|
Name |
Accession |
Description |
Interval |
E-value |
| GCOM2 |
pfam15328 |
Putative GRINL1B complex locus protein 2; This protein family is named Putative GRINL1B ... |
435-638 |
1.10e-87 |
|
Putative GRINL1B complex locus protein 2; This protein family is named Putative GRINL1B complex locus protein 2. GRINL1B is short for: glutamate receptor, ionotropic, N-methyl D-aspartate-like 1B. The name indicates what sort of receptor it is thought to be, a ligand gated ion channel specific to the neurotransmitter Glutamate. This family of proteins is found in eukaryotes. Proteins in this family are typically between 325 and 463 amino acids in length. The protein is thought to be the product of a pseudogene with a role in helping assemble a gene transcription unit.
Pssm-ID: 464649 Cd Length: 214 Bit Score: 275.49 E-value: 1.10e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 435 RKFICKLPDKGKKIFDSFAKLKAAIAECEEVRRKSELFNPVSLDCKLRQKAIAEVdVGTDKAQNSDPILDTSSLVPGCSS 514
Cdd:pfam15328 12 KKFICKLPDKGKKILDFVEKLKAAIAEREEVERTAELLSPVNIDSKGKQKATALV-LDSDKAQNSDQLLDTSSGTPHSSS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 515 VDNIKSSQT-SQNQGLGRPTLEGDEETSEVEYTVNKGPASSnRDRVPPSSEASEHHPRHRVSSQAEDTSSSFDNLFIDRL 593
Cdd:pfam15328 91 VDVIKPSKTlSTQQDLAHIEEFGTEEAPESEYTVNKCPASS-RASATSPSEASEILPQHGVSKQAEDLSSSSDNLLIDAL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 553726985 594 QRITIADQGEQQSEENASTKNLTGLSSGTEKKPHYMEVLEMRAKN 638
Cdd:pfam15328 170 QRITIADTEEHHSEENTSAEEKFGLRSGPPKKPHYMEVLEMRAKN 214
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
122-426 |
4.66e-12 |
|
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: 69.70 E-value: 4.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 122 YDEMRQKIRQLtqELSVSHAQQEYLENHIQTQSSALDRFNAMNSALASDSIGLQKTLVDVTLENSNIKDQIRNLQQTYEA 201
Cdd:TIGR02168 215 YKELKAELREL--ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 202 SMDKLREKQRQLEVAQVENQLLKMKVESSQEANAEVMREmtkklysqyEEKLQEEQRKHSAEKEALLEETNSFLKAIEEA 281
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESK---------LDELAEELAELEEKLEELKEELESLEAELEEL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 282 NKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETemsgELTDSDKERYQQLEEASASLRERIRHLDDMVH 361
Cdd:TIGR02168 364 EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA----RLERLEDRRERLQQEIEELLKKLEEAELKELQ 439
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 553726985 362 CQQKKVKQMVEEIESLKKKLQQKQLLILQLLEKIS----FLEGENNELQSRLDYLTETQAKTEVETREI 426
Cdd:TIGR02168 440 AELEELEEELEELQEELERLEEALEELREELEEAEqaldAAERELAQLQARLDSLERLQENLEGFSEGV 508
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
96-449 |
2.29e-09 |
|
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: 61.24 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 96 QLKEEMNYIKDVRATLEKVRKRMYGDYDEMRQKIRQLTQELSVSHAQQEYLENHIQTQSSALDRFNAMNSALASDSIGLQ 175
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 176 KTLVDVTLENSNIKDQIRNLQQT---YEASMDKLREKQRQLEVAQVENQLLKMKVESSQeaNAEVMREMTKKLYS-QYEE 251
Cdd:TIGR02169 751 QEIENVKSELKELEARIEELEEDlhkLEEALNDLEARLSHSRIPEIQAELSKLEEEVSR--IEARLREIEQKLNRlTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 252 KLQEEQRKHSAEKEALLEET-NSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMSGE 330
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQiKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEL 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 331 LTDSDKERYQ--QLEEASASLRERIRHLDDMVHCQQ---------KKVKQMVEEIEslkkklqqkqllilqllEKISFLE 399
Cdd:TIGR02169 909 EAQIEKKRKRlsELKAKLEALEEELSEIEDPKGEDEeipeeelslEDVQAELQRVE-----------------EEIRALE 971
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 553726985 400 GENN-------ELQSRLDYLTETQAKTEVETREIgvgcdllpRKFICKLPDKGKKIF 449
Cdd:TIGR02169 972 PVNMlaiqeyeEVLKRLDELKEKRAKLEEERKAI--------LERIEEYEKKKREVF 1020
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
180-426 |
1.29e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 180 DVTLENSNIKDQIRNLQQTYEASMDKLREKQRQLEVAQVENQLLKMKVESSQEANAEVMREMTKklySQYEEKLQEEQRK 259
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR---LEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 260 HSAEKEALLEEtnsflkAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMSGELTDSDKERY 339
Cdd:COG1196 313 ELEERLEELEE------ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 340 QQLEEASA--SLRERIRHLDDMVHCQQKKVKQMVEEIESLKKKLQQKQLLILQLLEKISFLEGENNELQSRLDYLTETQA 417
Cdd:COG1196 387 ELLEALRAaaELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
....*....
gi 553726985 418 KTEVETREI 426
Cdd:COG1196 467 ELLEEAALL 475
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
108-375 |
1.71e-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: 58.14 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 108 RATLEKVRKRMygdyDEMRQKIRQLTQELSVSHAQQEYLENHIQTQSSALDRFNAMNSALASDSIGLQKTLVDVTLENSN 187
Cdd:TIGR02168 676 RREIEELEEKI----EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 188 IKDQIRNLQQTYEASMDKLREKQRQLEVAQVENQLLKMKVESSQEANaevmremtkklySQYEEKLQEEQRKHSAEKEAL 267
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL------------KALREALDELRAELTLLNEEA 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 268 LEETNsflkAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMSGELtdsdkERYQQLEEASA 347
Cdd:TIGR02168 820 ANLRE----RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALL-----NERASLEEALA 890
|
250 260
....*....|....*....|....*...
gi 553726985 348 SLRERIRHLDDMVHCQQKKVKQMVEEIE 375
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELE 918
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
174-418 |
1.93e-08 |
|
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: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 174 LQKTLVDVTLENSNIKDQIRNLQQTYEASMDKLREKQRQLEVAQVENQLLKMKVEssQEANAEVMREMTKKLYSQYEEKL 253
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA--RLEQDIARLEERRRELEERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 254 QEEQRKHSAEKEALLEETNSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMSGELTD 333
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 334 --SDKERYQQLEEASASLRERIRHLDDMVHCQQKKVKQMVEEIESLKKKLQQKQLLILQLLEKISFLEGENNELQSRLDY 411
Cdd:COG1196 402 leELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
....*..
gi 553726985 412 LTETQAK 418
Cdd:COG1196 482 LLEELAE 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
93-356 |
2.95e-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: 57.37 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 93 STSQLKEEMNYIKDVRATLEKVRKRMYGDYDEMRQKIRQLTQELSVSHAQQEYLENHIQTQSSALDRFNAMNSALASDSI 172
Cdd:TIGR02168 706 ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 173 GLQKTLVDVTLENSNIKDQIRNLQ--------------QTYEASMDKLREKQRQLEVAQ---VENQLLKMKVESSQEANA 235
Cdd:TIGR02168 786 ELEAQIEQLKEELKALREALDELRaeltllneeaanlrERLESLERRIAATERRLEDLEeqiEELSEDIESLAAEIEELE 865
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 236 EVMREMTKKLysqyeEKLQEEQRKHSAEKEALLEETNSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQ 315
Cdd:TIGR02168 866 ELIEELESEL-----EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 553726985 316 LQLQLLEHEtEMSGELtdsDKERYQQLEEASASLRERIRHL 356
Cdd:TIGR02168 941 LQERLSEEY-SLTLEE---AEALENKIEDDEEEARRRLKRL 977
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
104-347 |
3.21e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 104 IKDVRATLEKVRKRMYgdydEMRQKIRQLTQELSVSHAQQEYLENHIQTQSSALDRFNAMNSALASDSIGLQKTLVDVTL 183
Cdd:COG1196 262 LAELEAELEELRLELE----ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 184 ENSNIKDQIRNLQQTYEASMDKLREKQRQLEVAQvenQLLKMKVESSQEANAEVMREMTKKL-YSQYEEKLQEEQRKHSA 262
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAE---AELAEAEEELEELAEELLEALRAAAeLAAQLEELEEAEEALLE 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 263 EKEALLEETNSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMSGELTDSDKERYQQL 342
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
....*
gi 553726985 343 EEASA 347
Cdd:COG1196 495 LLLEA 499
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
192-426 |
8.93e-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: 8.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 192 IRNLQQTYEASMDKLREKQRQLEVAQVENQLLKMKVESSQEANAEVMREMTKkLYSQYEeKLQEEQRKHSAEKEALLEET 271
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISA-LRKDLA-RLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 272 NSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLleheTEMSGELTDSdKERYQQLEEASASLRE 351
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL----DELRAELTLL-NEEAANLRERLESLER 831
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 553726985 352 RIRHLDDMVHCQQKKVKQMVEEIESLKKKLQQKQLLILQLLEKISFLEGENNELQSRLDYLTETQAKTEVETREI 426
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
96-436 |
1.27e-06 |
|
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: 52.03 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 96 QLKEEMNYIKDVRATLEKVRKRMygdyDEMRQKIRQLTQELSVSHAQQEYLENHIQTQSSALDRFNAMNSALASDSIGLQ 175
Cdd:pfam05483 248 QITEKENKMKDLTFLLEESRDKA----NQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIAT 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 176 KTLVDVTLENSNIKDQIRNLQQTYEASMDK-----------LREKQRQLEVAQVENQLLKMKVessQEANAEvMREMTKk 244
Cdd:pfam05483 324 KTICQLTEEKEAQMEELNKAKAAHSFVVTEfeattcsleelLRTEQQRLEKNEDQLKIITMEL---QKKSSE-LEEMTK- 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 245 lYSQYEEKLQEEQRKHSAEKEALLEETNSFLKAIEEANKKMQaaeisleekdqrigELDRLIERMEKERHQLQLQL---- 320
Cdd:pfam05483 399 -FKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQ--------------ELIFLLQAREKEIHDLEIQLtaik 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 321 ----------------LEHETEMSGELT-DSDK---ERYQQLEEASASLRERIRHLDDMVHCqQKKVKQMVEEIESLKKK 380
Cdd:pfam05483 464 tseehylkevedlkteLEKEKLKNIELTaHCDKlllENKELTQEASDMTLELKKHQEDIINC-KKQEERMLKQIENLEEK 542
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 553726985 381 LQQKQLLILQLLEKisfLEGENNELQSRLDYLTETQAKTEVETREIGVGCDLLPRK 436
Cdd:pfam05483 543 EMNLRDELESVREE---FIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENK 595
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
127-418 |
2.79e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.79 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 127 QKIRQLTQELSVSHAQQEYLENHIQTQSsalDRFNAMNSALASdsigLQKTLVDVTLENSNIKDQIRNLQQTYEASMDKL 206
Cdd:TIGR04523 211 QKNKSLESQISELKKQNNQLKDNIEKKQ---QEINEKTTEISN----TQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 207 REKQRQLEvaQVENQLLKMKVESSQEANAEVMREMTK----------------KLYSQYEE-----------------KL 253
Cdd:TIGR04523 284 KELEKQLN--QLKSEISDLNNQKEQDWNKELKSELKNqekkleeiqnqisqnnKIISQLNEqisqlkkeltnsesensEK 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 254 QEEQRKHSAEKEALLEETNSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKErhqlqLQLLEHETEMSGELTD 333
Cdd:TIGR04523 362 QRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQE-----KELLEKEIERLKETII 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 334 SDKERYQQLEEASASLRERIRHLDDMVHCQQKKVKQMVEEIESLKKKLQQKQLLILQLLEKISFLEGENNELQSRLDYLT 413
Cdd:TIGR04523 437 KNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLT 516
|
....*
gi 553726985 414 ETQAK 418
Cdd:TIGR04523 517 KKISS 521
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
95-313 |
8.62e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 8.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 95 SQLKEEMNYIKDVRATLEKVRKRMYGDYDEMRQKIRQLTQELSVshaqqeyLENHIQTQSSALDRFNAMNSALASDSIGL 174
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRA-------LEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 175 QKTLvdvtlensniKDQIRNLQQTYEASMDKLREKQRQLEVAQVENQLLKmKVESSQEANAEVMREMTKKLYSQYEE--- 251
Cdd:COG4942 103 KEEL----------AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLK-YLAPARREQAEELRADLAELAALRAElea 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 553726985 252 ---KLQEEQRKHSAEKEALLEETNSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKER 313
Cdd:COG4942 172 eraELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
95-427 |
1.20e-05 |
|
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: 48.91 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 95 SQLKEEMNYIKDVRATLEKvrkrmygdYDEMRQKIRQ-----LTQELSVSHAQQEYLENHIQTQSSALDRFNAMNSALAS 169
Cdd:TIGR02169 194 DEKRQQLERLRREREKAER--------YQALLKEKREyegyeLLKEKEALERQKEAIERQLASLEEELEKLTEEISELEK 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 170 DSIGLQKTLVDVTLEnsnIKDQIRNLQQTYEASMDKLREKQRQLEVAQVENQLlKMKVESSQEANAEVMREMTKKLYSQY 249
Cdd:TIGR02169 266 RLEEIEQLLEELNKK---IKDLGEEEQLRVKEKIGELEAEIASLERSIAEKER-ELEDAEERLAKLEAEIDKLLAEIEEL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 250 EEKLQEEQRkhsaEKEALLEEtnsflkaIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMsg 329
Cdd:TIGR02169 342 EREIEEERK----RRDKLTEE-------YAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKREL-- 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 330 eltDSDKERYQQLEEASASLRERIRHLDDMVHCQQKKVKQMVEEIESLKKKLQQKQLLILQLLEKISFLEGENNELQSRL 409
Cdd:TIGR02169 409 ---DRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEL 485
|
330
....*....|....*...
gi 553726985 410 DYLTETQAKTEVETREIG 427
Cdd:TIGR02169 486 SKLQRELAEAEAQARASE 503
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
178-357 |
2.97e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 178 LVDVTLENSNIKDQIRNLQQTYEASMDKLREKQRQLEvaQVENQLLKMKVESSQEANAEVMREMTKKLY---SQYEEKLQ 254
Cdd:COG3206 207 LVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA--ALRAQLGSGPDALPELLQSPVIQQLRAQLAeleAELAELSA 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 255 EEQRKHSA--EKEALLEETNSFLKaiEEANKKMQAAEISLEEKDQRIGELDRLIERMEKE-----RHQLQLQLLEHETEM 327
Cdd:COG3206 285 RYTPNHPDviALRAQIAALRAQLQ--QEAQRILASLEAELEALQAREASLQAQLAQLEARlaelpELEAELRRLEREVEV 362
|
170 180 190
....*....|....*....|....*....|
gi 553726985 328 SGELTDSDKERYQQLEEASASLRERIRHLD 357
Cdd:COG3206 363 ARELYESLLQRLEEARLAEALTVGNVRVID 392
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
205-470 |
3.19e-05 |
|
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: 47.76 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 205 KLREKQRQLEVAQVENQLLKMKVESSQeanAEVMREMTKKL--YSQYEekLQEEQRKHSAEKEALLEETNSFLKAIEEAN 282
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREK---AERYQALLKEKreYEGYE--LLKEKEALERQKEAIERQLASLEEELEKLT 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 283 KKMQAAEISLEEKDQRIGELDRLIERM-EKERHQLQLQLLEHETEMSG----------ELTDSDKERyQQLEEASASLRE 351
Cdd:TIGR02169 258 EEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASlersiaekerELEDAEERL-AKLEAEIDKLLA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 352 RIRHLDDMVHCQQKKVKQMVEEIESLKKKLQQKQL--------------LILQLLEKISFLEGENNELQSRLDYLTETQA 417
Cdd:TIGR02169 337 EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAeleevdkefaetrdELKDYREKLEKLKREINELKRELDRLQEELQ 416
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 553726985 418 KTEVETREIGVgcdllprkficKLPDKGKKIFDSFAKLKAAIAECEEVRRKSE 470
Cdd:TIGR02169 417 RLSEELADLNA-----------AIAGIEAKINELEEEKEDKALEIKKQEWKLE 458
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
95-297 |
4.85e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 4.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 95 SQLKEEMNYIKDVRATLEKVRKRMYGDYDEMRQKIRQLTQELSVSHAQQEYLENHIQTQSSALDRFNAMNSALASDS--I 172
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALyrS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 173 GLQKTLVDVTLENSNIKDQIRNLQ-------------QTYEASMDKLREKQRQLEVAQVENQLLKMKVESSQEANAEVMR 239
Cdd:COG3883 99 GGSVSYLDVLLGSESFSDFLDRLSalskiadadadllEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 553726985 240 EMTKKLysqyeEKLQEEQRKHSAEKEALLEETNSFLKAIEEANKKMQAAEISLEEKDQ 297
Cdd:COG3883 179 EQEALL-----AQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
204-426 |
4.90e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 4.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 204 DKLREKQRQLEV--AQVEnqllkmKVESSQEANAEvMREMTKKLYSQYEEKLQEEQRKHSAEKEALLEEtnsflkaIEEA 281
Cdd:COG1196 193 DILGELERQLEPleRQAE------KAERYRELKEE-LKELEAELLLLKLRELEAELEELEAELEELEAE-------LEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 282 NKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMsgeltDSDKERYQQLEEASASLRERIRHLDDMVH 361
Cdd:COG1196 259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI-----ARLEERRRELEERLEELEEELAELEEELE 333
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 553726985 362 CQQKKVKQMVEEIESLKKKLQQKQLLILQLLEKISFLEGENNELQSRLDYLTETQAKTEVETREI 426
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
89-359 |
5.08e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 5.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 89 VYGWSTSQLKEEmnyIKDVRATLEKVRKRMYGDYDEMRQKIRQLTQELSVSHAQQEY---------LENHIQTQSSALDR 159
Cdd:COG4913 603 VLGFDNRAKLAA---LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYswdeidvasAEREIAELEAELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 160 FNAMNSALAsdsiGLQKTLVDVTLENSNIKDQIRNLQQTYEASMDKLREKQRQLEVAQVENQLLKMKVESSQEANAEVMR 239
Cdd:COG4913 680 LDASSDDLA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERF 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 240 --EMTKKLYSQYEEKLQEEQRKHSAEKEALLEEtnsFLKAIEEANKK----MQAAEISLEEKDQRIGELDRLI-ERMEKE 312
Cdd:COG4913 756 aaALGDAVERELRENLEERIDALRARLNRAEEE---LERAMRAFNREwpaeTADLDADLESLPEYLALLDRLEeDGLPEY 832
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 553726985 313 RHQLQLQLLEHETEMSGELtdsdkerYQQLEEASASLRERIRHLDDM 359
Cdd:COG4913 833 EERFKELLNENSIEFVADL-------LSKLRRAIREIKERIDPLNDS 872
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
187-376 |
7.39e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 7.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 187 NIKDQIRNLQQTYEAsMDKLREKQRQLEVAQVENQLLKMKVESSQEANAevMREMTKKLYSQYE-EKLQEEQRKHSAEKE 265
Cdd:COG4913 229 ALVEHFDDLERAHEA-LEDAREQIELLEPIRELAERYAAARERLAELEY--LRAALRLWFAQRRlELLEAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 266 ALLEETNSFLKAIEEANKKMQAAEISLEEKD-QRIGELDRLIERMEKERHQLQLQLLEHET-----EMSGELTDSD---- 335
Cdd:COG4913 306 RLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEAllaalGLPLPASAEEfaal 385
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 553726985 336 ----KERYQQLEEASASLRERIRHLDDMVHCQQKKVKQMVEEIES 376
Cdd:COG4913 386 raeaAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
96-376 |
9.34e-05 |
|
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: 46.26 E-value: 9.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 96 QLKEEMNYIKDVRATLEKVRKrMYGDYDEMRQKIRQLTQELSvshAQQEYLENHIQTQSSaldrfnaMNSALASDSIGLQ 175
Cdd:pfam15921 445 QMERQMAAIQGKNESLEKVSS-LTAQLESTKEMLRKVVEELT---AKKMTLESSERTVSD-------LTASLQEKERAIE 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 176 KTLVDVTLENSNIKDQIRNLQQtyeasmdkLREKQRQLEVAQVENQLLKMKVeSSQEANAEVMRemtkklysQYEEKLQE 255
Cdd:pfam15921 514 ATNAEITKLRSRVDLKLQELQH--------LKNEGDHLRNVQTECEALKLQM-AEKDKVIEILR--------QQIENMTQ 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 256 EQRKHSAEKEALLEETNSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERhqlqLQLLEHETEMSGELTDSD 335
Cdd:pfam15921 577 LVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEK----VKLVNAGSERLRAVKDIK 652
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 553726985 336 KERYQQLEEASASlRERIRHLDDMVHCQQKKVKQMVEEIES 376
Cdd:pfam15921 653 QERDQLLNEVKTS-RNELNSLSEDYEVLKRNFRNKSEEMET 692
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
206-360 |
9.36e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 9.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 206 LREKQRQLEVAQVENQLLKMKVESSQEANAEVMREMTKKLYSQYEEKLQEEQRKHSAEKEALLEETNSFLKAIEEANKKM 285
Cdd:COG1196 676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 286 QAAEISLEEKDQRIGELDRLIERME-------------KERHQlqlqllehetEMSGELTDsdkeryqqLEEASASLRER 352
Cdd:COG1196 756 LPEPPDLEELERELERLEREIEALGpvnllaieeyeelEERYD----------FLSEQRED--------LEEARETLEEA 817
|
....*...
gi 553726985 353 IRHLDDMV 360
Cdd:COG1196 818 IEEIDRET 825
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
127-348 |
1.20e-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: 45.14 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 127 QKIRQLTQELSVSHAQQEYLENHIQTQSSALDRFNAMNSALASDSIGLQKTLVDVTLENSNIKDQIRNLQQTYEASMDKL 206
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 207 REKQ----RQLEVAQVENQLLKMKV-ESSQEANAEVMREMTKKLYSQYEEKLQEEQRKHSAEKEALLEETNSFLKAIEEA 281
Cdd:COG4942 100 EAQKeelaELLRALYRLGRQPPLALlLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 553726985 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, ... |
251-425 |
2.34e-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: 44.37 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 251 EKLQEEQRKHSAEKEALLEETNSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMSGE 330
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 331 LTDSDK-ERYQQL------EEASASLReRIRHLDDMVHCQQKKVKQMVEEIESLKKKLQQKQLLILQLLEKISFLEGENN 403
Cdd:COG4942 110 LRALYRlGRQPPLalllspEDFLDAVR-RLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188
|
170 180
....*....|....*....|..
gi 553726985 404 ELQSRLDYLTETQAKTEVETRE 425
Cdd:COG4942 189 ALEALKAERQKLLARLEKELAE 210
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
251-425 |
2.68e-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: 43.98 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 251 EKLQEEQRKHSAEKEALLEETNSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQL---------- 320
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELaellralyrl 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 321 -----------------LEHETEMSGELTDSDKERYQQLEEASASLRERIRHLDDMVHCQQKKVKQMVEEIESLKKKLQQ 383
Cdd:COG4942 117 grqpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAE 196
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 553726985 384 KQLLILQLLEKISFLEGENNELQSRLDYLTETQAKTEVETRE 425
Cdd:COG4942 197 RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
95-370 |
2.70e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 44.35 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 95 SQLKEEMNYIKDVRATLEKVRKRMYGdYDEMRQKIRQLTQELSVSHAQQEYLENHIQTQSSALDRFNAMNSALASDSiGL 174
Cdd:pfam05557 125 LELQSTNSELEELQERLDLLKAKASE-AEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARIP-EL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 175 QKTLVDVTLENSNIKDQIRNLQ------QTYEASMDKLREKQRQLEVAQVENQLLKMKVESSQEANAEVMREM-TKKLYS 247
Cdd:pfam05557 203 EKELERLREHNKHLNENIENKLllkeevEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLrSPEDLS 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 248 QYEEKLQEEQRKHSAEKEALLEETNSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKerhqlQLQLLEHETEM 327
Cdd:pfam05557 283 RRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQR-----RVLLLTKERDG 357
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 553726985 328 SGELTDS-DKEryQQLEEASASLRERIRHLDDMVHCQQKKVKQM 370
Cdd:pfam05557 358 YRAILESyDKE--LTMSNYSPQLLERIEEAEDMTQKMQAHNEEM 399
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
95-427 |
3.63e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 95 SQLKEEMNYIKDVRATLEKVRKRM--YGDYDEMRQKIRQLTQELSVSHAQQEYLENHIQTQSSALDR-----------FN 161
Cdd:COG4717 98 EELEEELEELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEEleeleaelaelQE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 162 AMNSALASDSIGLQKTLVDVTLENSNIKDQIRNLQQTYEASMDKLREKQRQLE-------VAQVENQLLKMKVESSQEAN 234
Cdd:COG4717 178 ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEqleneleAAALEERLKEARLLLLIAAA 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 235 AEVMREMTKKLYSQYEE---------------KLQEEQRKHSAEKEALLEETNSFLKAIEEANKKMQAAEISLE------ 293
Cdd:COG4717 258 LLALLGLGGSLLSLILTiagvlflvlgllallFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPpdlspe 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 294 ---EKDQRIGELDRLIERMEKERHQLQLQLLEHETE--MSGELTDSDKERYQQLEEASA--SLRERIRHLDDMVHCQQKK 366
Cdd:COG4717 338 ellELLDRIEELQELLREAEELEEELQLEELEQEIAalLAEAGVEDEEELRAALEQAEEyqELKEELEELEEQLEELLGE 417
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 553726985 367 VKQMVEEIEslkkklqqkqllILQLLEKISFLEGENNELQSRLDYLTETQAKTEVETREIG 427
Cdd:COG4717 418 LEELLEALD------------EEELEEELEELEEELEELEEELEELREELAELEAELEQLE 466
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
186-375 |
4.56e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 186 SNIKDQIRNLQQTYEASMDKLREKQRQLEVAQVENQLLKMKVESSQEANAEVMR-EMTKKLYSQYEEKLQEEQrKHSAEK 264
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyIKLSEFYEEYLDELREIE-KRLSRL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 265 EALLEETNSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERhQLQLQLLEHETEMSGELTDSDKERYQQLEE 344
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAK-AKKEELERLKKRLTGLTPEKLEKELEELEK 398
|
170 180 190
....*....|....*....|....*....|.
gi 553726985 345 ASASLRERIRHLDDMVHCQQKKVKQMVEEIE 375
Cdd:PRK03918 399 AKEEIEEEISKITARIGELKKEIKELKKAIE 429
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
230-470 |
6.98e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 6.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 230 SQEANAEVMREMTK-KLYSQYEEKLQEEQRKHSAEKEALleetNSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIER 308
Cdd:PRK03918 143 SDESREKVVRQILGlDDYENAYKNLGEVIKEIKRRIERL----EKFIKRTENIEELIKEKEKELEEVLREINEISSELPE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 309 MEKERHQLQLQLLEHEtEMSGELTDSDKERyQQLEEASASLRERIRHLDDMVHCQQKKVKQM------VEEIESLKKKLQ 382
Cdd:PRK03918 219 LREELEKLEKEVKELE-ELKEEIEELEKEL-ESLEGSKRKLEEKIRELEERIEELKKEIEELeekvkeLKELKEKAEEYI 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 383 QKQLLILQLLEKISFLEGENNELQSRLDYLTETQAKTEVETREIGvgcdllprkficKLPDKGKKIFDSFAKLKAAIAEC 462
Cdd:PRK03918 297 KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE------------ELKKKLKELEKRLEELEERHELY 364
|
....*...
gi 553726985 463 EEVRRKSE 470
Cdd:PRK03918 365 EEAKAKKE 372
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
160-351 |
7.15e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 7.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 160 FNAMNSALASDSIG-LQKTLVDVTLENSNIKDQIRNLQQTYEASMDKLREKQRQLEVAQVENQLLKMKVESSQEANAEVM 238
Cdd:COG3883 6 LAAPTPAFADPQIQaKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 239 REMTKKLYSQYEEKLQeeqrkhSAEKEALLEETN--------SFLKAIEEANKKM----QAAEISLEEK----DQRIGEL 302
Cdd:COG3883 86 EELGERARALYRSGGS------VSYLDVLLGSESfsdfldrlSALSKIADADADLleelKADKAELEAKkaelEAKLAEL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 553726985 303 DRLIERMEKERHQLQLQLLEHETEMSgELTDSDKERYQQLEEASASLRE 351
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLA-QLSAEEAAAEAQLAELEAELAA 207
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
136-356 |
9.82e-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: 9.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 136 LSVSHAQQEYLENHIQTQSSALDRFNAMNSALA---SDSIGLQKTLVDVTLENSNIKDQIRNLQQtyeasmdKLREKQRQ 212
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAalkKEEKALLKQLAALERRIAALARRIRALEQ-------ELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 213 LEVAQVENQLLKMKVESSQEANAEVMREMTK-KLYSQYEEKLQEEQRKHSAEKEALLEETNSFLKA-IEEANKKMQAAEI 290
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEELAELLRALYRlGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREqAEELRADLAELAA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 553726985 291 SLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMSG--ELTDSDKERYQQLEEASASLRERIRHL 356
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARleKELAELAAELAELQQEAEELEALIARL 232
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
203-317 |
1.85e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.84 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 203 MDKLREKQRQLEVAQVENqllkMKVESSQEANAEVMREMTK--------KLYSQYEEKLQEEQRKHSAEK-EALLEETNS 273
Cdd:PRK05771 18 KDEVLEALHELGVVHIED----LKEELSNERLRKLRSLLTKlsealdklRSYLPKLNPLREEKKKVSVKSlEELIKDVEE 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 553726985 274 FLKAIEEankkmqaaeiSLEEKDQRIGELDRLIERMEKERHQLQ 317
Cdd:PRK05771 94 ELEKIEK----------EIKELEEEISELENEIKELEQEIERLE 127
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
95-344 |
1.87e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 95 SQLKEEMNYIKDVRATLEKVRKRmYGDYDEMRQKIRQLTQELSVSHAQQEYLENHIQtqssaldrfnamnsalasdsiGL 174
Cdd:PRK03918 207 REINEISSELPELREELEKLEKE-VKELEELKEEIEELEKELESLEGSKRKLEEKIR---------------------EL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 175 QKTLVDVTLENSNIKDQIRNLQ--QTYEASMDKLREKQRQLEVAQVENQLLKMKVESSQEANAEVMREMTKKlysqyEEK 252
Cdd:PRK03918 265 EERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK-----EER 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 253 LqEEQRKHSAEKEALLEETNSFLKAIEEANKKM-QAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEhETEMSGEL 331
Cdd:PRK03918 340 L-EELKKKLKELEKRLEELEERHELYEEAKAKKeELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISK-ITARIGEL 417
|
250
....*....|...
gi 553726985 332 TDSDKERYQQLEE 344
Cdd:PRK03918 418 KKEIKELKKAIEE 430
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
188-354 |
1.90e-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: 40.68 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 188 IKDQIRNLQQTYEASMDKLREKQRQLEVAQVENQLLKMKVessQEANAEVmREMTKKLysqyeEKLQEEQRKHSAEKE-- 265
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEI---KRLELEI-EEVEARI-----KKYEEQLGNVRNNKEye 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 266 ALLEETNSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMSGELTDSDKERYQQLEEA 345
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
170
....*....|..
gi 553726985 346 SASLR---ERIR 354
Cdd:COG1579 173 PPELLalyERIR 184
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
218-375 |
2.72e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 218 VENQLLKMKVESSQEANAEVMREMTKKLYSQYEEKLQEEQRKHSAEKEALLEETNSFLKAIEEANKKMQAAEISLEEKDQ 297
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 298 RIGELDRLIERMEKERHQLQLQLLEHETEMSGELTDSDK--ERYQQL--EEASASLRERIRhlDDMVHCQQKKVKQMVEE 373
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQelERISGLtaEEAKEILLEKVE--EEARHEAAVLIKEIEEE 181
|
..
gi 553726985 374 IE 375
Cdd:PRK12704 182 AK 183
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
128-338 |
2.78e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 128 KIRQLTQELSVSHAQQEYLENHIQTQSSALDRFNAMNSALASDSIGLQKTLV----DVTLENSNIKDQIRNL---QQTYE 200
Cdd:PHA02562 175 KIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVeeakTIKAEIEELTDELLNLvmdIEDPS 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 201 ASMDKLREKQRQLEvAQVE--NQLLKMKVESSQEANAEVMREMTKKLYSQYEEKLQEEQRKHSAEKEAlLEETNSFLKAI 278
Cdd:PHA02562 255 AALNKLNTAAAKIK-SKIEqfQKVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTA-IDELEEIMDEF 332
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 553726985 279 EEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMSG---ELTDSDKER 338
Cdd:PHA02562 333 NEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKlqdELDKIVKTK 395
|
|
| TOPEUc |
smart00435 |
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
171-297 |
3.75e-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: 40.41 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 171 SIGLQKTLVDVTLENSNIKDQI-----------------RNLQQTYEASMDKLREKQRQLEvaqveNQLLKMKVessqea 233
Cdd:smart00435 230 SITLQEQLKELTAKDGNVAEKIlaynranrevailcnhqRTVSKTHEKSMEKLQEKIKALK-----YQLKRLKK------ 298
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 553726985 234 nAEVMREMTKKLYSQYEEKLQEEQRKHSAEKEALLEETNSFL---KAIEEANKKMQAAEISLEEKDQ 297
Cdd:smart00435 299 -MILLFEMISDLKRKLKSKFERDNEKLDAEVKEKKKEKKKEEkkkKQIERLEERIEKLEVQATDKEE 364
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
262-426 |
4.23e-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: 40.82 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 262 AEKEALLEEtnsflkaIEEANKKMQAAEISLEEKDQRIGELDRliERMEKERHQ-LQLQLLEHE-TEMSGELTDSDKERY 339
Cdd:TIGR02169 170 RKKEKALEE-------LEEVEENIERLDLIIDEKRQQLERLRR--EREKAERYQaLLKEKREYEgYELLKEKEALERQKE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 340 Q------QLEEASASLRERIRHLDDMVHCQQKKVKQMVEEIESLKKKLQQKQLLILQLLE-KISFLEGENNELQSRLDYL 412
Cdd:TIGR02169 241 AierqlaSLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEaEIASLERSIAEKERELEDA 320
|
170
....*....|....
gi 553726985 413 TETQAKTEVETREI 426
Cdd:TIGR02169 321 EERLAKLEAEIDKL 334
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
46-425 |
5.67e-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: 40.10 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 46 EKKIERKEQLLDLSNGEPTRKLPQGVVYGVVRRSDQNQ-----QKEMVVYGWSTSQ-LKEEMnyIKDVRATLEKVRKRMY 119
Cdd:pfam15921 103 KQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQedlrnQLQNTVHELEAAKcLKEDM--LEDSNTQIEQLRKMML 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 120 gDYDEMRQKIRQLTQELSVSHAQQEYLENHIQTQssaldRFNAMNSALAsdsiglqKTLVDVTLENSNIKDQIRNLQQTY 199
Cdd:pfam15921 181 -SHEGVLQEIRSILVDFEEASGKKIYEHDSMSTM-----HFRSLGSAIS-------KILRELDTEISYLKGRIFPVEDQL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 200 EA----SMDK----LREKQRQLEVAQVENQL----LKMKVESSQ-EANA-----EVMREMTKKLYSQYEEKLQEEQRKHS 261
Cdd:pfam15921 248 EAlkseSQNKiellLQQHQDRIEQLISEHEVeitgLTEKASSARsQANSiqsqlEIIQEQARNQNSMYMRQLSDLESTVS 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 262 AEKEALLEETNSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMSGElTDSDKERYQQ 341
Cdd:pfam15921 328 QLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLE-KEQNKRLWDR 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 342 LEEASASLRERIRHLDDM---VHCQQKKVKQMVEEIESLKKKLQQKQLLILQLLEKISFLEGENNELQSRLDYLTE--TQ 416
Cdd:pfam15921 407 DTGNSITIDHLRRELDDRnmeVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEelTA 486
|
....*....
gi 553726985 417 AKTEVETRE 425
Cdd:pfam15921 487 KKMTLESSE 495
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
203-376 |
5.71e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 203 MDKLREKQRQLEVAQVENQLLKMKVESSQEANAEvmREMTKKLYSQYEEKLQE-----EQRKHSAEKEALLEETNSFLKA 277
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEELEEE--LEELEAELEELREELEKlekllQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 278 IEEankkmqaaeisLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMSGELTD---SDKERYQQLEEASASLRERIR 354
Cdd:COG4717 148 LEE-----------LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEelqDLAEELEELQQRLAELEEELE 216
|
170 180
....*....|....*....|..
gi 553726985 355 HLDDMVHCQQKKVKQMVEEIES 376
Cdd:COG4717 217 EAQEELEELEEELEQLENELEA 238
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
205-376 |
7.19e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 7.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 205 KLREKQRQLEVAQVENQLLKMKVESSQEAnaevmrEMTKKLYSQYEEKLQEEQRKHSAEKEALLEEtnsflkAIEEANKK 284
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSP------EELLELLDRIEELQELLREAEELEEELQLEE------LEQEIAAL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 285 MQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMSGELTDSD----KERYQQLEEASASLRERIRHLDDmv 360
Cdd:COG4717 376 LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeelEEELEELEEELEELEEELEELRE-- 453
|
170
....*....|....*.
gi 553726985 361 hcQQKKVKQMVEEIES 376
Cdd:COG4717 454 --ELAELEAELEQLEE 467
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
96-320 |
7.92e-03 |
|
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: 39.77 E-value: 7.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 96 QLKEEMNYIKDVRATLEKVRKRMYGDYDEMRQKIRQLT-----------------QELSVSHAQQEY----LENHIQTQS 154
Cdd:pfam01576 360 ELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQqakqdsehkrkklegqlQELQARLSESERqraeLAEKLSKLQ 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 155 SALDRFNAMNSALASDSIGLQKtlvDVTLENSNIKDQIRNLQQTYEASMdKLREKQRQLEvaqVENQLLKMKVESSQEAN 234
Cdd:pfam01576 440 SELESVSSLLNEAEGKNIKLSK---DVSSLESQLQDTQELLQEETRQKL-NLSTRLRQLE---DERNSLQEQLEEEEEAK 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 235 AEVMREMtkklySQYEEKLQEEQRKhsaekealLEETNSFLKAIEEANKKMQAaeiSLEEKDQRIGELDRLIERMEKERH 314
Cdd:pfam01576 513 RNVERQL-----STLQAQLSDMKKK--------LEEDAGTLEALEEGKKRLQR---ELEALTQQLEEKAAAYDKLEKTKN 576
|
....*.
gi 553726985 315 QLQLQL 320
Cdd:pfam01576 577 RLQQEL 582
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
257-468 |
8.21e-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: 39.65 E-value: 8.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 257 QRKHSAEK------------EALLEETNSFLKAIE-EANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEH 323
Cdd:TIGR02168 172 ERRKETERklertrenldrlEDILNELERQLKSLErQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 324 ETEMsgeltDSDKERYQQLEEASASLRERIRHLDDMVHCQQKKVKQMVEEIESLKKKLQQKQLLILQLLEKISFLEGENN 403
Cdd:TIGR02168 252 EEEL-----EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE 326
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 553726985 404 ELQSRLDYLTETQAKTEVETREIGVGCDLLPRkficKLPDKGKKIFDSFAKLKAAIAECEEVRRK 468
Cdd:TIGR02168 327 ELESKLDELAEELAELEEKLEELKEELESLEA----ELEELEAELEELESRLEELEEQLETLRSK 387
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
107-324 |
8.38e-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: 39.72 E-value: 8.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 107 VRATLEKVRKRMYGDyDEMRQKIRQLTQELSVSHAQQEyleNHIQTQSSALDRFNAmnsalasdsiglqKTLVDVTLENS 186
Cdd:pfam17380 394 VRQELEAARKVKILE-EERQRKIQQQKVEMEQIRAEQE---EARQREVRRLEEERA-------------REMERVRLEEQ 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 187 NIKDQIRNLQQTYEASMDKLREKQRQLEVAQVENQLLKMKVESSQEANAEVM------REMTKKLYSQYEEKLQEEQRKH 260
Cdd:pfam17380 457 ERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMieeerkRKLLEKEMEERQKAIYEEERRR 536
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 553726985 261 SAEKEALLEetnsflKAIEEANKKMQAAEISLEEKDQrigeldrlIERMEKERHQLQlQLLEHE 324
Cdd:pfam17380 537 EAEEERRKQ------QEMEERRRIQEQMRKATEERSR--------LEAMEREREMMR-QIVESE 585
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
146-377 |
8.89e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 39.63 E-value: 8.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 146 LENHIQTQSSALDRFNAMNSA-LASDSIGLQKTLVDVTLENSNIKDQIR-NLQQTYEASMDKLREKQRQLEVAQ-----V 218
Cdd:pfam05667 209 LERNAAELAAAQEWEEEWNSQgLASRLTPEEYRKRKRTKLLKRIAEQLRsAALAGTEATSGASRSAQDLAELLSsfsgsS 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 219 ENQLLKMK------VESSQEANAEVMREMTKKLYSQYEEKLQEEQRKHSAEKEALLEETNSFLKAIEEANKKMQAaeiSL 292
Cdd:pfam05667 289 TTDTGLTKgsrfthTEKLQFTNEAPAATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLES---SI 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553726985 293 EEKDQRIGELDRLIERMEKE---RHQLQLQLLEHETEMS--GELTDSDKERYQQL----EEASASLRERIRHLDDMVHCQ 363
Cdd:pfam05667 366 KQVEEELEELKEQNEELEKQykvKKKTLDLLPDAEENIAklQALVDASAQRLVELagqwEKHRVPLIEEYRALKEAKSNK 445
|
250
....*....|....
gi 553726985 364 QKKVKQMVEEIESL 377
Cdd:pfam05667 446 EDESQRKLEEIKEL 459
|
|
| |
