|
Name |
Accession |
Description |
Interval |
E-value |
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
18-280 |
1.58e-93 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 285.56 E-value: 1.58e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 18 LTSCEAELQELMKQIDIMVAHKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYK 97
Cdd:pfam17045 1 LSSCEAELQELMKQIDIMVAHKKSEWEGQTRALETRLDIREEELLSARNTLERKHKEIGLLRQQLEELEKGKQELVAKYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 98 QELKKLHEELCILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKAL 177
Cdd:pfam17045 81 QQLQKLQEELSKLKRSYEKLQRKQLKEAREEAKSREEDRSELSRLNGKLEEFRQKSLEWEQQRLQYQQQVASLEAQRKAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 178 AEQSEIIQA-----QLVNRKQKLEsvelSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKE 252
Cdd:pfam17045 161 AEQSSLIQSaayqvQLEGRKQCLE----ASQSEIQRLRSKLERAQDSLCAQELELERLRMRVSELGDSNRKLLEEQQRLL 236
|
250 260
....*....|....*....|....*...
gi 1212626320 253 EKLRESEKLLEALQEEKRELKAALQSQE 280
Cdd:pfam17045 237 EELRMSQRQLQVLQNELMELKATLQSQD 264
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
57-401 |
1.98e-11 |
|
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: 67.00 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 57 REQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHE---ELCILKRSYEKLQKKQMREFRGNTKNHR 133
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEElsrQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 134 ED---RSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRK---QKLESVELSSQSEIQ 207
Cdd:TIGR02168 755 ELtelEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNeeaANLRERLESLERRIA 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 208 HLSSKLERANDTICANELEIERLTMRVNDLvGTSMTVLQEQQQKEEKLRES-EKLLEALQEEKRELKAALQSQENLIHEA 286
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESLAAEIEEL-EELIEELESELEALLNERASlEEALALLRSELEELSEELRELESKRSEL 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 287 RIQKEKLQEKVKATNTQhaVEAIRPREESLAEkKYTSQGQGDLDSVLSQLNFTHTSEDLLQAEVTCLEGSLESVSAtckq 366
Cdd:TIGR02168 914 RRELEELREKLAQLELR--LEGLEVRIDNLQE-RLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGP---- 986
|
330 340 350
....*....|....*....|....*....|....*
gi 1212626320 367 LSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQ 401
Cdd:TIGR02168 987 VNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
23-367 |
2.70e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 66.24 E-value: 2.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 23 AELQELMKQIDIMVAHKKSEWEG----RTHAL---ETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTME 95
Cdd:TIGR02169 180 EEVEENIERLDLIIDEKRQQLERlrreREKAEryqALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 96 YKQELKKLHEELCILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRK 175
Cdd:TIGR02169 260 ISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIE 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 176 ALAEQSEIIQ---AQLVNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKE 252
Cdd:TIGR02169 340 ELEREIEEERkrrDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLS 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 253 EKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHaveaIRPREESLAEKKYTSQGQGDLDSV 332
Cdd:TIGR02169 420 EELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQEL----YDLKEEYDRVEKELSKLQRELAEA 495
|
330 340 350
....*....|....*....|....*....|....*
gi 1212626320 333 LSQLNFTHTSEDLLQAEVTCLEGSLESVSATCKQL 367
Cdd:TIGR02169 496 EAQARASEERVRGGRAVEEVLKASIQGVHGTVAQL 530
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
136-464 |
2.01e-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: 60.46 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 136 RSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVElssqSEIQHLSSKLER 215
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE----AEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 216 ANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQE 295
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 296 KVKATNTQhaveaIRPREESLAEkkytsqgqgdldsvlsqlnfthtsedlLQAEVTCLEGSLESVSATCKQLSQELMEKY 375
Cdd:TIGR02168 832 RIAATERR-----LEDLEEQIEE---------------------------LSEDIESLAAEIEELEELIEELESELEALL 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 376 EELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSALEgmkmEISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDK 455
Cdd:TIGR02168 880 NERASLEEALALLRSELEELSEELRELESKRSELRR----ELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEE 955
|
....*....
gi 1212626320 456 AVEHKEILD 464
Cdd:TIGR02168 956 AEALENKIE 964
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
37-338 |
2.48e-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: 56.99 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 37 AHKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEELCILKRSYEK 116
Cdd:TIGR02168 224 ELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 117 LQKKQMREfrgntknhREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLE 196
Cdd:TIGR02168 304 KQILRERL--------ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 197 SVE---LSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKE-----EKLRESEKLLEALQEE 268
Cdd:TIGR02168 376 ELEeqlETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElkelqAELEELEEELEELQEE 455
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1212626320 269 KRELKAALQSQENLIHEARIQKEKLQEKVK-ATNTQHAVEAIRPREESLAE-----KKYTSQGQGDLDSVLSQLNF 338
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAqLQARLDSLERLQENLEGFSEgvkalLKNQSGLSGILGVLSELISV 531
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
86-404 |
3.09e-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: 56.61 E-value: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 86 EKIKQEMTMEYKQELKKLHEELCILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQ 165
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 166 QVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVELS-SQSEIQHLSSKLERANDTICANELEIERLTMRVNDLvgtsmtv 244
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEEDLHKLEEALNDLEARlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRL------- 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 245 LQEQQQKEEKLRESEKLLEALQEEKRELKAAlqsqenlIHEARIQKEKLQEKVKatNTQHAVEAIRPREESLaekkytsq 324
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKE-------IENLNGKKEELEEELE--ELEAALRDLESRLGDL-------- 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 325 gQGDLDSVLSQLNFTHTSEDLLQAEVTCLEGSLESVSATCKQLSQELMEkYEELKRMEAHNNEYKAEIKKLKEQILQGEQ 404
Cdd:TIGR02169 888 -KKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSE-IEDPKGEDEEIPEEELSLEDVQAELQRVEE 965
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
95-362 |
2.39e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 95 EYKQELKKLHEELCILKRSYEKLQKKQmrefRGNTKNHREDRSEIERLTAKIEEFRQKSL-------DWEKQRLIYQQQV 167
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAEL----AELEAELEELRLELEELELELEEAQAEEYellaelaRLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 168 SSLEAQRKALAEQSEIIQAQLVNRKQKLESVELSSQS------EIQHLSSKLERANDTICANELEIERLTMRVNDLVGTS 241
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEaeeeleEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 242 MTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAIRPREESLAEKKY 321
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1212626320 322 TSQGQGDLDSVLSQLNFTHTSEDLLQAEVTCLEGSLESVSA 362
Cdd:COG1196 472 AALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKA 512
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
35-380 |
3.15e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.15 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 35 MVAHKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVE----EHEKIKQEMTmEYKQELKKLHEELCIL 110
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEqleqEEEKLKERLE-ELEEDLSSLEQEIENV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 111 KRSYEKLqkkqmrefrgntknhredRSEIERLTAKIEEFRQKSLDWEkqRLIYQQQVSSLEAQRKALAEQSEIIQAQLVN 190
Cdd:TIGR02169 757 KSELKEL------------------EARIEELEEDLHKLEEALNDLE--ARLSHSRIPEIQAELSKLEEEVSRIEARLRE 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 191 RKQKLESVELSSQ---SEIQHLSSKLERANDTICANELEIERLTMRVNDLvgtsmtvLQEQQQKEEKLRESEKLLEALQE 267
Cdd:TIGR02169 817 IEQKLNRLTLEKEyleKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL-------EEELEELEAALRDLESRLGDLKK 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 268 EKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAV--EAIRPREESLAEKKYTSQGQGDLDSV------------- 332
Cdd:TIGR02169 890 ERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEAleEELSEIEDPKGEDEEIPEEELSLEDVqaelqrveeeira 969
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1212626320 333 LSQLNFTHTSE-DLLQAEVTCLEGSLESVSATCKQLsQELMEKYEELKR 380
Cdd:TIGR02169 970 LEPVNMLAIQEyEEVLKRLDELKEKRAKLEEERKAI-LERIEEYEKKKR 1017
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
78-326 |
1.09e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 78 LHQQVEEHE-KIKQEMTMEYKQELKKLHEELcilkRSYEKlQKKQMREFRGNTK----NHREDRSEIERLTAKIEEFRQK 152
Cdd:PRK02224 192 LKAQIEEKEeKDLHERLNGLESELAELDEEI----ERYEE-QREQARETRDEADevleEHEERREELETLEAEIEDLRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 153 SLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQ----------LVNRKQKLESVELSSQSEIQHLSSKLERANDTICA 222
Cdd:PRK02224 267 IAETEREREELAEEVRDLRERLEELEEERDDLLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAES 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 223 NELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAA-------LQSQENLIHEARIQKEKLQE 295
Cdd:PRK02224 347 LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERfgdapvdLGNAEDFLEELREERDELRE 426
|
250 260 270
....*....|....*....|....*....|...
gi 1212626320 296 KVKATNT--QHAVEAIRPREESLAEKKYTSQGQ 326
Cdd:PRK02224 427 REAELEAtlRTARERVEEAEALLEAGKCPECGQ 459
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
159-482 |
1.35e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 51.38 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 159 QRLIYQQQVSSLEAQRKALAEQSEIIQAQLvNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDL- 237
Cdd:pfam12128 588 KRIDVPEWAASEEELRERLDKAEEALQSAR-EKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEk 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 238 VGTSMTVLQEQQQKEEKLRESEKLLEALqeeKRELKAALQSQENLIHEARIQK-EKLQEKVKATNTQHA--VEAIRPREE 314
Cdd:pfam12128 667 DKKNKALAERKDSANERLNSLEAQLKQL---DKKHQAWLEEQKEQKREARTEKqAYWQVVEGALDAQLAllKAAIAARRS 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 315 SLaeKKYTSQGQGDLDSVLSQLNFTHTSEDLLQAEVTCLEGSLESvsatCKQLSQELMEKYEELK-RMEAHNNEYKAEIK 393
Cdd:pfam12128 744 GA--KAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIER----IAVRRQEVLRYFDWYQeTWLQRRPRLATQLS 817
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 394 KLKEQILQGEQSYSSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLR-----AEMQKAEDKAVEHKEILDQLES 468
Cdd:pfam12128 818 NIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSklatlKEDANSEQAQGSIGERLAQLED 897
|
330
....*....|....
gi 1212626320 469 LKLENRHLSEMVMK 482
Cdd:pfam12128 898 LKLKRDYLSESVKK 911
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1-437 |
3.70e-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: 49.73 E-value: 3.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 1 MEALLEGIQNRGHGGGFLTSCE-AELQELMKQIDIMVAHKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLH 79
Cdd:pfam15921 297 IQSQLEIIQEQARNQNSMYMRQlSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLD 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 80 QQVEEhekikqemtmeYKQELKKLHEELCILKRSYEKLQKKQMrefrGNT------KNHREDRS-EIERLTAKIEEFRQK 152
Cdd:pfam15921 377 DQLQK-----------LLADLHKREKELSLEKEQNKRLWDRDT----GNSitidhlRRELDDRNmEVQRLEALLKAMKSE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 153 SLDWEKQRLIYQQ-------QVSSLEAQRKALAEQSEIIQAQLVNRKQKLESvelsSQSEIQHLSSKLERANDTICANEL 225
Cdd:pfam15921 442 CQGQMERQMAAIQgknesleKVSSLTAQLESTKEMLRKVVEELTAKKMTLES----SERTVSDLTASLQEKERAIEATNA 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 226 EIERLTMRVNdlvgtsmTVLQEQQQkeekLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKatntQHA 305
Cdd:pfam15921 518 EITKLRSRVD-------LKLQELQH----LKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVG----QHG 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 306 veaiRPREESLAEKKYTSQGQGDLDSVLSQLNFTHTSEDL----LQAEVTCLEgsLESVS---------ATCKQLSQELM 372
Cdd:pfam15921 583 ----RTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAkireLEARVSDLE--LEKVKlvnagserlRAVKDIKQERD 656
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1212626320 373 EKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSALEGMKMEISHLTQELHQRDITIASTKGS 437
Cdd:pfam15921 657 QLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGS 721
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
164-392 |
6.36e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 6.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 164 QQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVElssqsEIQHLSSKLERANDTicanELEIERLTMRvndlvgtsmt 243
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQ-----ERREALQRLAEYSWD----EIDVASAERE---------- 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 244 vLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQhaVEAIRPREESlAEKKYTS 323
Cdd:COG4913 670 -IAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE--LDELQDRLEA-AEDLARL 745
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1212626320 324 QGQGDLDSVLSQLNFTHTSEDLLQAevtcLEGSLESVSATCKQLSQELMEKyeelkrMEAHNNEYKAEI 392
Cdd:COG4913 746 ELRALLEERFAAALGDAVERELREN----LEERIDALRARLNRAEEELERA------MRAFNREWPAET 804
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
95-299 |
1.58e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.07 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 95 EYKQELKKLHEELCILKRSYEKLQKKQmrefrgntknhREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQR 174
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEE-----------KALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 175 KALAEQSEIIQAQLVNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEK 254
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1212626320 255 LRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKA 299
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
136-296 |
1.83e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 136 RSEIERLTAKIEEFRQKS--LDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESV-----ELSSQSEIQH 208
Cdd:COG3206 188 RKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGpdalpELLQSPVIQQ 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 209 LSSKLERAndticanELEIERLTMRVNDLvGTSMTVLQEQQQ--KEEKLRESEKLLEALQEEKRELKAALQSQENLIHEA 286
Cdd:COG3206 268 LRAQLAEL-------EAELAELSARYTPN-HPDVIALRAQIAalRAQLQQEAQRILASLEAELEALQAREASLQAQLAQL 339
|
170
....*....|
gi 1212626320 287 RIQKEKLQEK 296
Cdd:COG3206 340 EARLAELPEL 349
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
133-308 |
5.89e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 5.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 133 REDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVelssQSEIQHLSSK 212
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL----EKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 213 LERANDTI---------------------CANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRE 271
Cdd:COG4942 99 LEAQKEELaellralyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190
....*....|....*....|....*....|....*..
gi 1212626320 272 LKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEA 308
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAEL 215
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
157-485 |
1.34e-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: 44.66 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 157 EKQRLIYQQQVSSLEAQRKALAEQseiiqaqlvnrKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVND 236
Cdd:TIGR02168 224 ELELALLVLRLEELREELEELQEE-----------LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 237 LVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHaveairprEESL 316
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL--------EELE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 317 AEKKYTSQGQGDLDSVLSQLNfthtsedllqAEVTCLEGSLESVSAtckqlsqelmekyeELKRMEAHNNEYKAEIKKLK 396
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLR----------SKVAQLELQIASLNN--------------EIERLEARLERLEDRRERLQ 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 397 EQILQGEQSYSSA-LEGMKMEISHLTQELHQ---RDITIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEILDQLESLKLE 472
Cdd:TIGR02168 421 QEIEELLKKLEEAeLKELQAELEELEEELEElqeELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN 500
|
330
....*....|...
gi 1212626320 473 NRHLSEMVMKLEL 485
Cdd:TIGR02168 501 LEGFSEGVKALLK 513
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
228-478 |
1.77e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 228 ERLTmRVNDL---VGTSMTVLQEQQQKEEKLREseklleaLQEEKRELKAALQSQEnlIHEARIQKEKLQEKVKATNTQH 304
Cdd:COG1196 186 ENLE-RLEDIlgeLERQLEPLERQAEKAERYRE-------LKEELKELEAELLLLK--LRELEAELEELEAELEELEAEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 305 AVEAirpREESLAEKKYTSQGQgDLDSVLSQLNFTHTSEDLLQAEVTCLEGSLESVSATCKQLSQELMEKYEELKRMEAH 384
Cdd:COG1196 256 EELE---AELAELEAELEELRL-ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 385 NNEYKAEIKKLKEQILQGEQSYSSALEgmkmEISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEILD 464
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEEAEA----ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
|
250
....*....|....
gi 1212626320 465 QLESLKLENRHLSE 478
Cdd:COG1196 408 AEEALLERLERLEE 421
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
131-303 |
2.85e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 131 NHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQ--VSSLEAQRKALAEQSEIIQAQLVNRKQKLESVelssQSEIQH 208
Cdd:COG3206 169 RREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEA----EARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 209 LSSKLERANDTICA--NELEIERLTMRVNDLVgtsmtvlQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQ-ENLIHE 285
Cdd:COG3206 245 LRAQLGSGPDALPEllQSPVIQQLRAQLAELE-------AELAELSARYTPNHPDVIALRAQIAALRAQLQQEaQRILAS 317
|
170
....*....|....*...
gi 1212626320 286 ARIQKEKLQEKVKATNTQ 303
Cdd:COG3206 318 LEAELEALQAREASLQAQ 335
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
98-281 |
3.26e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 98 QELKKLHEELCILKRSYEKLQkkQMREFRGNTKNHREDRSEIERLTAKIE-EFRQKSLDWEKQRLI-YQQQVSSLEAQRK 175
Cdd:COG4913 235 DDLERAHEALEDAREQIELLE--PIRELAERYAAARERLAELEYLRAALRlWFAQRRLELLEAELEeLRAELARLEAELE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 176 ALAEQSEIIQAQLVNRKQKLESVELSS----QSEIQHLSSKLERANDTICANELEIERLTMRVND-----------LVGT 240
Cdd:COG4913 313 RLEARLDALREELDELEAQIRGNGGDRleqlEREIERLERELEERERRRARLEALLAALGLPLPAsaeefaalraeAAAL 392
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1212626320 241 SMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQEN 281
Cdd:COG4913 393 LEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
57-301 |
4.78e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 4.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 57 REQELKSLRSQLDVTHKEVGMLHQQVEEHEKikqemtmeykqELKKLHEELCILKRSYEKLQKKQmrefrgntknhREDR 136
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLK-----------QLAALERRIAALARRIRALEQEL-----------AALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 137 SEIERLTAKIEEFRQKSLDWEKQ--RLIYQQQVSSLEAQRKALAEQSEIiqAQLVNRKQKLESVELSSQSEIQHLSSKLE 214
Cdd:COG4942 83 AELAELEKEIAELRAELEAQKEElaELLRALYRLGRQPPLALLLSPEDF--LDAVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 215 RANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQ 294
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
....*..
gi 1212626320 295 EKVKATN 301
Cdd:COG4942 241 ERTPAAG 247
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
54-489 |
5.37e-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: 42.70 E-value: 5.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 54 LKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEELCILKRSYEKLQKKQMREFRGNTKNhR 133
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKI-K 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 134 EDRSEIERLTAKIEEFR-QKSLDWEKQ-RLIYQQQVSSLEAQRKALAEQSEIIQ------AQLVNRKQKLESVELSSQSE 205
Cdd:TIGR04523 285 ELEKQLNQLKSEISDLNnQKEQDWNKElKSELKNQEKKLEEIQNQISQNNKIISqlneqiSQLKKELTNSESENSEKQRE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 206 IQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHE 285
Cdd:TIGR04523 365 LEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 286 ARIQKEKLQEKVKATNTQHAVEAIRPREESLAEKKYTS---QGQGDLDSVLSQLNFTHTSEDLLQAEVTCLEGSLESVSA 362
Cdd:TIGR04523 445 LTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQnleQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKE 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 363 TCKQLSQELMEKYEELKRMEAHNNEYKAEIKK--LKEQILQGEQSyssaLEGMKMEISHLTQELHQRDITIASTKGSSSD 440
Cdd:TIGR04523 525 KIEKLESEKKEKESKISDLEDELNKDDFELKKenLEKEIDEKNKE----IEELKQTQKSLKKKQEEKQELIDQKEKEKKD 600
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1212626320 441 MEKRLRAEMQKAEdkavehkEILDQLESLKLENRHLSEMVMKLELGLHE 489
Cdd:TIGR04523 601 LIKEIEEKEKKIS-------SLEKELEKAKKENEKLSSIIKNIKSKKNK 642
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
39-484 |
5.51e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 39 KKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMT------MEYKQELKKLHEELCILKR 112
Cdd:PRK03918 187 RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEelekelESLEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 113 SYEKLQK--KQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEiiqaqlvn 190
Cdd:PRK03918 267 RIEELKKeiEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE-------- 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 191 RKQKLESVELSSQSEIQHLSSKlERANDTICANELEIERLTMRVNDLvgtsmtvlqEQQQKEEKLRESEKLLEALQEEKR 270
Cdd:PRK03918 339 RLEELKKKLKELEKRLEELEER-HELYEEAKAKKEELERLKKRLTGL---------TPEKLEKELEELEKAKEEIEEEIS 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 271 ELKAALQSQENLIHEARIQKEKLQEK------VKATNTQHAVEAIRPR-----EESLAEKKYTSQGQGDLDSVLSQLNFT 339
Cdd:PRK03918 409 KITARIGELKKEIKELKKAIEELKKAkgkcpvCGRELTEEHRKELLEEytaelKRIEKELKEIEEKERKLRKELRELEKV 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 340 HTSEDLLQAEVTCLEGSLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQiLQGEQSYSSALEGMKMEISH 419
Cdd:PRK03918 489 LKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKE-LEKLEELKKKLAELEKKLDE 567
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1212626320 420 LTQELHQRdITIASTKGSSS--DMEKRLRaEMQKAEDKAVE----HKEILDQLESLKLENRHLSEMVMKLE 484
Cdd:PRK03918 568 LEEELAEL-LKELEELGFESveELEERLK-ELEPFYNEYLElkdaEKELEREEKELKKLEEELDKAFEELA 636
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
110-476 |
6.57e-04 |
|
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: 42.41 E-value: 6.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 110 LKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQ--RLIYQQQVSSLEAQRKALAEQSEIIQAQ 187
Cdd:pfam15921 160 LKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSmsTMHFRSLGSAISKILRELDTEISYLKGR 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 188 LVNRKQKLESVELSSQSEIQHL-SSKLERANDTICANELEIERLTMRVN------DLVGTSMTVLQEQ--QQKEEKLRES 258
Cdd:pfam15921 240 IFPVEDQLEALKSESQNKIELLlQQHQDRIEQLISEHEVEITGLTEKASsarsqaNSIQSQLEIIQEQarNQNSMYMRQL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 259 EKLLEALQEEKRELKAALQSQENLIheariqkEKLQEKVKATNTQHAveairpreESLAEKKYTSQGQGDLDSVLSQL-N 337
Cdd:pfam15921 320 SDLESTVSQLRSELREAKRMYEDKI-------EELEKQLVLANSELT--------EARTERDQFSQESGNLDDQLQKLlA 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 338 FTHTSEDLLQAEVTC---LEGSLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQ---------- 404
Cdd:pfam15921 385 DLHKREKELSLEKEQnkrLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQgkneslekvs 464
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1212626320 405 SYSSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEI-------LDQLESLKLENRHL 476
Cdd:pfam15921 465 SLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLrsrvdlkLQELQHLKNEGDHL 543
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
163-322 |
7.65e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 41.64 E-value: 7.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 163 YQQQVSSLEAQRKALAEQSEIIQAQlVNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDlvgtsM 242
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAE-LDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLAR-----R 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 243 TVLQEQQ-QKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAIRPREESLAEKKY 321
Cdd:pfam00529 130 RVLAPIGgISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLER 209
|
.
gi 1212626320 322 T 322
Cdd:pfam00529 210 T 210
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
54-398 |
8.84e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 8.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 54 LKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEELcilkrsyEKLQKKQMREFRGNTKNHR 133
Cdd:PRK03918 343 LKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEEL-------EKAKEEIEEEISKITARIG 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 134 EDRSEIERLTAKIEEFRQKSL----------DWEKQRLI--YQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLE----- 196
Cdd:PRK03918 416 ELKKEIKELKKAIEELKKAKGkcpvcgreltEEHRKELLeeYTAELKRIEKELKEIEEKERKLRKELRELEKVLKkesel 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 197 SVELSSQSEIQHLSSKLERAN-DTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAA 275
Cdd:PRK03918 496 IKLKELAEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAEL 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 276 LQSQENLIHEARIQ-KEKLQEKVKATNtqHAVEAIRPREESLAEKKYTSQGQGDLDSVLSQLNFTHTSEDLLQAEVTCLE 354
Cdd:PRK03918 576 LKELEELGFESVEElEERLKELEPFYN--EYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELE 653
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1212626320 355 GSL-----ESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQ 398
Cdd:PRK03918 654 KKYseeeyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE 702
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
136-305 |
1.01e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 136 RSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEI---------IQAQLVNRKQKLESVELSSqSEI 206
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYswdeidvasAEREIAELEAELERLDASS-DDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 207 QHLSSKLERAndticanELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKR-ELKAALQSQ-ENLIH 284
Cdd:COG4913 688 AALEEQLEEL-------EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlELRALLEERfAAALG 760
|
170 180
....*....|....*....|...
gi 1212626320 285 EARIQK--EKLQEKVKATNTQHA 305
Cdd:COG4913 761 DAVERElrENLEERIDALRARLN 783
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
270-487 |
1.05e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.97 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 270 RELKAALQSQENLIHEARIQKEKLQEKVKATNTqhavEAIRPREESLAEKKYTSQGQGDLDSVLSQLNFTHTSEDLLQAE 349
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEK----ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 350 VTCLEGSLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQgeqsYSSALEGMKMEISHLTQELHQRDI 429
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ----LKEELKALREALDELRAELTLLNE 817
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1212626320 430 TIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEILDQLESLKLENRHLSEMVMKLELGL 487
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL 875
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
20-220 |
1.68e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 20 SCEAELQELMKQIDIMVAhKKSEWEgrthALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQE--MTMEYK 97
Cdd:COG4913 665 SAEREIAELEAELERLDA-SSDDLA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDElqDRLEAA 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 98 QELKKLHEELCILKRSYEKLQKKQMREFRGNTKNHRED-RSEIERLTAKIEE-FRQKSLDWekqRLIYQQQVSSLEAQRK 175
Cdd:COG4913 740 EDLARLELRALLEERFAAALGDAVERELRENLEERIDAlRARLNRAEEELERaMRAFNREW---PAETADLDADLESLPE 816
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1212626320 176 ALAEQSEIIQAQLVNRKQKL-ESVELSSQSEIQHLSSKLERANDTI 220
Cdd:COG4913 817 YLALLDRLEEDGLPEYEERFkELLNENSIEFVADLLSKLRRAIREI 862
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
233-337 |
2.18e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 233 RVNDLVGTSMTVLQEQQQKEE----KLRESEKLLEALQEEKRELKAAlqsQENLIHEariQKEKLQEKVKAtnTQHAVEA 308
Cdd:PRK00409 517 KLNELIASLEELERELEQKAEeaeaLLKEAEKLKEELEEKKEKLQEE---EDKLLEE---AEKEAQQAIKE--AKKEADE 588
|
90 100
....*....|....*....|....*....
gi 1212626320 309 IRPREESLAEKKYTSQGQGDLDSVLSQLN 337
Cdd:PRK00409 589 IIKELRQLQKGGYASVKAHELIEARKRLN 617
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
24-458 |
2.31e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.98 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 24 ELQELMKQIDIMVAHKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKL 103
Cdd:pfam12128 280 ERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 104 HEELCILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLdwEKQRLIYQQQVSSL----EAQRKALAE 179
Cdd:pfam12128 360 EERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQL--AVAEDDLQALESELreqlEAGKLEFNE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 180 QSEIIQAQLVNRKQKLESVELSS---------QSEIQHLSSKLERANDTICANELEIERLTMR---VNDLVGTSMTVLQE 247
Cdd:pfam12128 438 EEYRLKSRLGELKLRLNQATATPelllqlenfDERIERAREEQEAANAEVERLQSELRQARKRrdqASEALRQASRRLEE 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 248 QQQKEEKLRE-----SEKLLEALQEEK---RELKAALQSQEnLIHEARIQKEKLQEKVKATNTQHAV------------- 306
Cdd:pfam12128 518 RQSALDELELqlfpqAGTLLHFLRKEApdwEQSIGKVISPE-LLHRTDLDPEVWDGSVGGELNLYGVkldlkridvpewa 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 307 ---EAIRpREESLAEKKYTSQG--QGDLDSVLSQLNfthTSEDLLQAEVTCLEGSLESVSATCKQLS----QELMEKYEE 377
Cdd:pfam12128 597 aseEELR-ERLDKAEEALQSARekQAAAEEQLVQAN---GELEKASREETFARTALKNARLDLRRLFdekqSEKDKKNKA 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 378 LKRMEAHNNEYKAEIKKLKEQILQGEQSYSSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDKAV 457
Cdd:pfam12128 673 LAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKAL 752
|
.
gi 1212626320 458 E 458
Cdd:pfam12128 753 E 753
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
18-455 |
2.51e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.80 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 18 LTSCEAELQELMKQIDIMVahkkseweGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYK 97
Cdd:TIGR00606 711 LKSTESELKKKEKRRDEML--------GLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEE 782
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 98 QE---------LKKLHEELCILKRSYEKLQKKQ-----MREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIY 163
Cdd:TIGR00606 783 SAkvcltdvtiMERFQMELKDVERKIAQQAAKLqgsdlDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHL 862
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 164 QQQVSSLEAQRKALAEQSEiiqaqlvnRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVgtsmt 243
Cdd:TIGR00606 863 KSKTNELKSEKLQIGTNLQ--------RRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELI----- 929
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 244 vlqeqQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARiQKEKLQEKVKATNTQHAVEAIRPREESLAEkkyts 323
Cdd:TIGR00606 930 -----SSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGK-DDYLKQKETELNTVNAQLEECEKHQEKINE----- 998
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 324 qgqgDLDSVLSQLNFTHTSEDLLQAEVTclegsLESVSATCKQLSQELMEKYEELKRMEAhnNEYKAEIKKLKEQILQGE 403
Cdd:TIGR00606 999 ----DMRLMRQDIDTQKIQERWLQDNLT-----LRKRENELKEVEEELKQHLKEMGQMQV--LQMKQEHQKLEENIDLIK 1067
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1212626320 404 QSYSSALEGMK---MEISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDK 455
Cdd:TIGR00606 1068 RNHVLALGRQKgyeKEIKHFKKELREPQFRDAEEKYREMMIVMRTTELVNKDLDI 1122
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
247-456 |
2.55e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 247 EQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQ--HAVEAIRPREESLAEKKYTSQ 324
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 325 GQGDLDSVLSQLNFTHTSEDLLQAEVTclegsLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQ 404
Cdd:COG3883 97 RSGGSVSYLDVLLGSESFSDFLDRLSA-----LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1212626320 405 SYSSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDKA 456
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
89-470 |
2.71e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.66 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 89 KQEMTMEYKQELKKLHEELCILKRSYEKLqKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQrliYQQQVS 168
Cdd:PRK01156 323 KYHAIIKKLSVLQKDYNDYIKKKSRYDDL-NNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAF---ISEILK 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 169 SLEAQRKALAEQSEIIQAQLVNRKQKLESVELSSQSEIQHLSSKLERAND-------TICANELEIERLTMRVNDLVgts 241
Cdd:PRK01156 399 IQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMlngqsvcPVCGTTLGEEKSNHIINHYN--- 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 242 mtvlQEQQQKEEKLRESEKLLEALQEEKRELKAALQ-----------SQENLIHEARIQKEKLQEKV-----KATNTQHA 305
Cdd:PRK01156 476 ----EKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEyleseeinksiNEYNKIESARADLEDIKIKInelkdKHDKYEEI 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 306 VEAIRPREESLAEKKYTS--------------QGQGDLDSVLSQLNFTHTSEDLLQAEVTCLEGSLESVSATCKQLSQEL 371
Cdd:PRK01156 552 KNRYKSLKLEDLDSKRTSwlnalavislidieTNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNL 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 372 MEKYEELKRMEAHNNEYKAEIKKLKEQIlQGEQSYSSALEGMKMEISHLTQELHQRDITIASTKGSSSDME---KRLRAE 448
Cdd:PRK01156 632 NNKYNEIQENKILIEKLRGKIDNYKKQI-AEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLEstiEILRTR 710
|
410 420
....*....|....*....|..
gi 1212626320 449 MQKAEDKAVEHKEILDQLESLK 470
Cdd:PRK01156 711 INELSDRINDINETLESMKKIK 732
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
38-399 |
3.10e-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: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 38 HKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTmEYKQELKKLHEELCILKRSYEKL 117
Cdd:TIGR04523 159 NKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNK-SLESQISELKKQNNQLKDNIEKK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 118 QKKQmrefrgntknhREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVN-RKQKLE 196
Cdd:TIGR04523 238 QQEI-----------NEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDlNNQKEQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 197 SVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAAL 276
Cdd:TIGR04523 307 DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 277 QSQENLIH--EARIQKEKLQEKVKATNTQHAVEAIRPREESLAEKKYTSQGQGDLDSVLS--------QLNFTHTSEDLL 346
Cdd:TIGR04523 387 KNLESQINdlESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTnqdsvkelIIKNLDNTRESL 466
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1212626320 347 QAEVTCLEGSLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQI 399
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKI 519
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
81-471 |
3.45e-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: 40.34 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 81 QVEEHEKIKQEMTMEYKQELKKLHEELCILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQR 160
Cdd:pfam02463 180 EETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 161 liyQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGT 240
Cdd:pfam02463 260 ---IEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 241 SmtvLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAIRPREESLAEKK 320
Cdd:pfam02463 337 I---EELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLEL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 321 ytsqgqgdLDSVLSQLNFTHTSEDLLQAEVTCLEGSLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQIL 400
Cdd:pfam02463 414 --------ARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQ 485
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1212626320 401 QGEQSYSSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEILDQLESLKL 471
Cdd:pfam02463 486 LELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSAT 556
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
58-336 |
3.95e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.94 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 58 EQELKSLRSQL-------DVTHKEVGMLHQQVEEHEKIKQ-------------EMTMEYKQELKKLHEELCILKRsyeKL 117
Cdd:PRK04863 389 EEEVDELKSQLadyqqalDVQQTRAIQYQQAVQALERAKQlcglpdltadnaeDWLEEFQAKEQEATEELLSLEQ---KL 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 118 QKKQM--REFRGNTKNHREDRSEIERLTAKiEEFRQKSLDWEKQRlIYQQQVSSLEAQRKALAEQSEIIQA--QLVNRKQ 193
Cdd:PRK04863 466 SVAQAahSQFEQAYQLVRKIAGEVSRSEAW-DVARELLRRLREQR-HLAEQLQQLRMRLSELEQRLRQQQRaeRLLAEFC 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 194 KLESVELSSQSEIQHLSSKLERandticanelEIERLTMRVNDLVGTSMTVLQEQQQKEEKLREseklLEALQEEKRELK 273
Cdd:PRK04863 544 KRLGKNLDDEDELEQLQEELEA----------RLESLSESVSEARERRMALRQQLEQLQARIQR----LAARAPAWLAAQ 609
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1212626320 274 AAL-----QSQENLIHEARI--QKEKLQEKVKAtnTQHAVEAIRPREESL-AEKKYTSQGQGDLDSVLSQL 336
Cdd:PRK04863 610 DALarlreQSGEEFEDSQDVteYMQQLLERERE--LTVERDELAARKQALdEEIERLSQPGGSEDPRLNAL 678
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
193-303 |
4.12e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.56 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 193 QKLESVELSSQ-SEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRE 271
Cdd:PRK09039 41 QFFLSREISGKdSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGE 120
|
90 100 110
....*....|....*....|....*....|..
gi 1212626320 272 LKAALQSQENLIHEARIQKEKLQEKVKATNTQ 303
Cdd:PRK09039 121 LAQELDSEKQVSARALAQVELLNQQIAALRRQ 152
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
133-331 |
4.95e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 133 REDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVeLSSQSEIQHLSSK 212
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER-ARALYRSGGSVSY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 213 LER---ANDTicaNELeIERLTMrVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQ 289
Cdd:COG3883 105 LDVllgSESF---SDF-LDRLSA-LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1212626320 290 KEKLQEKVKATNTQHAVEAIRPREESLAEKKYTSQGQGDLDS 331
Cdd:COG3883 180 QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
41-286 |
5.13e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.67 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 41 SEWEGRTHALETCLKIREQELKSLRSQLdvthkevgmlhqqveEHEKIKQEMTMEYKQELKKLHEELCILKRSYEKLQKK 120
Cdd:TIGR02169 808 SRIEARLREIEQKLNRLTLEKEYLEKEI---------------QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE 872
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 121 QMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLvnRKQKLESVEL 200
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPK--GEDEEIPEEE 950
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 201 SSQSEIQhlssklerandticaneLEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQE 280
Cdd:TIGR02169 951 LSLEDVQ-----------------AELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYE 1013
|
....*.
gi 1212626320 281 NLIHEA 286
Cdd:TIGR02169 1014 KKKREV 1019
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
58-303 |
5.60e-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: 39.39 E-value: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 58 EQELKSLRSQldvthkEVGMLHQQVEE----HEKIKQEMTMEYKQELKKLHEELCILKRSYEKLQK-KQMREfrgntKNH 132
Cdd:pfam01576 318 QQELRSKREQ------EVTELKKALEEetrsHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKaKQALE-----SEN 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 133 REDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVE---LSSQSEIQHL 209
Cdd:pfam01576 387 AELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEgknIKLSKDVSSL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 210 SSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQ 289
Cdd:pfam01576 467 ESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEG 546
|
250
....*....|....
gi 1212626320 290 KEKLQEKVKATNTQ 303
Cdd:pfam01576 547 KKRLQRELEALTQQ 560
|
|
| Gp58 |
pfam07902 |
gp58-like protein; Sequences found in this family are derived from a number of bacteriophage ... |
239-446 |
6.13e-03 |
|
gp58-like protein; Sequences found in this family are derived from a number of bacteriophage and prophage proteins. They are similar to gp58, a minor structural protein of Lactococcus delbrueckii bacteriophage LL-H.
Pssm-ID: 369586 [Multi-domain] Cd Length: 594 Bit Score: 39.17 E-value: 6.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 239 GTSMTVLQEQQQKEEKLRES-EKLLEALQEEKRELKAALQSQ-ENLIHEARIQKEKLQEKVKATNTQhaVEAIRPREESL 316
Cdd:pfam07902 132 GIATRISEDTDKKLALINETiSGIRREYQDADRQLSSSYQAGiEGLKATMASDKIGLQAEIQASAQG--LSQRYDNEIRK 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 317 AEKKYTSQGQGDLDSVLSQL-----NFTHTSEDLLQAEVTCLEGSLESVSATCKQLSQELMEKYEELKRMEahnneykAE 391
Cdd:pfam07902 210 LSAKITTTSSGTTEAYESKLddlraEFTRSNQGMRTELESKISGLQSTQQSTAYQISQEISNREGAVSRVQ-------QD 282
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1212626320 392 IKKLKEQILQGEQSYSS---ALEGMKMEISHLTQELHQRDITIA---STKGSSSDMEKRLR 446
Cdd:pfam07902 283 LDSYQRRLQDAEKNYSSltqTVKGLQSTVSDPNSKLESRITQLAgliEQKVTRGDVESIIR 343
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
133-299 |
6.96e-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: 38.37 E-value: 6.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 133 REDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVelSSQSEIQHLSSK 212
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV--RNNKEYEALQKE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 213 LERANDTICANELEIERLTMRVNDLvgtsmtvlqeQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEK 292
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEEL----------EEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
....*..
gi 1212626320 293 LQEKVKA 299
Cdd:COG1579 168 LAAKIPP 174
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
246-472 |
6.96e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.15 E-value: 6.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 246 QEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQhaVEAIRPREESLAEKKytsqg 325
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE--LARLEQDIARLEERR----- 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 326 qgdldsvlsqlnfthtsEDLLQAEVTcLEGSLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQS 405
Cdd:COG1196 312 -----------------RELEERLEE-LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1212626320 406 YSSALEgmkmEISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEILDQLESLKLE 472
Cdd:COG1196 374 LAEAEE----ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
97-299 |
7.26e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 38.90 E-value: 7.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 97 KQELKKLHEELCILKRSYEKLQKKQmrefrgntknhREDRSEIERLTAKIEEFRQ--------KSLDWEKQRLIYQQQV- 167
Cdd:COG0497 157 LEEYREAYRAWRALKKELEELRADE-----------AERARELDLLRFQLEELEAaalqpgeeEELEEERRRLSNAEKLr 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626320 168 SSLEAQRKALAEQSEIIQAQLVNRKQKLESVE-------------LSSQSEIQHLSSKLERANDTICANELEIERLTMRV 234
Cdd:COG0497 226 EALQEALEALSGGEGGALDLLGQALRALERLAeydpslaelaerlESALIELEEAASELRRYLDSLEFDPERLEEVEERL 305
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1212626320 235 NDLVGTS----------MTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQK-EKLQEKVKA 299
Cdd:COG0497 306 ALLRRLArkygvtveelLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKKAaKKLEKAVTA 381
|
|
| |
