|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
118-429 |
9.48e-155 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 443.21 E-value: 9.48e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 118 QEKEQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTAR-SNMDNMFESYINNLRRQLETLGQEKLKLEAELGNM 196
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEpSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 197 QGLVEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQLYEEEIRELQSQISDTSVVLSM 276
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 277 DNSRSLDMDSIIAEVKAQYEDIANRSRAEAESMYQIKYEELQSLAGKHGDDLRRTKTEISEMNRNISRLQAEIEGLKGQR 356
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 372466572 357 ASLEAAIADAEQRGELAIKDANAKLSELEAALQRAKQDMARQLREYQELMNVKLALDIEIATYRKLLEGEESR 429
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
113-431 |
9.07e-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: 71.24 E-value: 9.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 113 QAVRTQEKEQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTARSNMDNMFESYINNLRRQLETLGQEKLKLEAE 192
Cdd:TIGR02168 669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 193 LGNMQGLVEDFKNKYEDEINKRTEMENEFVlikkdvdEAYMNKVELESRLEGLTDEINFLRqlyeEEIRELQSQISDTSV 272
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELA-------EAEAEIEELEAQIEQLKEELKALR----EALDELRAELTLLNE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 273 VLSMDNSRSLDMDSIIAEVKAQYEDIANRSRAEAESMYQIK--YEELQSLAGKHGDDLRRTKTEISEMNRNISRLQAEIE 350
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAaeIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 351 GLKGQRASLEAAIADAEQrgelAIKDANAKLSELEAALQRAKQDMARQLR----EYQELMNVKLALDIEIATYRKLLEGE 426
Cdd:TIGR02168 898 ELSEELRELESKRSELRR----ELEELREKLAQLELRLEGLEVRIDNLQErlseEYSLTLEEAEALENKIEDDEEEARRR 973
|
....*
gi 372466572 427 ESRLE 431
Cdd:TIGR02168 974 LKRLE 978
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
184-432 |
1.08e-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: 61.23 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 184 QEKLKLEAELGNMQGLVEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQLYEEEIREL 263
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 264 QSQISDTSVVLSMDNSRSLDMDSIIAEVKAQYEDIANRSRAEAESMYQIK-----YEELQSLAGKHGDDLRRTKTEISEM 338
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDelraeLTLLNEEAANLRERLESLERRIAAT 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 339 NRNISRLQAEIEGLKGQRASLEAAIADAEQRGElaikDANAKLSELEAALQRAKQDMARQLREYQELMNVKLALDIEIAT 418
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIE----ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
250
....*....|....
gi 372466572 419 YRKLLEGEESRLES 432
Cdd:TIGR02168 913 LRRELEELREKLAQ 926
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
171-435 |
1.17e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.11 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 171 YINNLRRQLETLGQ-------EKLKLEAELGNMQGLVEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLE 243
Cdd:COG1196 233 KLRELEAELEELEAeleeleaELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 244 GLTDEInflrQLYEEEIRELQSQISDTSVVLSMDNSRSLDMDSIIAEVKAQYEDIANRSRAEAESMyqikyEELQSLAGK 323
Cdd:COG1196 313 ELEERL----EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL-----AEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 324 HGDDLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAI---ADAEQRGELAIKDANAKLSELEAALQRAKQDMARQLR 400
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELeelEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260 270
....*....|....*....|....*....|....*
gi 372466572 401 EYQELMNVKLALDIEIATYRKLLEGEESRLESGMQ 435
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
257-401 |
1.31e-08 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 56.51 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 257 EEEIRELQSQISDTSVVLSMDNSRSLDMDSIIAEVKAQYEDI-ANRSRAEAesMYQIKYEELQSLAGKHGD---DLRRTK 332
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAeAERSRLQA--LLAELAGAGAAAEGRAGElaqELDSEK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 333 TEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQRGelaiKDANAKL----SELEAALQRAKQDMAR-------QLRE 401
Cdd:PRK09039 130 QVSARALAQVELLNQQIAALRRQLAALEAALDASEKRD----RESQAKIadlgRRLNVALAQRVQELNRyrseffgRLRE 205
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
120-424 |
1.65e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.38 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 120 KEQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKtarSNMDNMFESyINNLRRQLETLGQEKLKLEAELGNMQGL 199
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEV---KELEELKEE-IEELEKELESLEGSKRKLEEKIRELEER 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 200 VEDFKNKYED------EINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGltdeinflrqlYEEEIRELQSQISDtsvv 273
Cdd:PRK03918 268 IEELKKEIEEleekvkELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSR-----------LEEEINGIEERIKE---- 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 274 LSMDNSRSLDMDSIIAEVKAQYEDIanRSRAEAESMYQIKYEELQSLAGKHG-----------DDLRRTKTEISEmnrNI 342
Cdd:PRK03918 333 LEEKEERLEELKKKLKELEKRLEEL--EERHELYEEAKAKKEELERLKKRLTgltpeklekelEELEKAKEEIEE---EI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 343 SRLQAEIEGLKGQRASLEAAIA----------------DAEQRGELaIKDANAKLSELEAALQRAKqDMARQLREYQELM 406
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEelkkakgkcpvcgrelTEEHRKEL-LEEYTAELKRIEKELKEIE-EKERKLRKELREL 485
|
330
....*....|....*...
gi 372466572 407 NVKLALDIEIATYRKLLE 424
Cdd:PRK03918 486 EKVLKKESELIKLKELAE 503
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
91-115 |
1.68e-08 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 53.51 E-value: 1.68e-08
10 20
....*....|....*....|....*
gi 372466572 91 ITAVTVNQSLLSPLVLEVDPNIQAV 115
Cdd:pfam16208 132 IQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
175-417 |
1.86e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.95 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 175 LRRQLETLGQEKLKLEAELgnmqglvEDFKNKyedeinkrtemeNEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQ 254
Cdd:COG3206 180 LEEQLPELRKELEEAEAAL-------EEFRQK------------NGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 255 LYEeeirELQSQISDTSVVLSmdnsrSLDMDSIIAEVKAQYEDiANRSRAEAESMYQIKYEELQSLAGKhgddLRRTKTE 334
Cdd:COG3206 241 RLA----ALRAQLGSGPDALP-----ELLQSPVIQQLRAQLAE-LEAELAELSARYTPNHPDVIALRAQ----IAALRAQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 335 I-SEMNRNISRLQAEIEGLKGQRASLEAAIADAEQRgelaikdaNAKLSELEAALQRAKQDMARQLREYQELMNVKLALD 413
Cdd:COG3206 307 LqQEAQRILASLEAELEALQAREASLQAQLAQLEAR--------LAELPELEAELRRLEREVEVARELYESLLQRLEEAR 378
|
....
gi 372466572 414 IEIA 417
Cdd:COG3206 379 LAEA 382
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
120-438 |
5.11e-08 |
|
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: 55.80 E-value: 5.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 120 KEQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTARSNMDNMFESYINNLRRQLETLGQEKLKLEAELGNMQGL 199
Cdd:TIGR04523 130 EKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKK 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 200 VEDFKnKYEDEINkrtEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQLYEEEIRELQSQISDtsvvLSMDNS 279
Cdd:TIGR04523 210 IQKNK-SLESQIS---ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE----LEQNNK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 280 RSLDMDSIIAEVKAQYEDIANRsrAEAESMYQIKyEELQSLAgkhgDDLRRTKTEISEMNRNISRLQAEIEGLKGQRASL 359
Cdd:TIGR04523 282 KIKELEKQLNQLKSEISDLNNQ--KEQDWNKELK-SELKNQE----KKLEEIQNQISQNNKIISQLNEQISQLKKELTNS 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 360 EA-------AIADAEQRGELAIKDANAKLSELEaALQRAKQDMARQLREYQELMNVKlalDIEIatyrKLLEGEESRLES 432
Cdd:TIGR04523 355 ESensekqrELEEKQNEIEKLKKENQSYKQEIK-NLESQINDLESKIQNQEKLNQQK---DEQI----KKLQQEKELLEK 426
|
....*.
gi 372466572 433 GMQNMS 438
Cdd:TIGR04523 427 EIERLK 432
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
237-432 |
6.93e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 6.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 237 ELESRLEGLTDEINFLR-QLYEEEIRELQSQISDTSVVLSMDNSRSLDMDSIIAEVKAQYEDIANRSRAEAESMYQIKyE 315
Cdd:COG1196 217 ELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL-A 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 316 ELQSLAGkhgdDLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQRGELA---IKDANAKLSELEAALQRAK 392
Cdd:COG1196 296 ELARLEQ----DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAeeeLEEAEAELAEAEEALLEAE 371
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 372466572 393 QDMARQLREYQELMNVKLALDIEIATYRKLLEGEESRLES 432
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
119-424 |
8.84e-08 |
|
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: 55.07 E-value: 8.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 119 EKEQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTarsnmdnmfesyinNLRRQLETLGQEKLKLEAELGNMQG 198
Cdd:TIGR02169 714 ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE--------------NVKSELKELEARIEELEEDLHKLEE 779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 199 LVEDFKNKYEDEINKrtEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQLYEE---EIRELQSQISDTSVVLS 275
Cdd:TIGR02169 780 ALNDLEARLSHSRIP--EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQElqeQRIDLKEQIKSIEKEIE 857
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 276 MDNSRSLDMDSIIAEVKAQYEDI--------ANRSRAEAE-SMYQIKYEELqslagkhgddlrrtKTEISEMNRNISRLQ 346
Cdd:TIGR02169 858 NLNGKKEELEEELEELEAALRDLesrlgdlkKERDELEAQlRELERKIEEL--------------EAQIEKKRKRLSELK 923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 347 AEIEGLKGQRASLEAAIADAEQ--RGELAIKDANAKLSELEAALQ-------RAKQDMARQLREYQELMNVKLALDIEIA 417
Cdd:TIGR02169 924 AKLEALEEELSEIEDPKGEDEEipEEELSLEDVQAELQRVEEEIRalepvnmLAIQEYEEVLKRLDELKEKRAKLEEERK 1003
|
....*..
gi 372466572 418 TYRKLLE 424
Cdd:TIGR02169 1004 AILERIE 1010
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
121-437 |
2.04e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.92 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 121 EQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTARSNMDNMFESYINNLRRQLETLGQEKLKLEAELGNmqglV 200
Cdd:TIGR02169 681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN----V 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 201 EDFKNKYEDEINkrtEMENEFVLIKKDVDEAYMNkvELESRLEGLTDEINFLrqlyEEEIRELQSQISDTSVVLSMDNSR 280
Cdd:TIGR02169 757 KSELKELEARIE---ELEEDLHKLEEALNDLEAR--LSHSRIPEIQAELSKL----EEEVSRIEARLREIEQKLNRLTLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 281 SLDMDSIIAEVKAQYEDIANR--SRAEAESMYQIKYEELQSlagkhgdDLRRTKTEISEMNRNISRLQAEIEGLKGQRAS 358
Cdd:TIGR02169 828 KEYLEKEIQELQEQRIDLKEQikSIEKEIENLNGKKEELEE-------ELEELEAALRDLESRLGDLKKERDELEAQLRE 900
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 372466572 359 LEAAIADAeqrgELAIKDANAKLSELEAALQRAKQdmarQLREYQELMNVKLALDIEIATYRKLLEgEESRLESGMQNM 437
Cdd:TIGR02169 901 LERKIEEL----EAQIEKKRKRLSELKAKLEALEE----ELSEIEDPKGEDEEIPEEELSLEDVQA-ELQRVEEEIRAL 970
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
138-432 |
2.93e-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: 53.52 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 138 RFLEQQNKMLETKWSLLQQQKTArsnmdnmFESYINNLRRQLETLGQEKLKLEAELGNMQGLVEDFKNKyedeinkRTEM 217
Cdd:TIGR02168 214 RYKELKAELRELELALLVLRLEE-------LREELEELQEELKEAEEELEELTAELQELEEKLEELRLE-------VSEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 218 ENEFVLIKKDVDEAYMNKVELESRLegltdeinflrQLYEEEIRELQSQISDTSVVLSMDNSRSLDMDSIIAEVKAQYED 297
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQK-----------QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 298 IANRSRAEAESM--YQIKYEELQSLAGKHGDDLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQRGELAIK 375
Cdd:TIGR02168 349 LKEELESLEAELeeLEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 372466572 376 DA-NAKLSELEAALQRAKQDMARQLREYQELMNVKLALDIEIATYRKLLEGEESRLES 432
Cdd:TIGR02168 429 KLeEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
253-435 |
5.90e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 5.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 253 RQLYEEEIRELQSQISDTsvvlsmdnsrsldmDSIIAEVKAQYEDIANRSRA----EAESMYQIKY----EELQSLAGKH 324
Cdd:COG4913 612 LAALEAELAELEEELAEA--------------EERLEALEAELDALQERREAlqrlAEYSWDEIDVasaeREIAELEAEL 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 325 gDDLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQRgelaIKDANAKLSELEAALQRAKQDMARQLRE--- 401
Cdd:COG4913 678 -ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE----LEQAEEELDELQDRLEAAEDLARLELRAlle 752
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 372466572 402 --YQELM------NVKLALDIEIATYRKLLEGEESRLESGMQ 435
Cdd:COG4913 753 erFAAALgdaverELRENLEERIDALRARLNRAEEELERAMR 794
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
186-438 |
1.34e-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: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 186 KLKLEAELGNMQGLVEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRqlyeEEIRELQS 265
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLK----ERLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 266 QISDTSVVLSMDNSrslDMDSIIAEVKAQYEDIANRSRAEAE---SMYQIKYEELQSLAGKHGDDLRRTKTEISEMNRNI 342
Cdd:TIGR02169 745 DLSSLEQEIENVKS---ELKELEARIEELEEDLHKLEEALNDleaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKL 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 343 SR-------LQAEIEGLKGQRASLEAAIADAEQR---GELAIKDANAKLSELEAA----------LQRAKQDMARQLREY 402
Cdd:TIGR02169 822 NRltlekeyLEKEIQELQEQRIDLKEQIKSIEKEienLNGKKEELEEELEELEAAlrdlesrlgdLKKERDELEAQLREL 901
|
250 260 270
....*....|....*....|....*....|....*.
gi 372466572 403 QELMNvKLALDIEIAtyRKLLEGEESRLESGMQNMS 438
Cdd:TIGR02169 902 ERKIE-ELEAQIEKK--RKRLSELKAKLEALEEELS 934
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
169-401 |
1.54e-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: 50.15 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 169 ESYINNLRRQLETLGQEKLKLEAELGNMQGLVEDFknkyEDEINKRTEMENEfvlIKKDVDEAYMNKVELESRLEGLTDE 248
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAAL----ERRIAALARRIRA---LEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 249 INFLRQLYEEEIRELQ--SQISDTSVVLSMDNSRSldmdsiiAEVKAQYEDIANRSRAEAESMYQIKYEELQSLAgkhgD 326
Cdd:COG4942 99 LEAQKEELAELLRALYrlGRQPPLALLLSPEDFLD-------AVRRLQYLKYLAPARREQAEELRADLAELAALR----A 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 372466572 327 DLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQRGELAIKDANAKLSELEAALQRAKQDMARQLRE 401
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
327-408 |
3.89e-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: 3.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 327 DLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQR---GELAIKDANAKLSELEAALQRAKQDMARQLREYQ 403
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELA 107
|
....*
gi 372466572 404 ELMNV 408
Cdd:COG4942 108 ELLRA 112
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
238-435 |
6.57e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 6.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 238 LESRLEGLTDEinfLRQLyEEEIRELQSQ--ISDTSVVLSMDNSRSLDMDSIIAEVKAQYEDIANRsRAEAESMYQIKYE 315
Cdd:COG3206 180 LEEQLPELRKE---LEEA-EAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR-LAALRAQLGSGPD 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 316 ELQSLAGkhGDDLRRTKTEISEMNRNISRLQA-------EIEGLKGQRASLEAAIADAEQRGELAIKDANAKLSELEAAL 388
Cdd:COG3206 255 ALPELLQ--SPVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASL 332
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 372466572 389 QRAKQDMARQLREYQELMNVKLALDIEIATYRKLLEG-----EESRLESGMQ 435
Cdd:COG3206 333 QAQLAQLEARLAELPELEAELRRLEREVEVARELYESllqrlEEARLAEALT 384
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
111-390 |
7.54e-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: 48.90 E-value: 7.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 111 NIQAVRTQEKEQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQktarsnmdnmfesyINNLRRQLETLGQEKLKLE 190
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ--------------IEQLKEELKALREALDELR 809
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 191 AELGNMQGLVEDFKNKYEDeinkrteMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLrqlyEEEIRELQSQisdt 270
Cdd:TIGR02168 810 AELTLLNEEAANLRERLES-------LERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL----EELIEELESE---- 874
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 271 svvlsmdnsrsldmdsiIAEVKAQYEDIaNRSRAEAESMYQIKYEELQSLAGKHG---DDLRRTKTEISEMNRNISRLQA 347
Cdd:TIGR02168 875 -----------------LEALLNERASL-EEALALLRSELEELSEELRELESKRSelrRELEELREKLAQLELRLEGLEV 936
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 372466572 348 EIEGLKGQ---RASLEAAIADAEQRG-ELAIKDANAKLSELEAALQR 390
Cdd:TIGR02168 937 RIDNLQERlseEYSLTLEEAEALENKiEDDEEEARRRLKRLENKIKE 983
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
100-360 |
9.01e-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: 48.53 E-value: 9.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 100 LLSPLVLEVDPNIQAVRTQEKEQIKTLNNKFASFIDKVRFLEQQNKMLEtkwsllQQQKTARSNMDNMfESYINNLRRQL 179
Cdd:TIGR02169 273 LLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE------ERLAKLEAEIDKL-LAEIEELEREI 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 180 ETLGQEKLKLEAElgnmqglVEDFKNKYEDEINKRTEMENEFvlikkdvDEAYMNKVELESRLEGLTDEINFLRQlyeeE 259
Cdd:TIGR02169 346 EEERKRRDKLTEE-------YAELKEELEDLRAELEEVDKEF-------AETRDELKDYREKLEKLKREINELKR----E 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 260 IRELQSQISDTSVVLSMDNSRSLDMDSIIAEVKAQYEDIANRSRAEAEsmyqiKYEELQSLAGKHGDDLRRTKTEISEMN 339
Cdd:TIGR02169 408 LDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEW-----KLEQLAADLSKYEQELYDLKEEYDRVE 482
|
250 260
....*....|....*....|.
gi 372466572 340 RNISRLQAEIEGLKGQRASLE 360
Cdd:TIGR02169 483 KELSKLQRELAEAEAQARASE 503
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
116-406 |
2.29e-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: 46.81 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 116 RTQEKEQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTARSNMDNMFESYINNLRRQLETLGQEKLKLEAELGN 195
Cdd:pfam07888 75 RRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 196 MQGLVEDFKNKYEDEINKRTEMEN-------EFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQL------YEEEIRE 262
Cdd:pfam07888 155 MKERAKKAGAQRKEEEAERKQLQAklqqteeELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKlttahrKEAENEA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 263 LQSQISDTSVVLSMDNSRSLDMDSIIAEVKAQyedianRSRAEAEsMYQIKYEELQ--------SLAGKHG--------D 326
Cdd:pfam07888 235 LLEELRSLQERLNASERKVEGLGEELSSMAAQ------RDRTQAE-LHQARLQAAQltlqladaSLALREGrarwaqerE 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 327 DLRRT----KTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQRGELAIKDANAKLSELEAALQRAKQDMARQLREY 402
Cdd:pfam07888 308 TLQQSaeadKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEK 387
|
....
gi 372466572 403 QELM 406
Cdd:pfam07888 388 QELL 391
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
258-440 |
3.47e-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: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 258 EEIRELQSQISDTSVVLSMDNSRSLD-----MDSIIAEVKAQYEDIANRSRAEAESMYQIKYE--ELQSLAGKHGDDLRR 330
Cdd:TIGR02168 213 ERYKELKAELRELELALLVLRLEELReeleeLQEELKEAEEELEELTAELQELEEKLEELRLEvsELEEEIEELQKELYA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 331 TKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQRGELAIKDAN---AKLSELEAALQRAKQDMARQLREYQELMN 407
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAeleEKLEELKEELESLEAELEELEAELEELES 372
|
170 180 190
....*....|....*....|....*....|....*.
gi 372466572 408 VKLALDIEIATYRK---LLEGEESRLESGMQNMSIH 440
Cdd:TIGR02168 373 RLEELEEQLETLRSkvaQLELQIASLNNEIERLEAR 408
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
140-398 |
4.71e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 46.32 E-value: 4.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 140 LEQQNKMLETKWSLLQQQKTARSNMDNMFESyinnLRRQLETLGQEklkLEAELGNMQGLVEDFKNKYEDEINKRTEMEN 219
Cdd:pfam01576 31 LEKKHQQLCEEKNALQEQLQAETELCAEAEE----MRARLAARKQE---LEEILHELESRLEEEEERSQQLQNEKKKMQQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 220 EFVLIKKDVDEA-------YMNKVELESRLEGLTDEINFL----------RQLYEEEIRELQSQISDTSVVLSMDNSRSL 282
Cdd:pfam01576 104 HIQDLEEQLDEEeaarqklQLEKVTTEAKIKKLEEDILLLedqnsklskeRKLLEERISEFTSNLAEEEEKAKSLSKLKN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 283 DMDSIIAevkaqyeDIANRSRAEAESmyqikYEELQSLAgkhgddlRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAA 362
Cdd:pfam01576 184 KHEAMIS-------DLEERLKKEEKG-----RQELEKAK-------RKLEGESTDLQEQIAELQAQIAELRAQLAKKEEE 244
|
250 260 270
....*....|....*....|....*....|....*....
gi 372466572 363 IADAEQRGELAIKDANA---KLSELEAALQRAKQDMARQ 398
Cdd:pfam01576 245 LQAALARLEEETAQKNNalkKIRELEAQISELQEDLESE 283
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
237-405 |
5.49e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 5.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 237 ELESRLEGLTDEINFLrqlyEEEIRELQSQISDTSVVLSmdnsrslDMDSIIAEVKAQYEDIANR-SRAEAESMYQIKYE 315
Cdd:COG1579 21 RLEHRLKELPAELAEL----EDELAALEARLEAAKTELE-------DLEKEIKRLELEIEEVEARiKKYEEQLGNVRNNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 316 ELQSLAG---KHGDDLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQRGELAIKDANAKLSELEAALQRAK 392
Cdd:COG1579 90 EYEALQKeieSLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
170
....*....|....
gi 372466572 393 QDM-ARQLREYQEL 405
Cdd:COG1579 170 AKIpPELLALYERI 183
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
279-432 |
6.95e-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: 45.82 E-value: 6.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 279 SRSLDMDSIIAEVKAQYEDIANRSRAEAEsmYQIKYEELQSLAGKHGDDLRRTKTEISEMNRNISRLQAEIEGLKGQRAS 358
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAE--LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 359 LEAAIADAEQR----------GELAIKDANAKLSELEAALQRAKQDMARQLREYQELMNVKLALDIEIATYRKLLEGEES 428
Cdd:TIGR02168 752 LSKELTELEAEieeleerleeAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831
|
....
gi 372466572 429 RLES 432
Cdd:TIGR02168 832 RIAA 835
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
117-392 |
7.20e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.40 E-value: 7.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 117 TQEKEQIKTLNNKFASFIDKVRFLEQQNKMLETKwsLLQQQKTArsnmdnmfesyiNNLRRQLETLGQEKLKLEAELGNM 196
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKNLESQINDLESK--IQNQEKLN------------QQKDEQIKKLQQEKELLEKEIERL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 197 QGLVEDFKNKYEDEINKRTEMENEFVLIKKDVDeaymnkvELESRLEGLTDEINFLRQLYEEEIRELQSQISDtsvvLSM 276
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQDSVKELIIKNLDNTRE-------SLETQLKVLSRSINKIKQNLEQKQKELKSKEKE----LKK 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 277 DNSRSLDMDSIIAEVKAQYEDIANRSRAEAESMYQIKYE--ELQSLAGKHGDDLRRT--KTEISEMNRNISRLQAEIEGL 352
Cdd:TIGR04523 501 LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKisDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQTQKSL 580
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 372466572 353 KGQRASLEAAIADAEQ-----RGELAIKDanAKLSELEAALQRAK 392
Cdd:TIGR04523 581 KKKQEEKQELIDQKEKekkdlIKEIEEKE--KKISSLEKELEKAK 623
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
236-406 |
7.44e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 7.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 236 VELESRLEGLTDEInfLRQLYEEEIRELqsqisdtsvvLSMDNSRSLDMDSIIAEVKAQYEDIANRsRAEAESMYQIKYE 315
Cdd:COG4717 350 QELLREAEELEEEL--QLEELEQEIAAL----------LAEAGVEDEEELRAALEQAEEYQELKEE-LEELEEQLEELLG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 316 ELQSLAGKHgdDLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQRGElaikdanakLSELEAALQRAKQDM 395
Cdd:COG4717 417 ELEELLEAL--DEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE---------LAELLQELEELKAEL 485
|
170
....*....|.
gi 372466572 396 ARQLREYQELM 406
Cdd:COG4717 486 RELAEEWAALK 496
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
112-405 |
7.97e-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: 45.44 E-value: 7.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 112 IQAVRTQEKEQIKTLNNKFASfidKVRFLEQQNKMLETKWS--LLQQQKTARSnmdnmFESYINNLRRQLETLGQEKLKL 189
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEE---IEQLLEELNKKIKDLGEeeQLRVKEKIGE-----LEAEIASLERSIAEKERELEDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 190 EAELgnmqglvedfkNKYEDEINK-RTEMENefvlIKKDVDEAYMNKVELESRLEGLTDEINFLRQlyeeeirelqsqis 268
Cdd:TIGR02169 321 EERL-----------AKLEAEIDKlLAEIEE----LEREIEEERKRRDKLTEEYAELKEELEDLRA-------------- 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 269 dtsvvlsmdnsrsldmdsiiaevKAQYEDIANRSRAEAESMYQIKYEELQSlagkhgddlrrtktEISEMNRNISRLQAE 348
Cdd:TIGR02169 372 -----------------------ELEEVDKEFAETRDELKDYREKLEKLKR--------------EINELKRELDRLQEE 414
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 349 IEGLKGQRASLEAAIADAEQRG---ELAIKDANAKLSELEAALQRAKQDMARQLREYQEL 405
Cdd:TIGR02169 415 LQRLSEELADLNAAIAGIEAKInelEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL 474
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
172-432 |
9.20e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 9.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 172 INNLRRQLETLGQEKLKLEAELGnmqglVEDFKNkyEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINF 251
Cdd:PRK02224 281 VRDLRERLEELEEERDDLLAEAG-----LDDADA--EAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADD 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 252 LRQLYE---EEIRELQSQISDTSVVLSMDNSRSLDMDSIIAEVKAQYEDIANRsRAEAESMYQIKYEELQSLAGKHGdDL 328
Cdd:PRK02224 354 LEERAEelrEEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVD-LGNAEDFLEELREERDELREREA-EL 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 329 RRTKTEISEMNRNISRLQAE------------------IEGLKGQRASLEAAIADAEqrgelaikdanAKLSELEAALQR 390
Cdd:PRK02224 432 EATLRTARERVEEAEALLEAgkcpecgqpvegsphvetIEEDRERVEELEAELEDLE-----------EEVEEVEERLER 500
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 372466572 391 AKqDMARQLREYQELMNVKLALDIEIATYRKLLEGEESRLES 432
Cdd:PRK02224 501 AE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEE 541
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
111-298 |
1.34e-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: 44.63 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 111 NIQAVRTQEKEQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQ-KTARSNMDNMfESYINNLRRQLETLGQEKLKL 189
Cdd:TIGR04523 430 RLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSiNKIKQNLEQK-QKELKSKEKELKKLNEEKKEL 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 190 EAELGNMQGLVEDFKNKYEDEINKRTEMENEFVLIKKDV--DEAYMNKVELESRLEGLTDEINFLRQLY----------E 257
Cdd:TIGR04523 509 EEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELnkDDFELKKENLEKEIDEKNKEIEELKQTQkslkkkqeekQ 588
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 372466572 258 EEIRELQSQISDTSVVLSMDNSRSLDMDSIIAEVKAQYEDI 298
Cdd:TIGR04523 589 ELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKL 629
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
326-405 |
2.04e-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: 43.60 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 326 DDLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQRgelaIKDANAKLSELEAALQRAKQDMARQLREYQEL 405
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELAELEKEIAEL 95
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
135-401 |
2.07e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 135 DKVRFLEQQNKMLETKWSLLQQQKtarsnmdNMFESYINNLRrqletlgqeklKLEAElgnmqgLVEDFKNKYEDEINkr 214
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQI-------KTYNKNIEEQR-----------KKNGE------NIARKQNKYDELVE-- 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 215 tEMENefvlIKKDVDEAYMNKVELESRLEGLTDEINFLRQLYEeeirELQSQISDTSVVLSMDNSRSL---------DMD 285
Cdd:PHA02562 228 -EAKT----IKAEIEELTDELLNLVMDIEDPSAALNKLNTAAA----KIKSKIEQFQKVIKMYEKGGVcptctqqisEGP 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 286 SIIAEVKAQYEDIANRSRAEaesmyQIKYEELQSLAgkhgDDLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIad 365
Cdd:PHA02562 299 DRITKIKDKLKELQHSLEKL-----DTAIDELEEIM----DEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAI-- 367
|
250 260 270
....*....|....*....|....*....|....*.
gi 372466572 366 aeQRGELAIKDANAKLSELEAALQRAKQDMARQLRE 401
Cdd:PHA02562 368 --EELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
120-405 |
3.20e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 120 KEQIKTLNNKFASFIDKVRFLEQQNKMLETKwslLQQQKTARSNMDNMFEsyINNLRRQLETLGQEKLKLEAEL-----G 194
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELRELEKV---LKKESELIKLKELAEQ--LKELEEKLKKYNLEELEKKAEEyeklkE 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 195 NMQGLVEDFKNkYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRL--------EGLTDEINFLRQLYEEEIrELQSQ 266
Cdd:PRK03918 533 KLIKLKGEIKS-LKKELEKLEELKKKLAELEKKLDELEEELAELLKELeelgfesvEELEERLKELEPFYNEYL-ELKDA 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 267 ISDTSVVLSMDNSRSLDMDSI---IAEVKAQYEDIANRsraeaesmyqikYEELQSLAGKhgDDLRRTKTEISEMNRNIS 343
Cdd:PRK03918 611 EKELEREEKELKKLEEELDKAfeeLAETEKRLEELRKE------------LEELEKKYSE--EEYEELREEYLELSRELA 676
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 372466572 344 RLQAEIEGLKGQRASLEAAIADAEQRGElAIKDANAKLSELEAALQRAkQDMARQLREYQEL 405
Cdd:PRK03918 677 GLRAELEELEKRREEIKKTLEKLKEELE-EREKAKKELEKLEKALERV-EELREKVKKYKAL 736
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
178-413 |
3.60e-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: 43.57 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 178 QLETLGQE-KLKLEAELGNMQGLVEDFKNKYEDEINKRTE-----------MENEFVLIK---KDVDEAYMNKV-ELESR 241
Cdd:pfam15921 246 QLEALKSEsQNKIELLLQQHQDRIEQLISEHEVEITGLTEkassarsqansIQSQLEIIQeqaRNQNSMYMRQLsDLEST 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 242 LEGLTDEINFLRQLYEEEIRELQSQI----SDTSVVLSMDNSRSLDMDSIIAEVKAQYEDIANRsraeaESMYQIKYEEL 317
Cdd:pfam15921 326 VSQLRSELREAKRMYEDKIEELEKQLvlanSELTEARTERDQFSQESGNLDDQLQKLLADLHKR-----EKELSLEKEQN 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 318 QSLAGKHG------DDLRRtktEISEMNRNISRLQAEIEGLKGQ-RASLEAAIADAEQRGElaikdANAKLSELEAALQR 390
Cdd:pfam15921 401 KRLWDRDTgnsitiDHLRR---ELDDRNMEVQRLEALLKAMKSEcQGQMERQMAAIQGKNE-----SLEKVSSLTAQLES 472
|
250 260
....*....|....*....|...
gi 372466572 391 AKQdMARQLREyqELMNVKLALD 413
Cdd:pfam15921 473 TKE-MLRKVVE--ELTAKKMTLE 492
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
168-409 |
4.65e-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: 43.18 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 168 FESYINNLRRQLETLGQEKLKLEAELGNMQGLVEDFKNKYEDEINKRTEMENEFVLIKKDVDEaYMNKVEL-ESRLEGLT 246
Cdd:pfam15921 595 LEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQ-LLNEVKTsRNELNSLS 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 247 DEINFLRQLYEEEIREL--------------QSQISDTSVVL-SMDNSrslDMDSIIAEVKAQYEDIANRSRAEA-ESMY 310
Cdd:pfam15921 674 EDYEVLKRNFRNKSEEMetttnklkmqlksaQSELEQTRNTLkSMEGS---DGHAMKVAMGMQKQITAKRGQIDAlQSKI 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 311 QIkYEELQSLAGKHGDDLRRTKT----EISEMNRNISRLQAEIEGLKGQRASLEAAIADAeqrgELAIKDANAKLSELEA 386
Cdd:pfam15921 751 QF-LEEAMTNANKEKHFLKEEKNklsqELSTVATEKNKMAGELEVLRSQERRLKEKVANM----EVALDKASLQFAECQD 825
|
250 260
....*....|....*....|...
gi 372466572 387 ALQRAKQDMARQlrEYQELMNVK 409
Cdd:pfam15921 826 IIQRQEQESVRL--KLQHTLDVK 846
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
289-431 |
5.17e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 5.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 289 AEVKAQYEDIANRSRAEAESMYQIKYEELQSLAGKHGDDLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQ 368
Cdd:COG1196 209 AEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQA 288
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 372466572 369 RgelaIKDANAKLSELEAALQRAKQDMARQLREYQELMNVKLALDIEIATYRKLLEGEESRLE 431
Cdd:COG1196 289 E----EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE 347
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
146-373 |
5.73e-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: 5.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 146 MLETKwSLLQQQKTARSNMDNMFESY--INNLRRQLETL------GQEKLKLEAELGNMQGLVEDFkNKYEDEInKRTEM 217
Cdd:COG4913 217 MLEEP-DTFEAADALVEHFDDLERAHeaLEDAREQIELLepirelAERYAAARERLAELEYLRAAL-RLWFAQR-RLELL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 218 ENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQLYEE----EIRELQSQISDTSVVLSMDNSRSLDMDSIIAEVKA 293
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEALLAALGL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 294 QYEDIA-----NRSRAEAESmyqikyEELQSLAGKHGDDLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAeq 368
Cdd:COG4913 374 PLPASAeefaaLRAEAAALL------EALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL-- 445
|
....*
gi 372466572 369 RGELA 373
Cdd:COG4913 446 RDALA 450
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
169-404 |
6.58e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 6.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 169 ESYINNLRRQLETLGQEKLKLEAELGNMQGLVEDFKNKYEDeinkrtemenefvlIKKDVDEAYMNKVELESRLEGLTDE 248
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE--------------LQAELEALQAEIDKLQAEIAEAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 249 INFLRQLYEEEIRELQSQISDTSVVLSMDNSRSLDmdsiiaevkaqyeDIANRSRAeaesmyqikyeeLQSLAGKHGDDL 328
Cdd:COG3883 81 IEERREELGERARALYRSGGSVSYLDVLLGSESFS-------------DFLDRLSA------------LSKIADADADLL 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 372466572 329 RRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQrgelAIKDANAKLSELEAALQRAKQDMARQLREYQE 404
Cdd:COG3883 136 EELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA----QQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
327-430 |
9.72e-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: 40.68 E-value: 9.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 327 DLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQR---GELAIKDANAKLSELEAALQR--AKQDMARQLRE 401
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTEledLEKEIKRLELEIEEVEARIKKyeEQLGNVRNNKE 90
|
90 100
....*....|....*....|....*....
gi 372466572 402 YQelmnvklALDIEIATYRKLLEGEESRL 430
Cdd:COG1579 91 YE-------ALQKEIESLKRRISDLEDEI 112
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
172-373 |
1.01e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 172 INNLRRQLETLGQEKLKLEAELGNMQGLVEDFKNKYEDEINKRTEMENefVLIKKDVDEAYMNKVELESRLEGLTDEINF 251
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK--LEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 252 LRQlYEEEIRELQSQIsdtsvvlsmdnsrsldmdsiiAEVKAQYEDIANRSRAEAESMYQIKYEELQSLAgkhgDDLRRT 331
Cdd:COG4717 151 LEE-RLEELRELEEEL---------------------EELEAELAELQEELEELLEQLSLATEEELQDLA----EELEEL 204
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 372466572 332 KTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQRGELA 373
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLK 246
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
113-342 |
1.22e-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: 41.96 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 113 QAVRTQEKEQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTARSNMDNMFESYINNLRRQ-LETLGQEKLKLEA 191
Cdd:TIGR01612 1161 KAISNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKGINLSYGKNLGKLfLEKIDEEKKKSEH 1240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 192 ELGNMQGLVEDFknkyeDEINKRTEMENEFVLIKKDVDeAYMNKVELESRLEgltDEINFLRQLYEEEIrelqSQISDTS 271
Cdd:TIGR01612 1241 MIKAMEAYIEDL-----DEIKEKSPEIENEMGIEMDIK-AEMETFNISHDDD---KDHHIISKKHDENI----SDIREKS 1307
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 372466572 272 VVLSMDNSRSLDMDSI-------IAEVKAQYEDIaNRSRAEAESMYQI-KYEELQSLAgkhgDDLRRTKTEISEMNRNI 342
Cdd:TIGR01612 1308 LKIIEDFSEESDINDIkkelqknLLDAQKHNSDI-NLYLNEIANIYNIlKLNKIKKII----DEVKEYTKEIEENNKNI 1381
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
313-429 |
1.23e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.10 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 313 KYEELQSLAGKHG---DDLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQRGElaikDANAKLSELEAALQ 389
Cdd:PRK09039 51 KDSALDRLNSQIAelaDLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGA----AAEGRAGELAQELD 126
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 372466572 390 RAKQDMARQLREYqELMNVKL-ALDIEIATYRKLLEGEESR 429
Cdd:PRK09039 127 SEKQVSARALAQV-ELLNQQIaALRRQLAALEAALDASEKR 166
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
148-443 |
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: 41.64 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 148 ETKWSLLQQQKTARSNMDNMFESYINNLRRQLETLGQEKLKLEAELGNM----QGLVE------DFKNKYEDEINKRT-E 216
Cdd:pfam15921 390 EKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMksecQGQMErqmaaiQGKNESLEKVSSLTaQ 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 217 MENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLR------QLYEEEIRELQSQISDTSVVLSMDNSRSLDMDSIIAE 290
Cdd:pfam15921 470 LESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQekeraiEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTE 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 291 VKAQYEDIANRSRAEAESMYQIkyEELQSLAGKHGDDLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQRG 370
Cdd:pfam15921 550 CEALKLQMAEKDKVIEILRQQI--ENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARV 627
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 372466572 371 ---EL-AIKDANAKlSELEAALQRAKQDMARQLREYQELMNVKLALDIEIATYRKLLEGEESRLESGMQNMSIHTKT 443
Cdd:pfam15921 628 sdlELeKVKLVNAG-SERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKS 703
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
283-432 |
1.37e-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: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 283 DMDSIIAEVKAQYEDIaNRSRAEAESMY-QIK--------YEELQSLAGKHGD-DLRRTKTEISEMNRNISRLQAEIEGL 352
Cdd:COG4913 222 DTFEAADALVEHFDDL-ERAHEALEDAReQIEllepirelAERYAAARERLAElEYLRAALRLWFAQRRLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 353 KGQRASLEAAIADAEQRgelaIKDANAKLSELEAA------------------LQRAKQDMARQLREYQELMN-VKLALD 413
Cdd:COG4913 301 RAELARLEAELERLEAR----LDALREELDELEAQirgnggdrleqlereierLERELEERERRRARLEALLAaLGLPLP 376
|
170
....*....|....*....
gi 372466572 414 IEIATYRKLLEGEESRLES 432
Cdd:COG4913 377 ASAEEFAALRAEAAALLEA 395
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
327-431 |
2.69e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 327 DLRRTKTE--ISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQ----RGELAIKDAN---AKLSELEAALQRAKQDMAR 397
Cdd:COG1196 171 KERKEEAErkLEATEENLERLEDILGELERQLEPLERQAEKAERyrelKEELKELEAElllLKLRELEAELEELEAELEE 250
|
90 100 110
....*....|....*....|....*....|....
gi 372466572 398 QLREYQELMNVKLALDIEIATYRKLLEGEESRLE 431
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEELELELE 284
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
288-431 |
4.36e-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: 38.75 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 288 IAEVKAQYEDIANRsRAEAESMYQIKYEELQSLAgkhgDDLRRTKTEISEMNRNISRLQAEIEGLKGQR--ASLEAAIAD 365
Cdd:COG1579 26 LKELPAELAELEDE-LAALEARLEAAKTELEDLE----KEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyEALQKEIES 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 372466572 366 AEQRGELA---IKDANAKLSELEAALQRAKQDMARQLREYQELmnvKLALDIEIATYRKLLEGEESRLE 431
Cdd:COG1579 101 LKRRISDLedeILELMERIEELEEELAELEAELAELEAELEEK---KAELDEELAELEAELEELEAERE 166
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
275-394 |
4.89e-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: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 275 SMDNSRSLDMDSIiAEVKAQYEDIANRSR-AEAESMY-QIKYEELQSLAGKHGDDlRRTKTEISEMNRNISRLQAEIEGL 352
Cdd:NF012221 1661 QLDDAKKISGKQL-ADAKQRHVDNQQKVKdAVAKSEAgVAQGEQNQANAEQDIDD-AKADAEKRKDDALAKQNEAQQAES 1738
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 372466572 353 KGqraslEAAIADAEQRGELAIKDANAKLSELEAALQRAKQD 394
Cdd:NF012221 1739 DA-----NAAANDAQSRGEQDASAAENKANQAQADAKGAKQD 1775
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
288-400 |
4.95e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 39.06 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 288 IAEVKAQYEDIANRSRAEAESM--YQIKY---------EELQSLAGKHGDDLRRTKTEISEMNRNISRLQAEIEGLKGQR 356
Cdd:COG3524 179 VRFAEEEVERAEERLRDAREALlaFRNRNgildpeataEALLQLIATLEGQLAELEAELAALRSYLSPNSPQVRQLRRRI 258
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 372466572 357 ASLEAAIAdaEQRGELAIKDA----NAKLSELE-----------------AALQRAKQDMARQLR 400
Cdd:COG3524 259 AALEKQIA--AERARLTGASGgdslASLLAEYErlelerefaekaytsalAALEQARIEAARQQR 321
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
121-296 |
5.60e-03 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 38.57 E-value: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 121 EQIKTLNNKFASFIDKVRFLEQQNKML-------ETKWSLLQQQKTARSNMDNMFESYINNLRRQLETLGQEKLKLEAEL 193
Cdd:pfam17078 31 SKLEIAQQKESKFLENLASLKHENDNLssmlnrkERRLKDLEDQLSELKNSYEELTESNKQLKKRLENSSASETTLEAEL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 194 GNMQ----GLVE---DFKNKYEDEINK--------RTEMENEFVLIKKDVDEaymNKVELESRLEGLTDEINFLRQLYEE 258
Cdd:pfam17078 111 ERLQiqydALVDsqnEYKDHYQQEINTlqesledlKLENEKQLENYQQRISS---NDKDIDTKLDSYNNKFKNLDNIYVN 187
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 372466572 259 EIRELQSQISDTSVVLSMDNSRSL--DMDSIIAEVKAQYE 296
Cdd:pfam17078 188 KNNKLLTKLDSLAQLLDLPSWLNLypESRNKILEYAEKME 227
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
260-438 |
5.97e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 39.23 E-value: 5.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 260 IRELQSQISDTSVVLsmdnsrsldmDSIIAEVKAQ--YEDIANRSRAEAESMYQIKYEELQSLAGKHGDDLRRTKTEISE 337
Cdd:PHA02562 176 IRELNQQIQTLDMKI----------DHIQQQIKTYnkNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 338 MNRNISRLQAEIEGLKGQRASLEAAIADA-------EQRGEL-----AIKDANAKLSELEA----------ALQRAKQDM 395
Cdd:PHA02562 246 LVMDIEDPSAALNKLNTAAAKIKSKIEQFqkvikmyEKGGVCptctqQISEGPDRITKIKDklkelqhsleKLDTAIDEL 325
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 372466572 396 ARQLREYQELMNVKLALDIEIATYRKLLEGEES---RLESGMQNMS 438
Cdd:PHA02562 326 EEIMDEFNEQSKKLLELKNKISTNKQSLITLVDkakKVKAAIEELQ 371
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
118-436 |
7.32e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 39.23 E-value: 7.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 118 QEKEQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTARSNMDNMFESYINNLRRQLETLGQEKLKLEAELGNMQ 197
Cdd:TIGR04523 51 NKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 198 GLVEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEIN--------------------FLRQLYE 257
Cdd:TIGR04523 131 KQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLniqknidkiknkllklelllSNLKKKI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 258 EEIRELQSQISD----TSVVLSMDNSRSLDMDSIIAEVKAQYEDIANRSRAEAESMYQIKYEELQslagkhgddLRRTKT 333
Cdd:TIGR04523 211 QKNKSLESQISElkkqNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE---------LEQNNK 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 334 EISEMNRNISRLQAEIEGLKGQRAS-LEAAIADAEQRGELAIKDANAKLSELEAALQRAKQDMARQLREYQELMNVKLAL 412
Cdd:TIGR04523 282 KIKELEKQLNQLKSEISDLNNQKEQdWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEK 361
|
330 340
....*....|....*....|....
gi 372466572 413 DIEIATYRKLLEGEESRLESGMQN 436
Cdd:TIGR04523 362 QRELEEKQNEIEKLKKENQSYKQE 385
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
172-307 |
8.66e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 37.98 E-value: 8.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372466572 172 INNLRRQLETLGQEKLKLEAELGNMQGLVEDFKNKYEDEINKRTEMENEF--VLIKKDVDEAYMNKVELESRLEGLTDEI 249
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIeeVEARIKKYEEQLGNVRNNKEYEALQKEI 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 372466572 250 NFL---RQLYEEEIRELQSQISDTSVVLSMDNSRSLDMDSIIAEVKAQYEDIANRSRAEAE 307
Cdd:COG1579 99 ESLkrrISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
|
|
| |
