|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
122-398 |
2.39e-10 |
|
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: 62.77 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 122 YDEMRQKIRQLtqELSVSHAQQEYLENHIQTQSSALDRFNAMNSALASDSIGLQKTLVDVTLENSNIKDQIRNLQQTYEA 201
Cdd:TIGR02168 215 YKELKAELREL--ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 202 SMDKLREKQRQLEVAQVENQLLKMKVESSQEANAEVMREmtkklysqyEEKLQEEQRKHSAEKEALLEETNSFLKAIEEA 281
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESK---------LDELAEELAELEEKLEELKEELESLEAELEEL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 282 NKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETemsgELTDSDKERYQQLEEASASLRERIRHLDDMVH 361
Cdd:TIGR02168 364 EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA----RLERLEDRRERLQQEIEELLKKLEEAELKELQ 439
|
250 260 270
....*....|....*....|....*....|....*..
gi 111494235 362 CQQKKVKQMVEennELQSRLDYLTETQAKTEVETREI 398
Cdd:TIGR02168 440 AELEELEEELE---ELQEELERLEEALEELREELEEA 473
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
108-398 |
4.75e-10 |
|
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: 62.00 E-value: 4.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 108 RATLEKVRKRMygdyDEMRQKIRQLTQELSVSHAQQEYLENHIQTQSSALDRFNAMNSALASDSIGLQKTLVDVTLENSN 187
Cdd:TIGR02168 676 RREIEELEEKI----EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 188 IKDQIRNLQQTYEASMDKLREKQRQLEVAQVENQLLKMKVESSQEANaevmremtkklySQYEEKLQEEQRKHSAEKEAL 267
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL------------KALREALDELRAELTLLNEEA 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 268 LEETNsflkAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMSGELtdsdkERYQQLEEASA 347
Cdd:TIGR02168 820 ANLRE----RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALL-----NERASLEEALA 890
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 111494235 348 SLRERIRHLDDMVHCQQKKVKQMVEENNELQSRLDYLTETQAKTEVETREI 398
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
93-386 |
7.64e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 7.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 93 STSQLKEEMNYIKDVRATLEKVRKRMYGDYDEMRQKIRQLTQELSVSHAQQEYLENHIQTQSSALDRFNAMNSALASDSI 172
Cdd:TIGR02168 706 ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 173 GLQKTLVDVTLENSNIKDQIRNLQ--------------QTYEASMDKLREKQRQLEVAQ---VENQLLKMKVESSQEANA 235
Cdd:TIGR02168 786 ELEAQIEQLKEELKALREALDELRaeltllneeaanlrERLESLERRIAATERRLEDLEeqiEELSEDIESLAAEIEELE 865
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 236 EVMREMTKKLysqyeEKLQEEQRKHSAEKEALLEETNSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQ 315
Cdd:TIGR02168 866 ELIEELESEL-----EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 111494235 316 LQLQLLEHEtEMSGELtdsDKERYQQLEEASASLRERIRHLddmvhcqQKKVKQM-------VEENNELQSRLDYLTE 386
Cdd:TIGR02168 941 LQERLSEEY-SLTLEE---AEALENKIEDDEEEARRRLKRL-------ENKIKELgpvnlaaIEEYEELKERYDFLTA 1007
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
174-398 |
8.00e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 8.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 174 LQKTLVDVTLENSNIKDQIRNLQQTYEASMDKLREKQRQLEVAQVENQLLKMKVEssQEANAEVMREMTKKLYSQYEEKL 253
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA--RLEQDIARLEERRRELEERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 254 QEEQRKHSAEKEALLEETNSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMSGELTD 333
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 111494235 334 ---------SDKERYQQLEEASASLRERIRHLDDMVHCQQKKVKQMVEENNELQSRLDYLTETQAKTEVETREI 398
Cdd:COG1196 402 leeleeaeeALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
105-393 |
3.55e-08 |
|
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: 55.83 E-value: 3.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 105 KDVRATLEKVRKRMYG-DYDEMRQKIRQLTQELSVSHAQQEYLENHIQTQSSALDRFNAMNSALASDSIGLQKTLVDVTL 183
Cdd:TIGR02168 216 KELKAELRELELALLVlRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 184 ENSNIKDQIRNLQQTYEASMDKLREKQRQLEVAQVENQLLKMKVESSQEANAEVMREMtkklysqyeeklqEEQRKHSAE 263
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL-------------ESLEAELEE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 264 KEALLEETNSFLKAIEEANKKMQAAEISLEEKdqrIGELDRLIERMEKERHQLQLQLLEHETEMSGELTDSD----KERY 339
Cdd:TIGR02168 363 LEAELEELESRLEELEEQLETLRSKVAQLELQ---IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeaelKELQ 439
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 111494235 340 QQLEEASASLRERIRHLDDMVHCQQKKVKQMVEENNELQSRLDYLTETQAKTEV 393
Cdd:TIGR02168 440 AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
104-347 |
6.73e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 6.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 104 IKDVRATLEKVRKRMYgdydEMRQKIRQLTQELSVSHAQQEYLENHIQTQSSALDRFNAMNSALASDSIGLQKTLVDVTL 183
Cdd:COG1196 262 LAELEAELEELRLELE----ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 184 ENSNIKDQIRNLQQTYEASMDKLREKQRQLEVAQVENQLLKMKVESSQEANAEVMREMTKKLysQYEEKLQEEQRKHSAE 263
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA--AQLEELEEAEEALLER 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 264 KEALLEETNSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMSGELTDSDKERYQQLE 343
Cdd:COG1196 416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
....
gi 111494235 344 EASA 347
Cdd:COG1196 496 LLEA 499
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
96-398 |
1.66e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.92 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 96 QLKEEMNYIKDVRATLEKVRKRMYGDYDEMRQKIRQLTQELSVSHAQQEYLENHIQTQSSALDRFNAMNSALASDSIGLQ 175
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 176 KTLVDVTLENSNIKDQIRNLQQT---YEASMDKLREKQRQLEVAQVENQLLKMKVESSQeaNAEVMREMTKKLYS-QYEE 251
Cdd:TIGR02169 751 QEIENVKSELKELEARIEELEEDlhkLEEALNDLEARLSHSRIPEIQAELSKLEEEVSR--IEARLREIEQKLNRlTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 252 KLQEEQRKHSAEKEALLEET-NSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMSGE 330
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQiKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEL 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 331 LTDSDKERYQ--QLEEASASLRERIRHLDDMVHCQQ---------KKVKQMV------------------EENNELQSRL 381
Cdd:TIGR02169 909 EAQIEKKRKRlsELKAKLEALEEELSEIEDPKGEDEeipeeelslEDVQAELqrveeeiralepvnmlaiQEYEEVLKRL 988
|
330
....*....|....*..
gi 111494235 382 DYLTETQAKTEVETREI 398
Cdd:TIGR02169 989 DELKEKRAKLEEERKAI 1005
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
180-398 |
1.78e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 180 DVTLENSNIKDQIRNLQQTYEASMDKLREKQRQLEVAQVENQLLKMKVESSQEANAEVMREMTKklySQYEEKLQEEQRK 259
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR---LEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 260 HSAEKEALLEEtnsflkAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMSGELTDSDKERY 339
Cdd:COG1196 313 ELEERLEELEE------ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 111494235 340 QQLEEASA--SLRERIRHLDDMVHCQQKKVKQMVEENNELQSRLDYLTETQAKTEVETREI 398
Cdd:COG1196 387 ELLEALRAaaELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
95-359 |
7.02e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.53 E-value: 7.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 95 SQLKEEMNYIKDVRATLEKVRKRMYGDYDEMRQKIRQLTQELSVSHAQQ-----EYLENHIQTQSSALDRFNAMNSALAS 169
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEiqaelSKLEEEVSRIEARLREIEQKLNRLTL 826
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 170 DSIGLQKTLVDVTLENSNIKDQIRNLQQTYEASMDKLREKQRQLE-----VAQVENQLLKMKVESSQ-EANAEVMREMTK 243
Cdd:TIGR02169 827 EKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEeleaaLRDLESRLGDLKKERDElEAQLRELERKIE 906
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 244 KLYSQYEEKlqeeqRKHSAEKEALLEETNSFLKAIEEANKKMQ---AAEISLEEKDQRIGELDRLIERMEkERHQLQLQL 320
Cdd:TIGR02169 907 ELEAQIEKK-----RKRLSELKAKLEALEEELSEIEDPKGEDEeipEEELSLEDVQAELQRVEEEIRALE-PVNMLAIQE 980
|
250 260 270
....*....|....*....|....*....|....*....
gi 111494235 321 LEHETEMSGELtdsdKERYQQLEEASASLRERIRHLDDM 359
Cdd:TIGR02169 981 YEEVLKRLDEL----KEKRAKLEEERKAILERIEEYEKK 1015
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
189-397 |
2.81e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 189 KDQIRNLQQTYEASMDKLREKQRQLEVAQVENQLLKMKVESSQEANAEVMR-------EMTKKLYSQYEEKLQEEQRKHS 261
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKaeelkkaEEEKKKVEQLKKKEAEEKKKAE 1650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 262 AEKEallEETNSFLKAIEEANK----KMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMSGELTDSDKE 337
Cdd:PTZ00121 1651 ELKK---AEEENKIKAAEEAKKaeedKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEE 1727
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 111494235 338 RYQQLEEASASLRERIRHLDDMV--HCQQKKVKQMVEENNELQSRLDYLTETQAKTEVETRE 397
Cdd:PTZ00121 1728 NKIKAEEAKKEAEEDKKKAEEAKkdEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEED 1789
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
95-313 |
3.51e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 3.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 95 SQLKEEMNYIKDVRATLEKVRKRMYGDYDEMRQKIRQLTQELSVshaqqeyLENHIQTQSSALDRFNAMNSALASDSIGL 174
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRA-------LEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 175 QKTLvdvtlensniKDQIRNLQQTYEASMDKLREKQRQLEVAQVENQLLKmKVESSQEANAEVMREMTKKLYSQYEE--- 251
Cdd:COG4942 103 KEEL----------AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLK-YLAPARREQAEELRADLAELAALRAElea 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 111494235 252 ---KLQEEQRKHSAEKEALLEETNSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKER 313
Cdd:COG4942 172 eraELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
96-386 |
8.63e-05 |
|
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: 45.10 E-value: 8.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 96 QLKEEMNYIKDVRATLEKVRKRMygdyDEMRQKIRQLTQELSVSHAQQEYLENHIQTQSSALDRFNAMNSALASDSIGLQ 175
Cdd:pfam05483 248 QITEKENKMKDLTFLLEESRDKA----NQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIAT 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 176 KTLVDVTLENSNIKDQIRNLQQTYEASMDK-----------LREKQRQLEVAQVENQLLKMKVESSQEAnaevMREMTKk 244
Cdd:pfam05483 324 KTICQLTEEKEAQMEELNKAKAAHSFVVTEfeattcsleelLRTEQQRLEKNEDQLKIITMELQKKSSE----LEEMTK- 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 245 lYSQYEEKLQEEQRKHSAEKEALLEETNSFLKAIEEANKKMQaaeisleekdqrigELDRLIERMEKERHQLQLQL---- 320
Cdd:pfam05483 399 -FKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQ--------------ELIFLLQAREKEIHDLEIQLtaik 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 321 ----------------LEHETEMSGELT-DSDK---ERYQQLEEASASLRERIRHLDDMVHCQQ------KKVKQMVEEN 374
Cdd:pfam05483 464 tseehylkevedlkteLEKEKLKNIELTaHCDKlllENKELTQEASDMTLELKKHQEDIINCKKqeermlKQIENLEEKE 543
|
330
....*....|..
gi 111494235 375 NELQSRLDYLTE 386
Cdd:pfam05483 544 MNLRDELESVRE 555
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
95-297 |
1.07e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 95 SQLKEEMNYIKDVRATLEKVRKRMYGDYDEMRQKIRQLTQELSVSHAQQEYLENHIQTQSSALDRFNAMNSALASDS--I 172
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALyrS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 173 GLQKTLVDVTLENSNIKDQIRNLQ-------------QTYEASMDKLREKQRQLEVAQVENQLLKMKVESSQEANAEVMR 239
Cdd:COG3883 99 GGSVSYLDVLLGSESFSDFLDRLSalskiadadadllEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 111494235 240 EMTKKLysqyeEKLQEEQRKHSAEKEALLEETNSFLKAIEEANKKMQAAEISLEEKDQ 297
Cdd:COG3883 179 EQEALL-----AQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
178-357 |
1.13e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 178 LVDVTLENSNIKDQIRNLQQTYEASMDKLREKQRQLEvaQVENQLLKMKVESSQEANAEVMREMTKKLY---SQYEEKLQ 254
Cdd:COG3206 207 LVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA--ALRAQLGSGPDALPELLQSPVIQQLRAQLAeleAELAELSA 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 255 EEQRKHSA--EKEALLEETNSFLKaiEEANKKMQAAEISLEEKDQRIGELDRLIERMEKE-----RHQLQLQLLEHETEM 327
Cdd:COG3206 285 RYTPNHPDviALRAQIAALRAQLQ--QEAQRILASLEAELEALQAREASLQAQLAQLEARlaelpELEAELRRLEREVEV 362
|
170 180 190
....*....|....*....|....*....|
gi 111494235 328 SGELTDSDKERYQQLEEASASLRERIRHLD 357
Cdd:COG3206 363 ARELYESLLQRLEEARLAEALTVGNVRVID 392
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
89-359 |
1.18e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 89 VYGWSTSQLKEEmnyIKDVRATLEKVRKRMYGDYDEMRQKIRQLTQELSVSHAQQEY---------LENHIQTQSSALDR 159
Cdd:COG4913 603 VLGFDNRAKLAA---LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYswdeidvasAEREIAELEAELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 160 FNAMNSALAsdsiGLQKTLVDVTLENSNIKDQIRNLQQTYEASMDKLREKQRQLEVAQVENQLLKMKVESSQEANAEVMR 239
Cdd:COG4913 680 LDASSDDLA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERF 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 240 --EMTKKLYSQYEEKLQEEQRKHSAEKEALLEEtnsFLKAIEEANKK----MQAAEISLEEKDQRIGELDRLI-ERMEKE 312
Cdd:COG4913 756 aaALGDAVERELRENLEERIDALRARLNRAEEE---LERAMRAFNREwpaeTADLDADLESLPEYLALLDRLEeDGLPEY 832
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 111494235 313 RHQLQLQLLEHETEMSGELtdsdkerYQQLEEASASLRERIRHLDDM 359
Cdd:COG4913 833 EERFKELLNENSIEFVADL-------LSKLRRAIREIKERIDPLNDS 872
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
95-394 |
1.26e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.24 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 95 SQLKEEMNYIKDVRATLEKVRKRMYGDYDEMRQKIRQLTQELSVshaQQEYLENHIQTQSSALDrFNAMNSALASDSIGL 174
Cdd:TIGR04523 162 NDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSN---LKKKIQKNKSLESQISE-LKKQNNQLKDNIEKK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 175 QKTLVDVTLENSNIKDQIRNLQQTYEASMDKLREKQRQLEVA-----QVENQLLKMKVESS---QEANAEVMREMTKKLY 246
Cdd:TIGR04523 238 QQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNnkkikELEKQLNQLKSEISdlnNQKEQDWNKELKSELK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 247 SQyEEKLQEEQRKHSAEKEALleetNSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETE 326
Cdd:TIGR04523 318 NQ-EKKLEEIQNQISQNNKII----SQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQ 392
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 111494235 327 MSgeltdSDKERYQQLEEASASLRERIRHLDDMVHCQQKKVKQMVEENNELQSRLDYLTETQAKTEVE 394
Cdd:TIGR04523 393 IN-----DLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI 455
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
204-381 |
2.01e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 204 DKLREKQRQL-----EVAQVENQLLKMKVESSQ-EANAEVMREMTKKLYSQYE-EKLQEEQRKHSAEKEALlEETNSFLK 276
Cdd:COG4913 610 AKLAALEAELaeleeELAEAEERLEALEAELDAlQERREALQRLAEYSWDEIDvASAEREIAELEAELERL-DASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 277 AIEEankKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMSGELTDSDKERYQQLEEASASLRERiRHL 356
Cdd:COG4913 689 ALEE---QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGD-AVE 764
|
170 180
....*....|....*....|....*
gi 111494235 357 DDMVHCQQKKVKQMVEENNELQSRL 381
Cdd:COG4913 765 RELRENLEERIDALRARLNRAEEEL 789
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
206-360 |
2.73e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 206 LREKQRQLEVAQVENQLLKMKVESSQEANAEVMREMTKKLYSQYEEKLQEEQRKHSAEKEALLEETNSFLKAIEEANKKM 285
Cdd:COG1196 676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 286 QAAEISLEEKDQRIGELDRLIERME-------------KERHQlqlqllehetEMSGELTDsdkeryqqLEEASASLRER 352
Cdd:COG1196 756 LPEPPDLEELERELERLEREIEALGpvnllaieeyeelEERYD----------FLSEQRED--------LEEARETLEEA 817
|
....*...
gi 111494235 353 IRHLDDMV 360
Cdd:COG1196 818 IEEIDRET 825
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
204-393 |
2.79e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 43.35 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 204 DKLREKQRQLEVAQVENQLlKMKVESSQEANAEVMREMTKKLYSQY-EEKLQEEQRKHSAEKE-ALLEETNSFLKAIEEA 281
Cdd:PLN02939 166 EALQGKINILEMRLSETDA-RIKLAAQEKIHVEILEEQLEKLRNELlIRGATEGLCVHSLSKElDVLKEENMLLKDDIQF 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 282 nkkmqaaeisLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMSGELTDSDKERYQQLEeasaSLRERIRHLDDMVH 361
Cdd:PLN02939 245 ----------LKAELIEVAETEERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSPLQYD----CWWEKVENLQDLLD 310
|
170 180 190
....*....|....*....|....*....|....*
gi 111494235 362 CQQKKVKQMV---EENNELQSRLDYLTETQAKTEV 393
Cdd:PLN02939 311 RATNQVEKAAlvlDQNQDLRDKVDKLEASLKEANV 345
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
127-348 |
3.59e-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: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 127 QKIRQLTQELSVSHAQQEYLENHIQTQSSALDRFNAMNSALASDSIGLQKTLVDVTLENSNIKDQIRNLQQTYEASMDKL 206
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 207 REKQ----RQLEVAQVENQLLKMKV-ESSQEANAEVMREMTKKLYSQYEEKLQEEQRKHSAEKEALLEETNSFLKAIEEA 281
Cdd:COG4942 100 EAQKeelaELLRALYRLGRQPPLALlLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 111494235 282 NKKMQAAEISLE-EKDQRIGELDRLIERMEKERHQLQlQLLEHETEMSGELTDSDKERYQQLEEASAS 348
Cdd:COG4942 180 LAELEEERAALEaLKAERQKLLARLEKELAELAAELA-ELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
251-398 |
3.68e-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: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 251 EKLQEEQRKHSAEKEALLEETNSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMSGE 330
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 111494235 331 LTDSDK-ERYQQL------EEASASLReRIRHLDDMVHCQQKKVKQMVEENNELQSRLDYLTETQAKTEVETREI 398
Cdd:COG4942 110 LRALYRlGRQPPLalllspEDFLDAVR-RLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
186-399 |
4.03e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 186 SNIKDQIRNLQQTYEA---SMDKLREKQRQL--EVAQVENQLLKMKVESSQEANAEVMREMTKKLYSQYEEKLQ--EEQR 258
Cdd:PRK03918 189 ENIEELIKEKEKELEEvlrEINEISSELPELreELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRelEERI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 259 KHSAEKEALLEETNSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQL--LEHETEMSGELTDSDK 336
Cdd:PRK03918 269 EELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIkeLEEKEERLEELKKKLK 348
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 111494235 337 ERYQQLEEASASLRERIRHLDDMVHCQQKKVKQMVEENNELQSRLDYLTETQAKTEVETREIG 399
Cdd:PRK03918 349 ELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKIT 411
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
258-393 |
5.94e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 5.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 258 RKHSAEKEALLEEtNSFLKAIEEANKKMQAA--EISLEEKD---QRIGELDRLIERMEKERHQLQLQLLEHETEMSGELT 332
Cdd:PRK12704 25 RKKIAEAKIKEAE-EEAKRILEEAKKEAEAIkkEALLEAKEeihKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 111494235 333 DSDKERyQQLEEASASLRERIRHLDDmvhcQQKKVKQMVEENNELQSRLDYLTETQAKTEV 393
Cdd:PRK12704 104 LLEKRE-EELEKKEKELEQKQQELEK----KEEELEELIEEQLQELERISGLTAEEAKEIL 159
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
186-379 |
6.53e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 6.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 186 SNIKDQIRNLQQTYEASMDKLREKQRQLEVAQVENQLLKMKVESSQEANAEVMR-EMTKKLYSQYEEKLQEEQRkhsaEK 264
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyIKLSEFYEEYLDELREIEK----RL 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 265 EALLEETNSFLKAIEEANKKmqaaEISLEEKDQRIGELDRLIERMEK------ERHQLQLQLLEHETEMSGELTDSDKER 338
Cdd:PRK03918 317 SRLEEEINGIEERIKELEEK----EERLEELKKKLKELEKRLEELEErhelyeEAKAKKEELERLKKRLTGLTPEKLEKE 392
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 111494235 339 YQQLEEASASLRERIRHLDDMVHCQQKKVKQMVEENNELQS 379
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK 433
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
203-317 |
8.62e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.84 E-value: 8.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 203 MDKLREKQRQLEVAQVENqllkMKVESSQEANAEVMREMTK--------KLYSQYEEKLQEEQRKHSAEK-EALLEETNS 273
Cdd:PRK05771 18 KDEVLEALHELGVVHIED----LKEELSNERLRKLRSLLTKlsealdklRSYLPKLNPLREEKKKVSVKSlEELIKDVEE 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 111494235 274 FLKAIEEankkmqaaeiSLEEKDQRIGELDRLIERMEKERHQLQ 317
Cdd:PRK05771 94 ELEKIEK----------EIKELEEEISELENEIKELEQEIERLE 127
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
96-394 |
1.18e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.26 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 96 QLKEEMNYIKDVRATLEKVRKrMYGDYDEMRQKIRQLTQELSvshAQQEYLENHIQTQSSaldrfnaMNSALASDSIGLQ 175
Cdd:pfam15921 445 QMERQMAAIQGKNESLEKVSS-LTAQLESTKEMLRKVVEELT---AKKMTLESSERTVSD-------LTASLQEKERAIE 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 176 KTLVDVTLENSNIKDQIRNLQQtyeasmdkLREKQRQLEVAQVENQLLKMKVeSSQEANAEVMRemtkklysQYEEKLQE 255
Cdd:pfam15921 514 ATNAEITKLRSRVDLKLQELQH--------LKNEGDHLRNVQTECEALKLQM-AEKDKVIEILR--------QQIENMTQ 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 256 EQRKHSAEKEALLEETNSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERhqlqLQLLEHETEMSGELTDSD 335
Cdd:pfam15921 577 LVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEK----VKLVNAGSERLRAVKDIK 652
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 111494235 336 KERYQQLEEASASlRERIRHLDDMVHCQQKKVKQMVEENNELQSRLDYLTETqAKTEVE 394
Cdd:pfam15921 653 QERDQLLNEVKTS-RNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKS-AQSELE 709
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
208-398 |
1.32e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.26 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 208 EKQRQLEVAQVENQLLKMKVESSQEANAEVMREMTKKLYSQYEEKLQ----EEQRKHSAEKEALLEETNSFLKAIEEANK 283
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARqaemDRQAAIYAEQERMAMERERELERIRQEER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 284 KMQAAEISLEE---KDQRIGELDRL-IER-------------------MEKERHQLQLQLLEHETEMSGELTDSDKERYQ 340
Cdd:pfam17380 359 KRELERIRQEEiamEISRMRELERLqMERqqknervrqeleaarkvkiLEEERQRKIQQQKVEMEQIRAEQEEARQREVR 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 111494235 341 QLEEASASLRERIRHLDDMVHCQQKKVKQMVEENNELQSRLDYLTETQAKTEVETREI 398
Cdd:pfam17380 439 RLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKI 496
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
122-397 |
1.42e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.88 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 122 YDEMRQ-KIRQLTQELSVSHAQQEYLENHIQTQSSALDRFNAMNSALASDSIGLQKTLVDVTLEnsnikDQIRNLQQTYE 200
Cdd:pfam17380 293 FEKMEQeRLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQE-----ERKRELERIRQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 201 ASMDKLREKQRQLEVAQVENQL--------------LKMKVESSQEANAEVMREMtKKLYSQYEEKLQEEQRKHSAEKEA 266
Cdd:pfam17380 368 EEIAMEISRMRELERLQMERQQknervrqeleaarkVKILEEERQRKIQQQKVEM-EQIRAEQEEARQREVRRLEEERAR 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 267 LLEETNsflkaIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKER-HQLQLQLLEHETEMSGELTDSDKERYQQLEEA 345
Cdd:pfam17380 447 EMERVR-----LEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRaEEQRRKILEKELEERKQAMIEEERKRKLLEKE 521
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 111494235 346 SASLRERIRHLDDMVHCQQKKVKQM-VEENNELQSRLDYLTETQAKTEVETRE 397
Cdd:pfam17380 522 MEERQKAIYEEERRREAEEERRKQQeMEERRRIQEQMRKATEERSRLEAMERE 574
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
128-338 |
2.25e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.38 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 128 KIRQLTQELSVSHAQQEYLENHIQTQSSALDRFNAMNSALASDSIGLQKTLV----DVTLENSNIKDQIRNL---QQTYE 200
Cdd:PHA02562 175 KIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVeeakTIKAEIEELTDELLNLvmdIEDPS 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 201 ASMDKLREKQRQLEvAQVE--NQLLKMKVESSQEANAEVMREMTKKLYSQYEEKLQEEQRKHSAEKEAlLEETNSFLKAI 278
Cdd:PHA02562 255 AALNKLNTAAAKIK-SKIEqfQKVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTA-IDELEEIMDEF 332
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 111494235 279 EEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMSG---ELTDSDKER 338
Cdd:PHA02562 333 NEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKlqdELDKIVKTK 395
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
160-351 |
2.40e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 160 FNAMNSALASDSIG-LQKTLVDVTLENSNIKDQIRNLQQTYEASMDKLREKQRQLEVAQVENQLLKMKVESSQEANAEVM 238
Cdd:COG3883 6 LAAPTPAFADPQIQaKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 239 REMTKKLYSQYEEKLQeeqrkhSAEKEALLEETN--------SFLKAIEEANKKM----QAAEISLEEK----DQRIGEL 302
Cdd:COG3883 86 EELGERARALYRSGGS------VSYLDVLLGSESfsdfldrlSALSKIADADADLleelKADKAELEAKkaelEAKLAEL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 111494235 303 DRLIERMEKERHQLQLQLLEHETEMSgELTDSDKERYQQLEEASASLRE 351
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLA-QLSAEEAAAEAQLAELEAELAA 207
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
95-370 |
2.65e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.11 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 95 SQLKEEMNYIKDVRATLEKVRKRMYGdYDEMRQKIRQLTQELSVSHAQQEYLENHIQTQSSALDRFNAMNSALASDSiGL 174
Cdd:pfam05557 125 LELQSTNSELEELQERLDLLKAKASE-AEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARIP-EL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 175 QKTLVDVTLENSNIKDQIRNLQ------QTYEASMDKLREKQRQLEVAQVENQLLKMKVESSQEANAEVMREM-TKKLYS 247
Cdd:pfam05557 203 EKELERLREHNKHLNENIENKLllkeevEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLrSPEDLS 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 248 QYEEKLQEEQRKHSAEKEALLEETNSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKerhqlQLQLLEHETEM 327
Cdd:pfam05557 283 RRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQR-----RVLLLTKERDG 357
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 111494235 328 SGELTDS-DKEryQQLEEASASLRERIRHLDDMVHCQQKKVKQM 370
Cdd:pfam05557 358 YRAILESyDKE--LTMSNYSPQLLERIEEAEDMTQKMQAHNEEM 399
|
|
| TOPEUc |
smart00435 |
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
171-297 |
2.65e-03 |
|
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras
Pssm-ID: 214661 [Multi-domain] Cd Length: 391 Bit Score: 40.03 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 171 SIGLQKTLVDVTLENSNIKDQI-----------------RNLQQTYEASMDKLREKQRQLEvaqveNQLLKMKVessqea 233
Cdd:smart00435 230 SITLQEQLKELTAKDGNVAEKIlaynranrevailcnhqRTVSKTHEKSMEKLQEKIKALK-----YQLKRLKK------ 298
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 111494235 234 nAEVMREMTKKLYSQYEEKLQEEQRKHSAEKEALLEETNSFL---KAIEEANKKMQAAEISLEEKDQ 297
Cdd:smart00435 299 -MILLFEMISDLKRKLKSKFERDNEKLDAEVKEKKKEKKKEEkkkKQIERLEERIEKLEVQATDKEE 364
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
136-356 |
3.19e-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: 39.75 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 136 LSVSHAQQEYLENHIQTQSSALDRFNAMNSALA---SDSIGLQKTLVDVTLENSNIKDQIRNLQQTYEASMDKLREKQRQ 212
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAalkKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 213 LEVaqvenqlLKMKVESSQEANAEVMREMTK-KLYSQYEEKLQEEQRKHSAEKEALLEETNSFLKA-IEEANKKMQAAEI 290
Cdd:COG4942 92 IAE-------LRAELEAQKEELAELLRALYRlGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREqAEELRADLAELAA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 111494235 291 SLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMSG--ELTDSDKERYQQLEEASASLRERIRHL 356
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARleKELAELAAELAELQQEAEELEALIARL 232
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
97-394 |
3.43e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 40.04 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 97 LKEEMNYIKDVRATLEKVRK--RMYGDY----DEMRQKIRQLTQE-------LSVSHAQQEYLE--NHIQTQSSAL---- 157
Cdd:PRK10929 50 LQSALNWLEERKGSLERAKQyqQVIDNFpklsAELRQQLNNERDEprsvppnMSTDALEQEILQvsSQLLEKSRQAqqeq 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 158 DRFNAMnsalaSDSIG-LQKTLVDVTLENSNIKDQIRNLQQTYEAsmdklrEKQRQLEVAQVENQLLKMKV---ESSQ-E 232
Cdd:PRK10929 130 DRAREI-----SDSLSqLPQQQTEARRQLNEIERRLQTLGTPNTP------LAQAQLTALQAESAALKALVdelELAQlS 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 233 AN--AEVMR---EMTKKLYSQYEEKLQE------EQRKHSAEK-----EALLEETNSFLKAIEEANKKMQAAEISLEEKD 296
Cdd:PRK10929 199 ANnrQELARlrsELAKKRSQQLDAYLQAlrnqlnSQRQREAERalestELLAEQSGDLPKSIVAQFKINRELSQALNQQA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 297 QRIgelDRLIERMEKERHQ-LQL-QLLEHETEMSGELTDS---------------DKERYQQLEEASASLRERIRHLDDM 359
Cdd:PRK10929 279 QRM---DLIASQQRQAASQtLQVrQALNTLREQSQWLGVSnalgealraqvarlpEMPKPQQLDTEMAQLRVQRLRYEDL 355
|
330 340 350
....*....|....*....|....*....|....*
gi 111494235 360 VHCQQKKVKQMVEENNELQSRLDYLTETQAKTEVE 394
Cdd:PRK10929 356 LNKQPQLRQIRQADGQPLTAEQNRILDAQLRTQRE 390
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
218-373 |
3.72e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.38 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 218 VENQLLKMKVESSQEANAEVMREMTKKLYSQYEEKLQEEQRKHSAEKEALLEETNSFLKAIEEANKKMQAAEISLEEKDQ 297
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 298 RIGELDRLIERMEKERHQLQLQLLEHETEMSGELTDSDK--ERYQQL--EEASASLRERIRhlDDMVHCQQKKVKQMVEE 373
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQelERISGLtaEEAKEILLEKVE--EEARHEAAVLIKEIEEE 181
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
160-405 |
4.71e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 39.23 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 160 FNAMNSALASDSIGLQKTLVDVTLENSNIKDQIrNLQQTYEASMDKL-----REKQRQLEVAQVENQLLKMKVESSQEAN 234
Cdd:PHA02562 165 LSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQI-KTYNKNIEEQRKKngeniARKQNKYDELVEEAKTIKAEIEELTDEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 235 AEVMREMTKklYSQYEEKLQEEQRKHSAEKEALLEETNSFLK---------AIEEANKKMQAAEISLEEKDQRIGELDRL 305
Cdd:PHA02562 244 LNLVMDIED--PSAALNKLNTAAAKIKSKIEQFQKVIKMYEKggvcptctqQISEGPDRITKIKDKLKELQHSLEKLDTA 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 306 IERMEKERHQLqlqlleheTEMSGELTDSdKERYQQLEEASASLRERIRHLDDMVHCQQKKVKQMVEENNELQSRLDYLT 385
Cdd:PHA02562 322 IDELEEIMDEF--------NEQSKKLLEL-KNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIV 392
|
250 260
....*....|....*....|
gi 111494235 386 ETQAKTEVETREIGVGCDLL 405
Cdd:PHA02562 393 KTKSELVKEKYHRGIVTDLL 412
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
205-384 |
4.78e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.28 E-value: 4.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 205 KLREKQRQLEVAQVENQLLKMKVESSQeanAEVMREMTKKL--YSQYE-----EKLQEEQRKHSAEKEALLEETNSFLKA 277
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREK---AERYQALLKEKreYEGYEllkekEALERQKEAIERQLASLEEELEKLTEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 278 IEEANKKMQAAEISLEEKDQRI-----GELDRLIERMEK---ERHQLQLQLLEHETEMSgeltDSDKERyQQLEEASASL 349
Cdd:TIGR02169 260 ISELEKRLEEIEQLLEELNKKIkdlgeEEQLRVKEKIGEleaEIASLERSIAEKERELE----DAEERL-AKLEAEIDKL 334
|
170 180 190
....*....|....*....|....*....|....*
gi 111494235 350 RERIRHLDDMVHCQQKKVKQMVEENNELQSRLDYL 384
Cdd:TIGR02169 335 LAEIEELEREIEEERKRRDKLTEEYAELKEELEDL 369
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
229-356 |
5.07e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 38.81 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 229 SSQEANAEVMREMTKKLYSQyeEKLQEEQRkhsAEKEALLEETNSFLKAIEEANKKMQAAEISLEEkdqrigELDRLIER 308
Cdd:pfam02841 183 QSKEAVEEAILQTDQALTAK--EKAIEAER---AKAEAAEAEQELLREKQKEEEQMMEAQERSYQE------HVKQLIEK 251
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 111494235 309 MEKERHQLQLQ---LLEHETEMSGELtdsdkeRYQQLEEASASLRERIRHL 356
Cdd:pfam02841 252 MEAEREQLLAEqerMLEHKLQEQEEL------LKEGFKTEAESLQKEIQDL 296
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
251-397 |
7.74e-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: 38.21 E-value: 7.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 251 EKLQEEQRKHSAEKEALLEETNSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQ------------- 317
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKeelaellralyrl 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 318 ---------------------LQLLEHETEMSGELTDSDKERYQQLEEASASLRERIRHLDDMVHCQQKKVKQMVEENNE 376
Cdd:COG4942 117 grqpplalllspedfldavrrLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAE 196
|
170 180
....*....|....*....|.
gi 111494235 377 LQSRLDYLTETQAKTEVETRE 397
Cdd:COG4942 197 RQKLLARLEKELAELAAELAE 217
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
188-354 |
9.97e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 37.60 E-value: 9.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 188 IKDQIRNLQQTYEASMDKLREKQRQLEVAQVENQLLKMKVESSQEANAEVMREMtkklysqyeEKLQEEQRKHSAEKE-- 265
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI---------KKYEEQLGNVRNNKEye 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111494235 266 ALLEETNSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMSGELTDSDKERYQQLEEA 345
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
170
....*....|..
gi 111494235 346 SASLR---ERIR 354
Cdd:COG1579 173 PPELLalyERIR 184
|
|
| |
