|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
84-396 |
2.46e-151 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 432.42 E-value: 2.46e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 84 EEREQIKTLNNKFASFIDKVRFLEQQNKMLETKWALLQEQKSAKSSQLPRIFEAQIAGLRQQLETLQLDGGRLEVELRNM 163
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 164 QDVVEDFKNKYEEEINRRTAAENEFVLLKKDVDAAYTNKVELEAKADSLQDEINFLKTLHETELAELQSQISDTSVVLSM 243
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 244 DNSRSLDLDGIIADVKAQYEEMANHSRAEAEAWYQTKFETLQAQAGKHGDDLRNTRNEIAEMNRSIQRLQAEIDTLKNQR 323
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14861854 324 AKLESSIAEAEEQGELAIKDAHAKQGELEAALQKAKQDVARQLREYQELLNTKLALDIEIATYRKLLEGEESR 396
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
5-81 |
3.65e-16 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 75.46 E-value: 3.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 5 FSSRSTAYPGRGAQVRLSSGRASFGSRSLYGLGSSR---PRVAVRSA--------------------------------- 48
Cdd:pfam16208 17 YSSVSSSRRGGGGGGGGGGGGGGFGSRSLYNLGGSKsisISVAGGGSrpgsgfgfgggggggfgggfgggggggfggggg 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 49 -------------------------YGGPVGA--GIREITINQSLLAPLSVDIDPTIQQV 81
Cdd:pfam16208 97 fgggfggggyggggfggggfggrggFGGPPCPpgGIQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
79-407 |
1.96e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.78 E-value: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 79 QQVRQEEREQIKTLNNKFASFIDKVRFLEQQNKMLETKWALLQEQKSAKSSQLPRIfEAQIAGLRQQLETLQLDGGRLEV 158
Cdd:TIGR02168 669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL-SRQISALRKDLARLEAEVEQLEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 159 ELRNMQDVVEDFKNKYEEEINRRTAAENEFVllkkdvdAAYTNKVELEAKADSLQDEINFLktlhETELAELQSQISDTS 238
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELA-------EAEAEIEELEAQIEQLKEELKAL----REALDELRAELTLLN 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 239 VVLsmdnsrsldldgiiadvkAQYEEMANHSRAEAEAWyQTKFETLQAQAGKHGDDLRNTRNEIAEMNRSIQRLQAEIDT 318
Cdd:TIGR02168 817 EEA------------------ANLRERLESLERRIAAT-ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 319 LKNQRAKLESSIAEAEEQGELAIKDAH-----------------AKQGELEAALQKAKQDVARQLR----EYQELLNTKL 377
Cdd:TIGR02168 878 LLNERASLEEALALLRSELEELSEELReleskrselrreleelrEKLAQLELRLEGLEVRIDNLQErlseEYSLTLEEAE 957
|
330 340 350
....*....|....*....|....*....|..
gi 14861854 378 ALDIEIATYRKLLEGEESRLSG--DGMGPVNI 407
Cdd:TIGR02168 958 ALENKIEDDEEEARRRLKRLENkiKELGPVNL 989
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
82-373 |
8.85e-09 |
|
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: 57.60 E-value: 8.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 82 RQEEREQIKTLNNKFASFIDKVRFLEQQNKMLETKWALLQEQKSAKSSQLPRiFEAQIAGLRQQLETLQLDGGRLEVELR 161
Cdd:pfam07888 75 RRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAA-HEARIRELEEDIKTLTQRVLERETELE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 162 NMQDVVEDFKN-KYEEEINRRT------AAENEFVLLKKDVDAAYTNKVELEAKADSLQDEINFLKTL------HETELA 228
Cdd:pfam07888 154 RMKERAKKAGAqRKEEEAERKQlqaklqQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKlttahrKEAENE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 229 ELQSQISDTSVVLSMDNSRSLDLDGIIADVKAQYE---------------------EMANHSRAEAEAWYQTKfETLQAQ 287
Cdd:pfam07888 234 ALLEELRSLQERLNASERKVEGLGEELSSMAAQRDrtqaelhqarlqaaqltlqlaDASLALREGRARWAQER-ETLQQS 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 288 AGKHGDdlrntrnEIAEMNRSIQRLQAEIDTLKNQRAKLESSIAEAEEQGELAIKDAHAKQGELEAALQKAKQDVARQLR 367
Cdd:pfam07888 313 AEADKD-------RIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQA 385
|
....*.
gi 14861854 368 EYQELL 373
Cdd:pfam07888 386 EKQELL 391
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
86-329 |
2.12e-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: 56.61 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 86 REQIKTLNNKFASFIDKVRFLEQQNKMLETKWALLQEQKSAKssqlprifEAQIAGLRQQLETLQLDGGRLEVELRNMQD 165
Cdd:TIGR02169 293 KEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKL--------LAEIEELEREIEEERKRRDKLTEEYAELKE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 166 VVEDFKNKYEEEINRRTAAENEFVLLKKDVDAAYTNKVELEAKADSLQDEinfLKTLHEtELAELQSQISDtsvvlsmdn 245
Cdd:TIGR02169 365 ELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE---LQRLSE-ELADLNAAIAG--------- 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 246 srsldldgIIADVKAQYEEMANhsrAEAEAWYQT-KFETLQAQAGKHGDDLRNTRNEIAEMNRSIQRLQAEIDTLKNQRA 324
Cdd:TIGR02169 432 --------IEAKINELEEEKED---KALEIKKQEwKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAR 500
|
....*
gi 14861854 325 KLESS 329
Cdd:TIGR02169 501 ASEER 505
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
247-397 |
1.64e-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: 53.91 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 247 RSLDLDGIIADVKAQYEEMANHSRAEAEAwyQTKFETLQAQAGKHGDDLRNTRNEIAEMNRSIQRLQAEIDTLKNQRAKL 326
Cdd:TIGR02168 223 RELELALLVLRLEELREELEELQEELKEA--EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14861854 327 ESSIAEAEEQGELAIKDAHAKQGELEAALQK---AKQDVARQLREYQELLNTKLALDIEIATYRKLLEGEESRL 397
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKldeLAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
204-398 |
4.24e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 4.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 204 ELEAKADSLQDEINFLK-TLHETELAELQSQISDTSVVLSMDNSRSLDLDGIIADVKAQYEEMANHSRAEAEAWYQTKFE 282
Cdd:COG1196 217 ELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 283 TLQAQAGK--HGDDLRNTRNEIAEMNRSIQRLQAEIDTLKNQRAKLESSIAEAEEQ---GELAIKDAHAKQGELEAALQK 357
Cdd:COG1196 297 LARLEQDIarLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEleeAEAELAEAEEALLEAEAELAE 376
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 14861854 358 AKQDVARQLREYQELLNTKLALDIEIATYRKLLEGEESRLS 398
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
77-364 |
5.26e-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: 5.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 77 TIQQVRQEEREQIKTLNNKFASFIDKVRFLEQQNKMLETKWALLQEQKSAKSSQLPRIfEAQIAGLRQQLETLQLDGGRL 156
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL-EEELEELEEELEELEEELEEA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 157 EVELRNMQDVVEDFKNKYEEEINRRTAAENEFVLLKKDVDAAYTNKVELEAKADSLQDEINFLktlhETELAELQSQIsd 236
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL----LERLERLEEEL-- 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 237 tsvvlsmdnsRSLDLDGIIADVKAQYEEMANHSRAEAEAWYQTKFETLQAQAGKHGDDLRNTRNEIAEMNRSIQRLQAEI 316
Cdd:COG1196 424 ----------EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 14861854 317 DTLKNQRAKLESSIAEAEEQGELAIKDAHAKQGELEAALQKAKQDVAR 364
Cdd:COG1196 494 LLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE 541
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
71-406 |
5.27e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 52.36 E-value: 5.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 71 SVDIDPTIQQVRQEEREQIKTLNNKFASFIDKVRFLEQQNKMLETKWALLQEQKSAKSS-----QLPRIFEAQIAGLRQQ 145
Cdd:TIGR00606 817 GSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQigtnlQRRQQFEEQLVELSTE 896
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 146 LETLQLDGGRLEVELRNMQDVVEDFKNKYEEEINRRTA----AENEFVLLKKDVDAAYTNKVELEAKadsLQDEINFLKT 221
Cdd:TIGR00606 897 VQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETsnkkAQDKVNDIKEKVKNIHGYMKDIENK---IQDGKDDYLK 973
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 222 LHETELAELQSQISDTSVVLSMDNSrslDLDGIIADVKAQYEEMA----NHSRAEAEAWYQTKFETLQAQAGKHGDDlrn 297
Cdd:TIGR00606 974 QKETELNTVNAQLEECEKHQEKINE---DMRLMRQDIDTQKIQERwlqdNLTLRKRENELKEVEEELKQHLKEMGQM--- 1047
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 298 trnEIAEMNRSIQRLQAEIDTLKNQRAKLESSIAEAEEQGELAIKDAHAKQGeleaalqkakQDVARQLREYQELLNTKL 377
Cdd:TIGR00606 1048 ---QVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQF----------RDAEEKYREMMIVMRTTE 1114
|
330 340
....*....|....*....|....*....
gi 14861854 378 ALDIEIATYRKLLEGEESRLSGDGMGPVN 406
Cdd:TIGR00606 1115 LVNKDLDIYYKTLDQAIMKFHSMKMEEIN 1143
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
121-384 |
7.64e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.56 E-value: 7.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 121 QEQKSAKSSQLPRIFEAQIAGLRQQLETLQLDggrlevelrnmqdvVEDFKnkyeeeinrrtaAENEFVLLKKDVDAAYT 200
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAA--------------LEEFR------------QKNGLVDLSEEAKLLLQ 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 201 NKVELEAKADSLQDEINFLktlhETELAELQSQISDTSVVLSmdnsrSLDLDGIIADVKAQYEEManhsraeaeawyQTK 280
Cdd:COG3206 220 QLSELESQLAEARAELAEA----EARLAALRAQLGSGPDALP-----ELLQSPVIQQLRAQLAEL------------EAE 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 281 FETLQAQAGKHGDDLRNTRNEIAEMNRSIQR--------LQAEIDTLKNQRAKLESSIAEAEEQgelaikdaHAKQGELE 352
Cdd:COG3206 279 LAELSARYTPNHPDVIALRAQIAALRAQLQQeaqrilasLEAELEALQAREASLQAQLAQLEAR--------LAELPELE 350
|
250 260 270
....*....|....*....|....*....|..
gi 14861854 353 AALQKAKQDVARQLREYQELLNTKLALDIEIA 384
Cdd:COG3206 351 AELRRLEREVEVARELYESLLQRLEEARLAEA 382
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
136-406 |
1.78e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 136 EAQIAGLRQQLETLQLDGGRLEVELRNMQDVVEDFKNKYEEEINRRTAAENEFVLLKKDVDAAYTNKVELEAKADSLQDE 215
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 216 INFLKT---------------LH--ETELAELQSQISDTSVVLSMDNSRSLD-----LDGIIADVKA------QYEEMAN 267
Cdd:TIGR02169 753 IENVKSelkelearieeleedLHklEEALNDLEARLSHSRIPEIQAELSKLEeevsrIEARLREIEQklnrltLEKEYLE 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 268 HSRAEAEAwyqtKFETLQAQAGKHGDDLRNTRNEIAEMNRSIQRLQAEIDTLKNQRAKLESSIAEAEEQgelaIKDAHAK 347
Cdd:TIGR02169 833 KEIQELQE----QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQ----LRELERK 904
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14861854 348 QGELEAALQKAKQDVAR----------QLREYQELLNTKLALDIEIATYRKL---LEGEESRLSgdGMGPVN 406
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSElkaklealeeELSEIEDPKGEDEEIPEEELSLEDVqaeLQRVEEEIR--ALEPVN 974
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
224-397 |
2.02e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 224 ETELAELQSQISDtsvvlsmdnsrsldLDGIIADVKAQYEEMAN----HSRAEAEAWYQTKFETLQAQAGKHGD---DLR 296
Cdd:COG4913 616 EAELAELEEELAE--------------AEERLEALEAELDALQErreaLQRLAEYSWDEIDVASAEREIAELEAeleRLD 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 297 NTRNEIAEMNRSIQRLQAEIDTLKNQRAKLESSIAEAEEQgelaIKDAHAKQGELEAALQKAKQDVARQLRE-----YQE 371
Cdd:COG4913 682 ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE----LEQAEEELDELQDRLEAAEDLARLELRAlleerFAA 757
|
170 180 190
....*....|....*....|....*....|..
gi 14861854 372 LLNTKL------ALDIEIATYRKLLEGEESRL 397
Cdd:COG4913 758 ALGDAVerelreNLEERIDALRARLNRAEEEL 789
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
137-368 |
3.30e-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: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 137 AQIAGLRQQLETLQldggrleVELRNMQDVVEDFKNKYEEEINRRTAAENEFVLLKKDVDAAYTNKVELEAKADSLQDEI 216
Cdd:COG4942 20 DAAAEAEAELEQLQ-------QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 217 NFLktlhETELAELQSQISDTSVVLSMdNSRSLDLDGII-------ADVKAQYEEMANHSRAEAEAWYQTKFETLQAQAg 289
Cdd:COG4942 93 AEL----RAELEAQKEELAELLRALYR-LGRQPPLALLLspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALR- 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14861854 290 khgDDLRNTRNEIAEMNRSIQRLQAEIDTLKNQRAKLESSIAEAEEQGELAIKDAHAKQGELEAALQKAKQDVARQLRE 368
Cdd:COG4942 167 ---AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
77-351 |
5.56e-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: 48.86 E-value: 5.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 77 TIQQVRQEEREQIKTLNNKFASFIDKVRFLEQQNKMLETKWALLQEQKSAKSSQLPRIfEAQIAGLRQQLETLQLDGGRL 156
Cdd:TIGR04523 374 KLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERL-KETIIKNNSEIKDLTNQDSVK 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 157 EVELRNMQDVVEDFKNK---YEEEINR-RTAAEN---EFVLLKKDVDAAYTNKVELEAKADSLQDEINFLKTLH---ETE 226
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQlkvLSRSINKiKQNLEQkqkELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIeklESE 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 227 LAELQSQISDTSVVLSMDNSrslDLDgiiadvKAQYEEMANHSRAEAEAWYQTKFETLQAQ------AGKHGDDLRNTRN 300
Cdd:TIGR04523 533 KKEKESKISDLEDELNKDDF---ELK------KENLEKEIDEKNKEIEELKQTQKSLKKKQeekqelIDQKEKEKKDLIK 603
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 14861854 301 EIAEMNRSIQRLQAEIDTLKNQRAKLESSIAEAEEQGELAIKDAHAKQGEL 351
Cdd:TIGR04523 604 EIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETI 654
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
87-398 |
1.14e-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: 47.71 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 87 EQIKTLNNKFASFIDKVRFLEQQNKMLETKWALLQEQKSAKSSQLpRIFEAQIAGLRQQLETLQLDGGRLEVELRNMQDV 166
Cdd:TIGR04523 131 KQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENEL-NLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKK 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 167 VEDFKnKYEEEINRrtaAENEFVLLKKDVDAAYTNKVELEAKADSLQDEINFLKTLHETELAELQSQISDtsvvLSMDNS 246
Cdd:TIGR04523 210 IQKNK-SLESQISE---LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE----LEQNNK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 247 RSLDLDGIIADVKAQYEEMANHSRAEaeaWYQTKFETLQAQAgkhgDDLRNTRNEIAEMNRSIQRLQAEIDTLKNQRAKL 326
Cdd:TIGR04523 282 KIKELEKQLNQLKSEISDLNNQKEQD---WNKELKSELKNQE----KKLEEIQNQISQNNKIISQLNEQISQLKKELTNS 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 327 ESS-------IAEAEEQGELAIKDAHAKQGELEaALQKAKQDVARQLREYQELLNTKlalDIEIATYRK---LLEGEESR 396
Cdd:TIGR04523 355 ESEnsekqreLEEKQNEIEKLKKENQSYKQEIK-NLESQINDLESKIQNQEKLNQQK---DEQIKKLQQekeLLEKEIER 430
|
..
gi 14861854 397 LS 398
Cdd:TIGR04523 431 LK 432
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
224-368 |
1.32e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 46.88 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 224 ETELAELQSQISDTSVVLSMDNSRSLDLDGIIADVKAQYEEmANHSRAEAEAWY---QTKFETLQAQAGKHGDDLRNTRN 300
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSA-AEAERSRLQALLaelAGAGAAAEGRAGELAQELDSEKQ 130
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14861854 301 EIAEMNRSIQRLQAEIDTLKNQRAKLESSIAEAEEQGELAIKDAHAKQGELEAALQKAKQDVAR-------QLRE 368
Cdd:PRK09039 131 VSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNVALAQRVQELNRyrseffgRLRE 205
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
204-388 |
1.85e-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: 45.69 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 204 ELEAKADSLQDEINFLktlhETELAELQSQISDtsvvlsmdnsrsldLDGIIADVKAQYeemanhSRAEAEAwyqtkfET 283
Cdd:COG1579 21 RLEHRLKELPAELAEL----EDELAALEARLEA--------------AKTELEDLEKEI------KRLELEI------EE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 284 LQAQAGKHGDDLRNTRNeiaemNRSIQRLQAEIDTLKNQRAKLESSIAEAEEQgelaIKDAHAKQGELEAALQKAKQDVA 363
Cdd:COG1579 71 VEARIKKYEEQLGNVRN-----NKEYEALQKEIESLKRRISDLEDEILELMER----IEELEEELAELEAELAELEAELE 141
|
170 180
....*....|....*....|....*
gi 14861854 364 RQLREYQELLNtklALDIEIATYRK 388
Cdd:COG1579 142 EKKAELDEELA---ELEAELEELEA 163
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
294-370 |
2.14e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 294 DLRNTRNEIAEMNRSIQRLQAEIDTLKNQRAKLESSIAEAEE-----QGELA-----IKDAHAKQGELEAALQKAKQDVA 363
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARriralEQELAaleaeLAELEKEIAELRAELEAQKEELA 107
|
....*..
gi 14861854 364 RQLREYQ 370
Cdd:COG4942 108 ELLRALY 114
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
193-397 |
2.38e-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: 46.97 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 193 KDVDAAYTNKVELEAKADSLQDEINFLKTLHE---TELAELQSQISDTSVVLSMDNSRSLDLDG-------IIADVKAQy 262
Cdd:TIGR02168 225 LELALLVLRLEELREELEELQEELKEAEEELEeltAELQELEEKLEELRLEVSELEEEIEELQKelyalanEISRLEQQ- 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 263 EEMANHSRAEAE---AWYQTKFETLQAQAGKHGDDLRNTRNEIAEMNRSIQRLQAEIDTLKNQRAKLESSIAEAEEQGE- 338
Cdd:TIGR02168 304 KQILRERLANLErqlEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLEt 383
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14861854 339 ---------LAIKDAHAKQGELEAALQKAKQDVARQLREYQELL-----NTKLALDIEIATYRKLLEGEESRL 397
Cdd:TIGR02168 384 lrskvaqleLQIASLNNEIERLEARLERLEDRRERLQQEIEELLkkleeAELKELQAELEELEEELEELQEEL 456
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
77-376 |
2.51e-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: 46.94 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 77 TIQQVRQEEREQIKTLNNKFASFIDKVRFLEQQNKMLETKwalLQEQKsaKSSQLprifeaqiagLRQQLETLQLDGGRL 156
Cdd:TIGR04523 360 EKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESK---IQNQE--KLNQQ----------KDEQIKKLQQEKELL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 157 EVELRNMQDVVEDFKNKYEEEINRRTAAENEFVLLKKDVDaaytnkvELEAKADSLQDEINFLKtlheTELAELQSQISD 236
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRE-------SLETQLKVLSRSINKIK----QNLEQKQKELKS 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 237 TSVVLSMDNSRSLDLDGIIADVKAQYEEMANhsraeaeawyqtKFETLQAQAGKHGDDLRNTRNEIAEMN---------R 307
Cdd:TIGR04523 494 KEKELKKLNEEKKELEEKVKDLTKKISSLKE------------KIEKLESEKKEKESKISDLEDELNKDDfelkkenleK 561
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14861854 308 SIQRLQAEIDTLKNQRAKLESSIAEAEE---QGELAIKDAHAKQGELEAALQKAKQDVARQLREYQELLNTK 376
Cdd:TIGR04523 562 EIDEKNKEIEELKQTQKSLKKKQEEKQElidQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSII 633
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
58-332 |
2.57e-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: 46.97 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 58 REITINQSLLAPLSVDIDPTIQQVRQEEREqIKTLNNKFASFIDKVRFLEQQNKMLETKWALLQEQKSAKSSQLpRIFEA 137
Cdd:TIGR02168 726 RQISALRKDLARLEAEVEQLEERIAQLSKE-LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL-KALRE 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 138 QIAGLRQQLETLQLDGGRLEVELRNMQDVVEDFKNKYEEEINRRTAAENEFVLLKKDVDAAYTNKVELEAKADSLQDEIN 217
Cdd:TIGR02168 804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERA 883
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 218 FLKT---LHETELAELQSQISDTSVVLSMDNSRSLDLDGIIADVKAQYEEM---ANHSRAEAEAWYQTKFETLQAQAGKH 291
Cdd:TIGR02168 884 SLEEalaLLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLevrIDNLQERLSEEYSLTLEEAEALENKI 963
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14861854 292 GDDLRNTRNEIAEMNRSIQR---------------------LQAEIDTLKNQRAKLESSIAE 332
Cdd:TIGR02168 964 EDDEEEARRRLKRLENKIKElgpvnlaaieeyeelkerydfLTAQKEDLTEAKETLEEAIEE 1025
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
62-336 |
3.08e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 62 INQSLLAPLSVDIDPTIQQVRQEEREqiktLNNKFASFIDKVRFLEQQNKMLETKWALLQEQKSAKSSQLPRIFEAQIAG 141
Cdd:PRK04863 823 IGSHLAVAFEADPEAELRQLNRRRVE----LERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETLADRVEE 898
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 142 LRQQLETLQLD-------GGRLE-VE-----LRNMQDVVEDFKNKYEEEINRRTAAENEFVLLKkDVDA-----AYTNKV 203
Cdd:PRK04863 899 IREQLDEAEEAkrfvqqhGNALAqLEpivsvLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALT-EVVQrrahfSYEDAA 977
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 204 ELEAKADSLQDEinfLKTLHE----------TELAELQSQISDTSVVL-SMDNSRSLDLDgIIADVKAQYEEMANHSRAE 272
Cdd:PRK04863 978 EMLAKNSDLNEK---LRQRLEqaeqertrarEQLRQAQAQLAQYNQVLaSLKSSYDAKRQ-MLQELKQELQDLGVPADSG 1053
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14861854 273 AEAWYQTKFETLQAQagkhgddLRNTRNEIAEMNRSIQRLQAEIDTLKNQRAKLESSIAEAEEQ 336
Cdd:PRK04863 1054 AEERARARRDELHAR-------LSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQ 1110
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
77-402 |
4.13e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 77 TIQQVRQEEREQIKTLNNKFASFIDKVRFLEQ--QNKMLETKWALLQEQKSAKSSQLPRIFE--AQIAGLRQQLETLQLD 152
Cdd:COG4717 92 ELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEErlEELRELEEELEELEAE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 153 GGRLEVELRN-MQDVVEDFKNKYEEEINRRTAAENEFVLLKKDVDAAYTNKVELEAKADSLQDEINFLKTLHETELAELQ 231
Cdd:COG4717 172 LAELQEELEElLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 232 SQISDTSVVLSMDNSRSLDLDGIIADVKA------------QYEEMANHSRAEAEAWYQTKFETLQAQ-----AGKHGDD 294
Cdd:COG4717 252 LLIAAALLALLGLGGSLLSLILTIAGVLFlvlgllallfllLAREKASLGKEAEELQALPALEELEEEeleelLAALGLP 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 295 LRNTRNEIAEMNRSIQRLQaeidTLKNQRAKLESSIAEAEEQGELAIKDAHAKQGELEAALQKAKQdvarqLREYQELLN 374
Cdd:COG4717 332 PDLSPEELLELLDRIEELQ----ELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQ-----AEEYQELKE 402
|
330 340
....*....|....*....|....*...
gi 14861854 375 TKLALDIEIATYRKLLEGEESRLSGDGM 402
Cdd:COG4717 403 ELEELEEQLEELLGELEELLEALDEEEL 430
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
119-358 |
6.29e-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: 45.55 E-value: 6.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 119 LLQE---QKSAKSSQLpRIFEAQIAGLRQQLETLQLDGGRLEVELRNMQDVVEDFKNKYEEEINRRTAAENEFVLLKKDV 195
Cdd:pfam01576 476 LLQEetrQKLNLSTRL-RQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQREL 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 196 DAAYTNKVELEAKADSLQDEINFLKTLHETELAELQSQISdtsvVLSMDNSRSLDLDGIIADVK---AQYEEmaNHSRAE 272
Cdd:pfam01576 555 EALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQ----LVSNLEKKQKKFDQMLAEEKaisARYAE--ERDRAE 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 273 AEAW-YQTKFETLqaqaGKHGDDLRNTRNEIAEMNRSiqrLQAEIDTLKNQRAKLESSIAEAEEQG---ELAIKDAHAKQ 348
Cdd:pfam01576 629 AEAReKETRALSL----ARALEEALEAKEELERTNKQ---LRAEMEDLVSSKDDVGKNVHELERSKralEQQVEEMKTQL 701
|
250
....*....|
gi 14861854 349 GELEAALQKA 358
Cdd:pfam01576 702 EELEDELQAT 711
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
205-410 |
7.05e-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: 7.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 205 LEAKADSLQDEINFLktlhETELAELQSQISDTSVVLS--MDNSRSLDLDG-------IIADVKAQYEEmANHSRAEAEA 275
Cdd:COG3206 166 LELRREEARKALEFL----EEQLPELRKELEEAEAALEefRQKNGLVDLSEeaklllqQLSELESQLAE-ARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 276 WYQTkfetLQAQAGKHGDD---------LRNTRNEIAEMNRSIQRLQA-------EIDTLKNQRAKLESSIAEAEEQG-- 337
Cdd:COG3206 241 RLAA----LRAQLGSGPDAlpellqspvIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQEAQRIla 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14861854 338 --ELAIKDAHAKQGELEAALQKAKQDVARQLREYQELLNTKLALDIEIATYRKLLEG-EESRLSGdGMGPVNISVV 410
Cdd:COG3206 317 slEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRlEEARLAE-ALTVGNVRVI 391
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
284-396 |
7.77e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.57 E-value: 7.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 284 LQAQAGKHGDDLRNTRNEIAEMNRSIQRLQAEIDTLKNQRAKLESSIAEAEEQGElaikDAHAKQGELEAALQKAKQDVA 363
Cdd:PRK09039 58 LNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGA----AAEGRAGELAQELDSEKQVSA 133
|
90 100 110
....*....|....*....|....*....|....
gi 14861854 364 RQLREYqELLNTKL-ALDIEIATYRKLLEGEESR 396
Cdd:PRK09039 134 RALAQV-ELLNQQIaALRRQLAALEAALDASEKR 166
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
78-385 |
9.83e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 9.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 78 IQQVRQEEREQIKTLNNKFASF---IDKVRFLEQQNKMLETKWALLQEQKSAKSSQLPRIFEAQIAGLRQQLETLQLDGG 154
Cdd:COG4717 137 LEAELAELPERLEELEERLEELrelEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 155 RLEVELRNMQDVVEDFKNKYEEEINRRTAAENEFVL--------LKKDVDAAYTNKVEL--------------------- 205
Cdd:COG4717 217 EAQEELEELEEELEQLENELEAAALEERLKEARLLLliaaallaLLGLGGSLLSLILTIagvlflvlgllallflllare 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 206 EAKADSLQDEINFLKTLHETELAELQSQISDTSVVLSMDNSRSLDLDGIIADVKAQYEEMANHSRAEAEAWYQTKFETLQ 285
Cdd:COG4717 297 KASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALL 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 286 AQAGKHGDDlrnTRNEIAEMNRSIQRLQAEIDTLKNQRAKLESSIAEAEEQGELAikdahakqgELEAALQKAKQDVARQ 365
Cdd:COG4717 377 AEAGVEDEE---ELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE---------ELEEELEELEEELEEL 444
|
330 340
....*....|....*....|
gi 14861854 366 LREYQELLNTKLALDIEIAT 385
Cdd:COG4717 445 EEELEELREELAELEAELEQ 464
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
202-394 |
1.51e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 44.35 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 202 KVELEAKADSLQDEINFLKTLHETELAELQSQISDTSVVLSMDNSRSLDLDGIIADVKAQYEEMANHSRAEAE-AWYQTK 280
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAElNRLKKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 281 FETLQAQAGKHGDDL--------RNTRNEIAEMNRSIQRLQAEIDT-------LKNQRAKLESSIAEAEE--------QG 337
Cdd:pfam05557 84 YLEALNKKLNEKESQladareviSCLKNELSELRRQIQRAELELQStnseleeLQERLDLLKAKASEAEQlrqnlekqQS 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14861854 338 ELAIKDAHAKQGELEAALQ--------KAKQDVAR---------QLREYQELLNT----KLALDIEIATYRKLLEGEE 394
Cdd:pfam05557 164 SLAEAEQRIKELEFEIQSQeqdseivkNSKSELARipelekeleRLREHNKHLNEnienKLLLKEEVEDLKRKLEREE 241
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
119-380 |
1.80e-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: 43.95 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 119 LLQEQKSAKSSQLPRIFEAQiaglrQQLETLQLDG-GRLEVELRNMQDVVEDFKNKYEEEINRRT-----------AAEN 186
Cdd:pfam15921 225 ILRELDTEISYLKGRIFPVE-----DQLEALKSESqNKIELLLQQHQDRIEQLISEHEVEITGLTekassarsqanSIQS 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 187 EFVLLK---KDVDAAYTNKV-ELEAKADSLQDEINFLKTLHETELAELQSQISDTSVVLS---------MDNSRSLD--L 251
Cdd:pfam15921 300 QLEIIQeqaRNQNSMYMRQLsDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTearterdqfSQESGNLDdqL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 252 DGIIADVKAQYEEMANHSRAEAEAWYQTKFETLQaqagkhgddLRNTRNEIAEMNRSIQRLQAEIDTLKNQ-RAKLESSI 330
Cdd:pfam15921 380 QKLLADLHKREKELSLEKEQNKRLWDRDTGNSIT---------IDHLRRELDDRNMEVQRLEALLKAMKSEcQGQMERQM 450
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 14861854 331 AEAEEQGElaikdAHAKQGELEAALQKAKQdVARQLREyqELLNTKLALD 380
Cdd:pfam15921 451 AAIQGKNE-----SLEKVSSLTAQLESTKE-MLRKVVE--ELTAKKMTLE 492
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
87-391 |
3.00e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 87 EQIKTLNNKFASFIDKVRFLEQQNKMLETKWALLQEQKSakssQLPRIFEaQIAGLRQQLETLQLDGGRLEVELRNMQDV 166
Cdd:PRK03918 193 ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK----ELEELKE-EIEELEKELESLEGSKRKLEEKIRELEER 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 167 VEDFKNKYEE-EINRRTAAEnefvlLKKDVDaAYTNKVELEAKADSLQDEINFLKTLHETELAELQSQISDtsvvLSMDN 245
Cdd:PRK03918 268 IEELKKEIEElEEKVKELKE-----LKEKAE-EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE----LEEKE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 246 SRSLDLDGIIADVKAQYEEMANHSRAEAEAwYQTKFETLQAQAGKHGDDLRNTRNEIAEMNRSIQRLQAEIDTLKNQRAK 325
Cdd:PRK03918 338 ERLEELKKKLKELEKRLEELEERHELYEEA-KAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 326 LESSIAE-----------------------AEEQGELaIKDAHAKQGELEAALQKAKqDVARQLREYQELLNTKLALDIE 382
Cdd:PRK03918 417 LKKEIKElkkaieelkkakgkcpvcgreltEEHRKEL-LEEYTAELKRIEKELKEIE-EKERKLRKELRELEKVLKKESE 494
|
....*....
gi 14861854 383 IATYRKLLE 391
Cdd:PRK03918 495 LIKLKELAE 503
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
135-392 |
3.26e-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: 43.13 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 135 FEAQIAGLRQQLETLQLDGGRLEV---ELRNMQDVVEDFKNKYEE-EINRRTAAENEFVLLKKDVDAAYTNKVELEAKAD 210
Cdd:TIGR02169 168 FDRKKEKALEELEEVEENIERLDLiidEKRQQLERLRREREKAERyQALLKEKREYEGYELLKEKEALERQKEAIERQLA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 211 SLqdeinflktlhETELAELQSQISDTsvvlsmdNSRSLDLDGIIADVKAQYEEMANhsraEAEAWYQTKFETLQAQAGK 290
Cdd:TIGR02169 248 SL-----------EEELEKLTEEISEL-------EKRLEEIEQLLEELNKKIKDLGE----EEQLRVKEKIGELEAEIAS 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 291 HGDDLRNTRNEIAEMNRSIQRLQAEIDTLKNQRAKLESSIaeAEEQGELAikdahakqgELEAALQKAKQDVARQLREYQ 370
Cdd:TIGR02169 306 LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREI--EEERKRRD---------KLTEEYAELKEELEDLRAELE 374
|
250 260
....*....|....*....|..
gi 14861854 371 ELLNTKLALDIEIATYRKLLEG 392
Cdd:TIGR02169 375 EVDKEFAETRDELKDYREKLEK 396
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
184-445 |
4.02e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 184 AENEFVLLKKDVDAAYTNKVELEAKADSLQDEINFLKTLH---ETELAELQSQISDTSVvlsmdnsrslDLDGIIADVKA 260
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYnelQAELEALQAEIDKLQA----------EIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 261 QYEEMANHSRAEAEAWYQTKFETLQAQAGKHGDDLRN--TRNEIAEMNRS-IQRLQAEIDTLKNQRAKLESSIAEAEEQg 337
Cdd:COG3883 84 RREELGERARALYRSGGSVSYLDVLLGSESFSDFLDRlsALSKIADADADlLEELKADKAELEAKKAELEAKLAELEAL- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 338 elaIKDAHAKQGELEAALQKAKQDVARQLREYQELLNTKLALDIEIATYRKLLEGEESRLSGDGMGPVNISVVNSTGGNG 417
Cdd:COG3883 163 ---KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
250 260
....*....|....*....|....*...
gi 14861854 418 GKLIFGGTMGSNALSFSGGPGALRAYSI 445
Cdd:COG3883 240 AAAAASAAGAGAAGAAGAAAGSAGAAGA 267
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
83-393 |
4.72e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.80 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 83 QEEREQIKTLNNKFASFIDKVRFLEQQNKMLETKWALLQEQKSAKSSQLPRIFEAQ--IAGLRQQLETL-QLDG------ 153
Cdd:pfam15921 506 QEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDkvIEILRQQIENMtQLVGqhgrta 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 154 GRLEVElrnmqdvvedfKNKYEEEINRRTAAENEFVLLKKDVDAAYTnkvELEAKADSLQdeinflktLHETELAELQSQ 233
Cdd:pfam15921 586 GAMQVE-----------KAQLEKEINDRRLELQEFKILKDKKDAKIR---ELEARVSDLE--------LEKVKLVNAGSE 643
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 234 isDTSVVLSMDNSRsldlDGIIADVKAQYEEMANHSRaeaeawyqtKFETLQaqagkhgddlRNTRNEIAEMNRSIQRL- 312
Cdd:pfam15921 644 --RLRAVKDIKQER----DQLLNEVKTSRNELNSLSE---------DYEVLK----------RNFRNKSEEMETTTNKLk 698
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 313 ------QAEIDTLKNQRAKLESSIAEAEEQGELAIKDAHAKQGELEAA------LQKAKQDVARQ---LREYQELLNTKL 377
Cdd:pfam15921 699 mqlksaQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALqskiqfLEEAMTNANKEkhfLKEEKNKLSQEL 778
|
330
....*....|....*.
gi 14861854 378 AldiEIATYRKLLEGE 393
Cdd:pfam15921 779 S---TVATEKNKMAGE 791
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
136-444 |
4.92e-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: 4.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 136 EAQIAGLRQQLETLQLDGGRLEVELRNMQDVVEDFKNKYEEEINRRTAAENEFVLLKKDVDaaytnkvELEAKADSLQDE 215
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA-------EAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 216 InflktlhETELAELQSQISDTSVVLSMDNSRSLD-----LDGIIADVKAQYEEMANHSRAEAEAwyqtkfETLQAQAGK 290
Cdd:COG3883 88 L-------GERARALYRSGGSVSYLDVLLGSESFSdfldrLSALSKIADADADLLEELKADKAEL------EAKKAELEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 291 HGDDLRNTRNEIAEMNRSIQRLQAE----IDTLKNQRAKLESSIAEAEEQGELAIKDAHAKQGELEAALQKAKQDVARQL 366
Cdd:COG3883 155 KLAELEALKAELEAAKAELEAQQAEqealLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAA 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14861854 367 REYQELLNTKLALDIEIATYRKLLEGEESRLSGDGMGPVNISVVNSTGGNGGKLIFGGTMGSNALSFSGGPGALRAYS 444
Cdd:COG3883 235 AAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGG 312
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
198-397 |
5.55e-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: 5.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 198 AYTNKVELEAKADSLQDEINFLKTLHET---ELAELQSQISDTSVVLSmdnsrslDLDGIIADVKAQYEEMANHSRAEAE 274
Cdd:TIGR02169 665 GILFSRSEPAELQRLRERLEGLKRELSSlqsELRRIENRLDELSQELS-------DASRKIGEIEKEIEQLEQEEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 275 awyqtKFETLQAQAGKHGDDLRNTRNEIAEMNRSIQRLQAEIDTLKNQRAKLESSIAEA---EEQGEL-AIKDAHAKQ-- 348
Cdd:TIGR02169 738 -----RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSripEIQAELsKLEEEVSRIea 812
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 14861854 349 --GELEAALQKAKQDVARQLREYQELLNTKLALDIEIATYRKLLEGEESRL 397
Cdd:TIGR02169 813 rlREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKK 863
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
193-388 |
5.65e-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: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 193 KDVDAAYTNKVELEAKADSLQDeinfLKTLHEtELAELQSQISDTSVVLSM-----DNSRSLDLDGIIADVKAQY----E 263
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEP----IRELAE-RYAAARERLAELEYLRAAlrlwfAQRRLELLEAELEELRAELarleA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 264 EMANHSRAEAEAwyQTKFETLQAQAGKH-GDDLRNTRNEIAEMNRSIQRLQAEIDTLKNQRAKLESSIAEAEEQGELAIK 342
Cdd:COG4913 310 ELERLEARLDAL--REELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRA 387
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 14861854 343 DAHAKQGELEAALQKAKQDVARQLREYQELLNTKLALDIEIATYRK 388
Cdd:COG4913 388 EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
72-400 |
9.61e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 41.76 E-value: 9.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 72 VDIDPtIQQVRQEEREQIKTLNNKFASFIDKvrfLEQQnkMLETKWALLQEQKSAKSSQLPR--------IFEAQIA-GL 142
Cdd:PLN03229 411 VPVDP-ERKVNMKKREAVKTPVRELEGEVEK---LKEQ--ILKAKESSSKPSELALNEMIEKlkkeidleYTEAVIAmGL 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 143 RQQLETLQLDGGRLEVELRNMQDVVEDFKNKYEEEINRRTAAENEFVLLK------KDVDAAYTNkVELEAKADSLQDEI 216
Cdd:PLN03229 485 QERLENLREEFSKANSQDQLMHPVLMEKIEKLKDEFNKRLSRAPNYLSLKykldmlNEFSRAKAL-SEKKSKAEKLKAEI 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 217 N--FLKTLHETELAELQSQISDTSVVLSMDNSRSLDLDGIIADVKAQYE---EMAN---HSRAEAEAWYQTKFETLQAQA 288
Cdd:PLN03229 564 NkkFKEVMDRPEIKEKMEALKAEVASSGASSGDELDDDLKEKVEKMKKEielELAGvlkSMGLEVIGVTKKNKDTAEQTP 643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 289 gkhGDDLRNTRNEI-AEMNRSIQRLQAEIDtLKNQRAKLESSIAEAEEQGELAIKDahakqgELEAALQKAKQDVARQLr 367
Cdd:PLN03229 644 ---PPNLQEKIESLnEEINKKIERVIRSSD-LKSKIELLKLEVAKASKTPDVTEKE------KIEALEQQIKQKIAEAL- 712
|
330 340 350
....*....|....*....|....*....|...
gi 14861854 368 EYQELLNTKLALDIEIATYRKLLEGEESRLSGD 400
Cdd:PLN03229 713 NSSELKEKFEELEAELAAARETAAESNGSLKND 745
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
78-335 |
1.14e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 78 IQQVRqEEREQIKTLNNKFASFIDKVRFLEQQNKMLETKWALLQEQKSAKSSQL---------PRIFEAQIAGLRQQLET 148
Cdd:COG1340 49 NAQVK-ELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELaelnkaggsIDKLRKEIERLEWRQQT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 149 LQLDggrLEVElrnmQDVVEDFKnKYEEEINRRTAAENEFVLLKkdvdaaytnkvELEAKADSLQDEINflkTLHE--TE 226
Cdd:COG1340 128 EVLS---PEEE----KELVEKIK-ELEKELEKAKKALEKNEKLK-----------ELRAELKELRKEAE---EIHKkiKE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 227 LAELQSQISDtsvvlsmdnsrsldldgIIADVKAQYEEManhsRAEAEAwYQTKFETLQAQAGKHGDDLRNTRNEIAEMN 306
Cdd:COG1340 186 LAEEAQELHE-----------------EMIELYKEADEL----RKEADE-LHKEIVEAQEKADELHEEIIELQKELRELR 243
|
250 260
....*....|....*....|....*....
gi 14861854 307 RSIQRLQAEIDTLKNQRAKlESSIAEAEE 335
Cdd:COG1340 244 KELKKLRKKQRALKREKEK-EELEEKAEE 271
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
79-368 |
1.54e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.96 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 79 QQVRQEEREQIKTLNNKFASFIDKVRFLEQQNKMLETKWALLQEQKSAKSSQLpRIFEAQIAGLRQQLETLQLDG----- 153
Cdd:pfam10174 358 ESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQL-RDKDKQLAGLKERVKSLQTDSsntdt 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 154 --GRLEVELRNMQDVVEDFKNKYEEEINRRTaaeNEFVLLKKDvdaaytNKvELEAKADSLQDEinflKTLHETELAELQ 231
Cdd:pfam10174 437 alTTLEEALSEKERIIERLKEQREREDRERL---EELESLKKE------NK-DLKEKVSALQPE----LTEKESSLIDLK 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 232 SQISdtsvvlsmdnsrSLDLDGIIADVKAQYEEMANHSRAEAEAWYQTKFETLQAQA------GKHGDDLRNTRNEIAEM 305
Cdd:pfam10174 503 EHAS------------SLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEeavrtnPEINDRIRLLEQEVARY 570
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 306 NRSIQRLQAEIDTL-------KNQRAKLESSIAEAEEQGELAIKDAHAKQGELEAALQKAKQDVARQLRE 368
Cdd:pfam10174 571 KEESGKAQAEVERLlgilrevENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEE 640
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
120-336 |
1.69e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.98 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 120 LQEQKSAKSSQLPRIFEAQIAGL---RQQLETLQLDGGRLEVELRNMQDVVEDFKNKYEEEIN-RRTAAENEFVLLKKDV 195
Cdd:pfam12128 619 KQAAAEEQLVQANGELEKASREEtfaRTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANeRLNSLEAQLKQLDKKH 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 196 DA-----------------AYTNKVE--LEAKADSLQDEINFLKTLHETELAELQSQISDTSVVLSMDNSRSLDLDGIIA 256
Cdd:pfam12128 699 QAwleeqkeqkreartekqAYWQVVEgaLDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIR 778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 257 DVKAQYEEMANHsRAEAEAWYQTKFETLQAQAGKHGDDLRNTRNEIAEMNRSIQRLQAEIdtlKNQRAKLESSIAEAEEQ 336
Cdd:pfam12128 779 TLERKIERIAVR-RQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADT---KLRRAKLEMERKASEKQ 854
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
65-336 |
2.02e-03 |
|
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: 40.13 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 65 SLLAPLSVDIDPTIQQVRQEEREQIKTLNNKFASFIDKVRFLEQQNKMLEtkwallqeQKSAKSSQLPRIFEAQIAGLRQ 144
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALE--------RRIAALARRIRALEQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 145 QLETLQLDGGRLEVELRNMQDVVEDFKNKYEEEINRRTAAeneFVLLKKDVDAAYTNKVELEAKADSLQDEINFLKTLHE 224
Cdd:COG4942 84 ELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLA---LLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 225 tELAELQSQIsdtsvvlsmdNSRSLDLDGIIADVKAQYEEmanhsraeaeawyqtkfetLQAQAGKHGDDLRNTRNEIAE 304
Cdd:COG4942 161 -ELAALRAEL----------EAERAELEALLAELEEERAA-------------------LEALKAERQKLLARLEKELAE 210
|
250 260 270
....*....|....*....|....*....|..
gi 14861854 305 MNRSIQRLQAEIDTLKNQRAKLESSIAEAEEQ 336
Cdd:COG4942 211 LAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
279-398 |
2.44e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 279 TKFETLQAQAGKHGDDLRNTRNEIAEMNRSIQRLQAEIDTLKNQRAKLESSIAEAEEQgelaIKDAHAKQG------ELE 352
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR----IKKYEEQLGnvrnnkEYE 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 14861854 353 aALQKAKQDVARQLREYQELLntkLALDIEIATYRKLLEGEESRLS 398
Cdd:COG1579 93 -ALQKEIESLKRRISDLEDEI---LELMERIEELEEELAELEAELA 134
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
155-400 |
2.52e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 155 RLEVE--LRNMQDVVEDFKNKYEE-EINRRTAAENEFVLLKKDVDAAYTNKVELEAKADSLQDEINFLKTLHE---TELA 228
Cdd:PRK02224 175 RLGVErvLSDQRGSLDQLKAQIEEkEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEerrEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 229 ELQSQISDTSVVLSMDNSRSLDLDGIIADVKAQYEEMANH----------SRAEAEAWYQTKfETLQAQAGKHGDDLRNT 298
Cdd:PRK02224 255 TLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEErddllaeaglDDADAEAVEARR-EELEDRDEELRDRLEEC 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 299 RNEIAEMNRSIQRLQAEIDTL-------KNQRAKLESSIAEAEEqgelAIKDAHAKQGELEAALQKAKQDVArqlreyqe 371
Cdd:PRK02224 334 RVAAQAHNEEAESLREDADDLeeraeelREEAAELESELEEARE----AVEDRREEIEELEEEIEELRERFG-------- 401
|
250 260
....*....|....*....|....*....
gi 14861854 372 llNTKLALDiEIATYRKLLEGEESRLSGD 400
Cdd:PRK02224 402 --DAPVDLG-NAEDFLEELREERDELRER 427
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
221-396 |
2.71e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.00 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 221 TLHETELAELQSQISDTSVvlsmdnsrslDLDGIIADVKAQ--YEEMANHSRAEAEAWYQTKFETLQAQAGKHGDDLRNT 298
Cdd:PHA02562 170 KLNKDKIRELNQQIQTLDM----------KIDHIQQQIKTYnkNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEEL 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 299 RNEIAEMNRSIQRLQAEIDTLKNQRAKLESSIA-------------------EAEEQGELAIKDAHAK----QGELEaAL 355
Cdd:PHA02562 240 TDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEqfqkvikmyekggvcptctQQISEGPDRITKIKDKlkelQHSLE-KL 318
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 14861854 356 QKAKQDVARQLREYQELLNTKLALDIEIATYRKLLEGEESR 396
Cdd:PHA02562 319 DTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDK 359
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
104-220 |
4.10e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 39.10 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 104 RFLEQQNKM----LETKWALLQEQKSAKSSQLPR-IFEAQIAGLRQQLETLQLdggRLEVELRNMQDVVEDFKNKYEEEI 178
Cdd:cd16269 174 EFLQSKEAEaeaiLQADQALTEKEKEIEAERAKAeAAEQERKLLEEQQRELEQ---KLEDQERSYEEHLRQLKEKMEEER 250
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 14861854 179 nRRTAAENEFVLLKKDVDAAYTNKVELEAKADSLQDEINFLK 220
Cdd:cd16269 251 -ENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
136-323 |
4.34e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 136 EAQIAGLRQQLETLQLDGGRLEVELrnMQDVVEDFKNKYEEEINRRTAAENEFVLLKKDVDAAYtnkvelEAKADSLQDE 215
Cdd:COG4913 268 RERLAELEYLRAALRLWFAQRRLEL--LEAELEELRAELARLEAELERLEARLDALREELDELE------AQIRGNGGDR 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 216 INFLktlhETELAELQSQISDTSVVLSMDNSRSLDLDGIIADVKAQYEEMANHSRAEAEAWyQTKFETLQAQAGKHGDDL 295
Cdd:COG4913 340 LEQL----EREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL-EEELEALEEALAEAEAAL 414
|
170 180
....*....|....*....|....*...
gi 14861854 296 RNTRNEIAEmnrsiqrLQAEIDTLKNQR 323
Cdd:COG4913 415 RDLRRELRE-------LEAEIASLERRK 435
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
296-365 |
5.22e-03 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 37.30 E-value: 5.22e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14861854 296 RNTRNE-IAEMNRSIQRLQAEIDTLKNQRAKLESSIAEAEEQgelaIKDAHAKQGELEAALQKAKQDVARQ 365
Cdd:pfam11559 54 RESLNEtIRTLEAEIERLQSKIERLKTQLEDLERELALLQAK----ERQLEKKLKTLEQKLKNEKEELQRL 120
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
75-398 |
5.80e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.25 E-value: 5.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 75 DPTIQQVRQEEREQIKTLNNKFASFIDKVRFLEQQNKMLETKWALLQEQKSAKSSQLpRIFEAQIAGLRQQLETLQLDGG 154
Cdd:PRK02224 323 DEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAV-EDRREEIEELEEEIEELRERFG 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 155 RLEVELRNmqdvVEDFKNKYEEEINRRTAAENEfvllkkdvdaaytnkveLEAKADSLQDEINFLKTLHET-ELAELQSQ 233
Cdd:PRK02224 402 DAPVDLGN----AEDFLEELREERDELREREAE-----------------LEATLRTARERVEEAEALLEAgKCPECGQP 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 234 ISDTSVVLSMDNSRSL--DLDGIIADVKAQYEEMAN-HSRAEaeawyqtkfetlqaqagkhgddlrntrneiaemnrSIQ 310
Cdd:PRK02224 461 VEGSPHVETIEEDRERveELEAELEDLEEEVEEVEErLERAE-----------------------------------DLV 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 311 RLQAEIDTLKNQRAKLESSIAEAE---EQGELAIKDAHAKQGELEAALQkAKQDVARQLREYQE-------LLNTKLAld 380
Cdd:PRK02224 506 EAEDRIERLEERREDLEELIAERRetiEEKRERAEELRERAAELEAEAE-EKREAAAEAEEEAEeareevaELNSKLA-- 582
|
330
....*....|....*...
gi 14861854 381 iEIATYRKLLEGEESRLS 398
Cdd:PRK02224 583 -ELKERIESLERIRTLLA 599
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
204-360 |
6.21e-03 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 36.89 E-value: 6.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 204 ELEAKADSLQDEINFLktlhETELAELQSqiSDTSVVLSMDNSRsldldGIIADVKAQYEEMANHSRaeaeawyqtkfeT 283
Cdd:pfam10473 14 ESERKADSLKDKVENL----ERELEMSEE--NQELAILEAENSK-----AEVETLKAEIEEMAQNLR------------D 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14861854 284 LQAqagkhgdDLRNTRNEIAEMNRSIQRLQAEIDTLKNQRAKLESSIAEAEEQGELAIKDAHAKQGELEAALQKAKQ 360
Cdd:pfam10473 71 LEL-------DLVTLRSEKENLTKELQKKQERVSELESLNSSLENLLEEKEQEKVQMKEESKTAVEMLQTQLKELNE 140
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
78-322 |
6.21e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.28 E-value: 6.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 78 IQQVRQEEREQIKTLNNKFASFIDkvrfLEQQNKMLETKWALLQEQKSAKSSQLpRIFEAQIAGLRQQLETLQLDGGRLE 157
Cdd:TIGR02169 793 IPEIQAELSKLEEEVSRIEARLRE----IEQKLNRLTLEKEYLEKEIQELQEQR-IDLKEQIKSIEKEIENLNGKKEELE 867
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 158 VELRNMQDVVEDFKNKY---EEEINRrtaaenefvlLKKDVDAAYTNKVELEAKADSLQDEINFLKTLHETELAELqSQI 234
Cdd:TIGR02169 868 EELEELEAALRDLESRLgdlKKERDE----------LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL-SEI 936
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 235 SDTSVVLSMDNSRSLDLDGIIADVKAQYEEMAN----HSRAEAEawYQtkfETLQAQagkhgDDLRNTRNEIAEMNRSIQ 310
Cdd:TIGR02169 937 EDPKGEDEEIPEEELSLEDVQAELQRVEEEIRAlepvNMLAIQE--YE---EVLKRL-----DELKEKRAKLEEERKAIL 1006
|
250
....*....|..
gi 14861854 311 RLQAEIDTLKNQ 322
Cdd:TIGR02169 1007 ERIEEYEKKKRE 1018
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
86-236 |
6.22e-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: 6.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 86 REQIKTLNNKFASFIDKVRFLEQQNKMLETKWALLQEQKSAKSSQLPRIFEAQIAGLRQQLETL--QLDGGRLEvelrnm 163
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERfaAALGDAVE------ 764
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14861854 164 QDVVEDFKNKYEEEINRRTAAENEFVLLKKDVDAAYTN-KVELEAKADSLQDEINFLKTLHETELAELQSQISD 236
Cdd:COG4913 765 RELRENLEERIDALRARLNRAEEELERAMRAFNREWPAeTADLDADLESLPEYLALLDRLEEDGLPEYEERFKE 838
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
204-371 |
6.55e-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: 6.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 204 ELEAKADSLQDEINFLKTL---HETELAELQSQISDTSVVLSMDNSRsLDLDGI---IADVKAQYEEMANHS------RA 271
Cdd:COG4913 614 ALEAELAELEEELAEAEERleaLEAELDALQERREALQRLAEYSWDE-IDVASAereIAELEAELERLDASSddlaalEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 272 EAEAWyQTKFETLQAQAGKHGDDLRNTRNEIAEMNRSIQRLQAEIDTLKN-----QRAKLESSIAEA--EEQGELAIKDA 344
Cdd:COG4913 693 QLEEL-EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDlarleLRALLEERFAAAlgDAVERELRENL 771
|
170 180
....*....|....*....|....*..
gi 14861854 345 HAKQGELEAALQKAKQDVARQLREYQE 371
Cdd:COG4913 772 EERIDALRARLNRAEEELERAMRAFNR 798
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
87-373 |
7.20e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.89 E-value: 7.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 87 EQIKTLNNKFASFidKVRFLEQQNKMLETKWALLQEQKSAKSSQLPRIFEaqIAGLRQQLETLQLDGGRLEVELRNMQDV 166
Cdd:PRK03918 503 EQLKELEEKLKKY--NLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEK--LEELKKKLAELEKKLDELEEELAELLKE 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 167 VEDFKNKYEEEINRRTaaenefvllkKDVDAAYTNKVELEAKADSLQDEINFLKTLhETELAELQSQISDTSVVLSMDNS 246
Cdd:PRK03918 579 LEELGFESVEELEERL----------KELEPFYNEYLELKDAEKELEREEKELKKL-EEELDKAFEELAETEKRLEELRK 647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 247 RsldldgiIADVKAQYEEmanhsraeaeawyqtkfetlqaqagkhgDDLRNTRNEIAEMNRSIQRLQAEIDTLKNQRAKL 326
Cdd:PRK03918 648 E-------LEELEKKYSE----------------------------EEYEELREEYLELSRELAGLRAELEELEKRREEI 692
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 14861854 327 ESSIAEAEEQGElAIKDAHAKQGELEAALQKAkQDVARQLREYQELL 373
Cdd:PRK03918 693 KKTLEKLKEELE-EREKAKKELEKLEKALERV-EELREKVKKYKALL 737
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
175-338 |
7.24e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.98 E-value: 7.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 175 EEEINRRTAAENEFVLLKKDVDAAYTNKVELEAKADSLQDEINFLKTLHE-----TELAELQSQISDtsvvlsmdnsrsl 249
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllplyQELEALEAELAE------------- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 250 dLDGIIADVKAQYEEMANHSRAEAEAwyQTKFETLQAQAGKHGDDLRN-TRNEIAEMNRSIQRLQAEIDTLKNQRAKLES 328
Cdd:COG4717 144 -LPERLEELEERLEELRELEEELEEL--EAELAELQEELEELLEQLSLaTEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170
....*....|
gi 14861854 329 SIAEAEEQGE 338
Cdd:COG4717 221 ELEELEEELE 230
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
129-369 |
8.43e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 38.46 E-value: 8.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 129 SQLPRIFEAQIAGLRQQLETLqldggrlEVELRNMQDVVeDFKNKYEEEINRRTAAENEfvLLKKDVDAAYTNKVELEAK 208
Cdd:PHA02562 166 SEMDKLNKDKIRELNQQIQTL-------DMKIDHIQQQI-KTYNKNIEEQRKKNGENIA--RKQNKYDELVEEAKTIKAE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 209 ADSLQDEI-NFLKTLHE---------TELAELQSQISDTSVVLSMDNSRSL---------DLDGIIADVKAQYEEManhs 269
Cdd:PHA02562 236 IEELTDELlNLVMDIEDpsaalnklnTAAAKIKSKIEQFQKVIKMYEKGGVcptctqqisEGPDRITKIKDKLKEL---- 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 270 raeaeawyQTKFETLQaqagKHGDDLRNTRNEIAEMNRSIQRLQAEIDTLKNQRAKLESSIAEAEEQGELAIKDAHAKQG 349
Cdd:PHA02562 312 --------QHSLEKLD----TAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAE 379
|
250 260
....*....|....*....|
gi 14861854 350 ELeAALQKAKQDVARQLREY 369
Cdd:PHA02562 380 EL-AKLQDELDKIVKTKSEL 398
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
77-322 |
8.49e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 38.66 E-value: 8.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 77 TIQQVRQEEREQIKTLNNKFASFIDKVRFLEQQNKMLETKwallQEQKSAKSSQLPRIFeaqiaglRQQLETLQLDggRL 156
Cdd:PTZ00440 788 TILNKENKISNDINILKENKKNNQDLLNSYNILIQKLEAH----TEKNDEELKQLLQKF-------PTEDENLNLK--EL 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 157 EVELRNMQDVVEDFKNKYEEE------INRRTAAENEFVLLKKDVDAAYTNKVELEAKADS------------LQDEINF 218
Cdd:PTZ00440 855 EKEFNENNQIVDNIIKDIENMnkniniIKTLNIAINRSNSNKQLVEHLLNNKIDLKNKLEQhmkiintdniiqKNEKLNL 934
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14861854 219 LKTLHEtELAELQSQISDTSvvlsmdnsrsldldgiIADVKAQYEEMAN---HSRAEAEAWYQTKFETLQaqagKHGDDL 295
Cdd:PTZ00440 935 LNNLNK-EKEKIEKQLSDTK----------------INNLKMQIEKTLEyydKSKENINGNDGTHLEKLD----KEKDEW 993
|
250 260
....*....|....*....|....*..
gi 14861854 296 RNTRNEIAEMNRSIQRLQAEIDTLKNQ 322
Cdd:PTZ00440 994 EHFKSEIDKLNVNYNILNKKIDDLIKK 1020
|
|
| |
