|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
33-312 |
5.90e-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: 59.69 E-value: 5.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 33 HQLSLGAGESSMNPSATLYRRQNIGSEVETstIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLlswEEDRQKVLTLEE 112
Cdd:TIGR02168 715 EQLRKELEELSRQISALRKDLARLEAEVEQ--LEERIAQLSKELTELEAEIEELEERLEEAEEEL---AEAEAEIEELEA 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 113 RCSKLEGELHKRTDIIKSLMKKVKTLESNQAECQTALQKTQQQLQEMAQKATHSTLLSEDLEARNENLSSTLVDLSAQDK 192
Cdd:TIGR02168 790 QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 193 DIIEAVNHISDCSGKFKLLEHALRDakmaetcvvrEKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKS 272
Cdd:TIGR02168 870 ELESELEALLNERASLEEALALLRS----------ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 568937051 273 CLHDELiftveREKRKDELLDIAKSKQDRTNSELQNLRQI 312
Cdd:TIGR02168 940 NLQERL-----SEEYSLTLEEAEALENKIEDDEEEARRRL 974
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
62-298 |
1.36e-08 |
|
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: 57.47 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 62 TSTIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESN 141
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 142 QAECQTALQKTQQQLQEMAQKATHSTLLSEDLEARNENLSSTLVDLSAQDKDIIEAVNHISDcsgKFKLLEHALRDAKMA 221
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA---ELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568937051 222 ETCVVREKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKSCLHDELIFTVEREKRKDELLDIAKSK 298
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
48-321 |
2.00e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 48 ATLYRRQNIGSEVET--STIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQKVLTLEERCSKLEGELHKRT 125
Cdd:COG1196 229 LLLLKLRELEAELEEleAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 126 DIIKSLMKKVKTLESNQAECQTALQKTQQQLQEMAQKATHSTLLSEDLEARNENLSSTLVDLSAQDKDIIEAvnhisdcs 205
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE-------- 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 206 gkfkllEHALRDAKMAETcvvREKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKSCLHDELIFTVERE 285
Cdd:COG1196 381 ------LEELAEELLEAL---RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
250 260 270
....*....|....*....|....*....|....*.
gi 568937051 286 KRKDELLDIAKSKQDRTNSELQNLRQIYVKQQSDLQ 321
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
52-311 |
7.68e-08 |
|
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: 55.84 E-value: 7.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 52 RRQNIGSEVETSTIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQkvLTLEERCSKLEGELHKRTDIIKSL 131
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ--LRVKEKIGELEAEIASLERSIAEK 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 132 MKKVKTLESNQAECQTALQKTQQQLQ----EMAQKATHSTLLSEDLEARNENLSSTLVDLSAQDKDIIEAVNHISDCSGK 207
Cdd:TIGR02169 314 ERELEDAEERLAKLEAEIDKLLAEIEelerEIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 208 FKLLEHALRDAKMAETCVVREKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKSCLHDELiftverEKR 287
Cdd:TIGR02169 394 LEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADL------SKY 467
|
250 260
....*....|....*....|....
gi 568937051 288 KDELLDIaKSKQDRTNSELQNLRQ 311
Cdd:TIGR02169 468 EQELYDL-KEEYDRVEKELSKLQR 490
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
96-311 |
1.89e-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: 50.53 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 96 QLLSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQAECQTALQKTQQQL----QEMAQKATHSTLLSE 171
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELaaleAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 172 DLEARNENLSSTLVDLSAQDK-DIIEAVNHISDCSGKFKLLE--HALRDAKMAETCVVREKQdykQKLKALRIEVNKLKE 248
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRqPPLALLLSPEDFLDAVRRLQylKYLAPARREQAEELRADL---AELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568937051 249 DLNEKTTENNEQREEIIRLKQEKSCLHDELiftVEREKRKDELLDIAKSKQDRTNSELQNLRQ 311
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARL---EKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
65-311 |
4.12e-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: 50.45 E-value: 4.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 65 IEKQRKELQLLIGELKDRDKELNDMvavhqRQLLSWEEdrQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQAE 144
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRIENRLDEL-----SQELSDAS--RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 145 CQTALQKTQQQLQEMAQKATHSTLLSEDLEARN-----ENLSSTLVDLSAQDKDIIEAVNHISDCSGKFKLLEHALRDAK 219
Cdd:TIGR02169 756 VKSELKELEARIEELEEDLHKLEEALNDLEARLshsriPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 220 MAETCVVRE----KQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKSCLHDELiftVEREKRKDEL---L 292
Cdd:TIGR02169 836 QELQEQRIDlkeqIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL---RELERKIEELeaqI 912
|
250
....*....|....*....
gi 568937051 293 DIAKSKQDRTNSELQNLRQ 311
Cdd:TIGR02169 913 EKKRKRLSELKAKLEALEE 931
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
71-247 |
9.88e-06 |
|
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: 48.96 E-value: 9.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 71 ELQLLIGELKDRDKELNdmVAVHQRQLLsWEEDRQKVLTLEErcskLEGELHKRTDIIKSLMKKVKTLESnqaECQTALQ 150
Cdd:pfam15921 378 QLQKLLADLHKREKELS--LEKEQNKRL-WDRDTGNSITIDH----LRRELDDRNMEVQRLEALLKAMKS---ECQGQME 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 151 KTQQQLQEMAQKATHSTLLSEDLEARNENLSSTLVDLSAQDKDIIEAVNHISDCSGKFKLLEHALrDAKMAETCVVREKQ 230
Cdd:pfam15921 448 RQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAI-EATNAEITKLRSRV 526
|
170
....*....|....*...
gi 568937051 231 DYK-QKLKALRIEVNKLK 247
Cdd:pfam15921 527 DLKlQELQHLKNEGDHLR 544
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
63-335 |
1.36e-05 |
|
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: 48.48 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 63 STIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQ 142
Cdd:TIGR04523 398 SKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSI 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 143 AECQTALQKTQQQL----QEMAQKATHSTLLSEDLEARNENLSSTLVDLSAQDKDIIEAVNHISDCSGKFKLLEHALRDA 218
Cdd:TIGR04523 478 NKIKQNLEQKQKELkskeKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKE 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 219 KMAEtcVVREKQ----DYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKSCLHDELIFTVEREKRKDELLDI 294
Cdd:TIGR04523 558 NLEK--EIDEKNkeieELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKN 635
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 568937051 295 AKSKQDRTNSELQNLRQIYVKQQSDLQFLNFNIESSQELIQ 335
Cdd:TIGR04523 636 IKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKID 676
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
64-260 |
6.52e-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: 6.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 64 TIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWE------EDRQKVLTLEERCSKLEGELHKrtdiIKSLMKKVKT 137
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQrlaeysWDEIDVASAEREIAELEAELER----LDASSDDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 138 LESNQAECQTALQKTQQQLQEMAQKAThstllseDLEARNENLSSTLVDLSAQDKDIIEAVnhisdCSGKFKLLEHALRD 217
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIG-------RLEKELEQAEEELDELQDRLEAAEDLA-----RLELRALLEERFAA 757
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 568937051 218 AkMAETCVVREKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQ 260
Cdd:COG4913 758 A-LGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNRE 799
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
125-335 |
6.65e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.20 E-value: 6.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 125 TDIIKSLMKKVKTLESnQAECQTALQKTQQQLqemaqKATHSTLLSEDLEARNENLSSTLVDLSAqdkdiieavnhisdc 204
Cdd:TIGR02168 192 EDILNELERQLKSLER-QAEKAERYKELKAEL-----RELELALLVLRLEELREELEELQEELKE--------------- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 205 sgkfklLEHALRDAKmaetcvvREKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKSCLHDELIFTVER 284
Cdd:TIGR02168 251 ------AEEELEELT-------AELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568937051 285 EKRKDELLDIAKSKQDRTNSELQNLRQIYVKQQSDLQFLNFNIESSQELIQ 335
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
65-269 |
7.10e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 7.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 65 IEKQRKEL--------QLLIGELKDRDKELNDMvavhQRQLLSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSLMKKVK 136
Cdd:COG4717 51 LEKEADELfkpqgrkpELNLKELKELEEELKEA----EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 137 TLESNQaecqtALQKTQQQLQEMAQKAthstllsEDLEARNENLSSTLVDLSAQDKDIIEAVNHISDCSGKFKL-LEHAL 215
Cdd:COG4717 127 LLPLYQ-----ELEALEAELAELPERL-------EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLaTEEEL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568937051 216 RDAKMAETCVVREKQDYKQKLKALRIEVNKLKEDLN--EKTTENNEQREEIIRLKQ 269
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEqlENELEAAALEERLKEARL 250
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
117-350 |
1.13e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.43 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 117 LEGELHKRTDIIKSLMKKVKTLESNQAECQTALQKTQQQLQEMAQKAthstllsEDLEARNENLSSTLVDLSAQDKDIIE 196
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEI-------EELQKELYALANEISRLEQQKQILRE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 197 AvnhisdcsgkfklLEHALRDAKMAETcvvrEKQDYKQKLkalrievNKLKEDLNEKTTENNEQREEIIRLKQEKSCLHD 276
Cdd:TIGR02168 310 R-------------LANLERQLEELEA----QLEELESKL-------DELAEELAELEEKLEELKEELESLEAELEELEA 365
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568937051 277 ELIFTVEREKRKDELLDIAKSKQDRTNSELQNLRQIYVKQQSDLQFLNFNIESSQELIQIHGLKMEEPKALECS 350
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQ 439
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
59-343 |
1.70e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.07 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 59 EVETSTIEKQRKELQLLIGELKDRdKELNDMVAvhQRQLLSWEEDRQKVL-TLEERCSKLEGE-LHKRTDIIKSLMKKVK 136
Cdd:COG5022 786 LVDYELKWRLFIKLQPLLSLLGSR-KEYRSYLA--CIIKLQKTIKREKKLrETEEVEFSLKAEvLIQKFGRSLKAKKRFS 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 137 TL--ESNQAECQTALQKTQQQLQEMAQKATHSTLLSEdleaRNENLSSTLVDLSAQ-DKDIIEAVNHISDCSGKFK--LL 211
Cdd:COG5022 863 LLkkETIYLQSAQRVELAERQLQELKIDVKSISSLKL----VNLELESEIIELKKSlSSDLIENLEFKTELIARLKklLN 938
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 212 EHALRDAKMAETCVVREKQDYKQKLKALRiEVNKLKEDLNEKTT----ENNEQREEIIRLKQEKSCLHDELIFTVEREKR 287
Cdd:COG5022 939 NIDLEEGPSIEYVKLPELNKLHEVESKLK-ETSEEYEDLLKKSTilvrEGNKANSELKNFKKELAELSKQYGALQESTKQ 1017
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 568937051 288 KDELldiakskqDRTNSELQNLRQIYVKQQSDLQFLNfnieSSQELIQIHGLKMEE 343
Cdd:COG5022 1018 LKEL--------PVEVAELQSASKIISSESTELSILK----PLQKLKGLLLLENNQ 1061
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
54-342 |
2.45e-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: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 54 QNIGSEVETSTIEKQRKELQLLIGELKDRDKELNDMvavhQRQLlswEEDRQKVLTLEERCSKLEGELH-------KRTD 126
Cdd:TIGR04523 291 NQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEI----QNQI---SQNNKIISQLNEQISQLKKELTnsesensEKQR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 127 IIKSLMKKVKTLESNQAECQTALQKTQQQLQEMAQKATHSTLLSEDLEARNENLSSTLVDLSAQDKD----IIEAVNHIS 202
Cdd:TIGR04523 364 ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERlketIIKNNSEIK 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 203 DCSGKFKLLEHALRDAKmaetcvvREKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKSCLHDELiftV 282
Cdd:TIGR04523 444 DLTNQDSVKELIIKNLD-------NTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKV---K 513
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 283 EREKRKDELldiaKSKQDRTNSELQNLRQIYVKQQSDLQFLNFNIESSQELIQIHGLKME 342
Cdd:TIGR04523 514 DLTKKISSL----KEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKE 569
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
65-309 |
3.74e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 65 IEKQRKELQLLIGELKDRDKELND-MVAVHQRQLLS--------------WEEDRQKVLTLEERCSKLEGELHKRTDIIK 129
Cdd:PRK03918 343 LKKKLKELEKRLEELEERHELYEEaKAKKEELERLKkrltgltpeklekeLEELEKAKEEIEEEISKITARIGELKKEIK 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 130 SLMKKVKTLESNQAECQTAlqktqqqlqemaqkathSTLLSEdlEARNENLSSTLVDLSAQDKDIIEAVNHISDCSGKFK 209
Cdd:PRK03918 423 ELKKAIEELKKAKGKCPVC-----------------GRELTE--EHRKELLEEYTAELKRIEKELKEIEEKERKLRKELR 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 210 LLEHALRDakmaETCVVREKQDYKQkLKALRIEVNKL-KEDLNEKTTENNEQREEIIRLKQEKSCLHDELIFTVEREKRK 288
Cdd:PRK03918 484 ELEKVLKK----ESELIKLKELAEQ-LKELEEKLKKYnLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKL 558
|
250 260
....*....|....*....|.
gi 568937051 289 DELldiaKSKQDRTNSELQNL 309
Cdd:PRK03918 559 AEL----EKKLDELEEELAEL 575
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
72-336 |
6.40e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 6.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 72 LQLLIGELKDRDKELNDMVAVHQR--QLLSWEEDRQKVLTLEERcSKLEGELHKRTDIIKSLMKKVKTLESNQAECQTAL 149
Cdd:COG1196 191 LEDILGELERQLEPLERQAEKAERyrELKEELKELEAELLLLKL-RELEAELEELEAELEELEAELEELEAELAELEAEL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 150 QKTQQQLQEmaqkathstlLSEDLEARNENLSSTLVDLSAQDKDIIEAVNHISDCSGKFKLLEHALRDAKMAETCVVREK 229
Cdd:COG1196 270 EELRLELEE----------LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 230 QDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEII-RLKQEKSCLHDELIFTVEREKRKDELLDIAKSKQDRTNSELQN 308
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAeAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
250 260
....*....|....*....|....*...
gi 568937051 309 LRQIYVKQQSDLQFLNFNIESSQELIQI 336
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEA 447
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
65-279 |
7.52e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 7.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 65 IEKQRKELQLL--IGELKDRDKELNDMVAVHQ--RQLLSWEEDRQKVLTLEERCSKLEGELhkrtdiikslmkkvKTLES 140
Cdd:COG4913 244 LEDAREQIELLepIRELAERYAAARERLAELEylRAALRLWFAQRRLELLEAELEELRAEL--------------ARLEA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 141 NQAECQTALQKTQQQLQEM-AQKATHSTLLSEDLEARNENLSSTLVDLSAQDKDIIEAVNHIsdcsgKFKLLEHALRDAK 219
Cdd:COG4913 310 ELERLEARLDALREELDELeAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAL-----GLPLPASAEEFAA 384
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 220 MAETcVVREKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKSCLHDELI 279
Cdd:COG4913 385 LRAE-AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLL 443
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
64-390 |
1.07e-03 |
|
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: 42.31 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 64 TIEKQRKELQLLIGELKDRDKELNDMVavhqrqllsweedrqkvltleercSKLEGELHKRTDIIKSLMKKVKTLESNQA 143
Cdd:TIGR04523 208 KKIQKNKSLESQISELKKQNNQLKDNI------------------------EKKQQEINEKTTEISNTQTQLNQLKDEQN 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 144 ECQTALQKTQQQLQemaqkaTHSTLLSEdLEARNENLSSTLVDLSAQ-DKDIIEAVN-HISDCSGKFKLLEHALRDAKMA 221
Cdd:TIGR04523 264 KIKKQLSEKQKELE------QNNKKIKE-LEKQLNQLKSEISDLNNQkEQDWNKELKsELKNQEKKLEEIQNQISQNNKI 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 222 ETCVVREKQDYKQKLKALRIEVNKLKEDLNEKTT-------ENNEQREEIIRLKQEKSCLHDELIFTVEREKRKDELLDI 294
Cdd:TIGR04523 337 ISQLNEQISQLKKELTNSESENSEKQRELEEKQNeieklkkENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKK 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 295 AKSKQDRTNSELQNLRQIYVKQQSDLQFLNfNIESSQELIqihglkMEEPKALECSKDMCLSDLDNNYPKIDIKRERNQK 374
Cdd:TIGR04523 417 LQQEKELLEKEIERLKETIIKNNSEIKDLT-NQDSVKELI------IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQK 489
|
330
....*....|....*.
gi 568937051 375 SLVKDQTFEVMLAQHN 390
Cdd:TIGR04523 490 ELKSKEKELKKLNEEK 505
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
65-183 |
1.07e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 65 IEKQRKELQlliGELKDRDKELNDMvavhQRQLLsweedrQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQAE 144
Cdd:PRK12704 66 IHKLRNEFE---KELRERRNELQKL----EKRLL------QKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEE 132
|
90 100 110
....*....|....*....|....*....|....*....
gi 568937051 145 CQTALQKTQQQLQEMAQkathstlLSEDlEARNENLSST 183
Cdd:PRK12704 133 LEELIEEQLQELERISG-------LTAE-EAKEILLEKV 163
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
219-347 |
1.38e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 219 KMAETCVVREKQDYKQKLKALRIEVNKLKEdlnEKTTEnneQREEIIRLKQEkscLHDEL------IFTVE-REKRKDEL 291
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKEAEAIKK---EALLE---AKEEIHKLRNE---FEKELrerrneLQKLEkRLLQKEEN 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568937051 292 LDIAKSKQDRTNSELQNLRQIYVKQQSDLQFLNFNIESS-----QELIQIHGLKMEEPKAL 347
Cdd:PRK12704 98 LDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELieeqlQELERISGLTAEEAKEI 158
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
59-383 |
1.52e-03 |
|
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: 42.02 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 59 EVETSTIEKQRKELQLLIGELKDRDKELNDMVAVHQrQLLSWEEDRQKVLTLEercsklegeLHKRTDIIKSLMKKVKTL 138
Cdd:pfam05483 334 EAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQ-QRLEKNEDQLKIITME---------LQKKSSELEEMTKFKNNK 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 139 ESNQAECQTALQKTQQQLQEMAQKAThstlLSEDLEARNENLSSTLvdlSAQDKDIIEavnhisdcsgkfklLEHALRDA 218
Cdd:pfam05483 404 EVELEELKKILAEDEKLLDEKKQFEK----IAEELKGKEQELIFLL---QAREKEIHD--------------LEIQLTAI 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 219 KMAETCVVREKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKSCLHDELIFTVEREKRKDELLDIAKSK 298
Cdd:pfam05483 463 KTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEK 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 299 QDRTNSELQNLRQIYVKQQSDLQFLNFNIESSQELIQIHGLKMEEPKALECSKDMCLSDLDNNYPKIDIKRERNQKSLVK 378
Cdd:pfam05483 543 EMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKK 622
|
....*
gi 568937051 379 DQTFE 383
Cdd:pfam05483 623 KGSAE 627
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
59-299 |
1.52e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.98 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 59 EVETSTIEKQRKELQLLIGELKDRDKELNDMVAVH-----QRQLLSWEEDRQKvltLEERCSKLEGELHKRTDIIKSLMK 133
Cdd:TIGR02169 757 KSELKELEARIEELEEDLHKLEEALNDLEARLSHSripeiQAELSKLEEEVSR---IEARLREIEQKLNRLTLEKEYLEK 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 134 KVKTLESNQAECQTALQKTQQQLQEMAQKAthstllsEDLEARNENLSSTLVDLSAQDKDIieavnhisdcsgkfklleh 213
Cdd:TIGR02169 834 EIQELQEQRIDLKEQIKSIEKEIENLNGKK-------EELEEELEELEAALRDLESRLGDL------------------- 887
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 214 alrdakmaetcvVREKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKSCLHDELIFTVEREKRKDELLD 293
Cdd:TIGR02169 888 ------------KKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLED 955
|
....*.
gi 568937051 294 IAKSKQ 299
Cdd:TIGR02169 956 VQAELQ 961
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
65-292 |
2.76e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 65 IEKQRKELQLLIGELKDRDKELndmvavhQRQLLSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQAE 144
Cdd:COG4372 68 LEQARSELEQLEEELEELNEQL-------QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 145 CQTALQKTQQQLQEMAQKATHstLLSEDLEARNENLSSTLVDLSAQDKDIIEAVNHISDCSGKFKLLEHALRDAKMAETC 224
Cdd:COG4372 141 LQSEIAEREEELKELEEQLES--LQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAE 218
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568937051 225 VVREKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKSCLHDELIFTVEREKRKDELL 292
Cdd:COG4372 219 ELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELE 286
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
52-378 |
2.77e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.11 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 52 RRQNIGSEVETSTIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQKVLTLEERCSKLEGELHKRT--DIIK 129
Cdd:pfam02463 154 RRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLylDYLK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 130 SLMKKVKTLESNQAECQtalQKTQQQLQEMAQKATHSTLLSEDLEARNENLSSTLVDLSAQDKDIIEAVNHISdcsgKFK 209
Cdd:pfam02463 234 LNEERIDLLQELLRDEQ---EEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELL----KLE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 210 LLEHALRDAKMAETCVVREKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKSCLHDELIFTV----ERE 285
Cdd:pfam02463 307 RRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKklesERL 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 286 KRKDELLDIAKSKQDRTNSELQNLRQIYVKQQSDLQFLNFNIESSQELIQIHGLKMEEPKALECSKDMCLSDLDNNYPKI 365
Cdd:pfam02463 387 SSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELE 466
|
330
....*....|...
gi 568937051 366 DIKRERNQKSLVK 378
Cdd:pfam02463 467 LKKSEDLLKETQL 479
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
65-256 |
3.17e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.77 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 65 IEKQRK-------ELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQKVltlEERCSKLEGELHKRTDIIKSLMKKVKT 137
Cdd:PHA02562 204 IEEQRKkngeniaRKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDP---SAALNKLNTAAAKIKSKIEQFQKVIKM 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 138 LESNQaECQTALQK---TQQQLQEMAQKATHSTLLSEDLEARNENLSSTLVDLSAQDKDIIEAVNHISDCSGKFKLLEHA 214
Cdd:PHA02562 281 YEKGG-VCPTCTQQiseGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDK 359
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568937051 215 LRDAKMAETCVVREKQDYKQKLKALRIEVNKLKEDLNEKTTE 256
Cdd:PHA02562 360 AKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
63-203 |
3.48e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 63 STIEKQRKELQLLIGELKDRDKELNDMVAvHQRQLLSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQ 142
Cdd:COG4717 98 EELEEELEELEAELEELREELEKLEKLLQ-LLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQ 176
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568937051 143 AECQTALQK----TQQQLQEMAQKAthstllsEDLEARNENLSSTLVDLSAQDKDIIEAVNHISD 203
Cdd:COG4717 177 EELEELLEQlslaTEEELQDLAEEL-------EELQQRLAELEEELEEAQEELEELEEELEQLEN 234
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
133-295 |
3.70e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 133 KKVKTLESNQAECQTALQKTQQQLQEMAQKAthstllsEDLEARNENLSsTLVDLSAQDKDIIEAVNHISDcsgkfklLE 212
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAEL-------DALQERREALQ-RLAEYSWDEIDVASAEREIAE-------LE 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 213 HALRDAKMAetcvvrekqdyKQKLKALRIEVNKLKEDLNEkttenneQREEIIRLKQEKSCLHDELIFTVEREKRKDELL 292
Cdd:COG4913 675 AELERLDAS-----------SDDLAALEEQLEELEAELEE-------LEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
...
gi 568937051 293 DIA 295
Cdd:COG4913 737 EAA 739
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
138-336 |
3.90e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 138 LESNQAECQTALQKTQQQLQEMAQKatHSTLlseDLEARNENLSSTLVDLSAQdkdIIEAVNHISDCSGKFKLLEHALRD 217
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQK--NGLV---DLSEEAKLLLQQLSELESQ---LAEARAELAEAEARLAALRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 218 AKMAETCVVR--EKQDYKQKLKALRIEVnklkEDLNEKTTENNEQreeIIRLKQEKSCLHDELiftverEKRKDELLDIA 295
Cdd:COG3206 252 GPDALPELLQspVIQQLRAQLAELEAEL----AELSARYTPNHPD---VIALRAQIAALRAQL------QQEAQRILASL 318
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 568937051 296 KSKQDRTNSELQNLRQIYVKQQSDLQFLNfniESSQELIQI 336
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLAELP---ELEAELRRL 356
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
53-352 |
4.22e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 53 RQNIGSEVETSTIEKQRKELQLLIGELKDRDKELNDmvavhqrQLLSWEEDR-QKVLTLEERCSKLEGELHKRTDIiKSL 131
Cdd:PRK02224 185 QRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDE-------EIERYEEQReQARETRDEADEVLEEHEERREEL-ETL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 132 MKKVKTLESNQAECQTALQKTQQQLQEmaQKATHSTLLSEDLEARNEnlsstlVDLSAQDKDIIEAvnHISDCSGKFKLL 211
Cdd:PRK02224 257 EAEIEDLRETIAETEREREELAEEVRD--LRERLEELEEERDDLLAE------AGLDDADAEAVEA--RREELEDRDEEL 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 212 EHALRDAKMAETCVVREKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKSCLHDELIFTVEREKRKDEL 291
Cdd:PRK02224 327 RDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVD 406
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568937051 292 LDIAKSKQDRTNSELQNLRQIYVKQQSDLQFLNFNIESSQELiqihglkMEEPKALECSKD 352
Cdd:PRK02224 407 LGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAL-------LEAGKCPECGQP 460
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
63-307 |
4.39e-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: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 63 STIEKQRKELQLLIGELKDRDKELNDMvavhqrqllsweedRQKVLTLEERCSKLEGElhkrtdiIKSLMKKVKTLESNQ 142
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAELEEL--------------NEEYNELQAELEALQAE-------IDKLQAEIAEAEAEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 143 AECQTALQKtqqQLQEMAQKATHSTLLSEDLEArnENLSSTLvdlsaqdkDIIEAVNHISDcsgkfkllehalRDAKMae 222
Cdd:COG3883 82 EERREELGE---RARALYRSGGSVSYLDVLLGS--ESFSDFL--------DRLSALSKIAD------------ADADL-- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 223 tcvVREKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKSCLHDELIFTVEREKRKDELLDIAKSKQDRT 302
Cdd:COG3883 135 ---LEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
....*
gi 568937051 303 NSELQ 307
Cdd:COG3883 212 AAAAA 216
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
54-335 |
4.64e-03 |
|
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: 40.39 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 54 QNIGSEVETSTIEKQRKELQLLIGELKD-RDKELNDMVavhqrqllswEEDRQKVLTLEERCSKLEGELHKRTDIIKSLM 132
Cdd:TIGR04523 183 LNIQKNIDKIKNKLLKLELLLSNLKKKIqKNKSLESQI----------SELKKQNNQLKDNIEKKQQEINEKTTEISNTQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 133 KKVKTLESNQAECQTALQKTQQQLQEMAQKATHSTLLSEDLEA--------RNENLSSTL-VDLSAQDKDIIEAVNHISD 203
Cdd:TIGR04523 253 TQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSeisdlnnqKEQDWNKELkSELKNQEKKLEEIQNQISQ 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 204 CSGKFKLLEHALRDAKMAET---------------------CVVREKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQRE 262
Cdd:TIGR04523 333 NNKIISQLNEQISQLKKELTnsesensekqreleekqneieKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDE 412
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568937051 263 EIIRLKQEKSCLHDEL-IFTVEREKRKDELLDIAKSKQDRTNS--ELQNLRQIYVKQQSDLQFLNFNIESSQELIQ 335
Cdd:TIGR04523 413 QIKKLQQEKELLEKEIeRLKETIIKNNSEIKDLTNQDSVKELIikNLDNTRESLETQLKVLSRSINKIKQNLEQKQ 488
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
85-316 |
6.44e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 6.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 85 ELNDMVAVHQRQLLSWEeDRQKVLTLEERCSKLEGELhkrtdiikslmkkvktlesnqAECQTALQKTQQQLQEMAQKAt 164
Cdd:COG4913 591 EKDDRRRIRSRYVLGFD-NRAKLAALEAELAELEEEL---------------------AEAEERLEALEAELDALQERR- 647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 165 hstllseDLEARNENLSSTLVDLSAQDKDIIEAVNHISDC---SGKFKLLEHALRDAKMAETCVVREKQDYKQKLKALRI 241
Cdd:COG4913 648 -------EALQRLAEYSWDEIDVASAEREIAELEAELERLdasSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEK 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 242 EVNKLKEDLnEKTTENNEQREEIIRLKQEKSC---LHDELIFTVEREKRK--DELLDIAKSKQDRTNSELQNLRQIYVKQ 316
Cdd:COG4913 721 ELEQAEEEL-DELQDRLEAAEDLARLELRALLeerFAAALGDAVERELREnlEERIDALRARLNRAEEELERAMRAFNRE 799
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
61-324 |
6.51e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 39.41 E-value: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 61 ETSTIEKQRKELQLLIGELKDRDKELNDmvavhqrqllsweedrqkvltLEERCSKLEGELHKRTDIIKSLMKKVKTLES 140
Cdd:pfam15905 71 ESKDQKELEKEIRALVQERGEQDKRLQA---------------------LEEELEKVEAKLNAAVREKTSLSASVASLEK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 141 NQAECQTALQKTQQQLQEMAQKATHSTLLSEDLEARNENLSS----------TLVDLSAQDKDIIEAVNHISDCSGKFKL 210
Cdd:pfam15905 130 QLLELTRVNELLKAKFSEDGTQKKMSSLSMELMKLRNKLEAKmkevmakqegMEGKLQVTQKNLEHSKGKVAQLEEKLVS 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 211 LEhalrDAKMAETCVVREKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKSCLHDELIFTVER------ 284
Cdd:pfam15905 210 TE----KEKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDlnekck 285
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 568937051 285 --EKRKDELLDIAKSKQDRTNSELQNLRQIYVKQQSDLQFLN 324
Cdd:pfam15905 286 llESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQ 327
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
65-335 |
7.94e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.51 E-value: 7.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 65 IEKQRKELQLLIGELKDRDKELNDMvavhQRQLLSWEEDRQKVLtlEERCSKLEgelhkrtdiikslmkkVKTLESNQAE 144
Cdd:PRK11281 75 IDRQKEETEQLKQQLAQAPAKLRQA----QAELEALKDDNDEET--RETLSTLS----------------LRQLESRLAQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 145 CQTALQKTQQQLqemaqkATHSTLLSeDLEARNENLSSTLVDLSAQDKDIIEAVNHISDCSgkfKLLEHALRDAKMAETC 224
Cdd:PRK11281 133 TLDQLQNAQNDL------AEYNSQLV-SLQTQPERAQAALYANSQRLQQIRNLLKGGKVGG---KALRPSQRVLLQAEQA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 225 VVREKQDYKQKLkalrIEVNKLKEDLNEKttENNEQREEIIRLKQEKsclhdELIFTVEREKRKDElldiakSKQdrTNS 304
Cdd:PRK11281 203 LLNAQNDLQRKS----LEGNTQLQDLLQK--QRDYLTARIQRLEHQL-----QLLQEAINSKRLTL------SEK--TVQ 263
|
250 260 270
....*....|....*....|....*....|...
gi 568937051 305 ELQNLRQIYVKQQSDL--QFLNFNIESSQELIQ 335
Cdd:PRK11281 264 EAQSQDEAARIQANPLvaQELEINLQLSQRLLK 296
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
71-321 |
8.19e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.56 E-value: 8.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 71 ELQLLIGELKDRDKELNDMVAVHQRQllsweedRQKVLTLEERCSKLEgELHKRTDIIK--SLMKKVKTLESNQAECQTA 148
Cdd:PRK04863 838 ELRQLNRRRVELERALADHESQEQQQ-------RSQLEQAKEGLSALN-RLLPRLNLLAdeTLADRVEEIREQLDEAEEA 909
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 149 LQKTQQQLQEMAQKATHSTLLSED------LEARNENLSSTLVDLSAQD---KDIIEAVNHIS----------------D 203
Cdd:PRK04863 910 KRFVQQHGNALAQLEPIVSVLQSDpeqfeqLKQDYQQAQQTQRDAKQQAfalTEVVQRRAHFSyedaaemlaknsdlneK 989
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 204 CSGKFKLLEHALRDAKMAETCVVREKQDYKQ---KLK----ALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKscLHD 276
Cdd:PRK04863 990 LRQRLEQAEQERTRAREQLRQAQAQLAQYNQvlaSLKssydAKRQMLQELKQELQDLGVPADSGAEERARARRDE--LHA 1067
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 568937051 277 ELIftvEREKRKDELLdiakSKQDRTNSELQNLRQIYVKQQSDLQ 321
Cdd:PRK04863 1068 RLS---ANRSRRNQLE----KQLTFCEAEMDNLTKKLRKLERDYH 1105
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
51-271 |
9.90e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 9.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 51 YRRQNIGSEVE-TSTIEKQRKELQLLIGELKDRDKELNDM-------VAVHQRQLLSWEEDRQKVLTLEERCSKLEGELH 122
Cdd:PRK03918 176 RRIERLEKFIKrTENIEELIKEKEKELEEVLREINEISSElpelreeLEKLEKEVKELEELKEEIEELEKELESLEGSKR 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 123 KRTDIIKSLMKKVKTLESNQAEcqtaLQKTQQQLQEMAQKATHSTLLSE----------DLEARNENLSSTLVDLSAQDK 192
Cdd:PRK03918 256 KLEEKIRELEERIEELKKEIEE----LEEKVKELKELKEKAEEYIKLSEfyeeyldelrEIEKRLSRLEEEINGIEERIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937051 193 DIIEAVNHISDCSGKFKLLEHAL----RDAKMAETcvVREKQDYKQKLKA-----------------------LRIEVNK 245
Cdd:PRK03918 332 ELEEKEERLEELKKKLKELEKRLeeleERHELYEE--AKAKKEELERLKKrltgltpeklekeleelekakeeIEEEISK 409
|
250 260
....*....|....*....|....*.
gi 568937051 246 LKEDLNEKTTENNEQREEIIRLKQEK 271
Cdd:PRK03918 410 ITARIGELKKEIKELKKAIEELKKAK 435
|
|
| |
