|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
122-433 |
6.24e-133 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 386.20 E-value: 6.24e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 122 EEKEQIKCLNSKFAAFIDKVRFLEQQNKLLETKW-QFYQNQRCCESNLEPLFGGYIETLRREAECVEADGGRLAAELNHV 200
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKIsELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 201 QEAMEGYKKRYEEEVALRATAENEFVVLKKDVDCAYLRKSDLEANVEALVEESSFLKRLYEEEVRVLQAHISDTSVIVKM 280
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 281 DNSRDLNMDCVVAEIKAQYDDVASRSRAEAESWYRTKCEEMKATVIRHGETLRRTREEMNELNRIIQRLTAEIENAKCQR 360
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57012382 361 AKLETAVAEAEQQGEAALTDARGKLAELEAALQKAKQDMACLLKEYQEVMNSKLGLDIEIATYRRLLEGEEHR 433
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
17-119 |
6.82e-19 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 83.55 E-value: 6.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 17 NFSSCSAVAP-----KTGNRCCISAAPFRGVSCYRGLTGFSSRSLCN---PSPCGPRMAVGGFRSGSCGRS--------- 79
Cdd:pfam16208 1 GFSSCSAVVPsrsrrSYSSVSSSRRGGGGGGGGGGGGGGFGSRSLYNlggSKSISISVAGGGSRPGSGFGFgggggggfg 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57012382 80 -----------------------------------FGYRAGGVCGPSPP-CITTVSVNESLLTPLNLEIDPNAQCV 119
Cdd:pfam16208 81 ggfgggggggfgggggfgggfggggyggggfggggFGGRGGFGGPPCPPgGIQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
176-406 |
2.98e-10 |
|
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: 62.78 E-value: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 176 IETLRREAECVEADGGRLAAELNHVQEAMEGYKKRYEEEVALRATA--------ENEFVVLKKDVDCAYLRKSDLEANVE 247
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkkikdlgEEEQLRVKEKIGELEAEIASLERSIA 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 248 AL---VEESSFLKRLYEEEVRVLQAHISDTSVIVKMDNSRDLNMDCVVAEIKAQYDDVASRSRAEAESWYRTKCEEMKAT 324
Cdd:TIGR02169 312 EKereLEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 325 virhgETLRRTREEMNELNRIIQRLTAEIENAKCQRAKLETAVAEAEQ---QGEAALTDARGKLAELEAALQKAKQDMAC 401
Cdd:TIGR02169 392 -----EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAkinELEEEKEDKALEIKKQEWKLEQLAADLSK 466
|
....*
gi 57012382 402 LLKEY 406
Cdd:TIGR02169 467 YEQEL 471
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
140-443 |
3.08e-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: 53.14 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 140 KVRFLEQQNKLLEtKWQFYQNQrccESNLE-PLFGGYIETLRREAECVEADGGRLAAELNHVQEAMEGYKKRYEEEVALR 218
Cdd:TIGR02168 201 QLKSLERQAEKAE-RYKELKAE---LRELElALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEV 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 219 ATAENEFVVLKKDVDCAYLRKSDLEANVEALVEESSFLKRLYEEEVRVLQAHISDtsvivKMDNSRDLN-MDCVVAEIKA 297
Cdd:TIGR02168 277 SELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESK-----LDELAEELAeLEEKLEELKE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 298 QYDDVASRSRAEAESWyrtkcEEMKATVIRHGETLRRTREEMNELNRIIQRLTAEIENAKCQRAKLETAVAEAEQQGEAA 377
Cdd:TIGR02168 352 ELESLEAELEELEAEL-----EELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEL 426
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57012382 378 LTDA-RGKLAELEAALQKAKQDMACLLKEYQEVMNSKLGLDIEIATYRRLLEGEEHRCQQLPWRSHM 443
Cdd:TIGR02168 427 LKKLeEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
122-437 |
9.52e-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: 51.60 E-value: 9.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 122 EEKEQIKCLNSKFAAFIDKVRFLEQQNKLLETKWQFYQNQ----RCCESNLEPLFGGY---IETLRREAECVEADGGRLA 194
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEEleqlRKELEELSRQISALrkdLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 195 AELNHVQEAMEGYKKRYEEEVALRATAENEFVVLKKDVDCAylrKSDLEANVEALVEESSFLKRLYEEevrvlqahisdt 274
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL---KEELKALREALDELRAELTLLNEE------------ 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 275 svivkmdnsrdlnmdcvvaeikaqYDDVASRsraeaeswyRTKCEEMKATVIRHGETLRRTREEMNElnrIIQRLTAEIE 354
Cdd:TIGR02168 819 ------------------------AANLRER---------LESLERRIAATERRLEDLEEQIEELSE---DIESLAAEIE 862
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 355 NAKCQRAKLETAVAEAEQ---QGEAALTDARGKLAELEAALQKAKQDMACLLKEYQEvmnsklgLDIEIATYRRLLEGEE 431
Cdd:TIGR02168 863 ELEELIEELESELEALLNeraSLEEALALLRSELEELSEELRELESKRSELRRELEE-------LREKLAQLELRLEGLE 935
|
....*.
gi 57012382 432 HRCQQL 437
Cdd:TIGR02168 936 VRIDNL 941
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
215-425 |
5.35e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 5.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 215 VALRATAENEFVVLKKDVDCAYLRKSDLEANVEALVEESSFLKRLYEEevrvLQAHISDTSVivKMDNSRDlNMDCVVAE 294
Cdd:COG3883 8 APTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE----LQAELEALQA--EIDKLQA-EIAEAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 295 IKAQYDDVASRSRAEAESWYRTKCEEM------KATVIRHGETLRRTREEMNELNRIIQRLTAEIENAKcqrAKLETAVA 368
Cdd:COG3883 81 IEERREELGERARALYRSGGSVSYLDVllgsesFSDFLDRLSALSKIADADADLLEELKADKAELEAKK---AELEAKLA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 57012382 369 EAEQQgeaaLTDARGKLAELEAALQKAKQDMACLLKEYQEVMNSKLGLDIEIATYRR 425
Cdd:COG3883 158 ELEAL----KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
332-412 |
8.38e-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: 47.84 E-value: 8.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 332 LRRTREEMNELNRIIQRLTAEIENAKCQRAKLETAVAEAEQQ---GEAALTDARGKLAELEAALQKAKQDMACLLKEYQE 408
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
....
gi 57012382 409 VMNS 412
Cdd:COG4942 109 LLRA 112
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
292-399 |
2.12e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 46.79 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 292 VAEIKAQYDDVASRSRAEAESWYRTKCEEMKATVIRHGETLRRTREEmnELNRI-IQRLTAEIENAKCQRAKLETAVAEA 370
Cdd:COG2268 246 LAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREI--ELQEKeAEREEAELEADVRKPAEAEKQAAEA 323
|
90 100 110
....*....|....*....|....*....|
gi 57012382 371 EQQGEAALTDARGK-LAELEAALQKAKQDM 399
Cdd:COG2268 324 EAEAEAEAIRAKGLaEAEGKRALAEAWNKL 353
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
332-437 |
2.31e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 332 LRRTREEMNELNRIIQRLTAEIENAKCQRAKLETAVAEAEQQ---GEAALTDARGKLAELEAALQKAKQDMACLLKEYQE 408
Cdd:COG4372 47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQlqaAQAELAQAQEELESLQEEAEELQEELEELQKERQD 126
|
90 100
....*....|....*....|....*....
gi 57012382 409 VMNSKLGLDIEIATYRRLLEGEEHRCQQL 437
Cdd:COG4372 127 LEQQRKQLEAQIAELQSEIAEREEELKEL 155
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
235-428 |
3.62e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 235 AYLrKSDLEANVEALVEESSFL-KRL--YEEEVRVLQAHISD---TSVIVKMDNSRDLNMDcVVAEIKAQYDDVASRsRA 308
Cdd:COG3206 160 AYL-EQNLELRREEARKALEFLeEQLpeLRKELEEAEAALEEfrqKNGLVDLSEEAKLLLQ-QLSELESQLAEARAE-LA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 309 EAESWYRTKCEEMKATVIRHGE-----TLRRTREEMNELNR--------------IIQRLTAEIENAkcqRAKLETAVAE 369
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPEllqspVIQQLRAQLAELEAelaelsarytpnhpDVIALRAQIAAL---RAQLQQEAQR 313
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57012382 370 AEQQGEAALTDARGKLAELEAALQKAKQDMACL---LKEYQEVMNsklglDIEIA--TYRRLLE 428
Cdd:COG3206 314 ILASLEAELEALQAREASLQAQLAQLEARLAELpelEAELRRLER-----EVEVAreLYESLLQ 372
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
176-398 |
5.05e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 5.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 176 IETLRREAECVEADGGRLAAELNHVQEAMEGYKKRYEEEV-----ALRATAENEFVVLKKDVDcayLRKSDLEANVEAL- 249
Cdd:PTZ00121 1154 VEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELrkaedARKAEAARKAEEERKAEE---ARKAEDAKKAEAVk 1230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 250 -VEESsflkRLYEEEVRVLQaHISDTSVIVKMDNSRDLNMDCVVAEIKAQYDDVASRSRAEAEswyRTKCEEM-KATVIR 327
Cdd:PTZ00121 1231 kAEEA----KKDAEEAKKAE-EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE---KKKADEAkKAEEKK 1302
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57012382 328 HGETLRRTREEmnelNRIIQRLTAEIENAKCQRAKLETAVAEAEQQGEAALTDARGKLAELEAALQKAKQD 398
Cdd:PTZ00121 1303 KADEAKKKAEE----AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA 1369
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
320-437 |
9.93e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 9.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 320 EMKATVIRHGETLRRTREEMNELNRIIQRLTAEIENAKCQRAKLETAVAEAEQQGEAA---LTDARGKLAELEAALQKAK 396
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAeeeLEEAEAELAEAEEALLEAE 371
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 57012382 397 QDMACLLKEYQEVMNSKLGLDIEIATYRRLLEGEEHRCQQL 437
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
337-416 |
1.00e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.76 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 337 EEMNELNRIIQRLTAEIENAKCQRAKLETAVAEAEQQGEAALTDARGKLAELEAALQKAKQDM-ACLLKEYQEVMNSKLG 415
Cdd:COG1579 110 DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIpPELLALYERIRKRKNG 189
|
.
gi 57012382 416 L 416
Cdd:COG1579 190 L 190
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
176-425 |
1.36e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 176 IETLRREAECVEADGGRLAAELNHVQEAMEGYKKRyeeevaLRATaENEFVVLKKDVdcaylrkSDLEANVEALVEESSF 255
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALERRIAALARR------IRAL-EQELAALEAEL-------AELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 256 LKRLYEEEVRVLQAH--ISDTSVIVKMDNSRDlnmdcvvAEIKAQYDDVASRSRAEaeswyrtkceemkatvirHGETLR 333
Cdd:COG4942 102 QKEELAELLRALYRLgrQPPLALLLSPEDFLD-------AVRRLQYLKYLAPARRE------------------QAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 334 RTREEmnelnriIQRLTAEIENAKCQRAKLETAVAEAEQQGEAALTDARGKLAELEAALQKAKQDMACLLKEYQEVMNSK 413
Cdd:COG4942 157 ADLAE-------LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
250
....*....|..
gi 57012382 414 LGLDIEIATYRR 425
Cdd:COG4942 230 ARLEAEAAAAAE 241
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
178-435 |
1.45e-04 |
|
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: 44.40 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 178 TLRREAECVEADGGRLAAELNHVQEAMEGYKKRYEEEVALRATAENEFVVLKKDVDCAYLRKSDLEANVEALveessflk 257
Cdd:pfam01576 500 SLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKL-------- 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 258 rlyEEEVRVLQAHISDtsVIVKMDNSRDL---------NMDCVVAE---IKAQYDDvaSRSRAEAESwyRTKceEMKA-T 324
Cdd:pfam01576 572 ---EKTKNRLQQELDD--LLVDLDHQRQLvsnlekkqkKFDQMLAEekaISARYAE--ERDRAEAEA--REK--ETRAlS 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 325 VIRHGETLRRTREEMNELNriiqrltaeienaKCQRAKLETAVAEAEQQGEAALTDARGKLAeLEAALQKAKQDMACLLK 404
Cdd:pfam01576 641 LARALEEALEAKEELERTN-------------KQLRAEMEDLVSSKDDVGKNVHELERSKRA-LEQQVEEMKTQLEELED 706
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 57012382 405 EYQEVMNSKLGLDIEI----ATYRRLLE-----GEEHRCQ 435
Cdd:pfam01576 707 ELQATEDAKLRLEVNMqalkAQFERDLQardeqGEEKRRQ 746
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
320-410 |
2.64e-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: 43.35 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 320 EMKATVIRHGETLRRT----REEMNELNRIIQRLTAEIENAKCQRAKLETAVAEAEQQGEAALTDARGKLAELEAALQKA 395
Cdd:pfam07888 297 EGRARWAQERETLQQSaeadKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVA 376
|
90
....*....|....*
gi 57012382 396 KQDMACLLKEYQEVM 410
Cdd:pfam07888 377 QKEKEQLQAEKQELL 391
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
294-408 |
2.87e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 294 EIKAQYDDVASRSRAEAESWYRTKCEEMKAT---VIRHGETLRRTREEM----NELNRIIQRLTAEIENAKCQRAKLETA 366
Cdd:PRK12704 57 EALLEAKEEIHKLRNEFEKELRERRNELQKLekrLLQKEENLDRKLELLekreEELEKKEKELEQKQQELEKKEEELEEL 136
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 57012382 367 VAEAEQQGE--AALT--DARGKLaeLEAALQKAKQDMACLLKEYQE 408
Cdd:PRK12704 137 IEEQLQELEriSGLTaeEAKEIL--LEKVEEEARHEAAVLIKEIEE 180
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
177-408 |
1.09e-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: 41.59 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 177 ETLRREAECVEADGGRLAAELNHVQEAMEGYKKRYEEEVALRATAENEFVVLKKDVDCAYLRKSDLEANVEALVEEssfl 256
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE---- 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 257 KRLYEEEVRVLQAHISDtsvivkmdnsrdlnMDCVVAEIKAQYDDVASRSRAEAESWYRTKCEEMKATVIRHGETLRRTR 336
Cdd:TIGR02169 753 IENVKSELKELEARIEE--------------LEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIE 818
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57012382 337 EEMNELNRIIQRLTAEIENAKCQRAKLETAVAEAEQQGEaaltDARGKLAELEAALQKAKQDMACLLKEYQE 408
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE----NLNGKKEELEEELEELEAALRDLESRLGD 886
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
207-428 |
1.14e-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: 41.58 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 207 YKKRYEE-EVALRATAENefvvLKKDVDCAylrkSDLEANVEALVEESSFLKRL--YEEEVRVLQAHISdtsvivkmdns 283
Cdd:TIGR02168 170 YKERRKEtERKLERTREN----LDRLEDIL----NELERQLKSLERQAEKAERYkeLKAELRELELALL----------- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 284 rdlnmdcvVAEIKAQYDDVASRSRAEAEswYRTKCEEMKATVIRHGETLRRTREEMNELNRIIQRLTAEIENAKCQRAKL 363
Cdd:TIGR02168 231 --------VLRLEELREELEELQEELKE--AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 57012382 364 ETAVAEAEQQGEAALTD---ARGKLAELEAALQKAKQDMACLLKEYQEVMNSKLGLDIEIATYRRLLE 428
Cdd:TIGR02168 301 EQQKQILRERLANLERQleeLEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
295-428 |
1.19e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.77 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 295 IKAQYDDVASRSRAEA-ESWY--RTK-CEEMKATVIRHGETLRRTRE----EMNELNRIIQRLTAEIENAKCQRAKLETA 366
Cdd:smart00787 115 MDKQFQLVKTFARLEAkKMWYewRMKlLEGLKEGLDENLEGLKEDYKllmkELELLNSIKPKLRDRKDALEEELRQLKQL 194
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57012382 367 VAEAEQQGEAALTDARGKLAELEAALQKAKQDMACLLKEYQE-------VMNSKLGLDIEIATYRRLLE 428
Cdd:smart00787 195 EDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQEleskiedLTNKKSELNTEIAEAEKKLE 263
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
330-414 |
1.21e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 330 ETLRRTREEMNELNRIIQRLTAEIENAKCQRAKLET---AVAEAEQQGEAALTDARGKLAELEAALQKAKQDMACLLKEY 406
Cdd:COG4372 94 AELAQAQEELESLQEEAEELQEELEELQKERQDLEQqrkQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQEL 173
|
....*...
gi 57012382 407 QEVMNSKL 414
Cdd:COG4372 174 QALSEAEA 181
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
332-400 |
1.31e-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: 39.22 E-value: 1.31e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57012382 332 LRRTREEMNELNRIIQRLTAEIENAKCQRAKLETAVAEAEQQ---GEAALTDARGKLAELEAALQKAKQDMA 400
Cdd:pfam11559 47 RDRDLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLERElalLQAKERQLEKKLKTLEQKLKNEKEELQ 118
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
176-400 |
2.07e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 176 IETLRREAECVEADGGRLAAELNHVQEAMEGYKKRYEE----EVALR------ATAENEFVVLKKDVDCAYLRKSDLEAN 245
Cdd:PRK02224 215 LAELDEEIERYEEQREQARETRDEADEVLEEHEERREEletlEAEIEdlretiAETEREREELAEEVRDLRERLEELEEE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 246 VEALVEESSflkrLYEEEVRVLQAHISDTSVivKMDNSRDLNMDCVVA------EIKAQYDDVAS-RSRAEAEswyRTKC 318
Cdd:PRK02224 295 RDDLLAEAG----LDDADAEAVEARREELED--RDEELRDRLEECRVAaqahneEAESLREDADDlEERAEEL---REEA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 319 EEMKATVIRHGETLRRTREEMNELNRIIQRLTAEIENAKCQRAKLETAVAEAEqqgeAALTDARGKLAELEAALQKAKQD 398
Cdd:PRK02224 366 AELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELR----EERDELREREAELEATLRTARER 441
|
..
gi 57012382 399 MA 400
Cdd:PRK02224 442 VE 443
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
178-429 |
2.35e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 40.69 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 178 TLRREAeCVEADGGRLAAELNHVQEAMEGYKKRYEEEVALRATAENEFVVLKKDVDCAYLRKSDLEANVEALVEESSFLK 257
Cdd:PLN03188 875 AIRREM-ALEEFCTKQASEITQLNRLVQQYKHERECNAIIGQTREDKIIRLESLMDGVLSKEDFLEEELASLMHEHKLLK 953
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 258 RLYEEEVRVLQAHISDTSVIVKMDNSR---DLNMDCVVAE----IKAQ---YDDVASRSRAEAESWYRT--KCEEMKATV 325
Cdd:PLN03188 954 EKYENHPEVLRTKIELKRVQDELEHYRnfyDMGEREVLLEeiqdLRSQlqyYIDSSLPSARKRNSLLKLtySCEPSQAPP 1033
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 326 IrhgETLRRTREEMNELNRIIQRL---TAE---IENAKCQRAKLETAVAEAEQQGEAALTDARGKlAELEAALQKAKQDM 399
Cdd:PLN03188 1034 L---NTIPESTDESPEKKLEQERLrwtEAEskwISLAEELRTELDASRALAEKQKHELDTEKRCA-EELKEAMQMAMEGH 1109
|
250 260 270
....*....|....*....|....*....|
gi 57012382 400 ACLLKEYQEVMNSKLGLdieIATYRRLLEG 429
Cdd:PLN03188 1110 ARMLEQYADLEEKHIQL---LARHRRIQEG 1136
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
330-438 |
2.67e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 330 ETLRRTREEMNELNRIIQRLTAEIENAKCQR----------------AKLETAVAEAEQQgEAALTDARGKLAELEAALQ 393
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERRealqrlaeyswdeidvASAEREIAELEAE-LERLDASSDDLAALEEQLE 695
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 57012382 394 KAKQDMACLLKEYQEVMNSKLGLDIEIATYRRLLEGEEHRCQQLP 438
Cdd:COG4913 696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAE 740
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
293-400 |
3.03e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.28 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 293 AEIKAQYDDVASRSRAEAESwyrtkceemKATVIRHGETLR------RTREEMNELNRIIQRLTAEIENAKCQRAKLETA 366
Cdd:PRK11281 39 ADVQAQLDALNKQKLLEAED---------KLVQQDLEQTLAlldkidRQKEETEQLKQQLAQAPAKLRQAQAELEALKDD 109
|
90 100 110
....*....|....*....|....*....|....*.
gi 57012382 367 VAEAEQQGEAALTDAR--GKLAELEAALQKAKQDMA 400
Cdd:PRK11281 110 NDEETRETLSTLSLRQleSRLAQTLDQLQNAQNDLA 145
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
292-433 |
4.62e-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: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 292 VAEIKAQYDDVASRSRA----EAESWYRTKCEEMKATVIRHGETLRRTREEMNELNRI---IQRLTAEIENAKCQRAKLE 364
Cdd:COG4913 633 LEALEAELDALQERREAlqrlAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALeeqLEELEAELEELEEELDELK 712
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57012382 365 TAVAEAEQQGEAALTDARGKLAELEAALQKAKQDM-ACLLKEYQEVMNSKLG------LDIEIATYRRLLEGEEHR 433
Cdd:COG4913 713 GEIGRLEKELEQAEEELDELQDRLEAAEDLARLELrALLEERFAAALGDAVErelrenLEERIDALRARLNRAEEE 788
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
333-400 |
7.67e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 37.07 E-value: 7.67e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57012382 333 RRTREEMNELNriiQRLTAEIENAKCQRAK-LETAVAEAEQQGEAALTDARgklAELEAALQKAKQDMA 400
Cdd:COG0711 44 ERAKEEAEAAL---AEYEEKLAEARAEAAEiIAEARKEAEAIAEEAKAEAE---AEAERIIAQAEAEIE 106
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
176-396 |
8.15e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.89 E-value: 8.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 176 IETLRREAECVEADGGRLAAELNHVQEAMEGYKKRYEEevaLRATAEnEFVVLKKDVDcAYLRKSDLEanVEALVEESSF 255
Cdd:PRK03918 240 IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEE---LEEKVK-ELKELKEKAE-EYIKLSEFY--EEYLDELREI 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 256 LKRL--YEEEVRVLQAHISDTSvivkmdnsrdlNMDCVVAEIKAQYDDVaSRSRAEAESWYRtKCEEMKATVIRhgetLR 333
Cdd:PRK03918 313 EKRLsrLEEEINGIEERIKELE-----------EKEERLEELKKKLKEL-EKRLEELEERHE-LYEEAKAKKEE----LE 375
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57012382 334 RTREEMNELNriIQRLTAEIENAKcqRAKLEtaVAEAEQQGEAALTDARGKLAELEAA---LQKAK 396
Cdd:PRK03918 376 RLKKRLTGLT--PEKLEKELEELE--KAKEE--IEEEISKITARIGELKKEIKELKKAieeLKKAK 435
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
330-427 |
9.82e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.60 E-value: 9.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012382 330 ETLRRTREEMNELNRIIQRLTAEIENAK--CQRAKLETAVAEAEQQGEAA--LTDARGKLAELEAALQKAKQDMACLLKE 405
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQeeLEELLEQLSLATEEELQDLAeeLEELQQRLAELEEELEEAQEELEELEEE 228
|
90 100
....*....|....*....|....
gi 57012382 406 YQEVMNSKLGLDIE--IATYRRLL 427
Cdd:COG4717 229 LEQLENELEAAALEerLKEARLLL 252
|
|
| |
