|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
90-401 |
6.18e-150 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 430.11 E-value: 6.18e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 90 QEKEQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTAR-SNMDNMFESYINNLRRQLETLGQEKLKLEAELGNM 168
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEpSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 169 QGLVEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQLYEEEIRELQSQISDTSVVLSM 248
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 249 DNSRSLDMDSIIAEVKAQYEDIANRSRAEAESMYQIKYEELQSLAGKHGDDLRRTKTEISEMNRNISRLQAEIEGLKGQR 328
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462531885 329 ASLEAAIADAEQHGELAIKDANAKLSELEAALQRAKQDMARQLREYQELMNVKLALDIEIATYRKLLEGEESR 401
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
85-403 |
3.65e-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: 68.93 E-value: 3.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 85 QAVRTQEKEQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTARSNMDNMFESYINNLRRQLETLGQEKLKLEAE 164
Cdd:TIGR02168 669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 165 LGNMQGLVEDFKNKYEDEINKRTEMENEFVlikkdvdEAYMNKVELESRLEGLTDEINFLRqlyeEEIRELQSQISDTSV 244
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELA-------EAEAEIEELEAQIEQLKEELKALR----EALDELRAELTLLNE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 245 VLSMDNSRSLDMDSIIAEVKAQYEDIANRSRAEAESMYQIK--YEELQSLAGKHGDDLRRTKTEISEMNRNISRLQAEIE 322
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAaeIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 323 GLKGQRASLEAAIADAEQhgelAIKDANAKLSELEAALQRAKQDMARQLR----EYQELMNVKLALDIEIATYRKLLEGE 398
Cdd:TIGR02168 898 ELSEELRELESKRSELRR----ELEELREKLAQLELRLEGLEVRIDNLQErlseEYSLTLEEAEALENKIEDDEEEARRR 973
|
....*
gi 2462531885 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 |
3.51e-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: 3.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 156 QEKLKLEAELGNMQGLVEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQLYEEEIREL 235
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 236 QSQISDTSVVLSMDNSRSLDMDSIIAEVKAQYEDIANRSRAEAESMYQIK-----YEELQSLAGKHGDDLRRTKTEISEM 310
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDelraeLTLLNEEAANLRERLESLERRIAAT 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 311 NRNISRLQAEIEGLKGQRASLEAAIADAEQhgelAIKDANAKLSELEAALQRAKQDMARQLREYQELMNVKLALDIEIAT 390
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEE----LIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
250
....*....|....
gi 2462531885 391 YRKLLEGEESRLES 404
Cdd:TIGR02168 913 LRRELEELREKLAQ 926
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
143-404 |
4.25e-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: 4.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 143 YINNLRRQLETLGQ-------EKLKLEAELGNMQGLVEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLE 215
Cdd:COG1196 233 KLRELEAELEELEAeleeleaELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 216 GLTDEInflrQLYEEEIRELQSQISDTSVVLSMDNSRSLDMDSIIAEVKAQYEDIANRSRAEAESMyqikyEELQSLAGK 295
Cdd:COG1196 313 ELEERL----EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL-----AEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 296 HGDDLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQhgelAIKDANAKLSELEAALQRAKQDMARQLREYQ 375
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE----ALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
250 260
....*....|....*....|....*....
gi 2462531885 376 ELMNVKLALDIEIATYRKLLEGEESRLES 404
Cdd:COG1196 460 ALLELLAELLEEAALLEAALAELLEELAE 488
|
|
| 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
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
229-373 |
5.87e-08 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 54.59 E-value: 5.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 229 EEEIRELQSQISDTSVVLSMDNSRSLDMDSIIAEVKAQYEDI-ANRSRAEAesMYQIKYEELQSLAGKHGD---DLRRTK 304
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAeAERSRLQA--LLAELAGAGAAAEGRAGElaqELDSEK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 305 TEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQHGelaiKDANAKL----SELEAALQRAKQDMAR-------QLRE 373
Cdd:PRK09039 130 QVSARALAQVELLNQQIAALRRQLAALEAALDASEKRD----RESQAKIadlgRRLNVALAQRVQELNRyrseffgRLRE 205
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
147-389 |
1.93e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.48 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 147 LRRQLETLGQEKLKLEAELgnmqglvEDFKNKyedeinkrtemeNEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQ 226
Cdd:COG3206 180 LEEQLPELRKELEEAEAAL-------EEFRQK------------NGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 227 LYEeeirELQSQISDTSVVLSmdnsrSLDMDSIIAEVKAQYEDiANRSRAEAESMYQIKYEELQSLAGKhgddLRRTKTE 306
Cdd:COG3206 241 RLA----ALRAQLGSGPDALP-----ELLQSPVIQQLRAQLAE-LEAELAELSARYTPNHPDVIALRAQ----IAALRAQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 307 I-SEMNRNISRLQAEIEGLKGQRASLEAAIADAEQhgelaikdANAKLSELEAALQRAKQDMARQLREYQELMNVKLALD 385
Cdd:COG3206 307 LqQEAQRILASLEAELEALQAREASLQAQLAQLEA--------RLAELPELEAELRRLEREVEVARELYESLLQRLEEAR 378
|
....
gi 2462531885 386 IEIA 389
Cdd:COG3206 379 LAEA 382
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
91-396 |
4.68e-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: 52.76 E-value: 4.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 91 EKEQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTarsnmdnmfesyinNLRRQLETLGQEKLKLEAELGNMQG 170
Cdd:TIGR02169 714 ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE--------------NVKSELKELEARIEELEEDLHKLEE 779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 171 LVEDFKNKYEDEINKrtEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQLYEE---EIRELQSQISDTSVVLS 247
Cdd:TIGR02169 780 ALNDLEARLSHSRIP--EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQElqeQRIDLKEQIKSIEKEIE 857
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 248 MDNSRSLDMDSIIAEVKAQYEDI--------ANRSRAEAE-SMYQIKYEELqslagkhgddlrrtKTEISEMNRNISRLQ 318
Cdd:TIGR02169 858 NLNGKKEELEEELEELEAALRDLesrlgdlkKERDELEAQlRELERKIEEL--------------EAQIEKKRKRLSELK 923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 319 AEIEGLKGQRASLEAAIADAEQ--HGELAIKDANAKLSELEAALQ-------RAKQDMARQLREYQELMNVKLALDIEIA 389
Cdd:TIGR02169 924 AKLEALEEELSEIEDPKGEDEEipEEELSLEDVQAELQRVEEEIRalepvnmLAIQEYEEVLKRLDELKEKRAKLEEERK 1003
|
....*..
gi 2462531885 390 TYRKLLE 396
Cdd:TIGR02169 1004 AILERIE 1010
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
92-396 |
5.63e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 5.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 92 KEQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKtarSNMDNMFESyINNLRRQLETLGQEKLKLEAELGNMQGL 171
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEV---KELEELKEE-IEELEKELESLEGSKRKLEEKIRELEER 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 172 VEDFKNKYEDEINKRTEMENefvlIKKDVDEaYMNKVELESRLEGLTDEINFLRQLYEEEIRELQSQISDtsvvLSMDNS 251
Cdd:PRK03918 268 IEELKKEIEELEEKVKELKE----LKEKAEE-YIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE----LEEKEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 252 RSLDMDSIIAEVKAQYEDIanRSRAEAESMYQIKYEELQSLAGKHG-----------DDLRRTKTEISEmnrNISRLQAE 320
Cdd:PRK03918 339 RLEELKKKLKELEKRLEEL--EERHELYEEAKAKKEELERLKKRLTgltpeklekelEELEKAKEEIEE---EISKITAR 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 321 IEGLKGQRASLEAAIAD---------------AEQHGELAIKDANAKLSELEAALQRAKqDMARQLREYQELMNVKLALD 385
Cdd:PRK03918 414 IGELKKEIKELKKAIEElkkakgkcpvcgrelTEEHRKELLEEYTAELKRIEKELKEIE-EKERKLRKELRELEKVLKKE 492
|
330
....*....|.
gi 2462531885 386 IEIATYRKLLE 396
Cdd:PRK03918 493 SELIKLKELAE 503
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
209-404 |
6.33e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 6.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 209 ELESRLEGLTDEINFLR-QLYEEEIRELQSQISDTSVVLSMDNSRSLDMDSIIAEVKAQYEDIANRSRAEAESMYQIKyE 287
Cdd:COG1196 217 ELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL-A 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 288 ELQSLAGkhgdDLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQHGELA---IKDANAKLSELEAALQRAK 364
Cdd:COG1196 296 ELARLEQ----DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAeeeLEEAEAELAEAEEALLEAE 371
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2462531885 365 QDMARQLREYQELMNVKLALDIEIATYRKLLEGEESRLES 404
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
93-409 |
1.01e-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: 51.61 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 93 EQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTARSNMDNMFESYINNLRRQLETLGQEKLKLEAELGNmqglV 172
Cdd:TIGR02169 681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN----V 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 173 EDFKNKYEDEINkrtEMENEFVLIKKDVDEAYMNkvELESRLEGLTDEINFLrqlyEEEIRELQSQISDTSVVLSMDNSR 252
Cdd:TIGR02169 757 KSELKELEARIE---ELEEDLHKLEEALNDLEAR--LSHSRIPEIQAELSKL----EEEVSRIEARLREIEQKLNRLTLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 253 SLDMDSIIAEVKAQYEDIANR--SRAEAESMYQIKYEELQSlagkhgdDLRRTKTEISEMNRNISRLQAEIEGLKGQRAS 330
Cdd:TIGR02169 828 KEYLEKEIQELQEQRIDLKEQikSIEKEIENLNGKKEELEE-------ELEELEAALRDLESRLGDLKKERDELEAQLRE 900
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462531885 331 LEAAIADAeqhgELAIKDANAKLSELEAALQRAKQdmarQLREYQELMNVKLALDIEIATYRKLLEgEESRLESGMQNM 409
Cdd:TIGR02169 901 LERKIEEL----EAQIEKKRKRLSELKAKLEALEE----ELSEIEDPKGEDEEIPEEELSLEDVQA-ELQRVEEEIRAL 970
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
92-377 |
1.19e-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: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 92 KEQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTARSNMDNMFESYINNLRRQLETLGQEKLKLEAELGNMQGL 171
Cdd:TIGR04523 130 EKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKK 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 172 VEDFKnKYEDEINkrtEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQLYEEEIRELQSQISDtsvvLSMDNS 251
Cdd:TIGR04523 210 IQKNK-SLESQIS---ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE----LEQNNK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 252 RSLDMDSIIAEVKAQYEDIANRsrAEAESMYQIKyEELQSLAgkhgDDLRRTKTEISEMNRNISRLQAEIEGLKGQRASL 331
Cdd:TIGR04523 282 KIKELEKQLNQLKSEISDLNNQ--KEQDWNKELK-SELKNQE----KKLEEIQNQISQNNKIISQLNEQISQLKKELTNS 354
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2462531885 332 EA-------AIADAEQHGELAIKDANAKLSELEaALQRAKQDMARQLREYQEL 377
Cdd:TIGR04523 355 ESensekqrELEEKQNEIEKLKKENQSYKQEIK-NLESQINDLESKIQNQEKL 406
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
110-404 |
2.49e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 110 RFLEQQNKMLETKWSLLQQQKTArsnmdnmFESYINNLRRQLETLGQEKLKLEAELGNMQGLVEDFKNKyedeinkRTEM 189
Cdd:TIGR02168 214 RYKELKAELRELELALLVLRLEE-------LREELEELQEELKEAEEELEELTAELQELEEKLEELRLE-------VSEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 190 ENEFVLIKKDVDEAYMNKVELESRLegltdeinflrQLYEEEIRELQSQISDTSVVLSMDNSRSLDMDSIIAEVKAQYED 269
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQK-----------QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 270 IANRSRAEAESM--YQIKYEELQSLAGKHGDDLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQHGELAIK 347
Cdd:TIGR02168 349 LKEELESLEAELeeLEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462531885 348 DA-NAKLSELEAALQRAKQDMARQLREYQELMNVKLALDIEIATYRKLLEGEESRLES 404
Cdd:TIGR02168 429 KLeEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
225-407 |
3.03e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 225 RQLYEEEIRELQSQISDTsvvlsmdnsrsldmDSIIAEVKAQYEDIANRSRA----EAESMYQIKY----EELQSLAGKH 296
Cdd:COG4913 612 LAALEAELAELEEELAEA--------------EERLEALEAELDALQERREAlqrlAEYSWDEIDVasaeREIAELEAEL 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 297 gDDLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQhgelAIKDANAKLSELEAALQRAKQDMARQLREYQE 376
Cdd:COG4913 678 -ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEK----ELEQAEEELDELQDRLEAAEDLARLELRALLE 752
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2462531885 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 |
6.00e-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: 6.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 141 ESYINNLRRQLETLGQEKLKLEAELGNMQGLVEDFknkyEDEINKRTEMENEfvlIKKDVDEAYMNKVELESRLEGLTDE 220
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAAL----ERRIAALARRIRA---LEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 221 INFLRQLYEEEIRELQ--SQISDTSVVLSMDNSRSldmdsiiAEVKAQYEDIANRSRAEAESMYQIKYEELQSLAgkhgD 298
Cdd:COG4942 99 LEAQKEELAELLRALYrlGRQPPLALLLSPEDFLD-------AVRRLQYLKYLAPARREQAEELRADLAELAALR----A 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462531885 299 DLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQHGELAIKDANAKLSELEAALQRAKQDMARQLRE 373
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
299-375 |
3.22e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 299 DLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQ----------HGELAIKDANAKLSELEAALQRAKQDMA 368
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARriraleqelaALEAELAELEKEIAELRAELEAQKEELA 107
|
....*..
gi 2462531885 369 RQLREYQ 375
Cdd:COG4942 108 ELLRALY 114
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
72-332 |
3.23e-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: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 72 LLSPLVLEVDPNIQAVRTQEKEQIKTLNNKFASFIDKVRFLEQQNKMLEtkwsllQQQKTARSNMDNMfESYINNLRRQL 151
Cdd:TIGR02169 273 LLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE------ERLAKLEAEIDKL-LAEIEELEREI 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 152 ETLGQEKLKLEAElgnmqglVEDFKNKYEDEINKRTEMENEFvlikkdvDEAYMNKVELESRLEGLTDEINFLRQlyeeE 231
Cdd:TIGR02169 346 EEERKRRDKLTEE-------YAELKEELEDLRAELEEVDKEF-------AETRDELKDYREKLEKLKREINELKR----E 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 232 IRELQSQISDTSVVLSMDNSRSLDMDSIIAEVKAQYEDIANRSRAEAEsmyqiKYEELQSLAGKHGDDLRRTKTEISEMN 311
Cdd:TIGR02169 408 LDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEW-----KLEQLAADLSKYEQELYDLKEEYDRVE 482
|
250 260
....*....|....*....|.
gi 2462531885 312 RNISRLQAEIEGLKGQRASLE 332
Cdd:TIGR02169 483 KELSKLQRELAEAEAQARASE 503
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
83-383 |
3.68e-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: 3.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 83 NIQAVRTQEKEQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQktarsnmdnmfesyINNLRRQLETLGQEKLKLE 162
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ--------------IEQLKEELKALREALDELR 809
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 163 AELGNMQGLVEDFKNKYEDeinkrteMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQLYEEEIRELQSqisdt 242
Cdd:TIGR02168 810 AELTLLNEEAANLRERLES-------LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA----- 877
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 243 svvlsmdnsrsldmdsiIAEVKAQyediANRSRAEAESMYQIKYEELQSLAGKhgddLRRTKTEISEMNRNISRLQAEIE 322
Cdd:TIGR02168 878 -----------------LLNERAS----LEEALALLRSELEELSEELRELESK----RSELRRELEELREKLAQLELRLE 932
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462531885 323 GLKGQRASLEAAIADaeqHGELAIKDANAKLSELEAALQRAKQDMARQLREYQELMNVKLA 383
Cdd:TIGR02168 933 GLEVRIDNLQERLSE---EYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLA 990
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
88-378 |
7.04e-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: 7.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 88 RTQEKEQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTARSNMDNMFESYINNLRRQLETLGQEKLKLEAELGN 167
Cdd:pfam07888 75 RRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 168 MQGLVEDFKNKYEDEINKRTEMEN-------EFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQL------YEEEIRE 234
Cdd:pfam07888 155 MKERAKKAGAQRKEEEAERKQLQAklqqteeELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKlttahrKEAENEA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 235 LQSQISDTSVVLSMDNSRSLDMDSIIAEVKAQyedianRSRAEAEsMYQIKYEELQ--------SLAGKHG--------D 298
Cdd:pfam07888 235 LLEELRSLQERLNASERKVEGLGEELSSMAAQ------RDRTQAE-LHQARLQAAQltlqladaSLALREGrarwaqerE 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 299 DLRRT----KTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQHGELAIKDANAKLSELEAALQRAKQDMARQLREY 374
Cdd:pfam07888 308 TLQQSaeadKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEK 387
|
....
gi 2462531885 375 QELM 378
Cdd:pfam07888 388 QELL 391
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
210-407 |
7.82e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 7.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 210 LESRLEGLTDEinfLRQLyEEEIRELQSQ--ISDTSVVLSMDNSRSLDMDSIIAEVKAQYEDIANRsRAEAESMYQIKYE 287
Cdd:COG3206 180 LEEQLPELRKE---LEEA-EAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR-LAALRAQLGSGPD 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 288 ELQSLAGkhGDDLRRTKTEISEMNRNISRLQA-------EIEGLKGQRASLEAAIADAEQHGELAIKDANAKLSELEAAL 360
Cdd:COG3206 255 ALPELLQ--SPVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASL 332
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462531885 361 QRAKQDMARQLREYQELMNVKLALDIEIATYRKLLEG-----EESRLESGMQ 407
Cdd:COG3206 333 QAQLAQLEARLAELPELEAELRRLEREVEVARELYESllqrlEEARLAEALT 384
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
147-403 |
1.20e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 147 LRRQLETLGQEK------LKLEAELGNMQGLV-----EDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLE 215
Cdd:COG1196 198 LERQLEPLERQAekaeryRELKEELKELEAELlllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 216 GLTDEINFLRQLYEEEIRELQSQISDTSVVLSMDNSRSLDMDSIIAEVKAQYEDIANRSRAEAESmyQIKYEELQSLAGK 295
Cdd:COG1196 278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL--EEELEEAEEELEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 296 HGDDLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQ---HGELAIKDANAKLSELEAAL-QRAKQDMARQL 371
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAqleELEEAEEALLERLERLEEELeELEEALAELEE 435
|
250 260 270
....*....|....*....|....*....|..
gi 2462531885 372 REYQELMNVKLALDIEIATYRKLLEGEESRLE 403
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
148-396 |
1.29e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 148 RRQLETLGQEKLKLEAELGNMQGLVEDFKNKYEDEINKRtemenefvlikkdvdeaymnkvELESRLEGLTDEINFLRQL 227
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERR----------------------EALQRLAEYSWDEIDVASA 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 228 yEEEIRELQSQISDtsvvlsMDNSrsldmDSIIAEVKAQYEDiANRSRAEAESmyqiKYEELQSLAGKHGDDLRRTKTEI 307
Cdd:COG4913 667 -EREIAELEAELER------LDAS-----SDDLAALEEQLEE-LEAELEELEE----ELDELKGEIGRLEKELEQAEEEL 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 308 SEMNRNISRlqAEIEGLKGQRASLEAAIADA--EQHGELAIKDANAKLSELEAALQRAKQDMARQLREYQEL-MNVKLAL 384
Cdd:COG4913 730 DELQDRLEA--AEDLARLELRALLEERFAAAlgDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREwPAETADL 807
|
250
....*....|....*
gi 2462531885 385 DIEIAT---YRKLLE 396
Cdd:COG4913 808 DADLESlpeYLALLD 822
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
105-378 |
1.73e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.04 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 105 FIDKVRFLEQQNKMLETKWSLLQQQKTARsnmdnmfESYINNLRRQLETLGQEKLKLEAELGNMQGLVEDFK---NKYED 181
Cdd:pfam10174 466 RLEELESLKKENKDLKEKVSALQPELTEK-------ESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKeecSKLEN 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 182 EINKRTEMEN------EFVL--------IKKDVDEAYMNKVELEsRLEGLTDEINFLRQLYEEEIRELQS----QISDTS 243
Cdd:pfam10174 539 QLKKAHNAEEavrtnpEINDrirlleqeVARYKEESGKAQAEVE-RLLGILREVENEKNDKDKKIAELESltlrQMKEQN 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 244 VVLSMDNSRSLDMDSIIAEvkaQYEDIANRSRAEAESMYQIKYEELQSLAGKHGDDLRRTKTEISEMNRNISRLQAEIEG 323
Cdd:pfam10174 618 KKVANIKHGQQEMKKKGAQ---LLEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTN 694
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462531885 324 LKGQRASLEAAIADAEQHGELAI---KDANAKLSELEAALQRAKQDMARQL-REYQELM 378
Cdd:pfam10174 695 LRAERRKQLEEILEMKQEALLAAiseKDANIALLELSSSKKKKTQEEVMALkREKDRLV 753
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
209-404 |
2.31e-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: 43.90 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 209 ELESRLEGLTDEINFLRQlyeeEIRELQSQISDTSVVLSmDNSRSldmdsiIAEVKAQYEDIANRSRAEAESMYQIKyEE 288
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQS----ELRRIENRLDELSQELS-DASRK------IGEIEKEIEQLEQEEEKLKERLEELE-ED 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 289 LQSLAgkhgDDLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAE--------QHGELAIKDANAKLSELEAAL 360
Cdd:TIGR02169 746 LSSLE----QEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipeiqaelSKLEEEVSRIEARLREIEQKL 821
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462531885 361 QRAKQDMARQLREYQELMNVKLALDIEIATYRKLLEGEESRLES 404
Cdd:TIGR02169 822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE 865
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
138-373 |
2.56e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 138 NMFESYINNLRRQLETLGQEKLKLEAELGNMQGLVEDfknkYEDeinKRTEMENefvlIKKDVDEAYMNKVELESRLEGL 217
Cdd:PRK02224 209 NGLESELAELDEEIERYEEQREQARETRDEADEVLEE----HEE---RREELET----LEAEIEDLRETIAETEREREEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 218 TDEINFLRqlyeEEIRELQSQISDTSVVLSMDNSRSLDMDSIIAEVKAQYEDI----------ANRSRAEAESM------ 281
Cdd:PRK02224 278 AEEVRDLR----ERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELrdrleecrvaAQAHNEEAESLredadd 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 282 YQIKYEELQSLAGKHGDDLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQHGELAIK---DANAKLSELEA 358
Cdd:PRK02224 354 LEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREerdELREREAELEA 433
|
250
....*....|....*..
gi 2462531885 359 ALQRAKQDM--ARQLRE 373
Cdd:PRK02224 434 TLRTARERVeeAEALLE 450
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
251-404 |
2.84e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 251 SRSLDMDSIIAEVKAQYEDIANRSRAEAEsmYQIKYEELQSLAGKHGDDLRRTKTEISEMNRNISRLQAEIEGLKGQRAS 330
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAE--LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 331 LEAAIADAEQH----------GELAIKDANAKLSELEAALQRAKQDMARQLREYQELMNVKLALDIEIATYRKLLEGEES 400
Cdd:TIGR02168 752 LSKELTELEAEieeleerleeAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831
|
....
gi 2462531885 401 RLES 404
Cdd:TIGR02168 832 RIAA 835
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
144-404 |
3.12e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 144 INNLRRQLETLGQEKLKLEAELGnmqglVEDFKNkyEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINF 223
Cdd:PRK02224 281 VRDLRERLEELEEERDDLLAEAG-----LDDADA--EAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADD 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 224 LRQLYE---EEIRELQSQISDTSVVLSMDNSRSLDMDSIIAEVKAQYEDIANRsRAEAESMYQIKYEELQSLAGKHGDdL 300
Cdd:PRK02224 354 LEERAEelrEEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVD-LGNAEDFLEELREERDELREREAE-L 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 301 RRTKTEISEMNRNISRLQAE------------------IEGLKGQRASLEAAIADAEqhgelaikdanAKLSELEAALQR 362
Cdd:PRK02224 432 EATLRTARERVEEAEALLEAgkcpecgqpvegsphvetIEEDRERVEELEAELEDLE-----------EEVEEVEERLER 500
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2462531885 363 AKqDMARQLREYQELMNVKLALDIEIATYRKLLEGEESRLES 404
Cdd:PRK02224 501 AE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEE 541
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
298-377 |
4.69e-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: 42.44 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 298 DDLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQhgelAIKDANAKLSELEAALQRAKQDMARQLREYQEL 377
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER----RIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
84-377 |
5.09e-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: 42.75 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 84 IQAVRTQEKEQIKTLNNKFASfidKVRFLEQQNKMLETKWS--LLQQQKTARSnmdnmFESYINNLRRQLETLGQEKLKL 161
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEE---IEQLLEELNKKIKDLGEeeQLRVKEKIGE-----LEAEIASLERSIAEKERELEDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 162 EAELgnmqglvedfkNKYEDEINK-RTEMENefvlIKKDVDEAYMNKVELESRLEGLTDEINFLRQlyeeeirelqsqis 240
Cdd:TIGR02169 321 EERL-----------AKLEAEIDKlLAEIEE----LEREIEEERKRRDKLTEEYAELKEELEDLRA-------------- 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 241 dtsvvlsmdnsrsldmdsiiaevKAQYEDIANRSRAEAESMYQIKYEELQSlagkhgddlrrtktEISEMNRNISRLQAE 320
Cdd:TIGR02169 372 -----------------------ELEEVDKEFAETRDELKDYREKLEKLKR--------------EINELKRELDRLQEE 414
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 321 IEGLKGQRASLEAAIADAE-QHGEL--AIKDANAKLSELEAALQRAKQDMARQLREYQEL 377
Cdd:TIGR02169 415 LQRLSEELADLNAAIAGIEaKINELeeEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL 474
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
107-357 |
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 2462531885 107 DKVRFLEQQNKMLETKWSLLQQQKtarsnmdNMFESYINNLRRQletLGQEKLKLEAELGNMQGLVEDFKNkyedEINKR 186
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQI-------KTYNKNIEEQRKK---NGENIARKQNKYDELVEEAKTIKA----EIEEL 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 187 TEMENEFVLIKKDVDEAY----MNKVELESRLEGLTDEINFLRQlyEEEIRELQSQISDTSVVLSmdnsrslDMDSIIAE 262
Cdd:PHA02562 240 TDELLNLVMDIEDPSAALnklnTAAAKIKSKIEQFQKVIKMYEK--GGVCPTCTQQISEGPDRIT-------KIKDKLKE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 263 VKAQYEDIANRSRAEAESMyqIKYEELQSLAGKHGDDLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQHg 342
Cdd:PHA02562 311 LQHSLEKLDTAIDELEEIM--DEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDE- 387
|
250
....*....|....*
gi 2462531885 343 elaIKDANAKLSELE 357
Cdd:PHA02562 388 ---LDKIVKTKSELV 399
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
208-378 |
6.14e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 6.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 208 VELESRLEGLTDEInfLRQLYEEEIRELqsqisdtsvvLSMDNSRSLDMDSIIAEVKAQYEDIANRsRAEAESMYQIKYE 287
Cdd:COG4717 350 QELLREAEELEEEL--QLEELEQEIAAL----------LAEAGVEDEEELRAALEQAEEYQELKEE-LEELEEQLEELLG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 288 ELQSLAGKHgdDLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQHGElaikdanakLSELEAALQRAKQDM 367
Cdd:COG4717 417 ELEELLEAL--DEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE---------LAELLQELEELKAEL 485
|
170
....*....|.
gi 2462531885 368 ARQLREYQELM 378
Cdd:COG4717 486 RELAEEWAALK 496
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
83-270 |
7.33e-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: 7.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 83 NIQAVRTQEKEQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQ-KTARSNMDNMfESYINNLRRQLETLGQEKLKL 161
Cdd:TIGR04523 430 RLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSiNKIKQNLEQK-QKELKSKEKELKKLNEEKKEL 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 162 EAELGNMQGLVEDFKNKYEDEINKRTEMENEFVLIKKDV--DEAYMNKVELESRLEGLTDEINFLRQLY----------E 229
Cdd:TIGR04523 509 EEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELnkDDFELKKENLEKEIDEKNKEIEELKQTQkslkkkqeekQ 588
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2462531885 230 EEIRELQSQISDTSVVLSMDNSRSLDMDSIIAEVKAQYEDI 270
Cdd:TIGR04523 589 ELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKL 629
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
141-376 |
8.55e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 8.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 141 ESYINNLRRQLETLGQEKLKLEAELGNMQGLVEDFKNKYEDeinkrtemenefvlIKKDVDEAYMNKVELESRLEGLTDE 220
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE--------------LQAELEALQAEIDKLQAEIAEAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 221 INFLRQLYEEEIRELQSQISDTSVVLSMDNSRSLDmdsiiaevkaqyeDIANRSRAeaesmyqikyeeLQSLAGKHGDDL 300
Cdd:COG3883 81 IEERREELGERARALYRSGGSVSYLDVLLGSESFS-------------DFLDRLSA------------LSKIADADADLL 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462531885 301 RRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQhgelAIKDANAKLSELEAALQRAKQDMARQLREYQE 376
Cdd:COG3883 136 EELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA----QQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
89-381 |
9.57e-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: 9.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 89 TQEKEQIKTLNNKFASFIDKVRFLEQQNKMLETKwsLLQQQKTArsnmdnmfesyiNNLRRQLETLGQEKLKLEAELGNM 168
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKNLESQINDLESK--IQNQEKLN------------QQKDEQIKKLQQEKELLEKEIERL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 169 QGLVEDFKNKYEDEINKRTEMENEFVLIKKDVDeaymnkvELESRLEGLTDEINFLRQLYEEEIRELQSQISDtsvvLSM 248
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQDSVKELIIKNLDNTRE-------SLETQLKVLSRSINKIKQNLEQKQKELKSKEKE----LKK 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 249 DNSRSLDMDSIIAEVKAQYEDIANRSRAEAESMYQIKYE--ELQSLAGKHGDDLRRT--KTEISEMNRNISRLQAEIEGL 324
Cdd:TIGR04523 501 LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKisDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQTQKSL 580
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462531885 325 KGQRASLEAAIADAEQHgelaIKDANAKLSELEAALQRAKQDMARQLREYQELMNVK 381
Cdd:TIGR04523 581 KKKQEEKQELIDQKEKE----KKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSII 633
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
209-366 |
9.88e-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: 9.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 209 ELESRLEGLTDEINFLrqlyEEEIRELQSQISDTSVVLSmdnsrslDMDSIIAEVKAQYEDIANR-SRAEAESMYQIKYE 287
Cdd:COG1579 21 RLEHRLKELPAELAEL----EDELAALEARLEAAKTELE-------DLEKEIKRLELEIEEVEARiKKYEEQLGNVRNNK 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462531885 288 ELQSLAgkhgDDLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQHGELAIKDANAKLSELEAALQRAKQD 366
Cdd:COG1579 90 EYEALQ----KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
232-410 |
1.08e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 232 IRELQSQISDTSVVLsmdnsrsldmDSIIAEVKAQ--YEDIANRSRAEAESMYQIKYEELQSLAGKHGDDLRRTKTEISE 309
Cdd:PHA02562 176 IRELNQQIQTLDMKI----------DHIQQQIKTYnkNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 310 MNRNISRLQAEIEGLKGQRASLEAAIADA-------EQHGEL-----AIKDANAKLSELEA----------ALQRAKQDM 367
Cdd:PHA02562 246 LVMDIEDPSAALNKLNTAAAKIKSKIEQFqkvikmyEKGGVCptctqQISEGPDRITKIKDklkelqhsleKLDTAIDEL 325
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462531885 368 ARQLREYQELMNVKLALDIEIATYRKLLEGEES---RLESGMQNMS 410
Cdd:PHA02562 326 EEIMDEFNEQSKKLLELKNKISTNKQSLITLVDkakKVKAAIEELQ 371
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
140-381 |
1.20e-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: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 140 FESYINNLRRQLETLGQEKLKLEAELGNMQGLVEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTD 219
Cdd:pfam15921 595 LEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSE 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 220 EINFLRQLYEEEIREL--------------QSQISDTSVVL-SMDNSrslDMDSIIAEVKAQYEDIANRSRAEA-ESMYQ 283
Cdd:pfam15921 675 DYEVLKRNFRNKSEEMetttnklkmqlksaQSELEQTRNTLkSMEGS---DGHAMKVAMGMQKQITAKRGQIDAlQSKIQ 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 284 IkYEELQSLAGKHGDDLRRTKT----EISEMNRNISRLQAEIEGLKGQRASLEAAIADAeqhgELAIKDANAKLSELEAA 359
Cdd:pfam15921 752 F-LEEAMTNANKEKHFLKEEKNklsqELSTVATEKNKMAGELEVLRSQERRLKEKVANM----EVALDKASLQFAECQDI 826
|
250 260
....*....|....*....|..
gi 2462531885 360 LQRAKQDMARQlrEYQELMNVK 381
Cdd:pfam15921 827 IQRQEQESVRL--KLQHTLDVK 846
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
112-370 |
1.35e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.31 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 112 LEQQNKMLETKWSLLQQQKTARSNMDNMFESyinnLRRQLETLGQEklkLEAELGNMQGLVEDFKNKYEDEINKRTEMEN 191
Cdd:pfam01576 31 LEKKHQQLCEEKNALQEQLQAETELCAEAEE----MRARLAARKQE---LEEILHELESRLEEEEERSQQLQNEKKKMQQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 192 EFVLIKKDVDEA-------YMNKVELESRLEGLTDEINFL----------RQLYEEEIRELQSQISDTSVVLSMDNSRSL 254
Cdd:pfam01576 104 HIQDLEEQLDEEeaarqklQLEKVTTEAKIKKLEEDILLLedqnsklskeRKLLEERISEFTSNLAEEEEKAKSLSKLKN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 255 DMDSIIAevkaqyeDIANRSRAEAESmyqikYEELQSLAgkhgddlRRTKTEISEMNRNISRLQAEIEGLKGQRA----S 330
Cdd:pfam01576 184 KHEAMIS-------DLEERLKKEEKG-----RQELEKAK-------RKLEGESTDLQEQIAELQAQIAELRAQLAkkeeE 244
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2462531885 331 LEAAIADAEQHGeLAIKDANAKLSELEAALQRAKQDMARQ 370
Cdd:pfam01576 245 LQAALARLEEET-AQKNNALKKIRELEAQISELQEDLESE 283
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
285-401 |
2.83e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.95 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 285 KYEELQSLAGKHG---DDLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQhgelAIKDANAKLSELEAALQ 361
Cdd:PRK09039 51 KDSALDRLNSQIAelaDLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAG----AGAAAEGRAGELAQELD 126
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2462531885 362 RAKQDMARQLREYqELMNVKL-ALDIEIATYRKLLEGEESR 401
Cdd:PRK09039 127 SEKQVSARALAQV-ELLNQQIaALRRQLAALEAALDASEKR 166
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
120-415 |
3.03e-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: 40.49 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 120 ETKWSLLQQQKTARSNMDNMFESYINNLRRQLETLGQEKLKLEAELGNM----QGLVE------DFKNKYEDEINKRT-E 188
Cdd:pfam15921 390 EKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMksecQGQMErqmaaiQGKNESLEKVSSLTaQ 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 189 MENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLR------QLYEEEIRELQSQISDTSVVLSMDNSRSLDMDSIIAE 262
Cdd:pfam15921 470 LESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQekeraiEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTE 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 263 VKAQYEDIANRSRAEAESMYQIkyEELQSLAGKHGDDLRRTKTEISEMNRNISRLQAEIEGLK-------GQRASLEAAI 335
Cdd:pfam15921 550 CEALKLQMAEKDKVIEILRQQI--ENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKilkdkkdAKIRELEARV 627
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 336 ADAEQHgelAIKDANAKlSELEAALQRAKQDMARQLREYQELMNVKLALDIEIATYRKLLEGEESRLESGMQNMSIHTKT 415
Cdd:pfam15921 628 SDLELE---KVKLVNAG-SERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKS 703
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
118-338 |
3.42e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 118 MLETKwSLLQQQKTARSNMDNMFESY--INNLRRQLETL------GQEKLKLEAELGNMQGLVEDFkNKYEDEInKRTEM 189
Cdd:COG4913 217 MLEEP-DTFEAADALVEHFDDLERAHeaLEDAREQIELLepirelAERYAAARERLAELEYLRAAL-RLWFAQR-RLELL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 190 ENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQLYEE----EIRELQSQISDTSVVLSMDNSRSLDMDSIIAEVKA 265
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEALLAALGL 373
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462531885 266 QYEDIA-----NRSRAEAESmyqikyEELQSLAGKHGDDLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADA 338
Cdd:COG4913 374 PLPASAeefaaLRAEAAALL------EALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL 445
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
85-314 |
4.90e-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: 4.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 85 QAVRTQEKEQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTARSNMDNMFESYINNLRRQ-LETLGQEKLKLEA 163
Cdd:TIGR01612 1161 KAISNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKGINLSYGKNLGKLfLEKIDEEKKKSEH 1240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 164 ELGNMQGLVEDFknkyeDEINKRTEMENEFVLIKKDVDeAYMNKVELESRLEgltDEINFLRQLYEEEIrelqSQISDTS 243
Cdd:TIGR01612 1241 MIKAMEAYIEDL-----DEIKEKSPEIENEMGIEMDIK-AEMETFNISHDDD---KDHHIISKKHDENI----SDIREKS 1307
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462531885 244 VVLSMDNSRSLDMDSI-------IAEVKAQYEDIaNRSRAEAESMYQI-KYEELQSLAgkhgDDLRRTKTEISEMNRNI 314
Cdd:TIGR01612 1308 LKIIEDFSEESDINDIkkelqknLLDAQKHNSDI-NLYLNEIANIYNIlKLNKIKKII----DEVKEYTKEIEENNKNI 1381
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
299-402 |
5.36e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 38.37 E-value: 5.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 299 DLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQhgelAIKDANAKLSELEAALQ---------RAKQDMAR 369
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKT----ELEDLEKEIKRLELEIEevearikkyEEQLGNVR 86
|
90 100 110
....*....|....*....|....*....|...
gi 2462531885 370 QLREYQelmnvklALDIEIATYRKLLEGEESRL 402
Cdd:COG1579 87 NNKEYE-------ALQKEIESLKRRISDLEDEI 112
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
255-404 |
7.03e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 7.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 255 DMDSIIAEVKAQYEDIaNRSRAEAESMY-QIK--------YEELQSLAGKHG--DDLRRT------KTEISEMNRNISRL 317
Cdd:COG4913 222 DTFEAADALVEHFDDL-ERAHEALEDAReQIEllepirelAERYAAARERLAelEYLRAAlrlwfaQRRLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 318 QAEIEGLKGQRASLEAAIADAEQHgELAIKDA-----NAKLSELEAALQRAKQDMARQLREYQELMN----VKLALDIEI 388
Cdd:COG4913 301 RAELARLEAELERLEARLDALREE-LDELEAQirgngGDRLEQLEREIERLERELEERERRRARLEAllaaLGLPLPASA 379
|
170
....*....|....*.
gi 2462531885 389 ATYRKLLEGEESRLES 404
Cdd:COG4913 380 EEFAALRAEAAALLEA 395
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
144-345 |
7.06e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.98 E-value: 7.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 144 INNLRRQLETLGQEKLKLEAELGNMQGLVEDFKNKYEDEINKRTEMENefVLIKKDVDEAYMNKVELESRLEGLTDEINF 223
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK--LEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 224 LRQlYEEEIRELQSQIsdtsvvlsmdnsrsldmdsiiAEVKAQYEDIANRSRAEAESMYQIKYEELQSLAgkhgDDLRRT 303
Cdd:COG4717 151 LEE-RLEELRELEEEL---------------------EELEAELAELQEELEELLEQLSLATEEELQDLA----EELEEL 204
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2462531885 304 KTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQHGELA 345
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLK 246
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
92-377 |
7.40e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.89 E-value: 7.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 92 KEQIKTLNNKFASFIDKVRFLEQQNKMLETKwslLQQQKTARSNMDNMFEsyINNLRRQLETLGQEKLKLEAEL-----G 166
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELRELEKV---LKKESELIKLKELAEQ--LKELEEKLKKYNLEELEKKAEEyeklkE 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 167 NMQGLVEDFKNkYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRL--------EGLTDEINFLRQLYEEEIrELQSQ 238
Cdd:PRK03918 533 KLIKLKGEIKS-LKKELEKLEELKKKLAELEKKLDELEEELAELLKELeelgfesvEELEERLKELEPFYNEYL-ELKDA 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 239 ISDTSVVLSMDNSRSLDMDSI---IAEVKAQYEDIANRsraeaesmyqikYEELQSLAGKhgDDLRRTKTEISEMNRNIS 315
Cdd:PRK03918 611 EKELEREEKELKKLEEELDKAfeeLAETEKRLEELRKE------------LEELEKKYSE--EEYEELREEYLELSRELA 676
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462531885 316 RLQAEIEGLKGQRASLEAAIADAEQHGElAIKDANAKLSELEAALQRAkQDMARQLREYQEL 377
Cdd:PRK03918 677 GLRAELEELEKRREEIKKTLEKLKEELE-EREKAKKELEKLEKALERV-EELREKVKKYKAL 736
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
299-403 |
8.24e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 38.76 E-value: 8.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 299 DLRRTKTE--ISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQH----GELAIKDAN---AKLSELEAALQRAKQDMAR 369
Cdd:COG1196 171 KERKEEAErkLEATEENLERLEDILGELERQLEPLERQAEKAERYrelkEELKELEAElllLKLRELEAELEELEAELEE 250
|
90 100 110
....*....|....*....|....*....|....
gi 2462531885 370 QLREYQELMNVKLALDIEIATYRKLLEGEESRLE 403
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEELELELE 284
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
130-404 |
8.85e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 38.90 E-value: 8.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 130 KTARSNMDnMFESYINNLRRQLETLGQEKLKLEaelgnmqglvedfknKYeDEINKRTEmENEFVLIKKDVDEAYMNKVE 209
Cdd:TIGR02169 180 EEVEENIE-RLDLIIDEKRQQLERLRREREKAE---------------RY-QALLKEKR-EYEGYELLKEKEALERQKEA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 210 LESRLEGLtdeinflrqlyEEEIRELQSQISDTSVVLsmdNSRSLDMDSIIAEVKAQYEDIANRSRAEaesmyqikyeel 289
Cdd:TIGR02169 242 IERQLASL-----------EEELEKLTEEISELEKRL---EEIEQLLEELNKKIKDLGEEEQLRVKEK------------ 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531885 290 qslagkhgddLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAI-ADAEQHGEL--AIKDANAKLSELEAALQRAKQD 366
Cdd:TIGR02169 296 ----------IGELEAEIASLERSIAEKERELEDAEERLAKLEAEIdKLLAEIEELerEIEEERKRRDKLTEEYAELKEE 365
|
250 260 270
....*....|....*....|....*....|....*...
gi 2462531885 367 MARQLREYQELMNVKLALDIEIATYRKLLEGEESRLES 404
Cdd:TIGR02169 366 LEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINE 403
|
|
| |
