|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
110-421 |
1.40e-131 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 383.89 E-value: 1.40e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 110 EEKEQIKCLNSKFAAFIDKVRFLEQQNKLLETKWQFYQNRKCCE-SNMEPLFEGYIEALRREAECVEADSGRLAAELNHV 188
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEpSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 189 QESMEGYKKRYEEEVALRATSENEFVALKKDVDCAYLRKSDLEANAEALTQETDFLRQLYEEETRLLHSHISDTSVVVKM 268
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 269 DNSRDLNMDCVVAEIKAQYDDIASRSRAEAESWYRTKCEEMKATVIRHGETLRRTREEINELNRMIQRLTAEIENAKCQN 348
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 269914157 349 TKLEAAVTQSEQQGEAALTDARCKLAELEGALQKAKQDMACLLKEYQEVMNSKLGLDVEIITYRRLLEGEEQR 421
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
45-107 |
4.51e-14 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 69.68 E-value: 4.51e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 269914157 45 GLSGGFGSRSVCGPfrsGSCGRSFGYRSGGVCGPSPP-CITTVSVNESLLTPLNLEIDPNAQCV 107
Cdd:pfam16208 96 GFGGGFGGGGYGGG---GFGGGGFGGRGGFGGPPCPPgGIQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
160-394 |
4.79e-11 |
|
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: 65.47 E-value: 4.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 160 FEGYI-----EALRREAECVEADSGRLAAELNHVQESMEGYKKRYEEEVALRAT--------SENEFVALKKDVDCAYLR 226
Cdd:TIGR02169 223 YEGYEllkekEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEElnkkikdlGEEEQLRVKEKIGELEAE 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 227 KSDLEANAEALTQETDFL---RQLYEEETRLLHSHISDTSVVVKMDNSRDLNMDCVVAEIKAQYDDIASRSRAEAESWYR 303
Cdd:TIGR02169 303 IASLERSIAEKERELEDAeerLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 304 TKCEEMKATvirhgETLRRTREEINELNRMI-------QRLTAEIENAKCQNTKLEAAVTQSeqqgEAALTDARCKLAEL 376
Cdd:TIGR02169 383 TRDELKDYR-----EKLEKLKREINELKRELdrlqeelQRLSEELADLNAAIAGIEAKINEL----EEEKEDKALEIKKQ 453
|
250
....*....|....*...
gi 269914157 377 EGALQKAKQDMACLLKEY 394
Cdd:TIGR02169 454 EWKLEQLAADLSKYEQEL 471
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
99-410 |
7.72e-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: 51.98 E-value: 7.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 99 EIDPNAQCVKhEEKEQIKCLNSKFAAFIDKVRFLEQQNKLLETKWQfYQNRKCCESNMEplfegyIEALRREAECVEADS 178
Cdd:TIGR02168 678 EIEELEEKIE-ELEEKIAELEKALAELRKELEELEEELEQLRKELE-ELSRQISALRKD------LARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 179 GRLAAELNHVQESMEGYKKRYEEEVALRATSENEFVALKKDVDcaylrksDLEANAEALTQETDFLRqlyeEETRLLHSH 258
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIE-------QLKEELKALREALDELR----AELTLLNEE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 259 ISDTSVVVKMDNSRdlnmdcvVAEIKAQYDDIAsrsraeaeswyrtkceemkatvirhgETLRRTREEINELNRMIQRLT 338
Cdd:TIGR02168 819 AANLRERLESLERR-------IAATERRLEDLE--------------------------EQIEELSEDIESLAAEIEELE 865
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 269914157 339 AEIENAKCQNTKLEAAVTQSEQQGEAA---LTDARCKLAELEGALQKAKQDMACLLKEYQEVMNSKLGLDVEIIT 410
Cdd:TIGR02168 866 ELIEELESELEALLNERASLEEALALLrseLEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
130-422 |
1.45e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 130 RFLEQQNKLLETKWQFYQNRKccESnmeplFEGYIEALRREAECVEADSGRLAAELNHVQESMEGYKKRYEEevalratS 209
Cdd:TIGR02168 214 RYKELKAELRELELALLVLRL--EE-----LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE-------L 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 210 ENEFVALKKDVDCAYLRKSDLEANAEALTQETDFLRQLYEEETRLLHSHISDtsvvvKMDNSRDLN-MDCVVAEIKAQYD 288
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESK-----LDELAEELAeLEEKLEELKEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 289 DIASRSRAEAESWyrtkcEEMKATVIRHGETLRRTREEINELNRMIQRLTAEIENAKCQNTKLEAAVTQSEQQGEAALTD 368
Cdd:TIGR02168 355 SLEAELEELEAEL-----EELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK 429
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 269914157 369 A-RCKLAELEGALQKAKQDMACLLKEYQEVMNSKLGLDVEIITYRRLLEGEEQRL 422
Cdd:TIGR02168 430 LeEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL 484
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
195-422 |
5.53e-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: 49.28 E-value: 5.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 195 YKKRYEE-EVALRATSEN----EFVA--LKKDVDcaylrksDLEANAEALTQetdfLRQLYEEETRLLHShISDTSVVVK 267
Cdd:TIGR02168 170 YKERRKEtERKLERTRENldrlEDILneLERQLK-------SLERQAEKAER----YKELKAELRELELA-LLVLRLEEL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 268 MDNSRDLNMDcvVAEIKAQYDDIASRSRAEAESWYRTKCE--EMKATVIRHGETLRRTREEINELNRMIQRLTAEIENAK 345
Cdd:TIGR02168 238 REELEELQEE--LKEAEEELEELTAELQELEEKLEELRLEvsELEEEIEELQKELYALANEISRLEQQKQILRERLANLE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 346 CQNTKLEAAVTQSEQQGE---AALTDARCKLAELEGALQKAKQDMACLLKEYQEVMNSKLGLDVEIITYRRLLEGEEQRL 422
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDelaEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
166-383 |
3.88e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 46.32 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 166 ALRREAECVEADSGRLAAELNHVQESMEGYKKRYEEEVALRATSENEFVALKKDVDCAYLRKSDLEANAEALTQETDFLR 245
Cdd:pfam01576 500 SLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQ 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 246 QLYEEetrllhshisdtsVVVKMDNSRDL--NM-------DCVVAE---IKAQYDDiaSRSRAEAESwyRTKceEMKA-T 312
Cdd:pfam01576 580 QELDD-------------LLVDLDHQRQLvsNLekkqkkfDQMLAEekaISARYAE--ERDRAEAEA--REK--ETRAlS 640
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 269914157 313 VIRHGETLRRTREEINELNRMiqrLTAEIE---NAKCQNTKLEAAVTQSEQQGEAALTDARCKLAELEGALQKA 383
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQ---LRAEMEdlvSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQAT 711
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
320-388 |
2.08e-04 |
|
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: 41.53 E-value: 2.08e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 269914157 320 LRRTREEINELNRMIQRLTAEIENAKCQNTKLEAAVTQSEQQ---GEAALTDARCKLAELEGALQKAKQDMA 388
Cdd:pfam11559 47 RDRDLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLERElalLQAKERQLEKKLKTLEQKLKNEKEELQ 118
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
320-422 |
3.83e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 320 LRRTREEINELNRMIQRLTAEIENAKCQNTKLEAAVTQSEQQ---GEAALTDARCKLAELEGALQKAKQDMACLLKEYQE 396
Cdd:COG4372 47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQlqaAQAELAQAQEELESLQEEAEELQEELEELQKERQD 126
|
90 100
....*....|....*....|....*.
gi 269914157 397 VMNSKLGLDVEIITYRRLLEGEEQRL 422
Cdd:COG4372 127 LEQQRKQLEAQIAELQSEIAEREEEL 152
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
164-386 |
5.07e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 164 IEALRREAECVEADSGRLAAELNHVQESMEGYKKRyeeevaLRATsENEFVALKKDVdcaylrkSDLEANAEALTQETDF 243
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALERRIAALARR------IRAL-EQELAALEAEL-------AELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 244 LRQLYEEETRLL--HSHISDTSVVVKMDNSRDlnmdcvvAEIKAQYDDIASRSRAEaeswyrtkceemkatvirHGETLR 321
Cdd:COG4942 102 QKEELAELLRALyrLGRQPPLALLLSPEDFLD-------AVRRLQYLKYLAPARRE------------------QAEELR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 269914157 322 RTREEINELNRMIQRLTAEIENAKCQNTKLEAAVTQSEQQGEAALTDARCKLAELEGALQKAKQD 386
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
110-375 |
5.75e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 110 EEKEQIKCLNSKFAAFIDKVRFLEQQNKLLETKWQFYQNRKCCESNMEPLFEGYIEALRREAECVEADSGRLAAELNHVQ 189
Cdd:TIGR02168 786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 190 ESMEGYKKRYEEEVALRATSENEFVALKKdvdcaylRKSDLEANAEALTQETDFLRQLYEEETRLLHshisdtsvvvkmd 269
Cdd:TIGR02168 866 ELIEELESELEALLNERASLEEALALLRS-------ELEELSEELRELESKRSELRRELEELREKLA------------- 925
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 270 nsrDLNMDCvvAEIKAQYDDIASRSRAEaeswYRTKCEEMKATVIRHGETLRRTREEINELNRMIQR-----LTAeIENA 344
Cdd:TIGR02168 926 ---QLELRL--EGLEVRIDNLQERLSEE----YSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvnLAA-IEEY 995
|
250 260 270
....*....|....*....|....*....|.
gi 269914157 345 KCQNTKLEAAVTQSEQqgeaaLTDARCKLAE 375
Cdd:TIGR02168 996 EELKERYDFLTAQKED-----LTEAKETLEE 1021
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
320-400 |
6.31e-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: 42.06 E-value: 6.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 320 LRRTREEINELNRMIQRLTAEIENAKCQNTKLEAAVTQSEQQ---GEAALTDARCKLAELEGALQKAKQDMACLLKEYQE 396
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
....
gi 269914157 397 VMNS 400
Cdd:COG4942 109 LLRA 112
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
132-398 |
6.64e-04 |
|
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: 42.19 E-value: 6.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 132 LEQQNKLLETKWQFYQNRKccesNMEPLFEGYIEALRREAECVEADSGRLAAELNHVQESMEGYKKRYEEEVALRATSEN 211
Cdd:pfam07888 40 LQERAELLQAQEAANRQRE----KEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 212 EFVALKKDVDCAYLRKSDLEANAEALTQ-----ETDFLR----------QLYEEET-----------------------R 253
Cdd:pfam07888 116 EKDALLAQRAAHEARIRELEEDIKTLTQrvlerETELERmkerakkagaQRKEEEAerkqlqaklqqteeelrslskefQ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 254 LLHSHIS--DTSVVVKMD------------NSRDLNMDCVVAEIKAQYD--------------DIAS----RSRAEAE-- 299
Cdd:pfam07888 196 ELRNSLAqrDTQVLQLQDtittltqklttaHRKEAENEALLEELRSLQErlnaserkveglgeELSSmaaqRDRTQAElh 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 300 -------------SWYRTKCEEMKATVIRHGETLRRT----REEINELNRMIQRLTAEIENAKCQNTKLEAAVTQSEQQG 362
Cdd:pfam07888 276 qarlqaaqltlqlADASLALREGRARWAQERETLQQSaeadKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCN 355
|
330 340 350
....*....|....*....|....*....|....*.
gi 269914157 363 EAALTDARCKLAELEGALQKAKQDMACLLKEYQEVM 398
Cdd:pfam07888 356 RVQLSESRRELQELKASLRVAQKEKEQLQAEKQELL 391
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
160-345 |
9.37e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 41.75 E-value: 9.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 160 FEGYIEALRREAECVEADSGRLaaELNHVQESMEGYKKR----Y---EEEVALRAtseneFVALKKDVDCAYLRKsdLEA 232
Cdd:PRK04778 254 IEKEIQDLKEQIDENLALLEEL--DLDEAEEKNEEIQERidqlYdilEREVKARK-----YVEKNSDTLPDFLEH--AKE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 233 NAEALTQETDFLRQLYeeetrllhsHISDTsvvvKMDNSRDLNMDcvVAEIKAQYDDIASRS----------RAEAESWY 302
Cdd:PRK04778 325 QNKELKEEIDRVKQSY---------TLNES----ELESVRQLEKQ--LESLEKQYDEITERIaeqeiayselQEELEEIL 389
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 269914157 303 RTkCEEMKATVIRHGETLRRTREEINELNRMIQRLTAEIENAK 345
Cdd:PRK04778 390 KQ-LEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIK 431
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
318-402 |
1.20e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 318 ETLRRTREEINELNRMIQRLTAEIENAKCQNTKLEA---AVTQSEQQGEAALTDARCKLAELEGALQKAKQDMACLLKEY 394
Cdd:COG4372 94 AELAQAQEELESLQEEAEELQEELEELQKERQDLEQqrkQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQEL 173
|
....*...
gi 269914157 395 QEVMNSKL 402
Cdd:COG4372 174 QALSEAEA 181
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
281-388 |
1.27e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.44 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 281 AEIKAQYDDIASRSRAEAESwyrtkceemKATVIRHGETLR------RTREEINELNRMIQRLTAEIENAKCQNTKLEAA 354
Cdd:PRK11281 39 ADVQAQLDALNKQKLLEAED---------KLVQQDLEQTLAlldkidRQKEETEQLKQQLAQAPAKLRQAQAELEALKDD 109
|
90 100 110
....*....|....*....|....*....|....*.
gi 269914157 355 VTQSEQQGEAALTDARC--KLAELEGALQKAKQDMA 388
Cdd:PRK11281 110 NDEETRETLSTLSLRQLesRLAQTLDQLQNAQNDLA 145
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
164-386 |
1.31e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 164 IEALRREAECVEADSGRLAAELNHVQESmegykKRYEEEvalRATSEnefvalkkdvdcayLRKSDLEANAEALTQETDF 243
Cdd:PTZ00121 1178 AEAARKAEEVRKAEELRKAEDARKAEAA-----RKAEEE---RKAEE--------------ARKAEDAKKAEAVKKAEEA 1235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 244 LRQlyEEETRLLHShISDTSVVVKMDNSRDLNMDCVVAEIKAQYDDIASRSRAEAEswyRTKCEEM-KATVIRHGETLRR 322
Cdd:PTZ00121 1236 KKD--AEEAKKAEE-ERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE---KKKADEAkKAEEKKKADEAKK 1309
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 269914157 323 TREEinelNRMIQRLTAEIENAKCQNTKLEAAVTQSEQQGEAALTDARCKLAELEGALQKAKQD 386
Cdd:PTZ00121 1310 KAEE----AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA 1369
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
318-422 |
2.59e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 318 ETLRRTREEINELNRMIQRLTAEIENAKCQNTKLEAAVTQSEQQgeaaLTDARCKLAELEGALQKAKQDMACLLKEYQEV 397
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSE----LEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100
....*....|....*....|....*
gi 269914157 398 MNSKLGLDVEIITyrrlLEGEEQRL 422
Cdd:COG4372 107 QEEAEELQEELEE----LQKERQDL 127
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
180-365 |
3.18e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 180 RLAAELNHVQESMEGYKKRYEEEVALRATSENEFVALKkDVDC--AYLRKSD----LEANAEALTQETDFLRQLYEEETR 253
Cdd:PRK04863 925 PIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALT-EVVQrrAHFSYEDaaemLAKNSDLNEKLRQRLEQAEQERTR 1003
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 254 L---LHSHISD----TSVVVKMDNSRDLNMDcVVAEIKAQYDDIASRSRAEAESWYRTKCEEMkatvirHGEtLRRTREE 326
Cdd:PRK04863 1004 AreqLRQAQAQlaqyNQVLASLKSSYDAKRQ-MLQELKQELQDLGVPADSGAEERARARRDEL------HAR-LSANRSR 1075
|
170 180 190
....*....|....*....|....*....|....*....
gi 269914157 327 INELNRMIQRLTAEIENAKCQNTKLEAAVTQSEQQGEAA 365
Cdd:PRK04863 1076 RNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNA 1114
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
227-382 |
3.22e-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: 40.34 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 227 KSDLEANAEALTQETDFLRQLYEEETRLLHSHISDTSVVVKmdNSRDLNMDCVVAEIKAQYDDIASR---SRAEAESWYR 303
Cdd:TIGR00618 189 KKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELK--HLREALQQTQQSHAYLTQKREAQEeqlKKQQLLKQLR 266
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 269914157 304 TKCEEMKATVIRHGETlrrtREEINeLNRMIQRLTAEIEnakcqntkleaAVTQSEQQGEAALTDARCKLAELEGALQK 382
Cdd:TIGR00618 267 ARIEELRAQEAVLEET----QERIN-RARKAAPLAAHIK-----------AVTQIEQQAQRIHTELQSKMRSRAKLLMK 329
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
118-370 |
3.25e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 118 LNSKFAAFIDKVRFLEQQNKLLETKWQFYQNRkccesnmeplfegyIEALRREAECVEadsgrLAAELNHVQESMEGYKK 197
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAA--------------LEEFRQKNGLVD-----LSEEAKLLLQQLSELES 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 198 RYEEEVALRATSENEFVALKKDVDCAYLRKSDLEAN---AEALTQETDFLRQLYEEETRLLHSHISdtsvVVKMDNSRdl 274
Cdd:COG3206 227 QLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpviQQLRAQLAELEAELAELSARYTPNHPD----VIALRAQI-- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 275 nmdcvvAEIKAQYDDIASRSRAEAESWYrtkcEEMKATVIRHGETLRRTREEINELNRM---IQRLTAEIENAKCQNTKL 351
Cdd:COG3206 301 ------AALRAQLQQEAQRILASLEAEL----EALQAREASLQAQLAQLEARLAELPELeaeLRRLEREVEVARELYESL 370
|
250
....*....|....*....
gi 269914157 352 EAAVTQSEQQGEAALTDAR 370
Cdd:COG3206 371 LQRLEEARLAEALTVGNVR 389
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
227-365 |
3.50e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.32 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 227 KSDLEANAEALTQETDFLRQLYEEetrllhsHISDTSVVVKMDNSRDLNMDcVVAEIKAQYDDIASRSRAEAESWYRTKC 306
Cdd:COG3096 990 RARLEQAEEARREAREQLRQAQAQ-------YSQYNQVLASLKSSRDAKQQ-TLQELEQELEELGVQADAEAEERARIRR 1061
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 269914157 307 EEMKatvirhgETLRRTREEINELNRMIQRLTAEIENAKCQNTKLEAAVTQSEQQGEAA 365
Cdd:COG3096 1062 DELH-------EELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQA 1113
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
164-416 |
4.28e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 164 IEALRREAECVEADSGRLAAELNHVQESMEGYKKRYEEEVALRATSENEfvalkkdVDCAYLRK--SDLEANAEALTQET 241
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDE-------IDVASAEReiAELEAELERLDASS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 242 DFLRQLYEEetrllhshisdtsvvvkmdnsrdlnmdcvVAEIKAQYDDIASRSraeaeswyrtkcEEMKATVIRHGETLR 321
Cdd:COG4913 685 DDLAALEEQ-----------------------------LEELEAELEELEEEL------------DELKGEIGRLEKELE 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 322 RTREEINELNRMIQRLTAEIE---NAKCQNTKLEAAVTQSEQQGEAALTDARcklAELEGALQKAKQDMACLLKEYQEV- 397
Cdd:COG4913 724 QAEEELDELQDRLEAAEDLARlelRALLEERFAAALGDAVERELRENLEERI---DALRARLNRAEEELERAMRAFNREw 800
|
250 260
....*....|....*....|..
gi 269914157 398 --MNSKLGLDVE-IITYRRLLE 416
Cdd:COG4913 801 paETADLDADLEsLPEYLALLD 822
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
164-473 |
4.70e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 164 IEALRREAECVEADSGRLAAELNHVQESMEGYKKRYEEEVALRATSENEFVALKKDVDcaylrksDLEANAEALTQE-TD 242
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA-------EAEAEIEERREElGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 243 FLRQLYEEETRllhshISDTSVVVKMDNSRDL--NMDCVVAEIKAQYDDIASRSRAEAEswyrtkCEEMKATVIRHGETL 320
Cdd:COG3883 91 RARALYRSGGS-----VSYLDVLLGSESFSDFldRLSALSKIADADADLLEELKADKAE------LEAKKAELEAKLAEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 321 RRTREEINELNRMIQRLTAEIENAKCQNTKLEAAVTQSEQQGEAALTDARCKLAELEGALQKAKQDMACLLKEYQEVMNS 400
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 269914157 401 KLGLDVEIITYRRLLEGEEQRLCEGVGSVNVCVSSSRGGVTCGGLTYGTTPGRQIASGPSVTGGSITVMAPDS 473
Cdd:COG3883 240 AAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGG 312
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
280-422 |
5.41e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.53 E-value: 5.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 280 VAEIKAQYDDIASRSRAEAESWYrtkceEMKATVIRHGETLRRTREEINELNRMIQRLTAEIENAKCQNTKLEAAVTQSE 359
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEY-----ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE 343
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 269914157 360 QQGEAA---LTDARCKLAELEGALQKAKQDMACLLKEYQEVMNSKLGLDVEIITYRRLLEGEEQRL 422
Cdd:COG1196 344 EELEEAeeeLEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
281-396 |
5.66e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.38 E-value: 5.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269914157 281 AEIKAQYDdiASRSRAEAESWYRTKCEEMKA---TVIRHGETLRRTREEI----NELNRMIQRLTAEIENAKCQNTKLEA 353
Cdd:PRK12704 58 ALLEAKEE--IHKLRNEFEKELRERRNELQKlekRLLQKEENLDRKLELLekreEELEKKEKELEQKQQELEKKEEELEE 135
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 269914157 354 AVTQSEQQGE--AALT--DARCKLaeLEGALQKAKQDMACLLKEYQE 396
Cdd:PRK12704 136 LIEEQLQELEriSGLTaeEAKEIL--LEKVEEEARHEAAVLIKEIEE 180
|
|
| |
