|
Name |
Accession |
Description |
Interval |
E-value |
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
1-252 |
1.32e-91 |
|
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: 285.18 E-value: 1.32e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 1 MKQIDIMVAHKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEELC 80
Cdd:pfam17045 12 MKQIDIMVAHKKSEWEGQTRALETRLDIREEELLSARNTLERKHKEIGLLRQQLEELEKGKQELVAKYEQQLQKLQEELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 81 ILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQA-- 158
Cdd:pfam17045 92 KLKRSYEKLQRKQLKEAREEAKSREEDRSELSRLNGKLEEFRQKSLEWEQQRLQYQQQVASLEAQRKALAEQSSLIQSaa 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 159 ---QLVNRKQKLEsvelSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLE 235
Cdd:pfam17045 172 yqvQLEGRKQCLE----ASQSEIQRLRSKLERAQDSLCAQELELERLRMRVSELGDSNRKLLEEQQRLLEELRMSQRQLQ 247
|
250
....*....|....*..
gi 1370485258 236 ALQEEKRELKAALQSQE 252
Cdd:pfam17045 248 VLQNELMELKATLQSQD 264
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
29-373 |
9.19e-13 |
|
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: 72.01 E-value: 9.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 29 REQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHE---ELCILKRSYEKLQKKQMREFRGNTKNHR 105
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEElsrQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 106 ED---RSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRK---QKLESVELSSQSEIQ 179
Cdd:TIGR02168 755 ELtelEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNeeaANLRERLESLERRIA 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 180 HLSSKLERANDTICANELEIERLTMRVNDLvGTSMTVLQEQQQKEEKLRES-EKLLEALQEEKRELKAALQSQENLIHEA 258
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESLAAEIEEL-EELIEELESELEALLNERASlEEALALLRSELEELSEELRELESKRSEL 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 259 RIQKEKLQEKVKATNTQhaVEAIRPREESLAEkKYTSQGQGDLDSVLSQLNFTHTSEDLLQAEVTCLEGSLESVSAtckq 338
Cdd:TIGR02168 914 RRELEELREKLAQLELR--LEGLEVRIDNLQE-RLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGP---- 986
|
330 340 350
....*....|....*....|....*....|....*
gi 1370485258 339 LSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQ 373
Cdd:TIGR02168 987 VNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
27-339 |
5.21e-12 |
|
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: 69.33 E-value: 5.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 27 KIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEELCILKRSYEKLQKKQMREFRGNTKNHRE 106
Cdd:TIGR02169 219 EKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 107 DRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQ---AQLVNRKQKLESVELSSQSEIQHLSS 183
Cdd:TIGR02169 299 LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERkrrDKLTEEYAELKEELEDLRAELEEVDK 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 184 KLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKE 263
Cdd:TIGR02169 379 EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370485258 264 KLQEKVKATNTQHaveaIRPREESLAEKKYTSQGQGDLDSVLSQLNFTHTSEDLLQAEVTCLEGSLESVSATCKQL 339
Cdd:TIGR02169 459 QLAADLSKYEQEL----YDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQL 530
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
108-446 |
1.26e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.08 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 108 RSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVElssqSEIQHLSSKLER 187
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE----AEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 188 ANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQE 267
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 268 KVKATNTQhaveaIRPREESLAEkkytsqgqgdldsvlsqlnfthtsedlLQAEVTCLEGSLESVSATCKQLSQELMEKY 347
Cdd:TIGR02168 832 RIAATERR-----LEDLEEQIEE---------------------------LSEDIESLAAEIEELEELIEELESELEALL 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 348 EELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSALEgmkmEISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDK 427
Cdd:TIGR02168 880 NERASLEEALALLRSELEELSEELRELESKRSELRR----ELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEE 955
|
330
....*....|....*....
gi 1370485258 428 AVEHKEILDqLESLKLENR 446
Cdd:TIGR02168 956 AEALENKIE-DDEEEARRR 973
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
9-332 |
1.77e-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: 61.23 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 9 AHKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEELCILKRSYEK 88
Cdd:TIGR02168 224 ELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 89 LQKKQMREfrgntknhREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLE 168
Cdd:TIGR02168 304 KQILRERL--------ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 169 SVE---LSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKE-----EKLRESEKLLEALQEE 240
Cdd:TIGR02168 376 ELEeqlETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElkelqAELEELEEELEELQEE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 241 KRELKAALQSQENLIHEARIQKEKLQEKVK-ATNTQHAVEAIRPREESLAE-----KKYTSQGQGDLDSVLSQLNFThts 314
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAqLQARLDSLERLQENLEGFSEgvkalLKNQSGLSGILGVLSELISVD--- 532
|
330
....*....|....*...
gi 1370485258 315 EDLLQAEVTCLEGSLESV 332
Cdd:TIGR02168 533 EGYEAAIEAALGGRLQAV 550
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
58-376 |
2.40e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.85 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 58 EKIKQEMTMEYKQELKKLHEELCILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQ 137
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 138 QVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVELS-SQSEIQHLSSKLERANDTICANELEIERLTMRVNDLvgtsmtv 216
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEEDLHKLEEALNDLEARlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRL------- 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 217 LQEQQQKEEKLRESEKLLEALQEEKRELKAAlqsqenlIHEARIQKEKLQEKVKatNTQHAVEAIRPREESLaekkytsq 296
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKE-------IENLNGKKEELEEELE--ELEAALRDLESRLGDL-------- 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 297 gQGDLDSVLSQLNFTHTSEDLLQAEVTCLEGSLESVSATCKQLSQELMEkYEELKRMEAHNNEYKAEIKKLKEQILQGEQ 376
Cdd:TIGR02169 888 -KKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSE-IEDPKGEDEEIPEEELSLEDVQAELQRVEE 965
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
7-352 |
1.16e-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: 58.54 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 7 MVAHKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVE----EHEKIKQEMTmEYKQELKKLHEELCIL 82
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEqleqEEEKLKERLE-ELEEDLSSLEQEIENV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 83 KRSYEKLqkkqmrefrgntknhredRSEIERLTAKIEEFRQKSLDWEkqRLIYQQQVSSLEAQRKALAEQSEIIQAQLVN 162
Cdd:TIGR02169 757 KSELKEL------------------EARIEELEEDLHKLEEALNDLE--ARLSHSRIPEIQAELSKLEEEVSRIEARLRE 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 163 RKQKLESVELSSQ---SEIQHLSSKLERANDTICANELEIERLTMRVNDLvgtsmtvLQEQQQKEEKLRESEKLLEALQE 239
Cdd:TIGR02169 817 IEQKLNRLTLEKEyleKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL-------EEELEELEAALRDLESRLGDLKK 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 240 EKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAV--EAIRPREESLAEKKYTSQGQGDLDSV------------- 304
Cdd:TIGR02169 890 ERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEAleEELSEIEDPKGEDEEIPEEELSLEDVqaelqrveeeira 969
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1370485258 305 LSQLNFTHTSE-DLLQAEVTCLEGSLESVSATCKQLsQELMEKYEELKR 352
Cdd:TIGR02169 970 LEPVNMLAIQEyEEVLKRLDELKEKRAKLEEERKAI-LERIEEYEKKKR 1017
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
67-334 |
1.90e-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: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 67 EYKQELKKLHEELCILKRSYEKLQKKQmrefRGNTKNHREDRSEIERLTAKIEEFRQKSL-------DWEKQRLIYQQQV 139
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAEL----AELEAELEELRLELEELELELEEAQAEEYellaelaRLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 140 SSLEAQRKALAEQSEIIQAQLVNRKQKLESVELSSQS------EIQHLSSKLERANDTICANELEIERLTMRVNDLVGTS 213
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEaeeeleEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 214 MTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAIRPREESLAEKKY 293
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1370485258 294 TSQGQGDLDSVLSQLNFTHTSEDLLQAEVTCLEGSLESVSA 334
Cdd:COG1196 472 AALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKA 512
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
50-489 |
4.80e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.59 E-value: 4.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 50 LHQQVEEHE-KIKQEMTMEYKQELKKLHEELcilkRSYEKlQKKQMREFRGNTK----NHREDRSEIERLTAKIEEFRQK 124
Cdd:PRK02224 192 LKAQIEEKEeKDLHERLNGLESELAELDEEI----ERYEE-QREQARETRDEADevleEHEERREELETLEAEIEDLRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 125 SLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQ----------LVNRKQKLESVELSSQSEIQHLSSKLERANDTICA 194
Cdd:PRK02224 267 IAETEREREELAEEVRDLRERLEELEEERDDLLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAES 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 195 NELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAA-------LQSQENLIHEARIQKEKLQE 267
Cdd:PRK02224 347 LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERfgdapvdLGNAEDFLEELREERDELRE 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 268 KVKATNT--QHAVEAIRPREESLAEKKYTSQGQGdldsvlsqlnfthtsedllqaevtcLEGSlESVSAtckqlsqeLME 345
Cdd:PRK02224 427 REAELEAtlRTARERVEEAEALLEAGKCPECGQP-------------------------VEGS-PHVET--------IEE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 346 KYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSA--LEGMKMEISHLTQELHQRDITIASTKGSSSDMEKR---LRAE 420
Cdd:PRK02224 473 DRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEdrIERLEERREDLEELIAERRETIEEKRERAEELRERaaeLEAE 552
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 421 MQKAEDKAVE-HKEILDQLESLKLENRHLSEMVMKLElglHEAKEISLADLQENYIEALNKLVSENQQLQ 489
Cdd:PRK02224 553 AEEKREAAAEaEEEAEEAREEVAELNSKLAELKERIE---SLERIRTLLAAIADAEDEIERLREKREALA 619
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
200-500 |
7.46e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 7.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 200 ERLTmRVNDL---VGTSMTVLQEQQQKEEKLREseklleaLQEEKRELKAALQSQEnlIHEARIQKEKLQEKVKATNTQH 276
Cdd:COG1196 186 ENLE-RLEDIlgeLERQLEPLERQAEKAERYRE-------LKEELKELEAELLLLK--LRELEAELEELEAELEELEAEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 277 AVEAirpREESLAEKKYTSQGQgDLDSVLSQLNFTHTSEDLLQAEVTCLEGSLESVSATCKQLSQELMEKYEELKRMEAH 356
Cdd:COG1196 256 EELE---AELAELEAELEELRL-ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 357 NNEYKAEIKKLKEQILQGEQsyssALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEILD 436
Cdd:COG1196 332 LEELEEELEELEEELEEAEE----ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370485258 437 QLESLKLENRHLSEMVMKLELGL--HEAKEISLADLQENYIEALNKLVSENQQLQKDLMNTKSQLE 500
Cdd:COG1196 408 AEEALLERLERLEEELEELEEALaeLEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
131-454 |
2.76e-07 |
|
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: 54.07 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 131 QRLIYQQQVSSLEAQRKALAEQSEIIQAQLvNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDL- 209
Cdd:pfam12128 588 KRIDVPEWAASEEELRERLDKAEEALQSAR-EKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEk 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 210 VGTSMTVLQEQQQKEEKLRESEKLLEALqeeKRELKAALQSQENLIHEARIQK-EKLQEKVKATNTQHA--VEAIRPREE 286
Cdd:pfam12128 667 DKKNKALAERKDSANERLNSLEAQLKQL---DKKHQAWLEEQKEQKREARTEKqAYWQVVEGALDAQLAllKAAIAARRS 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 287 SLaeKKYTSQGQGDLDSVLSQLNFTHTSEDLLQAEVTCLEGSLESvsatCKQLSQELMEKYEELK-RMEAHNNEYKAEIK 365
Cdd:pfam12128 744 GA--KAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIER----IAVRRQEVLRYFDWYQeTWLQRRPRLATQLS 817
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 366 KLKEQILQGEQSYSSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLR-----AEMQKAEDKAVEHKEILDQLES 440
Cdd:pfam12128 818 NIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSklatlKEDANSEQAQGSIGERLAQLED 897
|
330
....*....|....
gi 1370485258 441 LKLENRHLSEMVMK 454
Cdd:pfam12128 898 LKLKRDYLSESVKK 911
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
11-484 |
7.37e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 7.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 11 KKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMT------MEYKQELKKLHEELCILKR 84
Cdd:PRK03918 187 RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEelekelESLEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 85 SYEKLQK--KQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEiiqaqlvn 162
Cdd:PRK03918 267 RIEELKKeiEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE-------- 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 163 RKQKLESVELSSQSEIQHLSSKlERANDTICANELEIERLTMRVNDLvgtsmtvlqEQQQKEEKLRESEKLLEALQEEKR 242
Cdd:PRK03918 339 RLEELKKKLKELEKRLEELEER-HELYEEAKAKKEELERLKKRLTGL---------TPEKLEKELEELEKAKEEIEEEIS 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 243 ELKAALQSQENLIHEARIQKEKLQEK------VKATNTQHAVEAIRPR-----EESLAEKKYTSQGQGDLDSVLSQLNFT 311
Cdd:PRK03918 409 KITARIGELKKEIKELKKAIEELKKAkgkcpvCGRELTEEHRKELLEEytaelKRIEKELKEIEEKERKLRKELRELEKV 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 312 HTSEDLLQAEVTCLEGSLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQiLQGEQSYSSALEGMKMEISH 391
Cdd:PRK03918 489 LKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKE-LEKLEELKKKLAELEKKLDE 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 392 LTQELHQRdITIASTKGSSS--DMEKRLRaEMQKAEDKAVE----HKEILDQLESLKLENRHLSEMVMKLELGLHEAKEI 465
Cdd:PRK03918 568 LEEELAEL-LKELEELGFESveELEERLK-ELEPFYNEYLElkdaEKELEREEKELKKLEEELDKAFEELAETEKRLEEL 645
|
490
....*....|....*....
gi 1370485258 466 sladlqENYIEALNKLVSE 484
Cdd:PRK03918 646 ------RKELEELEKKYSE 658
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
50-515 |
1.45e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 50 LHQQVEEHEKIKQEMTMEYKQELKKLHEELcilkrsyeKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWE 129
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEEL--------KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 130 KqrliyQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLEsvelssqsEIQHLSSKLERANDTICANELEIERLTMRVNdl 209
Cdd:COG4717 123 K-----LLQLLPLYQELEALEAELAELPERLEELEERLE--------ELRELEEELEELEAELAELQEELEELLEQLS-- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 210 vgtsmtvlqeqQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQhaveairpreESLA 289
Cdd:COG4717 188 -----------LATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE----------ERLK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 290 EKKYTSQGQGDLDSVLSQLNFTHTSEDLLQAEVTCLEGSLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKE 369
Cdd:COG4717 247 EARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 370 QI-LQGEQSYSSALEGMKM---------EISHLTQEL------HQRDITIASTKGSSSDMEKRLRAEMQKAEDKAVEHKE 433
Cdd:COG4717 327 ALgLPPDLSPEELLELLDRieelqellrEAEELEEELqleeleQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 434 ILDQLESLKLENRHLSEMV----MKLELGLHEAKEISLADLQENYIEALNKLVSENQQLQKDlmNTKSQLEISTQMCKKQ 509
Cdd:COG4717 407 LEEQLEELLGELEELLEALdeeeLEEELEELEEELEELEEELEELREELAELEAELEQLEED--GELAELLQELEELKAE 484
|
....*.
gi 1370485258 510 NDRIFK 515
Cdd:COG4717 485 LRELAE 490
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
67-295 |
1.52e-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: 50.92 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 67 EYKQELKKLHEELCILKRSYEKLQKKQmrefrgntknhREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQR 146
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEE-----------KALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 147 KALAEQSEIIQAQLVNRKQKLESVE-------LSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVgtsmtvlQE 219
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGrqpplalLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA-------AL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 220 QQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVK-----ATNTQHAVEAIRPREESLAEKKYT 294
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAelqqeAEELEALIARLEAEAAAAAERTPA 245
|
.
gi 1370485258 295 S 295
Cdd:COG4942 246 A 246
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
82-512 |
1.77e-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: 51.27 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 82 LKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQ--RLIYQQQVSSLEAQRKALAEQSEIIQAQ 159
Cdd:pfam15921 160 LKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSmsTMHFRSLGSAISKILRELDTEISYLKGR 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 160 LVNRKQKLESVELSSQSEIQHL-SSKLERANDTICANELEIERLTMRVN------DLVGTSMTVLQEQ--QQKEEKLRES 230
Cdd:pfam15921 240 IFPVEDQLEALKSESQNKIELLlQQHQDRIEQLISEHEVEITGLTEKASsarsqaNSIQSQLEIIQEQarNQNSMYMRQL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 231 EKLLEALQEEKRELKAALQSQENLIheariqkEKLQEKVKATNTQHAveairpreESLAEKKYTSQGQGDLDSVLSQL-N 309
Cdd:pfam15921 320 SDLESTVSQLRSELREAKRMYEDKI-------EELEKQLVLANSELT--------EARTERDQFSQESGNLDDQLQKLlA 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 310 FTHTSEDLLQAEVTC---LEGSLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQ---------- 376
Cdd:pfam15921 385 DLHKREKELSLEKEQnkrLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQgkneslekvs 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 377 SYSSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEI-------LDQLESLKLENRHLS 449
Cdd:pfam15921 465 SLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLrsrvdlkLQELQHLKNEGDHLR 544
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370485258 450 EMVMKLE-LGLHEAKEISLADLQENYIEALNKLVSENQQLQKDLMNTKSQLEistqmcKKQNDR 512
Cdd:pfam15921 545 NVQTECEaLKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLE------KEINDR 602
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
108-268 |
2.89e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 108 RSEIERLTAKIEEFRQKS--LDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESV-----ELSSQSEIQH 180
Cdd:COG3206 188 RKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGpdalpELLQSPVIQQ 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 181 LSSKLERAndticanELEIERLTMRVNDLvGTSMTVLQEQQQ--KEEKLRESEKLLEALQEEKRELKAALQSQENLIHEA 258
Cdd:COG3206 268 LRAQLAEL-------EAELAELSARYTPN-HPDVIALRAQIAalRAQLQQEAQRILASLEAELEALQAREASLQAQLAQL 339
|
170
....*....|
gi 1370485258 259 RIQKEKLQEK 268
Cdd:COG3206 340 EARLAELPEL 349
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
115-364 |
3.03e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 115 TAKIEEFRQksldwEKQRLiyQQQVSSLEAQRKALAEQseiiQAQLVNRKQKLESVELSSQSEIQHLSskLERAndtica 194
Cdd:COG4913 609 RAKLAALEA-----ELAEL--EEELAEAEERLEALEAE----LDALQERREALQRLAEYSWDEIDVAS--AERE------ 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 195 neleierltmrvndlvgtsmtvLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNT 274
Cdd:COG4913 670 ----------------------IAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEE 727
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 275 QhaVEAIRPREESlAEKKYTSQGQGDLDSVLSQLNFTHTSEDLLQAevtcLEGSLESVSATCKQLSQELMEKyeelkrME 354
Cdd:COG4913 728 E--LDELQDRLEA-AEDLARLELRALLEERFAAALGDAVERELREN----LEERIDALRARLNRAEEELERA------MR 794
|
250
....*....|
gi 1370485258 355 AHNNEYKAEI 364
Cdd:COG4913 795 AFNREWPAET 804
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
105-280 |
5.98e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 5.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 105 REDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVelssQSEIQHLSSK 184
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL----EKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 185 LERANDTI---------------------CANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRE 243
Cdd:COG4942 99 LEAQKEELaellralyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190
....*....|....*....|....*....|....*..
gi 1370485258 244 LKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEA 280
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAEL 215
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
218-505 |
6.45e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 6.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 218 QEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQhaVEAIRPREESLAEKKytsqg 297
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE--LARLEQDIARLEERR----- 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 298 qgdldsvlsqlnfthtsEDLLQAEVTcLEGSLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQS 377
Cdd:COG1196 312 -----------------RELEERLEE-LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 378 YSSALEgmkmEISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEILDQLESL--KLENRHLSEMVMKL 455
Cdd:COG1196 374 LAEAEE----ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELeeEEEEEEEALEEAAE 449
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1370485258 456 ELGLHEAKEISLADLQENYIEALNKLVSENQQLQKDLMNTKSQLEISTQM 505
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
242-500 |
7.38e-06 |
|
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: 49.28 E-value: 7.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 242 RELKAALQSQENLIHEARIQKEKLQEKvkATNTQHAVEAIRPREESLAEKkyTSQGQGDLDSVLSQLNFTHTSEDLLQAE 321
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEK--IAELEKALAELRKELEELEEE--LEQLRKELEELSRQISALRKDLARLEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 322 VTCLEGSLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQgeqsYSSALEGMKMEISHLTQELHQRDI 401
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ----LKEELKALREALDELRAELTLLNE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 402 TIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEILDQLESLKLENRHLSEMVMKLELGLHEAKEI---------SLADLQE 472
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNErasleealaLLRSELE 897
|
250 260
....*....|....*....|....*...
gi 1370485258 473 NYIEALNKLVSENQQLQKDLMNTKSQLE 500
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKLA 925
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
129-457 |
1.06e-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: 48.90 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 129 EKQRLIYQQQVSSLEAQRKALAEQseiiqaqlvnrKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVND 208
Cdd:TIGR02168 224 ELELALLVLRLEELREELEELQEE-----------LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 209 LVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHaveairprEESL 288
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL--------EELE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 289 AEKKYTSQGQGDLDSVLSQLNfthtsedllqAEVTCLEGSLESVSAtckqlsqelmekyeELKRMEAHNNEYKAEIKKLK 368
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLR----------SKVAQLELQIASLNN--------------EIERLEARLERLEDRRERLQ 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 369 EQILQGEQSYSSA-LEGMKMEISHLTQELHQ---RDITIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEILDQLESLKLE 444
Cdd:TIGR02168 421 QEIEELLKKLEEAeLKELQAELEELEEELEElqeELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN 500
|
330
....*....|...
gi 1370485258 445 NRHLSEMVMKLEL 457
Cdd:TIGR02168 501 LEGFSEGVKALLK 513
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
183-513 |
1.30e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.53 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 183 SKLERANDTICANELEIERLTmrvndlvgtsmTVLQEQQQKEEKLR-ESEKLLE--ALQEEKRELKAALQSQENLIHEAR 259
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLD-----------LIIDEKRQQLERLRrEREKAERyqALLKEKREYEGYELLKEKEALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 260 IQKEKLQEKVKATNTQHAVEAIRPREESLAEKkytsqgQGDLDSVLSQLNFTHTSEDL-LQAEVTCLEGSLESVSATCKQ 338
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEI------EQLLEELNKKIKDLGEEEQLrVKEKIGELEAEIASLERSIAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 339 LSQELMEKYEELKRMEAHNNEYKAEIKKLKEQI--LQGEQ-SYSSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEK 415
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLAEIEELEREIeeERKRRdKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 416 RLraemqkaEDKAVEHKEILDQLESLKLENRHLSEMV--MKLELGLHEAKEISLADLQENYIEALNKLVSENQQLQKDLM 493
Cdd:TIGR02169 393 KL-------EKLKREINELKRELDRLQEELQRLSEELadLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465
|
330 340
....*....|....*....|
gi 1370485258 494 NTKSQLEISTQMCKKQNDRI 513
Cdd:TIGR02169 466 KYEQELYDLKEEYDRVEKEL 485
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
29-273 |
3.86e-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: 46.30 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 29 REQELKSLRSQLDVTHKEVGMLHQQVEEHEKikqemtmeykqELKKLHEELCILKRSYEKLQKKQmrefrgntknhREDR 108
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLK-----------QLAALERRIAALARRIRALEQEL-----------AALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 109 SEIERLTAKIEEFRQKSLDWEKQ--RLIYQQQVSSLEAQRKALAEQSEIiqAQLVNRKQKLESVELSSQSEIQHLSSKLE 186
Cdd:COG4942 83 AELAELEKEIAELRAELEAQKEElaELLRALYRLGRQPPLALLLSPEDF--LDAVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 187 RANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQ 266
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
....*..
gi 1370485258 267 EKVKATN 273
Cdd:COG4942 241 ERTPAAG 247
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
12-409 |
3.94e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.04 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 12 KSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEhekikqemtmeYKQELKKLHEELCILKRSYEKLQK 91
Cdd:pfam15921 337 KRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQK-----------LLADLHKREKELSLEKEQNKRLWD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 92 KQMrefrGNT------KNHREDRS-EIERLTAKIEEFRQKSLDWEKQRLIYQQ-------QVSSLEAQRKALAEQSEIIQ 157
Cdd:pfam15921 406 RDT----GNSitidhlRRELDDRNmEVQRLEALLKAMKSECQGQMERQMAAIQgknesleKVSSLTAQLESTKEMLRKVV 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 158 AQLVNRKQKLESvelsSQSEIQHLSSKLERANDTICANELEIERLTMRVNdlvgtsmTVLQEQQQkeekLRESEKLLEAL 237
Cdd:pfam15921 482 EELTAKKMTLES----SERTVSDLTASLQEKERAIEATNAEITKLRSRVD-------LKLQELQH----LKNEGDHLRNV 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 238 QEEKRELKAALQSQENLIHEARIQKEKLQEKVKatntQHAveaiRPREESLAEKKYTSQGQGDLDSVLSQLNFTHTSEDL 317
Cdd:pfam15921 547 QTECEALKLQMAEKDKVIEILRQQIENMTQLVG----QHG----RTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDA 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 318 ----LQAEVTCLEgsLESVS---------ATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSALEG 384
Cdd:pfam15921 619 kireLEARVSDLE--LEKVKlvnagserlRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNK 696
|
410 420
....*....|....*....|....*
gi 1370485258 385 MKMEISHLTQELHQRDITIASTKGS 409
Cdd:pfam15921 697 LKMQLKSAQSELEQTRNTLKSMEGS 721
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
26-370 |
4.90e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 4.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 26 LKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEELcilkrsyEKLQKKQMREFRGNTKNHR 105
Cdd:PRK03918 343 LKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEEL-------EKAKEEIEEEISKITARIG 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 106 EDRSEIERLTAKIEEFRQKSL----------DWEKQRLI--YQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLE----- 168
Cdd:PRK03918 416 ELKKEIKELKKAIEELKKAKGkcpvcgreltEEHRKELLeeYTAELKRIEKELKEIEEKERKLRKELRELEKVLKkesel 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 169 SVELSSQSEIQHLSSKLERAN-DTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAA 247
Cdd:PRK03918 496 IKLKELAEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAEL 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 248 LQSQENLIHEARIQ-KEKLQEKVKATNtqHAVEAIRPREESLAEKKYTSQGQGDLDSVLSQLNFTHTSEDLLQAEVTCLE 326
Cdd:PRK03918 576 LKELEELGFESVEElEERLKELEPFYN--EYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELE 653
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1370485258 327 GSL-----ESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQ 370
Cdd:PRK03918 654 KKYseeeyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE 702
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
103-275 |
5.44e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 5.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 103 NHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQ--VSSLEAQRKALAEQSEIIQAQLVNRKQKLESVelssQSEIQH 180
Cdd:COG3206 169 RREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEA----EARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 181 LSSKLERANDTICA--NELEIERLTMRVNDLVgtsmtvlQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQ-ENLIHE 257
Cdd:COG3206 245 LRAQLGSGPDALPEllQSPVIQQLRAQLAELE-------AELAELSARYTPNHPDVIALRAQIAALRAQLQQEaQRILAS 317
|
170
....*....|....*...
gi 1370485258 258 ARIQKEKLQEKVKATNTQ 275
Cdd:COG3206 318 LEAELEALQAREASLQAQ 335
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
70-261 |
7.23e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 7.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 70 QELKKLHEELCILKRSYEKLQkkQMREFRGNTKNHREDRSEIERLTAKIE-EFRQKSLDWEKQRLI-YQQQVSSLEAQRK 147
Cdd:COG4913 235 DDLERAHEALEDAREQIELLE--PIRELAERYAAARERLAELEYLRAALRlWFAQRRLELLEAELEeLRAELARLEAELE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 148 ALAEQSEIIQAQLVNRKQKLESVELSS----QSEIQHLSSKLERANDTICANELEIERLTMRVND-----------LVGT 212
Cdd:COG4913 313 RLEARLDALREELDELEAQIRGNGGDRleqlEREIERLERELEERERRRARLEALLAALGLPLPAsaeefaalraeAAAL 392
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1370485258 213 SMTVLQEQQQKEEKLRESEKLLEALQEEKRELK---AALQSQENLIHEARIQ 261
Cdd:COG4913 393 LEALEEELEALEEALAEAEAALRDLRRELRELEaeiASLERRKSNIPARLLA 444
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
108-277 |
1.23e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 108 RSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQlvnrkQKLESVELSSqSEIQHLSSKLER 187
Cdd:COG4913 623 EEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELE-----AELERLDASS-DDLAALEEQLEE 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 188 AndticanELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKR-ELKAALQSQ-ENLIHEARIQK--E 263
Cdd:COG4913 697 L-------EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlELRALLEERfAAALGDAVERElrE 769
|
170
....*....|....
gi 1370485258 264 KLQEKVKATNTQHA 277
Cdd:COG4913 770 NLEERIDALRARLN 783
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
45-500 |
1.43e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.34 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 45 KEVGMLHQQVEEHEKIKQEMTMEYKQElKKLHEELCILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQk 124
Cdd:TIGR00618 163 KEKKELLMNLFPLDQYTQLALMEFAKK-KSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQ- 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 125 SLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVELSSQSE--------IQHLSSKLERANDTICANE 196
Cdd:TIGR00618 241 SHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAplaahikaVTQIEQQAQRIHTELQSKM 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 197 LEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEK--RELKAALQSQENLIHEARIQKEKLQEKVKA--- 271
Cdd:TIGR00618 321 RSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATsiREISCQQHTLTQHIHTLQQQKTTLTQKLQSlck 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 272 -----TNTQHAVEAIRPREESLAEKKYTSQGQGDLDSVLSQLNFTHTSEDL--LQAEVTCLEGSLESVSATCKQLS--QE 342
Cdd:TIGR00618 401 eldilQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAqcEKLEKIHLQESAQSLKEREQQLQtkEQ 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 343 LMEKYEELKRMEAHN-NEYKAEIKKLKEQILQGEQSYSSALE----------GMKMEISHLTQELHQRDITIASTKGSSS 411
Cdd:TIGR00618 481 IHLQETRKKAVVLARlLELQEEPCPLCGSCIHPNPARQDIDNpgpltrrmqrGEQTYAQLETSEEDVYHQLTSERKQRAS 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 412 DMEK--RLRAEMQKAEDKAVEHKEILDQLESLKLENRHLSEMVMKLELGLHEAKEISLADLQENyiEALNKLVSENQQLQ 489
Cdd:TIGR00618 561 LKEQmqEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPE--QDLQDVRLHLQQCS 638
|
490
....*....|.
gi 1370485258 490 KDLMNTKSQLE 500
Cdd:TIGR00618 639 QELALKLTALH 649
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
135-294 |
1.93e-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: 43.95 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 135 YQQQVSSLEAQRKALAEQSEIIQAQlVNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDlvgtsM 214
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAE-LDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLAR-----R 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 215 TVLQEQQ-QKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAIRPREESLAEKKY 293
Cdd:pfam00529 130 RVLAPIGgISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLER 209
|
.
gi 1370485258 294 T 294
Cdd:pfam00529 210 T 210
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
53-443 |
2.14e-04 |
|
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: 44.58 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 53 QVEEHEKIKQEMTMEYKQELKKLHEELCILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQR 132
Cdd:pfam02463 180 EETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 133 liyQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGT 212
Cdd:pfam02463 260 ---IEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 213 SmtvLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAIRPREESLAEKK 292
Cdd:pfam02463 337 I---EELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLEL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 293 ytsqgqgdLDSVLSQLNFTHTSEDLLQAEVTCLEGSLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQIL 372
Cdd:pfam02463 414 --------ARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQ 485
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370485258 373 QGEQSYSSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEILDQLESLKL 443
Cdd:pfam02463 486 LELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSAT 556
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
198-464 |
3.57e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.17 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 198 EIERLTMRVNDLVGTSMTVLQEQqqkeeklrESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATN---- 273
Cdd:COG3096 810 KLQRLHQAFSQFVGGHLAVAFAP--------DPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNkllp 881
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 274 -------TQHA--VEAIRPREESLAEKKYTSQGQGD----LDSVLSQLNFTHTSEDLLQAEVTCLEGSLESVSATCKQLS 340
Cdd:COG3096 882 qanlladETLAdrLEELREELDAAQEAQAFIQQHGKalaqLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALS 961
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 341 qELMEK-----YEELKRMEAHNNEYKaeiKKLKEQILQGEQSYSSALEGMKMEISHLTQeLHQRditIASTKGS------ 409
Cdd:COG3096 962 -EVVQRrphfsYEDAVGLLGENSDLN---EKLRARLEQAEEARREAREQLRQAQAQYSQ-YNQV---LASLKSSrdakqq 1033
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370485258 410 ----------------SSDMEKRLRAEMQKAEDKAVEHKEILDQLE----SLKLENRHLSEMVMKLELGLHEAKE 464
Cdd:COG3096 1034 tlqeleqeleelgvqaDAEAEERARIRRDELHEELSQNRSRRSQLEkqltRCEAEMDSLQKRLRKAERDYKQERE 1108
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
30-308 |
3.91e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 30 EQELKSLRSQL-------DVTHKEVGMLHQQVEEHEKIKQ-------------EMTMEYKQELKKLHEELCILKRsyeKL 89
Cdd:PRK04863 389 EEEVDELKSQLadyqqalDVQQTRAIQYQQAVQALERAKQlcglpdltadnaeDWLEEFQAKEQEATEELLSLEQ---KL 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 90 QKKQM--REFRGNTKNHREDRSEIERLTAKiEEFRQKSLDWEKQRlIYQQQVSSLEAQRKALAEQSEIIQA--QLVNRKQ 165
Cdd:PRK04863 466 SVAQAahSQFEQAYQLVRKIAGEVSRSEAW-DVARELLRRLREQR-HLAEQLQQLRMRLSELEQRLRQQQRaeRLLAEFC 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 166 KLESVELSSQSEIQHLSSKLERandticanelEIERLTMRVNDLVGTSMTVLQEQQQKEEKLREseklLEALQEEKRELK 245
Cdd:PRK04863 544 KRLGKNLDDEDELEQLQEELEA----------RLESLSESVSEARERRMALRQQLEQLQARIQR----LAARAPAWLAAQ 609
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370485258 246 AAL-----QSQENLIHEARI--QKEKLQEKVKAtnTQHAVEAIRPREESL-AEKKYTSQGQGDLDSVLSQL 308
Cdd:PRK04863 610 DALarlreQSGEEFEDSQDVteYMQQLLERERE--LTVERDELAARKQALdEEIERLSQPGGSEDPRLNAL 678
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
219-428 |
5.09e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 219 EQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQ--HAVEAIRPREESLAEKKYTSQ 296
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 297 GQGDLDSVLSQLnFTHTS-EDLLQAEVTclegsLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGE 375
Cdd:COG3883 97 RSGGSVSYLDVL-LGSESfSDFLDRLSA-----LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1370485258 376 QSYSSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDKA 428
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
117-292 |
5.90e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 5.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 117 KIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVelssQSEIQHLSSKLERANDTI---- 192
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL----QAEIAEAEAEIEERREELgera 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 193 --------CANELE-----------IERLTMrVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQEN 253
Cdd:COG3883 93 ralyrsggSVSYLDvllgsesfsdfLDRLSA-LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 1370485258 254 LIHEARIQKEKLQEKVKAtNTQHAVEAIRPREESLAEKK 292
Cdd:COG3883 172 ELEAQQAEQEALLAQLSA-EEAAAEAQLAELEAELAAAE 209
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
30-275 |
6.29e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.24 E-value: 6.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 30 EQELKSLRSQldvthkEVGMLHQQVEE----HEKIKQEMTMEYKQELKKLHEELCILKRSYEKLQK-KQMREfrgntKNH 104
Cdd:pfam01576 318 QQELRSKREQ------EVTELKKALEEetrsHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKaKQALE-----SEN 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 105 REDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVE---LSSQSEIQHL 181
Cdd:pfam01576 387 AELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEgknIKLSKDVSSL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 182 SSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQ 261
Cdd:pfam01576 467 ESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEG 546
|
250
....*....|....
gi 1370485258 262 KEKLQEKVKATNTQ 275
Cdd:pfam01576 547 KKRLQRELEALTQQ 560
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
33-512 |
6.67e-04 |
|
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: 42.90 E-value: 6.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 33 LKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEELcilkrsyeklqKKQMREFRGNTKNHRED----R 108
Cdd:pfam12128 253 LESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQW-----------KEKRDELNGELSAADAAvakdR 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 109 SEIERLTAKIEEFRQKSLDWEKQRL----IYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKlesVELSSQSEIQHLSSK 184
Cdd:pfam12128 322 SELEALEDQHGAFLDADIETAAADQeqlpSWQSELENLEERLKALTGKHQDVTAKYNRRRSK---IKEQNNRDIAGIKDK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 185 LERANDTI----CANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARI 260
Cdd:pfam12128 399 LAKIREARdrqlAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERARE 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 261 QKEKLQEKVKATNTQHAVEAIRPREESLA---EKKYTSQGQGDLDSVLSQLN-FTHTSEDLLQAEVTCLEGSLESVSATC 336
Cdd:pfam12128 479 EQEAANAEVERLQSELRQARKRRDQASEAlrqASRRLEERQSALDELELQLFpQAGTLLHFLRKEAPDWEQSIGKVISPE 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 337 KQLSQELMEKYEE---------------LKRMEAhnNEYKAEIKKLKEQILQGEQSYSSALEGMKMEISHLTQ-----EL 396
Cdd:pfam12128 559 LLHRTDLDPEVWDgsvggelnlygvkldLKRIDV--PEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQangelEK 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 397 HQRDITIASTKGSSSDME-KRLRAEMQKAEDKAveHKEILDQLESLKLENRHLSEMVMKLELGLHEAKEISLADLQENYI 475
Cdd:pfam12128 637 ASREETFARTALKNARLDlRRLFDEKQSEKDKK--NKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREART 714
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1370485258 476 EALNKL--VSENQQLQKDLMNT-----KSQLEISTQMCKKQNDR 512
Cdd:pfam12128 715 EKQAYWqvVEGALDAQLALLKAaiaarRSGAKAELKALETWYKR 758
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
21-192 |
7.10e-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: 7.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 21 ALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQE--MTMEYKQELKKLHEELCILKRSYEKLQKKQMREFR 98
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDElqDRLEAAEDLARLELRALLEERFAAALGDAVERELR 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 99 GNTKNHRED-RSEIERLTAKIEE-FRQKSLDWekqRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKL-ESVELSSQ 175
Cdd:COG4913 769 ENLEERIDAlRARLNRAEEELERaMRAFNREW---PAETADLDADLESLPEYLALLDRLEEDGLPEYEERFkELLNENSI 845
|
170
....*....|....*..
gi 1370485258 176 SEIQHLSSKLERANDTI 192
Cdd:COG4913 846 EFVADLLSKLRRAIREI 862
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
105-271 |
7.66e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 7.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 105 REDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVelSSQSEIQHLSSK 184
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV--RNNKEYEALQKE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 185 LERANDTICANELEIERLTMRVNDLvgtsmtvlqeQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEK 264
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEEL----------EEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
....*..
gi 1370485258 265 LQEKVKA 271
Cdd:COG1579 168 LAAKIPP 174
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
10-497 |
8.34e-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: 8.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 10 HKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTmEYKQELKKLHEELCILKRSYEKL 89
Cdd:TIGR04523 159 NKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNK-SLESQISELKKQNNQLKDNIEKK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 90 QKKQmrefrgntknhREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVN-RKQKLE 168
Cdd:TIGR04523 238 QQEI-----------NEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDlNNQKEQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 169 SVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAAL 248
Cdd:TIGR04523 307 DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 249 QSQENLIH--EARIQKEKLQEKVKATNTQHAVEAIRPREESLAEKKYTSQGQGDLDSVLS--------QLNFTHTSEDLL 318
Cdd:TIGR04523 387 KNLESQINdlESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTnqdsvkelIIKNLDNTRESL 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 319 QAEVTCLEGSLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQI---LQGEQSYSSALEGMKMEISHLTQE 395
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKIsslKEKIEKLESEKKEKESKISDLEDE 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 396 LHQRDITIASTKGSSSDMEK-----RLRAEMQKAEDKAVEHKEILDQLESLKLENRHLSEMVMKL------ELGLHEAKE 464
Cdd:TIGR04523 547 LNKDDFELKKENLEKEIDEKnkeieELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKisslekELEKAKKEN 626
|
490 500 510
....*....|....*....|....*....|...
gi 1370485258 465 ISLADLQENYIEALNKLVSENQQLQKDLMNTKS 497
Cdd:TIGR04523 627 EKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRN 659
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
13-258 |
9.23e-04 |
|
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: 42.75 E-value: 9.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 13 SEWEGRTHALETCLKIREQELKSLRSQLdvthkevgmlhqqveEHEKIKQEMTMEYKQELKKLHEELCILKRSYEKLQKK 92
Cdd:TIGR02169 808 SRIEARLREIEQKLNRLTLEKEYLEKEI---------------QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE 872
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 93 QMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLvnRKQKLESVEL 172
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPK--GEDEEIPEEE 950
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 173 SSQSEIQhlssklerandticaneLEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQE 252
Cdd:TIGR02169 951 LSLEDVQ-----------------AELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYE 1013
|
....*.
gi 1370485258 253 NLIHEA 258
Cdd:TIGR02169 1014 KKKREV 1019
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
205-309 |
1.41e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 205 RVNDLVGTSMTVLQEQQQKEE----KLRESEKLLEALQEEKRELKAAlqsQENLIHEariQKEKLQEKVKAtnTQHAVEA 280
Cdd:PRK00409 517 KLNELIASLEELERELEQKAEeaeaLLKEAEKLKEELEEKKEKLQEE---EDKLLEE---AEKEAQQAIKE--AKKEADE 588
|
90 100
....*....|....*....|....*....
gi 1370485258 281 IRPREESLAEKKYTSQGQGDLDSVLSQLN 309
Cdd:PRK00409 589 IIKELRQLQKGGYASVKAHELIEARKRLN 617
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
9-500 |
1.42e-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: 42.08 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 9 AHKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTME---YKQELKKLHEELCILKRS 85
Cdd:pfam01576 67 AARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEkvtTEAKIKKLEEDILLLEDQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 86 YEKLQKkqmrefrgnTKNHREDRseIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKalaeQSEIIQAQLVNRKQ 165
Cdd:pfam01576 147 NSKLSK---------ERKLLEER--ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLK----KEEKGRQELEKAKR 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 166 KLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLREsekLLEALQEEKRELK 245
Cdd:pfam01576 212 KLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISE---LQEDLESERAARN 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 246 AALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAIRPREESLAEKKYTSQGQGDlDSVLSQLNFTHTSE-DLLQAEVTC 324
Cdd:pfam01576 289 KAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSH-EAQLQEMRQKHTQAlEELTEQLEQ 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 325 LEGSLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQiLQGEQSYSSALEGMKMEISHLTQELHQRDITIA 404
Cdd:pfam01576 368 AKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQ-LQELQARLSESERQRAELAEKLSKLQSELESVS 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 405 STKGSSSDMEKRLRAEMQKAEDKAVEHKEILDQLESLKLEnrhLSEMVMKLelglhEAKEISLADLQENYIEALNKLVSE 484
Cdd:pfam01576 447 SLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLN---LSTRLRQL-----EDERNSLQEQLEEEEEAKRNVERQ 518
|
490
....*....|....*.
gi 1370485258 485 NQQLQKDLMNTKSQLE 500
Cdd:pfam01576 519 LSTLQAQLSDMKKKLE 534
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
67-484 |
1.74e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 67 EYKQELKKLHEELCILKRSYEKLQkkQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQR 146
Cdd:COG4717 92 ELQEELEELEEELEELEAELEELR--EELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 147 KALAEQSEIIQaqlvnrkQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDlvgtsmtvLQEQQQKEEK 226
Cdd:COG4717 170 AELAELQEELE-------ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE--------LEEELEQLEN 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 227 LRESEKLLEALQEEKRELKAA------------LQSQENLIHEARI---------------QKEKLQEKVKATNTQHAVE 279
Cdd:COG4717 235 ELEAAALEERLKEARLLLLIAaallallglggsLLSLILTIAGVLFlvlgllallflllarEKASLGKEAEELQALPALE 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 280 AIRPRE-ESLAEKKYTSQGQ-----GDLDSVLSQLNFTHTSEDLLQAEVTcLEGSLESVSATCKQLSQELMEKYEELKRM 353
Cdd:COG4717 315 ELEEEElEELLAALGLPPDLspeelLELLDRIEELQELLREAEELEEELQ-LEELEQEIAALLAEAGVEDEEELRAALEQ 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 354 EAHNNEYKAEIKKLKEQILQGEQSYSSALEGMKMEisHLTQELHQRDITIASTKGSSSDMEKR---LRAEMQKAEDKAvE 430
Cdd:COG4717 394 AEEYQELKEELEELEEQLEELLGELEELLEALDEE--ELEEELEELEEELEELEEELEELREElaeLEAELEQLEEDG-E 470
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1370485258 431 HKEILDQLESLKLENRHLSEMVMKLELGLHEAKEIsLADLQENYIEALNKLVSE 484
Cdd:COG4717 471 LAELLQELEELKAELRELAEEWAALKLALELLEEA-REEYREERLPPVLERASE 523
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
61-472 |
1.78e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.81 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 61 KQEMTMEYKQELKKLHEELCILKRSYEKLqKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQrliYQQQVS 140
Cdd:PRK01156 323 KYHAIIKKLSVLQKDYNDYIKKKSRYDDL-NNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAF---ISEILK 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 141 SLEAQRKALAEQSEIIQAQLVNRKQKLESVELSSQSEIQHLSSKLERAND-------TICANELEIERLTMRVNDLVgts 213
Cdd:PRK01156 399 IQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMlngqsvcPVCGTTLGEEKSNHIINHYN--- 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 214 mtvlQEQQQKEEKLRESEKLLEALQEEKRELKAAlqsqenlihEARIQKEKLQEKVKATN----TQHAVEAIRPREESLA 289
Cdd:PRK01156 476 ----EKKSRLEEKIREIEIEVKDIDEKIVDLKKR---------KEYLESEEINKSINEYNkiesARADLEDIKIKINELK 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 290 EK---------KYTSQGQGDLDSVLSQLNFTHTSEDLLQAEVtcLEGSLESVSATCKQLSQELMEKYEELKRMEAHNNEY 360
Cdd:PRK01156 543 DKhdkyeeiknRYKSLKLEDLDSKRTSWLNALAVISLIDIET--NRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKS 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 361 KAEIK---KLKEQILQGEQSYSSALEGMKMEISHLTQELHQRDITIASTKGSSS---DMEKRLRAEMQKAEDKAVEHKEI 434
Cdd:PRK01156 621 IREIEneaNNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSrinDIEDNLKKSRKALDDAKANRARL 700
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1370485258 435 LDQLESLKLENRHLSEMVMKLELGLHEAKEI--SLADLQE 472
Cdd:PRK01156 701 ESTIEILRTRINELSDRINDINETLESMKKIkkAIGDLKR 740
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
30-181 |
1.96e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 39.89 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 30 EQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMtMEYKQELKKLHEELCILKRSYEKLQKKqmrefrgNTKNHREDRS 109
Cdd:pfam13851 53 QQENKRLTEPLQKAQEEVEELRKQLENYEKDKQSL-KNLKARLKVLEKELKDLKWEHEVLEQR-------FEKVERERDE 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370485258 110 EIERLTAKIEEFRQKSldwEKQRLIYQQQVSSL-------EAQRKALAEQSEIIQAQLVNRKQKLESVELSSQSEIQHL 181
Cdd:pfam13851 125 LYDKFEAAIQDVQQKT---GLKNLLLEKKLQALgetlekkEAQLNEVLAAANLDPDALQAVTEKLEDVLESKNQLIKDL 200
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
69-271 |
2.03e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.21 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 69 KQELKKLHEELCILKRSYEKLQKKQmrefrgntknhREDRSEIERLTAKIEEFRQ--------KSLDWEKQRLIYQQQV- 139
Cdd:COG0497 157 LEEYREAYRAWRALKKELEELRADE-----------AERARELDLLRFQLEELEAaalqpgeeEELEEERRRLSNAEKLr 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 140 SSLEAQRKALAEQSEIIQAQLVNRKQKLESVE-------------LSSQSEIQHLSSKLERANDTICANELEIERLTMRV 206
Cdd:COG0497 226 EALQEALEALSGGEGGALDLLGQALRALERLAeydpslaelaerlESALIELEEAASELRRYLDSLEFDPERLEEVEERL 305
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370485258 207 NDLVGTS----------MTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQK-EKLQEKVKA 271
Cdd:COG0497 306 ALLRRLArkygvtveelLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKKAaKKLEKAVTA 381
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
165-275 |
2.28e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 165 QKLESVELSSQ-SEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRE 243
Cdd:PRK09039 41 QFFLSREISGKdSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGE 120
|
90 100 110
....*....|....*....|....*....|..
gi 1370485258 244 LKAALQSQENLIHEARIQKEKLQEKVKATNTQ 275
Cdd:PRK09039 121 LAQELDSEKQVSARALAQVELLNQQIAALRRQ 152
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
225-428 |
2.32e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 225 EKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAV-----------------------EAI 281
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAleqelaaleaelaelekeiaelrAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 282 RPREESLAEKKYTSQGQGDLDSVLSQLNfthtSEDLLQAEVTclEGSLESVSATCKQLSQELMEKYEELKRMEAHNNEYK 361
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLLS----PEDFLDAVRR--LQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370485258 362 AEIKKLKEQILQGEQSYSSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDKA 428
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
67-313 |
2.73e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 40.65 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 67 EYKQELKKLHEELCILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQR 146
Cdd:pfam07888 38 ECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 147 KALAEQSEiiqaqlvnrkqklesvelSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEK 226
Cdd:pfam07888 118 DALLAQRA------------------AHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 227 LRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHA-VEAIRPREESLAEKKYTSQGQ-----GD 300
Cdd:pfam07888 180 LQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAeNEALLEELRSLQERLNASERKveglgEE 259
|
250
....*....|...
gi 1370485258 301 LDSVLSQLNFTHT 313
Cdd:pfam07888 260 LSSMAAQRDRTQA 272
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
163-484 |
2.95e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 163 RKQKLESVELSSQSEIQHLSSKLERANDTICAnELEIERLTMRVNDLVgtsmtvlQEQQQKEEKLRESEKLLEALQEEKR 242
Cdd:PRK02224 476 RVEELEAELEDLEEEVEEVEERLERAEDLVEA-EDRIERLEERREDLE-------ELIAERRETIEEKRERAEELRERAA 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 243 ELKAALQSQENLIHEARIQKEKLQEKVKATNTQhaveairpreeslaekkytsqgQGDLDSVLSQLNFTHTSEDLLqaev 322
Cdd:PRK02224 548 ELEAEAEEKREAAAEAEEEAEEAREEVAELNSK----------------------LAELKERIESLERIRTLLAAI---- 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 323 tclegslesvsATCKQLSQELMEKYEELKRMeahNNEYKAEIKKLKEQILQGEQSY-SSALEGMKMEISHLTQELHQRDI 401
Cdd:PRK02224 602 -----------ADAEDEIERLREKREALAEL---NDERRERLAEKRERKRELEAEFdEARIEEAREDKERAEEYLEQVEE 667
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 402 TIASTKGSSSDMEKRLraemqkaedKAVEHKeiLDQLESLKLENRHLSEMVMKLELGLHEAKEIS------LADLQENYI 475
Cdd:PRK02224 668 KLDELREERDDLQAEI---------GAVENE--LEELEELRERREALENRVEALEALYDEAEELEsmygdlRAELRQRNV 736
|
....*....
gi 1370485258 476 EALNKLVSE 484
Cdd:PRK02224 737 ETLERMLNE 745
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
27-490 |
4.07e-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: 40.42 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 27 KIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEmtmeYKQELKKLHEELCILKRSYEKLQKKQMREfrgntknhre 106
Cdd:TIGR00606 573 KQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNH----INNELESKEEQLSSYEDKLFDVCGSQDEE---------- 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 107 drSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSeiiqaqlvnrkQKLESVELSSQSEIQHLSSKLE 186
Cdd:TIGR00606 639 --SDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVC-----------QRVFQTEAELQEFISDLQSKLR 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 187 RANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIhEARIQKEKLQ 266
Cdd:TIGR00606 706 LAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLL-GTIMPEEESA 784
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 267 E--KVKATNTQHAVEAIRPREESLAEKKYTSQGQgDLDSVLSQLNfthtsedllqAEVTCLEGSLESVSATCKQLSQELM 344
Cdd:TIGR00606 785 KvcLTDVTIMERFQMELKDVERKIAQQAAKLQGS-DLDRTVQQVN----------QEKQEKQHELDTVVSKIELNRKLIQ 853
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 345 EKYEELKRMEAHNNEYKAEIKKLKEQiLQGEQSYSSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKA 424
Cdd:TIGR00606 854 DQQEQIQHLKSKTNELKSEKLQIGTN-LQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSK 932
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370485258 425 EDkavEHKEILDQLESLKLENRHLSEMVMKLELGLHEAKEISLADlQENYIEALNKLVSENQQLQK 490
Cdd:TIGR00606 933 ET---SNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQ-KETELNTVNAQLEECEKHQE 994
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
8-430 |
4.23e-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: 40.59 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 8 VAHKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEELCILKRSYE 87
Cdd:pfam12128 292 LRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQ 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 88 KLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLdwEKQRLIYQQQVSSL----EAQRKALAEQSEIIQAQLVNR 163
Cdd:pfam12128 372 DVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQL--AVAEDDLQALESELreqlEAGKLEFNEEEYRLKSRLGEL 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 164 KQKLESVELS---------SQSEIQHLSSKLERANDTICANELEIERLTMR---VNDLVGTSMTVLQEQQQKEEKLRE-- 229
Cdd:pfam12128 450 KLRLNQATATpelllqlenFDERIERAREEQEAANAEVERLQSELRQARKRrdqASEALRQASRRLEERQSALDELELql 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 230 ---SEKLLEALQEEK---RELKAALQSQEnLIHEARIQKEKLQEKVKATNTQHAV----------------EAIRpREES 287
Cdd:pfam12128 530 fpqAGTLLHFLRKEApdwEQSIGKVISPE-LLHRTDLDPEVWDGSVGGELNLYGVkldlkridvpewaaseEELR-ERLD 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 288 LAEKKYTSQG--QGDLDSVLSQLNfthTSEDLLQAEVTCLEGSLESVSATCKQLS----QELMEKYEELKRMEAHNNEYK 361
Cdd:pfam12128 608 KAEEALQSARekQAAAEEQLVQAN---GELEKASREETFARTALKNARLDLRRLFdekqSEKDKKNKALAERKDSANERL 684
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370485258 362 AEIKKLKEQILQGEQSYSSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDKAVE 430
Cdd:pfam12128 685 NSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALE 753
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
26-427 |
5.25e-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: 40.03 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 26 LKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQE---------LKKLHEELCILKRSYEKLQKKQ--- 93
Cdd:TIGR00606 739 IDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAkvcltdvtiMERFQMELKDVERKIAQQAAKLqgs 818
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 94 --MREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEiiqaqlvnRKQKLESVE 171
Cdd:TIGR00606 819 dlDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQ--------RRQQFEEQL 890
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 172 LSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVgtsmtvlqeqQQKEEKLRESEKLLEALQEEKRELKAALQSQ 251
Cdd:TIGR00606 891 VELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELI----------SSKETSNKKAQDKVNDIKEKVKNIHGYMKDI 960
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 252 ENLIHEARiQKEKLQEKVKATNTQHAVEAIRPREESLAEkkytsqgqgDLDSVLSQLNFTHTSEDLLQAEVTclegsLES 331
Cdd:TIGR00606 961 ENKIQDGK-DDYLKQKETELNTVNAQLEECEKHQEKINE---------DMRLMRQDIDTQKIQERWLQDNLT-----LRK 1025
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 332 VSATCKQLSQELMEKYEELKRMEAhnNEYKAEIKKLKEQILQGEQSYSSALEGMK---MEISHLTQELHQRDITIASTKG 408
Cdd:TIGR00606 1026 RENELKEVEEELKQHLKEMGQMQV--LQMKQEHQKLEENIDLIKRNHVLALGRQKgyeKEIKHFKKELREPQFRDAEEKY 1103
|
410
....*....|....*....
gi 1370485258 409 SSSDMEKRLRAEMQKAEDK 427
Cdd:TIGR00606 1104 REMMIVMRTTELVNKDLDI 1122
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
112-441 |
7.90e-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: 39.64 E-value: 7.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 112 ERLTAKIEEFRQKSLDWEKQRLIYQQ-QVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVELSS-QSEIQHLSSKLERAN 189
Cdd:TIGR00606 189 ETLRQVRQTQGQKVQEHQMELKYLKQyKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNrLKEIEHNLSKIMKLD 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 190 DTICA---NELEIERLTMRVNDLVGTSMTVLQEQ------------QQKEEKLRESEKLLEALQEEKRELKAALQSQENL 254
Cdd:TIGR00606 269 NEIKAlksRKKQMEKDNSELELKMEKVFQGTDEQlndlyhnhqrtvREKERELVDCQRELEKLNKERRLLNQEKTELLVE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 255 IHEARIQKEKLQEKVKATNTQHAVEAIRPREESLAEKKYTS-----------QGQGDLDSVLSQL-NFTHTSEDLLQAEV 322
Cdd:TIGR00606 349 QGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSErqiknfhtlviERQEDEAKTAAQLcADLQSKERLKQEQA 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 323 TCLEGSLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKlkeqILQGEQSYSSALEGM-KMEISHLTQELHQRDI 401
Cdd:TIGR00606 429 DEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDR----ILELDQELRKAERELsKAEKNSLTETLKKEVK 504
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1370485258 402 tiaSTKGSSSDMEKRLRAEMQKAEDKAvEHKEILDQLESL 441
Cdd:TIGR00606 505 ---SLQNEKADLDRKLRKLDQEMEQLN-HHTTTRTQMEML 540
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
53-464 |
8.06e-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: 39.32 E-value: 8.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 53 QVEEHEKIKQEMTMEYKQELKKLHEELCILKRSYEKLQKKQmrefrgntKNHREDRSEIERLTAKIEEFRQKSLD-WEKQ 131
Cdd:pfam05483 272 QLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQ--------KALEEDLQIATKTICQLTEEKEAQMEeLNKA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 132 RLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVELssqsEIQHLSSKLERANDTICANELEIERLTmrvndlvg 211
Cdd:pfam05483 344 KAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITM----ELQKKSSELEEMTKFKNNKEVELEELK-------- 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 212 tsmTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKeklqeKVKATNTQHAVEAIRPREESLAEK 291
Cdd:pfam05483 412 ---KILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQL-----TAIKTSEEHYLKEVEDLKTELEKE 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 292 KYTSQGQGDLDSVLSQLNFTHTSEdllQAEVTCLEGSLESVSATCKQLSQELMEKYEELKRMEAhnnEYKAEIKKLKEQI 371
Cdd:pfam05483 484 KLKNIELTAHCDKLLLENKELTQE---ASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEM---NLRDELESVREEF 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485258 372 LQGEQSYSSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEILDQLESLKLENRHLSEM 451
Cdd:pfam05483 558 IQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIK 637
|
410
....*....|...
gi 1370485258 452 VMKLELGLHEAKE 464
Cdd:pfam05483 638 VNKLELELASAKQ 650
|
|
| |
