|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
73-386 |
6.06e-120 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 352.30 E-value: 6.06e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 73 NEKVTMQNLNDRLASYLENVQALEEANADLEQKIKDWYEKFGPGSCRgldhDYSRYFPIIDDLRTQIISATAQNANIVLQ 152
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSR----LYSLYEKEIEDLRRQLDTLTVERARLQLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 153 NDNARLTADDFRMKYENELALHQSVDADINGLRRVLDELTLCRTDLEVQLETLSEELAYLKKNHEEEMQALQC-AAGGNV 231
Cdd:pfam00038 77 LDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAqVSDTQV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 232 NVEMNAAPGVDLTVLLNNMRAEYEALAEQNRRDAEAWFQEKSASLQQQISDDAGATTSARNELTEMKRTLQTLEIELQSL 311
Cdd:pfam00038 157 NVEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSL 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57012442 312 LAMKHSLECSLTETEGNYCTQLAQIQAQISALEEQLHQVRTETEGQKLEYEQLLNVKAHLEKEIETYCLLIGGDE 386
Cdd:pfam00038 237 KKQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEE 311
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
166-376 |
1.07e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 166 KYENELALHQ--SVDADINGLRRVLDELTLCRTDLEVQLETLSEELAYLKKNHEEEMQALQcaaggnvnvEMNAapgvDL 243
Cdd:COG1196 224 ELEAELLLLKlrELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE---------EAQA----EE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 244 TVLLNNMRAEYEALAEQNRRDAEAwfQEKSASLQQQISDDAGATTSARNELTEMKRTLQTLEIELQSLLAMKHSLECSLT 323
Cdd:COG1196 291 YELLAELARLEQDIARLEERRREL--EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 57012442 324 ETEgnycTQLAQIQAQISALEEQLHQVRTETEGQKLEYEQLLNVKAHLEKEIE 376
Cdd:COG1196 369 EAE----AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
185-377 |
8.29e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 8.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 185 RRVLDELTLCRTDLEVQLETLSEELAYLKKNHEE----------------------EMQALQCAAGGNVNVEMNAAPGVD 242
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEEleeeleqlrkeleelsrqisalRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 243 LTVLLNNMRAEYEALAEQNRRDAEAwfQEKSASLQQQISDDAGATT-------SARNELTEMKRTLQTLEIELQSLLAMK 315
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEA--EAEIEELEAQIEQLKEELKalrealdELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57012442 316 HSLECSLTETEGnyctQLAQIQAQISALEEQLHQVRTETEGQKLEYEQLLNVKAHLEKEIET 377
Cdd:TIGR02168 834 AATERRLEDLEE----QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
80-377 |
5.47e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.82 E-value: 5.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 80 NLNDRLASYLENVQALEEANADLEQKIKDWYEKFgpgscRGLDHDYSRYFPIIDDLRTQIISATAQNANIVLQNDNARLT 159
Cdd:TIGR02168 730 ALRKDLARLEAEVEQLEERIAQLSKELTELEAEI-----EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA 804
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 160 ADDFRMKYENELALHQSVDADINGLRRVLDELTLCRTDLEVQLETLSEELAYLKKNHEEEMQALQcaaggnvnvEMNAAp 239
Cdd:TIGR02168 805 LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE---------ELESE- 874
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 240 gvdLTVLLNNMRAEYEALAEqnRRDAEAWFQEKSASLQQQISDDAGATTSARNELTEMKRTLQTLEIELQSLLAM---KH 316
Cdd:TIGR02168 875 ---LEALLNERASLEEALAL--LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlseEY 949
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57012442 317 SLECSLTETEGNYCT-QLAQIQAQISALEEQLHQ-------VRTETEGQKLEYEQLLNVKAHLEKEIET 377
Cdd:TIGR02168 950 SLTLEEAEALENKIEdDEEEARRRLKRLENKIKElgpvnlaAIEEYEELKERYDFLTAQKEDLTEAKET 1018
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
196-366 |
6.07e-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: 6.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 196 TDLEVQLETLSEELAylkknheeEMQALQCAAGGNVNVEMNAAPGVDLTVLLNNMRAEYEALaEQNRRDAEAWFQEKS-- 273
Cdd:COG3206 222 SELESQLAEARAELA--------EAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAEL-EAELAELSARYTPNHpd 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 274 -ASLQQQISDdagattsARNEL-TEMKRTLQTLEIELQSLLAMKHSLECSLTETEGNYcTQLAQIQAQISALEEQLhQVR 351
Cdd:COG3206 293 vIALRAQIAA-------LRAQLqQEAQRILASLEAELEALQAREASLQAQLAQLEARL-AELPELEAELRRLEREV-EVA 363
|
170
....*....|....*
gi 57012442 352 TETegqkleYEQLLN 366
Cdd:COG3206 364 REL------YESLLQ 372
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
198-378 |
9.20e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 9.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 198 LEVQLETLSEELAylkkNHEEEMQALQcAAGGNVNVEMNAAPGVDLTVLLNNMRAEyealAEQNRRDAEAwfqeKSASLQ 277
Cdd:COG3206 180 LEEQLPELRKELE----EAEAALEEFR-QKNGLVDLSEEAKLLLQQLSELESQLAE----ARAELAEAEA----RLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 278 QQISDDAGATTSARN--ELTEMKRTLQTLEIELQSLLAmkhslecslTETEGNycTQLAQIQAQISALEEQLHQ-VRTET 354
Cdd:COG3206 247 AQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSA---------RYTPNH--PDVIALRAQIAALRAQLQQeAQRIL 315
|
170 180
....*....|....*....|....
gi 57012442 355 EGQKLEYEQLLNVKAHLEKEIETY 378
Cdd:COG3206 316 ASLEAELEALQAREASLQAQLAQL 339
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
74-377 |
2.62e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.57 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 74 EKVTMQN----LNDRLASYLENVQALEEANADLE-------------QKIKDWYEKF--GPGSCRGLDHDYSRYFPIIDD 134
Cdd:pfam15921 487 KKMTLESsertVSDLTASLQEKERAIEATNAEITklrsrvdlklqelQHLKNEGDHLrnVQTECEALKLQMAEKDKVIEI 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 135 LRTQIISAT---AQNANIV--LQNDNARLTAD--DFRMKYENELALHQSVDADINGLRRVLDELTLCRTDLevqLETLSE 207
Cdd:pfam15921 567 LRQQIENMTqlvGQHGRTAgaMQVEKAQLEKEinDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKL---VNAGSE 643
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 208 ELAYLKKNHEEEMQALQcaaggNVNVEMNAapgvdltvlLNNMRAEYEALaEQNRRDAEAWFQEKSASLQQQISddagat 287
Cdd:pfam15921 644 RLRAVKDIKQERDQLLN-----EVKTSRNE---------LNSLSEDYEVL-KRNFRNKSEEMETTTNKLKMQLK------ 702
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 288 tSARNELTEMKRTLQTLEIELQSLLAMKHSLECSLTETEGnyctQLAQIQAQISALEEQLHQVRTETEGQKLEyeqllnv 367
Cdd:pfam15921 703 -SAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRG----QIDALQSKIQFLEEAMTNANKEKHFLKEE------- 770
|
330
....*....|
gi 57012442 368 KAHLEKEIET 377
Cdd:pfam15921 771 KNKLSQELST 780
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
175-358 |
2.76e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 175 QSVDADINGLRRVLDELTLCRTDLEVQLETLSEELAYLKKNHEEEMQALqcAAGGNVNVEMNAAPGvdLTVLLNN----- 249
Cdd:COG4942 58 AALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL--AELLRALYRLGRQPP--LALLLSPedfld 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 250 --MRAEY-EALAEQNRRDAEAwFQEKSASLQQQISddagATTSARNELTEMKRTLQTLEIELQSLLAMKHSLECSLTETE 326
Cdd:COG4942 134 avRRLQYlKYLAPARREQAEE-LRADLAELAALRA----ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKEL 208
|
170 180 190
....*....|....*....|....*....|..
gi 57012442 327 GNYCTQLAQIQAQISALEEQLHQVRTETEGQK 358
Cdd:COG4942 209 AELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
166-386 |
3.22e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.17 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 166 KYENELALHQSVDADINGlrrVLDELTLCRTDLEVQLETLSEELAYLKKNHEEEMQALQCAAGGNVNVEMNAAPGV---- 241
Cdd:pfam05483 173 KYEYEREETRQVYMDLNN---NIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLliqi 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 242 --------DLTVLLNNMRAEYEALAEQNRRDAEAWFQ-------------------EKSASLQQQISDDAGATTSARNEL 294
Cdd:pfam05483 250 tekenkmkDLTFLLEESRDKANQLEEKTKLQDENLKEliekkdhltkeledikmslQRSMSTQKALEEDLQIATKTICQL 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 295 TEMKRTlqtlEIELQSLLAMKHSLecSLTETEGNYCTQ---LAQIQAQISALEEQLHQVRTETEGQKLEYEQLLNVKAHL 371
Cdd:pfam05483 330 TEEKEA----QMEELNKAKAAHSF--VVTEFEATTCSLeelLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNK 403
|
250
....*....|....*
gi 57012442 372 EKEIETYCLLIGGDE 386
Cdd:pfam05483 404 EVELEELKKILAEDE 418
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
251-376 |
7.06e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 7.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 251 RAEYEALAEQNRR--DAEAWFQEKSASLQQQISDDAGAT-TSARNELTEMKRTLQTLEIELQSLLAMKHSLECSLTETEG 327
Cdd:COG4913 301 RAELARLEAELERleARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE 380
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 57012442 328 NYCTQLAQIQAQISALEEQLHQVRTETEGQKLEYEQLLNVKAHLEKEIE 376
Cdd:COG4913 381 EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
176-376 |
7.55e-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: 41.98 E-value: 7.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 176 SVDADINGLRRVLDELTLCRTDLEVQLETLSEELAYLKKNHEEEMQALQcaaggNVNVEMNAapgvdLTVLLNNMRAEYE 255
Cdd:TIGR02169 298 ELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIE-----EERKRRDK-----LTEEYAELKEELE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 256 AL---AEQNRRDAEAWFQEkSASLQQQISDdagaTTSARNEL-TEMKR---TLQTLEIELQSLLAMKHSLECSLTETEgn 328
Cdd:TIGR02169 368 DLraeLEEVDKEFAETRDE-LKDYREKLEK----LKREINELkRELDRlqeELQRLSEELADLNAAIAGIEAKINELE-- 440
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 57012442 329 ycTQLAQIQAQISALEEQLHQVRTETEGQKLEYEQLLNVKAHLEKEIE 376
Cdd:TIGR02169 441 --EEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELS 486
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
282-374 |
7.74e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 7.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 282 DDAGA-----TTSARNELTEMKRTLQTLEIELQSLLAmkhslecsltETEGNYCTQLAQIQAQISALEEQLHQVRTETEG 356
Cdd:COG0542 396 DEAAArvrmeIDSKPEELDELERRLEQLEIEKEALKK----------EQDEASFERLAELRDELAELEEELEALKARWEA 465
|
90
....*....|....*...
gi 57012442 357 QKLEYEQLLNVKAHLEKE 374
Cdd:COG0542 466 EKELIEEIQELKEELEQR 483
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
246-364 |
9.05e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 41.37 E-value: 9.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 246 LLNNM--RAEYEAL--AEQNRRDAEAWFQEKSASL-----QQQISDDAGATTSARNELTEMKRTLQTLEIELQSLLAmkh 316
Cdd:COG3524 166 LVNQLseRAREDAVrfAEEEVERAEERLRDAREALlafrnRNGILDPEATAEALLQLIATLEGQLAELEAELAALRS--- 242
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 57012442 317 slecslTETEGNycTQLAQIQAQISALEEQLHQVRTE----TEGQKL-----EYEQL 364
Cdd:COG3524 243 ------YLSPNS--PQVRQLRRRIAALEKQIAAERARltgaSGGDSLasllaEYERL 291
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
168-376 |
1.54e-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: 41.21 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 168 ENELAlhqSVDADINGLRRVLDELTLCRTDLEVQLETLSEELAYLKKNHE----------EEMQALQcAAGGNVNVEM-- 235
Cdd:TIGR02169 687 KRELS---SLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEklkerleeleEDLSSLE-QEIENVKSELke 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 236 NAAPGVDLTVLLNNMRaeyEALAEQNRRDAEAWFQEKSASLQQQisddagattsaRNELTEMKRTLQTLEIELQSLLAMK 315
Cdd:TIGR02169 763 LEARIEELEEDLHKLE---EALNDLEARLSHSRIPEIQAELSKL-----------EEEVSRIEARLREIEQKLNRLTLEK 828
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57012442 316 HSLECSLTETEG--NYCT-QLAQIQAQISALEEQLHQVRTETEGQKLEYEQLLNVKAHLEKEIE 376
Cdd:TIGR02169 829 EYLEKEIQELQEqrIDLKeQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERD 892
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
78-379 |
2.12e-03 |
|
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: 40.81 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 78 MQNLNDRLASYLENVQALEEANADLEQKIKDWYEKFgpgscRGLDHDYSRYFPIIDDLRTQII----SATAQNANI-VLQ 152
Cdd:TIGR02168 276 VSELEEEIEELQKELYALANEISRLEQQKQILRERL-----ANLERQLEELEAQLEELESKLDelaeELAELEEKLeELK 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 153 NDNARLTA--DDFRMKYENELALHQSVDADINGLRRVLDELTLCRTDLEVQLETLSEELAYLKKNHEEemqalqcaaggn 230
Cdd:TIGR02168 351 EELESLEAelEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER------------ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 231 vnvemnaapgvdltvLLNNMRAEYEALAEQNRRDAEAWFQEKSASLQQQISDDAGATT---SARNELTEMKRTLQTLEIE 307
Cdd:TIGR02168 419 ---------------LQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEaleELREELEEAEQALDAAERE 483
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57012442 308 LQSLLAMKHSLECSLTETEGNYCTQLAQIQAQisaleEQLHQVRteteGQKLEyeqLLNVKAHLEKEIETYC 379
Cdd:TIGR02168 484 LAQLQARLDSLERLQENLEGFSEGVKALLKNQ-----SGLSGIL----GVLSE---LISVDEGYEAAIEAAL 543
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
251-377 |
2.66e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 251 RAEYEALAEQNRRDAEAWFQEKSASLQQQISDDAGATTSARNELTEMKRTLQTLEIELQSLLAMKHSLECSLTETEGN-- 328
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDia 305
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 57012442 329 -YCTQLAQIQAQISALEEQLHQVRTETEGQKLEYEQLLNVKAHLEKEIET 377
Cdd:COG1196 306 rLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
134-377 |
3.18e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 39.95 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 134 DLRTQIISATAQnanIVLQNDNARLTaddfRMKYENELALHQSVDADINGLRRVLDEltlcRTDLEVQLETLSEELAYLK 213
Cdd:TIGR00618 421 DLQGQLAHAKKQ---QELQQRYAELC----AAAITCTAQCEKLEKIHLQESAQSLKE----REQQLQTKEQIHLQETRKK 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 214 KNHE---EEMQALQCAAGGNV---NVEMNAA--PGVDLTVLLnnmRAEYE-ALAEQNRRDAEAWFQEKSASLQ------Q 278
Cdd:TIGR00618 490 AVVLarlLELQEEPCPLCGSCihpNPARQDIdnPGPLTRRMQ---RGEQTyAQLETSEEDVYHQLTSERKQRAslkeqmQ 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 279 QISDDAGATTSARNELTEMKRTLQTLEIELQSLLAMKHSLECSLTEtegnyctqlaQIQAQISALEEQLHQVR-TETEGQ 357
Cdd:TIGR00618 567 EIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLAC----------EQHALLRKLQPEQDLQDvRLHLQQ 636
|
250 260
....*....|....*....|
gi 57012442 358 KLEYEQLLnvKAHLEKEIET 377
Cdd:TIGR00618 637 CSQELALK--LTALHALQLT 654
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
270-367 |
3.37e-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: 39.36 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 270 QEKSASLQQQISDdagattsARNELTEMKRTLQTLEIELQSLLAMKHSLECSLTETEG---NYCTQLAQIQAQISALEEQ 346
Cdd:COG4942 19 ADAAAEAEAELEQ-------LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARrirALEQELAALEAELAELEKE 91
|
90 100
....*....|....*....|.
gi 57012442 347 LHQVRTETEGQKLEYEQLLNV 367
Cdd:COG4942 92 IAELRAELEAQKEELAELLRA 112
|
|
| Gp58 |
pfam07902 |
gp58-like protein; Sequences found in this family are derived from a number of bacteriophage ... |
71-341 |
6.79e-03 |
|
gp58-like protein; Sequences found in this family are derived from a number of bacteriophage and prophage proteins. They are similar to gp58, a minor structural protein of Lactococcus delbrueckii bacteriophage LL-H.
Pssm-ID: 369586 [Multi-domain] Cd Length: 594 Bit Score: 38.78 E-value: 6.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 71 SGNEKVTMQNLNDRLASYLE-NVQALEEANADLEQKIKdwyekfgpGSCRGLDHDYSRyfpiiDDLRTQIISATAQNANI 149
Cdd:pfam07902 70 SGESTGLFKSLEEMLSQLKElNLELTDTKNSNLWSKIK--------LNNNGMLREYHN-----DTIKTEIVESAEGIATR 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 150 VLQNDNARL-----TADDFRMKYEN-ELALHQSVDADINGLRRVLDELTLcrtDLEVQLETLSEELAylkKNHEEEMQAL 223
Cdd:pfam07902 137 ISEDTDKKLalineTISGIRREYQDaDRQLSSSYQAGIEGLKATMASDKI---GLQAEIQASAQGLS---QRYDNEIRKL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 224 QCAAGGNVNVEMNAapgvdLTVLLNNMRAEYEALAEQNRRDAE-------AWFQEKSASLQQQISDDAGATTSARNELTE 296
Cdd:pfam07902 211 SAKITTTSSGTTEA-----YESKLDDLRAEFTRSNQGMRTELEskisglqSTQQSTAYQISQEISNREGAVSRVQQDLDS 285
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 57012442 297 MKRTLQTLEIELQSLLAMKHSLECSLTETEGNYCTQLAQIQAQIS 341
Cdd:pfam07902 286 YQRRLQDAEKNYSSLTQTVKGLQSTVSDPNSKLESRITQLAGLIE 330
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
185-353 |
9.81e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 38.36 E-value: 9.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 185 RRVLDELTLCRTDLEVQLETLSEELAYLK---KNHEEEMQALQcaaggnvnVEMNAAPGVDLTVLLNNMRAEYEALAEQN 261
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEarlDALREELDELE--------AQIRGNGGDRLEQLEREIERLERELEERE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012442 262 RRDAEawFQEKSASLQQQISDDAGATTSARNELTEMKRTLQTLEIELQSLLAmkhslecSLTETEGNYCTQLAQIQAQIS 341
Cdd:COG4913 359 RRRAR--LEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALA-------EAEAALRDLRRELRELEAEIA 429
|
170
....*....|....*....
gi 57012442 342 ALE-------EQLHQVRTE 353
Cdd:COG4913 430 SLErrksnipARLLALRDA 448
|
|
| |
