEYEEVLKRLDELKEKRAKLEEERK 1003
|
....*..
gi 400416 390 TYRKLLE 396
Cdd:TIGR02169 1004 AILERIE 1010
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
92-377 |
1.06e-06 |
|
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: 51.17 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 92 KEQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTARSNMDNMFESYINNLRRQLETLGQEKLKLEAELGNMQGL 171
Cdd:TIGR04523 130 EKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKK 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 172 VEDFKnKYEDEINkrtEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQLYEEEIRELQSQISDtsvvLSMDNS 251
Cdd:TIGR04523 210 IQKNK-SLESQIS---ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE----LEQNNK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 252 RSLDMDSIIAEVKAQYEDIANRsrAEAESMYQIKyEELQSLAgkhgDDLRRTKTEISEMNRNISRLQAEIEGLKGQRASL 331
Cdd:TIGR04523 282 KIKELEKQLNQLKSEISDLNNQ--KEQDWNKELK-SELKNQE----KKLEEIQNQISQNNKIISQLNEQISQLKKELTNS 354
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 400416 332 EA-------AIADAEQRGELAIKDANAKLSELEaALQRAKQDMARQLREYQEL 377
Cdd:TIGR04523 355 ESensekqrELEEKQNEIEKLKKENQSYKQEIK-NLESQINDLESKIQNQEKL 406
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
110-404 |
1.12e-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: 51.21 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 110 RFLEQQNKMLETKWSLLQQQKTArsnmdnmFESYINNLRRQLETLGQEKLKLEAELGNMQGLVEDFKNKyedeinkRTEM 189
Cdd:TIGR02168 214 RYKELKAELRELELALLVLRLEE-------LREELEELQEELKEAEEELEELTAELQELEEKLEELRLE-------VSEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 190 ENEFVLIKKDVDEAYMNKVELESRLegltdeinflrQLYEEEIRELQSQISDTSVVLSMDNSRSLDMDSIIAEVKAQYED 269
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQK-----------QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 270 IANRSRAEAESM--YQIKYEELQSLAGKHGDDLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQRGELAIK 347
Cdd:TIGR02168 349 LKEELESLEAELeeLEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 400416 348 DA-NAKLSELEAALQRAKQDMARQLREYQELMNVKLALDIEIATYRKLLEGEESRLES 404
Cdd:TIGR02168 429 KLeEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
93-409 |
1.37e-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: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 93 EQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTARSNMDNMFESYINNLRRQLETLGQEKLKLEAELGNmqglV 172
Cdd:TIGR02169 681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN----V 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 173 EDFKNKYEDEINkrtEMENEFVLIKKDVDEAYMNkvELESRLEGLTDEINFLrqlyEEEIRELQSQISDTSVVLSMDNSR 252
Cdd:TIGR02169 757 KSELKELEARIE---ELEEDLHKLEEALNDLEAR--LSHSRIPEIQAELSKL----EEEVSRIEARLREIEQKLNRLTLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 253 SLDMDSIIAEVKAQYEDIANR--SRAEAESMYQIKYEELQSlagkhgdDLRRTKTEISEMNRNISRLQAEIEGLKGQRAS 330
Cdd:TIGR02169 828 KEYLEKEIQELQEQRIDLKEQikSIEKEIENLNGKKEELEE-------ELEELEAALRDLESRLGDLKKERDELEAQLRE 900
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 400416 331 LEAAIADAeqrgELAIKDANAKLSELEAALQRAKQdmarQLREYQELMNVKLALDIEIATYRKLLEgEESRLESGMQNM 409
Cdd:TIGR02169 901 LERKIEEL----EAQIEKKRKRLSELKAKLEALEE----ELSEIEDPKGEDEEIPEEELSLEDVQA-ELQRVEEEIRAL 970
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
225-407 |
1.60e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 225 RQLYEEEIRELQSQISDTsvvlsmdnsrsldmDSIIAEVKAQYEDIANRSRA----EAESMYQIKY----EELQSLAGKH 296
Cdd:COG4913 612 LAALEAELAELEEELAEA--------------EERLEALEAELDALQERREAlqrlAEYSWDEIDVasaeREIAELEAEL 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 297 gDDLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQRgelaIKDANAKLSELEAALQRAKQDMARQLREYQE 376
Cdd:COG4913 678 -ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE----LEQAEEELDELQDRLEAAEDLARLELRALLE 752
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 400416 377 LM-----------NVKLALDIEIATYRKLLEGEESRLESGMQ 407
Cdd:COG4913 753 ERfaaalgdaverELRENLEERIDALRARLNRAEEELERAMR 794
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
141-373 |
4.25e-06 |
|
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: 48.99 E-value: 4.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 141 ESYINNLRRQLETLGQEKLKLEAELGNMQGLVEDFknkyEDEINKRTEMENEfvlIKKDVDEAYMNKVELESRLEGLTDE 220
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAAL----ERRIAALARRIRA---LEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 221 INFLRQLYEEEIRELQ--SQISDTSVVLSMDNSRSldmdsiiAEVKAQYEDIANRSRAEAESMYQIKYEELQSLAgkhgD 298
Cdd:COG4942 99 LEAQKEELAELLRALYrlGRQPPLALLLSPEDFLD-------AVRRLQYLKYLAPARREQAEELRADLAELAALR----A 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 400416 299 DLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQRGELAIKDANAKLSELEAALQRAKQDMARQLRE 373
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
158-410 |
6.52e-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: 48.91 E-value: 6.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 158 KLKLEAELGNMQGLVEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRqlyeEEIRELQS 237
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLK----ERLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 238 QISDTSVVLSMDNSrslDMDSIIAEVKAQYEDIANRSRAEAE---SMYQIKYEELQSLAGKHGDDLRRTKTEISEMNRNI 314
Cdd:TIGR02169 745 DLSSLEQEIENVKS---ELKELEARIEELEEDLHKLEEALNDleaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKL 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 315 SR-------LQAEIEGLKGQRASLEAAIADAEQRGEL----------AIKDANAKLSELEAALQRAKQDMARQLREYQEL 377
Cdd:TIGR02169 822 NRltlekeyLEKEIQELQEQRIDLKEQIKSIEKEIENlngkkeeleeELEELEAALRDLESRLGDLKKERDELEAQLREL 901
|
250 260 270
....*....|....*....|....*....|...
gi 400416 378 MNVKLALDIEIATYRKLLEGEESRLESGMQNMS 410
Cdd:TIGR02169 902 ERKIEELEAQIEKKRKRLSELKAKLEALEEELS 934
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
299-380 |
7.61e-06 |
|
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: 48.22 E-value: 7.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 299 DLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQR---GELAIKDANAKLSELEAALQRAKQDMARQLREYQ 375
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELA 107
|
....*
gi 400416 376 ELMNV 380
Cdd:COG4942 108 ELLRA 112
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
210-407 |
2.08e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 210 LESRLEGLTDEinfLRQLyEEEIRELQSQ--ISDTSVVLSMDNSRSLDMDSIIAEVKAQYEDIANRsRAEAESMYQIKYE 287
Cdd:COG3206 180 LEEQLPELRKE---LEEA-EAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR-LAALRAQLGSGPD 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 288 ELQSLAGkhGDDLRRTKTEISEMNRNISRLQA-------EIEGLKGQRASLEAAIADAEQRGELAIKDANAKLSELEAAL 360
Cdd:COG3206 255 ALPELLQ--SPVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASL 332
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 400416 361 QRAKQDMARQLREYQELMNVKLALDIEIATYRKLLEG-----EESRLESGMQ 407
Cdd:COG3206 333 QAQLAQLEARLAELPELEAELRRLEREVEVARELYESllqrlEEARLAEALT 384
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
72-332 |
3.64e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.60 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 72 LLSPLVLEVDPNIQAVRTQEKEQIKTLNNKFASFIDKVRFLEQQNKMLEtkwsllQQQKTARSNMDNMfESYINNLRRQL 151
Cdd:TIGR02169 273 LLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE------ERLAKLEAEIDKL-LAEIEELEREI 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 152 ETLGQEKLKLEAElgnmqglVEDFKNKYEDEINKRTEMENEFvlikkdvDEAYMNKVELESRLEGLTDEINFLRQlyeeE 231
Cdd:TIGR02169 346 EEERKRRDKLTEE-------YAELKEELEDLRAELEEVDKEF-------AETRDELKDYREKLEKLKREINELKR----E 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 232 IRELQSQISDTSVVLSMDNSRSLDMDSIIAEVKAQYEDIANRSRAEAEsmyqiKYEELQSLAGKHGDDLRRTKTEISEMN 311
Cdd:TIGR02169 408 LDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEW-----KLEQLAADLSKYEQELYDLKEEYDRVE 482
|
250 260
....*....|....*....|.
gi 400416 312 RNISRLQAEIEGLKGQRASLE 332
Cdd:TIGR02169 483 KELSKLQRELAEAEAQARASE 503
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
83-362 |
3.90e-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: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 83 NIQAVRTQEKEQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQktarsnmdnmfesyINNLRRQLETLGQEKLKLE 162
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ--------------IEQLKEELKALREALDELR 809
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 163 AELGNMQGLVEDFKNKYEDeinkrteMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQLYEEEIRELQSqisdt 242
Cdd:TIGR02168 810 AELTLLNEEAANLRERLES-------LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA----- 877
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 243 svvlsmdnsrsldmdsiIAEVKAQyediANRSRAEAESMYQIKYEELQSLAGKHG---DDLRRTKTEISEMNRNISRLQA 319
Cdd:TIGR02168 878 -----------------LLNERAS----LEEALALLRSELEELSEELRELESKRSelrRELEELREKLAQLELRLEGLEV 936
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 400416 320 EIEGLKGQ---RASLEAAIADAEQRG-ELAIKDANAKLSELEAALQR 362
Cdd:TIGR02168 937 RIDNLQERlseEYSLTLEEAEALENKiEDDEEEARRRLKRLENKIKE 983
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
88-378 |
7.62e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 45.27 E-value: 7.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 88 RTQEKEQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTARSNMDNMFESYINNLRRQLETLGQEKLKLEAELGN 167
Cdd:pfam07888 75 RRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 168 MQGLVEDFKNKYEDEINKRTEM-------ENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQL------YEEEIRE 234
Cdd:pfam07888 155 MKERAKKAGAQRKEEEAERKQLqaklqqtEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKlttahrKEAENEA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 235 LQSQISDTSVVLSMDNSRSLDMDSIIAEVKAQyedianRSRAEAEsMYQIKYEELQ--------SLAGKHG--------D 298
Cdd:pfam07888 235 LLEELRSLQERLNASERKVEGLGEELSSMAAQ------RDRTQAE-LHQARLQAAQltlqladaSLALREGrarwaqerE 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 299 DLRRT----KTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQRGELAIKDANAKLSELEAALQRAKQDMARQLREY 374
Cdd:pfam07888 308 TLQQSaeadKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEK 387
|
....
gi 400416 375 QELM 378
Cdd:pfam07888 388 QELL 391
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
230-412 |
9.79e-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: 45.05 E-value: 9.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 230 EEIRELQSQISDTSVVLSMDNSRSLD-----MDSIIAEVKAQYEDIANRSRAEAESMYQIKYE--ELQSLAGKHGDDLRR 302
Cdd:TIGR02168 213 ERYKELKAELRELELALLVLRLEELReeleeLQEELKEAEEELEELTAELQELEEKLEELRLEvsELEEEIEELQKELYA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 303 TKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQRGELAIKDAN---AKLSELEAALQRAKQDMARQLREYQELMN 379
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAeleEKLEELKEELESLEAELEELEAELEELES 372
|
170 180 190
....*....|....*....|....*....|....*.
gi 400416 380 VKLALDIEIATYRK---LLEGEESRLESGMQNMSIH 412
Cdd:TIGR02168 373 RLEELEEQLETLRSkvaQLELQIASLNNEIERLEAR 408
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
251-404 |
1.76e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 251 SRSLDMDSIIAEVKAQYEDIANRSRAEAEsmYQIKYEELQSLAGKHGDDLRRTKTEISEMNRNISRLQAEIEGLKGQRAS 330
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAE--LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 331 LEAAIADAEQRGE----------LAIKDANAKLSELEAALQRAKQDMARQLREYQELMNVKLALDIEIATYRKLLEGEES 400
Cdd:TIGR02168 752 LSKELTELEAEIEeleerleeaeEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831
|
....
gi 400416 401 RLES 404
Cdd:TIGR02168 832 RIAA 835
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
112-370 |
3.31e-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: 43.24 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 112 LEQQNKMLETKWSLLQQQKTARSNMDNMFESyinnLRRQLETLGQEklkLEAELGNMQGLVEDFKNKYEDEINKRTEMEN 191
Cdd:pfam01576 31 LEKKHQQLCEEKNALQEQLQAETELCAEAEE----MRARLAARKQE---LEEILHELESRLEEEEERSQQLQNEKKKMQQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 192 EFVLIKKDVDEA-------YMNKVELESRLEGLTDEINFL----------RQLYEEEIRELQSQISDTSVVLSMDNSRSL 254
Cdd:pfam01576 104 HIQDLEEQLDEEeaarqklQLEKVTTEAKIKKLEEDILLLedqnsklskeRKLLEERISEFTSNLAEEEEKAKSLSKLKN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 255 DMDSIIAevkaqyeDIANRSRAEAESmyqikYEELQSLAgkhgddlRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAA 334
Cdd:pfam01576 184 KHEAMIS-------DLEERLKKEEKG-----RQELEKAK-------RKLEGESTDLQEQIAELQAQIAELRAQLAKKEEE 244
|
250 260 270
....*....|....*....|....*....|....*....
gi 400416 335 IADAEQRGELAIKDANA---KLSELEAALQRAKQDMARQ 370
Cdd:pfam01576 245 LQAALARLEEETAQKNNalkKIRELEAQISELQEDLESE 283
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
208-378 |
3.32e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 208 VELESRLEGLTDEInfLRQLYEEEIRELqsqisdtsvvLSMDNSRSLDMDSIIAEVKAQYEDIANRsRAEAESMYQIKYE 287
Cdd:COG4717 350 QELLREAEELEEEL--QLEELEQEIAAL----------LAEAGVEDEEELRAALEQAEEYQELKEE-LEELEEQLEELLG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 288 ELQSLAGKHgdDLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQRGElaikdanakLSELEAALQRAKQDM 367
Cdd:COG4717 417 ELEELLEAL--DEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE---------LAELLQELEELKAEL 485
|
170
....*....|.
gi 400416 368 ARQLREYQELM 378
Cdd:COG4717 486 RELAEEWAALK 496
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
298-377 |
3.63e-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: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 298 DDLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQRgelaIKDANAKLSELEAALQRAKQDMARQLREYQEL 377
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELAELEKEIAEL 95
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
209-377 |
3.64e-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: 42.22 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 209 ELESRLEGLTDEINFLrqlyEEEIRELQSQISDTSVVLSmdnsrslDMDSIIAEVKAQYEDIANR-SRAEAESMYQIKYE 287
Cdd:COG1579 21 RLEHRLKELPAELAEL----EDELAALEARLEAAKTELE-------DLEKEIKRLELEIEEVEARiKKYEEQLGNVRNNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 288 ELQSLAG---KHGDDLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQRGELAIKDANAKLSELEAALQRAK 364
Cdd:COG1579 90 EYEALQKeieSLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
170
....*....|....
gi 400416 365 QDM-ARQLREYQEL 377
Cdd:COG1579 170 AKIpPELLALYERI 183
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
144-404 |
4.08e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 144 INNLRRQLETLGQEKLKLEAELGnmqglVEDFKNkyEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINF 223
Cdd:PRK02224 281 VRDLRERLEELEEERDDLLAEAG-----LDDADA--EAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADD 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 224 LRQLYE---EEIRELQSQISDTSVVLSMDNSRSLDMDSIIAEVKAQYEDIANRsRAEAESMYQIKYEELQSLAGKHGdDL 300
Cdd:PRK02224 354 LEERAEelrEEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVD-LGNAEDFLEELREERDELREREA-EL 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 301 RRTKTEISEMNRNISRLQAE------------------IEGLKGQRASLEAAIADAEqrgelaikdanAKLSELEAALQR 362
Cdd:PRK02224 432 EATLRTARERVEEAEALLEAgkcpecgqpvegsphvetIEEDRERVEELEAELEDLE-----------EEVEEVEERLER 500
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 400416 363 AKqDMARQLREYQELMNVKLALDIEIATYRKLLEGEESRLES 404
Cdd:PRK02224 501 AE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEE 541
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
107-373 |
5.82e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 5.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 107 DKVRFLEQQNKMLETKWSLLQQQKtarsnmdNMFESYINNLRrqletlgqeklKLEAElgnmqgLVEDFKNKYEDEINkr 186
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQI-------KTYNKNIEEQR-----------KKNGE------NIARKQNKYDELVE-- 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 187 tEMENefvlIKKDVDEAYMNKVELESRLEGLTDEINFLRQLYEeeirELQSQISDTSVVLSMDNSRSL---------DMD 257
Cdd:PHA02562 228 -EAKT----IKAEIEELTDELLNLVMDIEDPSAALNKLNTAAA----KIKSKIEQFQKVIKMYEKGGVcptctqqisEGP 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 258 SIIAEVKAQYEDIANRSRAEaesmyQIKYEELQSLAgkhgDDLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIad 337
Cdd:PHA02562 299 DRITKIKDKLKELQHSLEKL-----DTAIDELEEIM----DEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAI-- 367
|
250 260 270
....*....|....*....|....*....|....*.
gi 400416 338 aeQRGELAIKDANAKLSELEAALQRAKQDMARQLRE 373
Cdd:PHA02562 368 --EELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
84-377 |
6.09e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.36 E-value: 6.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 84 IQAVRTQEKEQIKTLNNKFASfidKVRFLEQQNKMLETKWS--LLQQQKTARSnmdnmFESYINNLRRQLETLGQEKLKL 161
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEE---IEQLLEELNKKIKDLGEeeQLRVKEKIGE-----LEAEIASLERSIAEKERELEDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 162 EAELgnmqglvedfkNKYEDEINK-RTEMENefvlIKKDVDEAYMNKVELESRLEGLTDEINFLRQlyeeeirelqsqis 240
Cdd:TIGR02169 321 EERL-----------AKLEAEIDKlLAEIEE----LEREIEEERKRRDKLTEEYAELKEELEDLRA-------------- 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 241 dtsvvlsmdnsrsldmdsiiaevKAQYEDIANRSRAEAESMYQIKYEELQSlagkhgddlrrtktEISEMNRNISRLQAE 320
Cdd:TIGR02169 372 -----------------------ELEEVDKEFAETRDELKDYREKLEKLKR--------------EINELKRELDRLQEE 414
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 321 IEGLKGQRASLEAAIADAEQRG---ELAIKDANAKLSELEAALQRAKQDMARQLREYQEL 377
Cdd:TIGR02169 415 LQRLSEELADLNAAIAGIEAKInelEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL 474
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
83-270 |
7.45e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 7.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 83 NIQAVRTQEKEQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQ-KTARSNMDNMfESYINNLRRQLETLGQEKLKL 161
Cdd:TIGR04523 430 RLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSiNKIKQNLEQK-QKELKSKEKELKKLNEEKKEL 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 162 EAELGNMQGLVEDFKNKYEDEINKRTEMENEFVLIKKDV--DEAYMNKVELESRLEGLTDEINFLRQLY----------E 229
Cdd:TIGR04523 509 EEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELnkDDFELKKENLEKEIDEKNKEIEELKQTQkslkkkqeekQ 588
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 400416 230 EEIRELQSQISDTSVVLSMDNSRSLDMDSIIAEVKAQYEDI 270
Cdd:TIGR04523 589 ELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKL 629
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
89-381 |
9.01e-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: 41.93 E-value: 9.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 89 TQEKEQIKTLNNKFASFIDKVRFLEQQNKMLETKwsLLQQQKTArsnmdnmfesyiNNLRRQLETLGQEKLKLEAELGNM 168
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKNLESQINDLESK--IQNQEKLN------------QQKDEQIKKLQQEKELLEKEIERL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 169 QGLVEDFKNKYEDEINKRTEMENEFVLIKKDVDeaymnkvELESRLEGLTDEINFLRQLYEEEIRELQSQISDtsvvLSM 248
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQDSVKELIIKNLDNTRE-------SLETQLKVLSRSINKIKQNLEQKQKELKSKEKE----LKK 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 249 DNSRSLDMDSIIAEVKAQYEDIANRSRAEAESMYQIKYE--ELQSLAGKHGDDLRRT--KTEISEMNRNISRLQAEIEGL 324
Cdd:TIGR04523 501 LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKisDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQTQKSL 580
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 400416 325 KGQRASLEAAIADAEQRgelaIKDANAKLSELEAALQRAKQDMARQLREYQELMNVK 381
Cdd:TIGR04523 581 KKKQEEKQELIDQKEKE----KKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSII 633
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
261-403 |
9.79e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 9.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 261 AEVKAQYEDIANRSRAEAESMYQIKYEELQSLAGKHGDDLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQ 340
Cdd:COG1196 209 AEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQA 288
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 400416 341 RgelaIKDANAKLSELEAALQRAKQDMARQLREYQELMNVKLALDIEIATYRKLLEGEESRLE 403
Cdd:COG1196 289 E----EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE 347
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
141-376 |
1.10e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 141 ESYINNLRRQLETLGQEKLKLEAELGNMQGLVEDFKNKYEDeinkrtemenefvlIKKDVDEAYMNKVELESRLEGLTDE 220
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE--------------LQAELEALQAEIDKLQAEIAEAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 221 INFLRQLYEEEIRELQSQISDTSVVLSMDNSRSLDmdsiiaevkaqyeDIANRSRAeaesmyqikyeeLQSLAGKHGDDL 300
Cdd:COG3883 81 IEERREELGERARALYRSGGSVSYLDVLLGSESFS-------------DFLDRLSA------------LSKIADADADLL 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 400416 301 RRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQrgelAIKDANAKLSELEAALQRAKQDMARQLREYQE 376
Cdd:COG3883 136 EELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA----QQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
150-385 |
1.17e-03 |
|
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: 41.64 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 150 QLETLGQE-KLKLEAELGNMQGLVEDFKNKYEDEINKRTE-----------MENEFVLIK---KDVDEAYMNKV-ELESR 213
Cdd:pfam15921 246 QLEALKSEsQNKIELLLQQHQDRIEQLISEHEVEITGLTEkassarsqansIQSQLEIIQeqaRNQNSMYMRQLsDLEST 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 214 LEGLTDEINFLRQLYEEEIRELQSQI----SDTSVVLSMDNSRSLDMDSIIAEVKAQYEDIANRsraeaESMYQIKYEEL 289
Cdd:pfam15921 326 VSQLRSELREAKRMYEDKIEELEKQLvlanSELTEARTERDQFSQESGNLDDQLQKLLADLHKR-----EKELSLEKEQN 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 290 QSLAGKHG------DDLRRtktEISEMNRNISRLQAEIEGLKGQ-RASLEAAIADAEQRGElaikdANAKLSELEAALQR 362
Cdd:pfam15921 401 KRLWDRDTgnsitiDHLRR---ELDDRNMEVQRLEALLKAMKSEcQGQMERQMAAIQGKNE-----SLEKVSSLTAQLES 472
|
250 260
....*....|....*....|...
gi 400416 363 AKQdMARQLREyqELMNVKLALD 385
Cdd:pfam15921 473 TKE-MLRKVVE--ELTAKKMTLE 492
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
140-381 |
1.34e-03 |
|
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: 41.26 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 140 FESYINNLRRQLETLGQEKLKLEAELGNMQGLVEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTD 219
Cdd:pfam15921 595 LEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSE 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 220 EINFLRQLYEEEIREL--------------QSQISDTSVVL-SMDNSrslDMDSIIAEVKAQYEDIANRSRAEA-ESMYQ 283
Cdd:pfam15921 675 DYEVLKRNFRNKSEEMetttnklkmqlksaQSELEQTRNTLkSMEGS---DGHAMKVAMGMQKQITAKRGQIDAlQSKIQ 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 284 IkYEELQSLAGKHGDDLRRTKT----EISEMNRNISRLQAEIEGLKGQRASLEAAIADAeqrgELAIKDANAKLSELEAA 359
Cdd:pfam15921 752 F-LEEAMTNANKEKHFLKEEKNklsqELSTVATEKNKMAGELEVLRSQERRLKEKVANM----EVALDKASLQFAECQDI 826
|
250 260
....*....|....*....|..
gi 400416 360 LQRAKQDMARQlrEYQELMNVK 381
Cdd:pfam15921 827 IQRQEQESVRL--KLQHTLDVK 846
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
285-401 |
1.53e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 285 KYEELQSLAGKHG---DDLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQRGElaikDANAKLSELEAALQ 361
Cdd:PRK09039 51 KDSALDRLNSQIAelaDLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGA----AAEGRAGELAQELD 126
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 400416 362 RAKQDMARQLREYqELMNVKL-ALDIEIATYRKLLEGEESR 401
Cdd:PRK09039 127 SEKQVSARALAQV-ELLNQQIaALRRQLAALEAALDASEKR 166
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
118-345 |
1.59e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 118 MLETKwSLLQQQKTARSNMDNMFESY--INNLRRQLETL------GQEKLKLEAELGNMQGLVEDFkNKYEDEInKRTEM 189
Cdd:COG4913 217 MLEEP-DTFEAADALVEHFDDLERAHeaLEDAREQIELLepirelAERYAAARERLAELEYLRAAL-RLWFAQR-RLELL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 190 ENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQLYEE----EIRELQSQISDTSVVLSMDNSRSLDMDSIIAEVKA 265
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEALLAALGL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 266 QYEDIA-----NRSRAEAESmyqikyEELQSLAGKHGDDLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAeq 340
Cdd:COG4913 374 PLPASAeefaaLRAEAAALL------EALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL-- 445
|
....*
gi 400416 341 RGELA 345
Cdd:COG4913 446 RDALA 450
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
120-415 |
3.22e-03 |
|
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: 40.10 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 120 ETKWSLLQQQKTARSNMDNMFESYINNLRRQLETLGQEKLKLEAELGNM----QGLVE------DFKNKYEDEINKRT-E 188
Cdd:pfam15921 390 EKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMksecQGQMErqmaaiQGKNESLEKVSSLTaQ 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 189 MENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLR------QLYEEEIRELQSQISDTSVVLSMDNSRSLDMDSIIAE 262
Cdd:pfam15921 470 LESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQekeraiEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTE 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 263 VKAQYEDIANRSRAEAESMYQIkyEELQSLAGKHGDDLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQRG 342
Cdd:pfam15921 550 CEALKLQMAEKDKVIEILRQQI--ENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARV 627
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 400416 343 ---EL-AIKDANAKlSELEAALQRAKQDMARQLREYQELMNVKLALDIEIATYRKLLEGEESRLESGMQNMSIHTKT 415
Cdd:pfam15921 628 sdlELeKVKLVNAG-SERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKS 703
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
255-404 |
3.60e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 255 DMDSIIAEVKAQYEDIaNRSRAEAESMY-QIK--------YEELQSLAGKHGD-DLRRTKTEISEMNRNISRLQAEIEGL 324
Cdd:COG4913 222 DTFEAADALVEHFDDL-ERAHEALEDAReQIEllepirelAERYAAARERLAElEYLRAALRLWFAQRRLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 325 KGQRASLEAAIADAEQRgelaIKDANAKLSELEAA------------------LQRAKQDMARQLREYQELMN-VKLALD 385
Cdd:COG4913 301 RAELARLEAELERLEAR----LDALREELDELEAQirgnggdrleqlereierLERELEERERRRARLEALLAaLGLPLP 376
|
170
....*....|....*....
gi 400416 386 IEIATYRKLLEGEESRLES 404
Cdd:COG4913 377 ASAEEFAALRAEAAALLEA 395
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
299-402 |
4.05e-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: 38.75 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 299 DLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQR---GELAIKDANAKLSELEAALQR--AKQDMARQLRE 373
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTEledLEKEIKRLELEIEEVEARIKKyeEQLGNVRNNKE 90
|
90 100
....*....|....*....|....*....
gi 400416 374 YQelmnvklALDIEIATYRKLLEGEESRL 402
Cdd:COG1579 91 YE-------ALQKEIESLKRRISDLEDEI 112
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
247-366 |
4.29e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 39.82 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 247 SMDNSRSLDMDSIiAEVKAQYEDIANRSR-AEAESMY-QIKYEELQSLAGKHGDDlRRTKTEISEMNRNISRLQAEIEGL 324
Cdd:NF012221 1661 QLDDAKKISGKQL-ADAKQRHVDNQQKVKdAVAKSEAgVAQGEQNQANAEQDIDD-AKADAEKRKDDALAKQNEAQQAES 1738
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 400416 325 KGqraslEAAIADAEQRGELAIKDANAKLSELEAALQRAKQD 366
Cdd:NF012221 1739 DA-----NAAANDAQSRGEQDASAAENKANQAQADAKGAKQD 1775
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
144-345 |
4.51e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 144 INNLRRQLETLGQEKLKLEAELGNMQGLVEDFKNKYEDEINKRTEMENefVLIKKDVDEAYMNKVELESRLEGLTDEINF 223
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK--LEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 224 LRQlYEEEIRELQSQIsdtsvvlsmdnsrsldmdsiiAEVKAQYEDIANRSRAEAESMYQIKYEELQSLAgkhgDDLRRT 303
Cdd:COG4717 151 LEE-RLEELRELEEEL---------------------EELEAELAELQEELEELLEQLSLATEEELQDLA----EELEEL 204
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 400416 304 KTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQRGELA 345
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLK 246
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
85-314 |
4.73e-03 |
|
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: 39.65 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 85 QAVRTQEKEQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTARSNMDNMFESYINNLRRQ-LETLGQEKLKLEA 163
Cdd:TIGR01612 1161 KAISNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKGINLSYGKNLGKLfLEKIDEEKKKSEH 1240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 164 ELGNMQGLVEDFknkyeDEINKRTEMENEFVLIKKDVDeAYMNKVELESRLEgltDEINFLRQLYEEEIrelqSQISDTS 243
Cdd:TIGR01612 1241 MIKAMEAYIEDL-----DEIKEKSPEIENEMGIEMDIK-AEMETFNISHDDD---KDHHIISKKHDENI----SDIREKS 1307
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 400416 244 VVLSMDNSRSLDMDSI-------IAEVKAQYEDIaNRSRAEAESMYQI-KYEELQSLAgkhgDDLRRTKTEISEMNRNI 314
Cdd:TIGR01612 1308 LKIIEDFSEESDINDIkkelqknLLDAQKHNSDI-NLYLNEIANIYNIlKLNKIKKII----DEVKEYTKEIEENNKNI 1381
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
92-377 |
4.73e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 92 KEQIKTLNNKFASFIDKVRFLEQQNKMLETKwslLQQQKTARSNMDNMFEsyINNLRRQLETLGQEKLKLEAEL-----G 166
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELRELEKV---LKKESELIKLKELAEQ--LKELEEKLKKYNLEELEKKAEEyeklkE 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 167 NMQGLVEDFKNkYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRL--------EGLTDEINFLRQLYEEEIrELQSQ 238
Cdd:PRK03918 533 KLIKLKGEIKS-LKKELEKLEELKKKLAELEKKLDELEEELAELLKELeelgfesvEELEERLKELEPFYNEYL-ELKDA 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 239 ISDTSVVLSMDNSRSLDMDSI---IAEVKAQYEDIANRsraeaesmyqikYEELQSLAGKhgDDLRRTKTEISEMNRNIS 315
Cdd:PRK03918 611 EKELEREEKELKKLEEELDKAfeeLAETEKRLEELRKE------------LEELEKKYSE--EEYEELREEYLELSRELA 676
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 400416 316 RLQAEIEGLKGQRASLEAAIADAEQRGElAIKDANAKLSELEAALQRAkQDMARQLREYQEL 377
Cdd:PRK03918 677 GLRAELEELEKRREEIKKTLEKLKEELE-EREKAKKELEKLEKALERV-EELREKVKKYKAL 736
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
299-403 |
6.00e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.15 E-value: 6.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 299 DLRRTKTE--ISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQ----RGELAIKDAN---AKLSELEAALQRAKQDMAR 369
Cdd:COG1196 171 KERKEEAErkLEATEENLERLEDILGELERQLEPLERQAEKAERyrelKEELKELEAElllLKLRELEAELEELEAELEE 250
|
90 100 110
....*....|....*....|....*....|....
gi 400416 370 QLREYQELMNVKLALDIEIATYRKLLEGEESRLE 403
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEELELELE 284
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
260-372 |
7.03e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 38.68 E-value: 7.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400416 260 IAEVKAQYEDIANRSRAEAESM--YQIKY---------EELQSLAGKHGDDLRRTKTEISEMNRNISRLQAEIEGLKGQR 328
Cdd:COG3524 179 VRFAEEEVERAEERLRDAREALlaFRNRNgildpeataEALLQLIATLEGQLAELEAELAALRSYLSPNSPQVRQLRRRI 258
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 400416 329 ASLEAAIAdaEQRGELAIKDANAKLSEL---------------------EAALQRAKQDMARQLR 372
Cdd:COG3524 259 AALEKQIA--AERARLTGASGGDSLASLlaeyerlelerefaekaytsaLAALEQARIEAARQQR 321
|
|
| |
