|
Name |
Accession |
Description |
Interval |
E-value |
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
18-280 |
2.42e-99 |
|
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: 305.98 E-value: 2.42e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 18 LTSCEAELQELMKQIDIMVAHKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYK 97
Cdd:pfam17045 1 LSSCEAELQELMKQIDIMVAHKKSEWEGQTRALETRLDIREEELLSARNTLERKHKEIGLLRQQLEELEKGKQELVAKYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 98 QELKKLHEELCILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKAL 177
Cdd:pfam17045 81 QQLQKLQEELSKLKRSYEKLQRKQLKEAREEAKSREEDRSELSRLNGKLEEFRQKSLEWEQQRLQYQQQVASLEAQRKAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 178 AEQSEIIQA-----QLVNRKQKLEsvelSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKE 252
Cdd:pfam17045 161 AEQSSLIQSaayqvQLEGRKQCLE----ASQSEIQRLRSKLERAQDSLCAQELELERLRMRVSELGDSNRKLLEEQQRLL 236
|
250 260
....*....|....*....|....*...
gi 530375321 253 EKLRESEKLLEALQEEKRELKAALQSQE 280
Cdd:pfam17045 237 EELRMSQRQLQVLQNELMELKATLQSQD 264
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
57-401 |
6.72e-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: 72.40 E-value: 6.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 57 REQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHE---ELCILKRSYEKLQKKQMREFRGNTKNHR 133
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEElsrQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 134 ED---RSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRK---QKLESVELSSQSEIQ 207
Cdd:TIGR02168 755 ELtelEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNeeaANLRERLESLERRIA 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 208 HLSSKLERANDTICANELEIERLTMRVNDLvGTSMTVLQEQQQKEEKLRES-EKLLEALQEEKRELKAALQSQENLIHEA 286
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESLAAEIEEL-EELIEELESELEALLNERASlEEALALLRSELEELSEELRELESKRSEL 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 287 RIQKEKLQEKVKATNTQhaVEAIRPREESLAEkKYTSQGQGDLDSVLSQLNFTHTSEDLLQAEVTCLEGSLESVSAtckq 366
Cdd:TIGR02168 914 RRELEELREKLAQLELR--LEGLEVRIDNLQE-RLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGP---- 986
|
330 340 350
....*....|....*....|....*....|....*
gi 530375321 367 LSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQ 401
Cdd:TIGR02168 987 VNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
23-367 |
1.84e-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: 70.87 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 23 AELQELMKQIDIMVAHKKSEWEG----RTHAL---ETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTME 95
Cdd:TIGR02169 180 EEVEENIERLDLIIDEKRQQLERlrreREKAEryqALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 96 YKQELKKLHEELCILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRK 175
Cdd:TIGR02169 260 ISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIE 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 176 ALAEQSEIIQ---AQLVNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKE 252
Cdd:TIGR02169 340 ELEREIEEERkrrDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLS 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 253 EKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHaveaIRPREESLAEKKYTSQGQGDLDSV 332
Cdd:TIGR02169 420 EELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQEL----YDLKEEYDRVEKELSKLQRELAEA 495
|
330 340 350
....*....|....*....|....*....|....*
gi 530375321 333 LSQLNFTHTSEDLLQAEVTCLEGSLESVSATCKQL 367
Cdd:TIGR02169 496 EAQARASEERVRGGRAVEEVLKASIQGVHGTVAQL 530
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
136-474 |
9.25e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.46 E-value: 9.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 136 RSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVElssqSEIQHLSSKLER 215
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE----AEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 216 ANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQE 295
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 296 KVKATNTQhaveaIRPREESLAEkkytsqgqgdldsvlsqlnfthtsedlLQAEVTCLEGSLESVSATCKQLSQELMEKY 375
Cdd:TIGR02168 832 RIAATERR-----LEDLEEQIEE---------------------------LSEDIESLAAEIEELEELIEELESELEALL 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 376 EELKRMEAHNNEYKAEIKKLKEQIlqgeQSYSSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDK 455
Cdd:TIGR02168 880 NERASLEEALALLRSELEELSEEL----RELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEE 955
|
330
....*....|....*....
gi 530375321 456 AVEHKEILDqLESLKLENR 474
Cdd:TIGR02168 956 AEALENKIE-DDEEEARRR 973
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
37-360 |
1.50e-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: 61.61 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 37 AHKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEELCILKRSYEK 116
Cdd:TIGR02168 224 ELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 117 LQKKQMREfrgntknhREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLE 196
Cdd:TIGR02168 304 KQILRERL--------ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 197 SVE---LSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKE-----EKLRESEKLLEALQEE 268
Cdd:TIGR02168 376 ELEeqlETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElkelqAELEELEEELEELQEE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 269 KRELKAALQSQENLIHEARIQKEKLQEKVK-ATNTQHAVEAIRPREESLAE-----KKYTSQGQGDLDSVLSQLNFThts 342
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAqLQARLDSLERLQENLEGFSEgvkalLKNQSGLSGILGVLSELISVD--- 532
|
330
....*....|....*...
gi 530375321 343 EDLLQAEVTCLEGSLESV 360
Cdd:TIGR02168 533 EGYEAAIEAALGGRLQAV 550
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
86-404 |
1.75e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.24 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 86 EKIKQEMTMEYKQELKKLHEELCILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQ 165
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 166 QVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVELS-SQSEIQHLSSKLERANDTICANELEIERLTMRVNDLvgtsmtv 244
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEEDLHKLEEALNDLEARlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRL------- 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 245 LQEQQQKEEKLRESEKLLEALQEEKRELKAAlqsqenlIHEARIQKEKLQEKVKatNTQHAVEAIRPREESLaekkytsq 324
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKE-------IENLNGKKEELEEELE--ELEAALRDLESRLGDL-------- 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 325 gQGDLDSVLSQLNFTHTSEDLLQAEVTCLEGSLESVSATCKQLSQELMEkYEELKRMEAHNNEYKAEIKKLKEQILQGEQ 404
Cdd:TIGR02169 888 -KKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSE-IEDPKGEDEEIPEEELSLEDVQAELQRVEE 965
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
35-380 |
8.29e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.93 E-value: 8.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 35 MVAHKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVE----EHEKIKQEMTmEYKQELKKLHEELCIL 110
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEqleqEEEKLKERLE-ELEEDLSSLEQEIENV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 111 KRSYEKLqkkqmrefrgntknhredRSEIERLTAKIEEFRQKSLDWEkqRLIYQQQVSSLEAQRKALAEQSEIIQAQLVN 190
Cdd:TIGR02169 757 KSELKEL------------------EARIEELEEDLHKLEEALNDLE--ARLSHSRIPEIQAELSKLEEEVSRIEARLRE 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 191 RKQKLESVELSSQ---SEIQHLSSKLERANDTICANELEIERLTMRVNDLvgtsmtvLQEQQQKEEKLRESEKLLEALQE 267
Cdd:TIGR02169 817 IEQKLNRLTLEKEyleKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL-------EEELEELEAALRDLESRLGDLKK 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 268 EKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAV--EAIRPREESLAEKKYTSQGQGDLDSV------------- 332
Cdd:TIGR02169 890 ERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEAleEELSEIEDPKGEDEEIPEEELSLEDVqaelqrveeeira 969
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 530375321 333 LSQLNFTHTSE-DLLQAEVTCLEGSLESVSATCKQLsQELMEKYEELKR 380
Cdd:TIGR02169 970 LEPVNMLAIQEyEEVLKRLDELKEKRAKLEEERKAI-LERIEEYEKKKR 1017
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
95-362 |
1.95e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 95 EYKQELKKLHEELCILKRSYEKLQKKQmrefRGNTKNHREDRSEIERLTAKIEEFRQKSL-------DWEKQRLIYQQQV 167
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAEL----AELEAELEELRLELEELELELEEAQAEEYellaelaRLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 168 SSLEAQRKALAEQSEIIQAQLVNRKQKLESVELSSQS------EIQHLSSKLERANDTICANELEIERLTMRVNDLVGTS 241
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEaeeeleEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 242 MTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAIRPREESLAEKKY 321
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 530375321 322 TSQGQGDLDSVLSQLNFTHTSEDLLQAEVTCLEGSLESVSA 362
Cdd:COG1196 472 AALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKA 512
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
78-517 |
4.45e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.59 E-value: 4.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 78 LHQQVEEHE-KIKQEMTMEYKQELKKLHEELcilkRSYEKlQKKQMREFRGNTK----NHREDRSEIERLTAKIEEFRQK 152
Cdd:PRK02224 192 LKAQIEEKEeKDLHERLNGLESELAELDEEI----ERYEE-QREQARETRDEADevleEHEERREELETLEAEIEDLRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 153 SLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQ----------LVNRKQKLESVELSSQSEIQHLSSKLERANDTICA 222
Cdd:PRK02224 267 IAETEREREELAEEVRDLRERLEELEEERDDLLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAES 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 223 NELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAA-------LQSQENLIHEARIQKEKLQE 295
Cdd:PRK02224 347 LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERfgdapvdLGNAEDFLEELREERDELRE 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 296 KVKATNT--QHAVEAIRPREESLAEKKYTSQGQGdldsvlsqlnfthtsedllqaevtcLEGSlESVSAtckqlsqeLME 373
Cdd:PRK02224 427 REAELEAtlRTARERVEEAEALLEAGKCPECGQP-------------------------VEGS-PHVET--------IEE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 374 KYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSA--LEGMKMEISHLTQELHQRDITIASTKGSSSDMEKR---LRAE 448
Cdd:PRK02224 473 DRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEdrIERLEERREDLEELIAERRETIEEKRERAEELRERaaeLEAE 552
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 449 MQKAEDKAVE-HKEILDQLESLKLENRHLSEMVMKLElglHEAKEISLADLQENYIEALNKLVSENQQLQ 517
Cdd:PRK02224 553 AEEKREAAAEaEEEAEEAREEVAELNSKLAELKERIE---SLERIRTLLAAIADAEDEIERLREKREALA 619
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
228-528 |
7.59e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 7.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 228 ERLTmRVNDL---VGTSMTVLQEQQQKEEKLREseklleaLQEEKRELKAALQSQEnlIHEARIQKEKLQEKVKATNTQH 304
Cdd:COG1196 186 ENLE-RLEDIlgeLERQLEPLERQAEKAERYRE-------LKEELKELEAELLLLK--LRELEAELEELEAELEELEAEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 305 AVEAirpREESLAEKKYTSQGQgDLDSVLSQLNFTHTSEDLLQAEVTCLEGSLESVSATCKQLSQELMEKYEELKRMEAH 384
Cdd:COG1196 256 EELE---AELAELEAELEELRL-ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 385 NNEYKAEIKKLKEQILQGEQsyssALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEILD 464
Cdd:COG1196 332 LEELEEELEELEEELEEAEE----ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530375321 465 QLESLKLENRHLSEMVMKLELGL--HEAKEISLADLQENYIEALNKLVSENQQLQKDLMNTKSQLE 528
Cdd:COG1196 408 AEEALLERLERLEEELEELEEALaeLEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
159-482 |
2.08e-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: 54.46 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 159 QRLIYQQQVSSLEAQRKALAEQSEIIQAQLvNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDL- 237
Cdd:pfam12128 588 KRIDVPEWAASEEELRERLDKAEEALQSAR-EKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEk 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 238 VGTSMTVLQEQQQKEEKLRESEKLLEALqeeKRELKAALQSQENLIHEARIQK-EKLQEKVKATNTQHA--VEAIRPREE 314
Cdd:pfam12128 667 DKKNKALAERKDSANERLNSLEAQLKQL---DKKHQAWLEEQKEQKREARTEKqAYWQVVEGALDAQLAllKAAIAARRS 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 315 SLaeKKYTSQGQGDLDSVLSQLNFTHTSEDLLQAEVTCLEGSLESvsatCKQLSQELMEKYEELK-RMEAHNNEYKAEIK 393
Cdd:pfam12128 744 GA--KAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIER----IAVRRQEVLRYFDWYQeTWLQRRPRLATQLS 817
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 394 KLKEQILQGEQSYSSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLR-----AEMQKAEDKAVEHKEILDQLES 468
Cdd:pfam12128 818 NIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSklatlKEDANSEQAQGSIGERLAQLED 897
|
330
....*....|....
gi 530375321 469 LKLENRHLSEMVMK 482
Cdd:pfam12128 898 LKLKRDYLSESVKK 911
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
39-512 |
3.27e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 39 KKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMT------MEYKQELKKLHEELCILKR 112
Cdd:PRK03918 187 RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEelekelESLEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 113 SYEKLQK--KQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEiiqaqlvn 190
Cdd:PRK03918 267 RIEELKKeiEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE-------- 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 191 RKQKLESVELSSQSEIQHLSSKlERANDTICANELEIERLTMRVNDLvgtsmtvlqEQQQKEEKLRESEKLLEALQEEKR 270
Cdd:PRK03918 339 RLEELKKKLKELEKRLEELEER-HELYEEAKAKKEELERLKKRLTGL---------TPEKLEKELEELEKAKEEIEEEIS 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 271 ELKAALQSQENLIHEARIQKEKLQEK------VKATNTQHAVEAIRPR-----EESLAEKKYTSQGQGDLDSVLSQLNFT 339
Cdd:PRK03918 409 KITARIGELKKEIKELKKAIEELKKAkgkcpvCGRELTEEHRKELLEEytaelKRIEKELKEIEEKERKLRKELRELEKV 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 340 HTSEDLLQAEVTCLEGSLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQiLQGEQSYSSALEGMKMEISH 419
Cdd:PRK03918 489 LKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKE-LEKLEELKKKLAELEKKLDE 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 420 LTQELHQRdITIASTKGSSS--DMEKRLRaEMQKAEDKAVE----HKEILDQLESLKLENRHLSEMVMKLELGLHEAKEI 493
Cdd:PRK03918 568 LEEELAEL-LKELEELGFESveELEERLK-ELEPFYNEYLElkdaEKELEREEKELKKLEEELDKAFEELAETEKRLEEL 645
|
490
....*....|....*....
gi 530375321 494 sladlqENYIEALNKLVSE 512
Cdd:PRK03918 646 ------RKELEELEKKYSE 658
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
110-540 |
6.23e-07 |
|
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: 53.20 E-value: 6.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 110 LKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQ--RLIYQQQVSSLEAQRKALAEQSEIIQAQ 187
Cdd:pfam15921 160 LKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSmsTMHFRSLGSAISKILRELDTEISYLKGR 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 188 LVNRKQKLESVELSSQSEIQHL-SSKLERANDTICANELEIERLTMRVN------DLVGTSMTVLQEQ--QQKEEKLRES 258
Cdd:pfam15921 240 IFPVEDQLEALKSESQNKIELLlQQHQDRIEQLISEHEVEITGLTEKASsarsqaNSIQSQLEIIQEQarNQNSMYMRQL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 259 EKLLEALQEEKRELKAALQSQENLIheariqkEKLQEKVKATNTQHAveairpreESLAEKKYTSQGQGDLDSVLSQL-N 337
Cdd:pfam15921 320 SDLESTVSQLRSELREAKRMYEDKI-------EELEKQLVLANSELT--------EARTERDQFSQESGNLDDQLQKLlA 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 338 FTHTSEDLLQAEVTC---LEGSLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQ---------- 404
Cdd:pfam15921 385 DLHKREKELSLEKEQnkrLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQgkneslekvs 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 405 SYSSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEI-------LDQLESLKLENRHLS 477
Cdd:pfam15921 465 SLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLrsrvdlkLQELQHLKNEGDHLR 544
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530375321 478 EMVMKLE-LGLHEAKEISLADLQENYIEALNKLVSENQQLQKDLMNTKSQLEistqmcKKQNDR 540
Cdd:pfam15921 545 NVQTECEaLKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLE------KEINDR 602
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1-437 |
8.04e-07 |
|
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: 52.81 E-value: 8.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 1 MEALLEGIQNRGHGGGFLTSCE-AELQELMKQIDIMVAHKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLH 79
Cdd:pfam15921 297 IQSQLEIIQEQARNQNSMYMRQlSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLD 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 80 QQVEEhekikqemtmeYKQELKKLHEELCILKRSYEKLQKKQMrefrGNT------KNHREDRS-EIERLTAKIEEFRQK 152
Cdd:pfam15921 377 DQLQK-----------LLADLHKREKELSLEKEQNKRLWDRDT----GNSitidhlRRELDDRNmEVQRLEALLKAMKSE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 153 SLDWEKQRLIYQQ-------QVSSLEAQRKALAEQSEIIQAQLVNRKQKLESvelsSQSEIQHLSSKLERANDTICANEL 225
Cdd:pfam15921 442 CQGQMERQMAAIQgknesleKVSSLTAQLESTKEMLRKVVEELTAKKMTLES----SERTVSDLTASLQEKERAIEATNA 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 226 EIERLTMRVNdlvgtsmTVLQEQQQkeekLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKatntQHA 305
Cdd:pfam15921 518 EITKLRSRVD-------LKLQELQH----LKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVG----QHG 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 306 veaiRPREESLAEKKYTSQGQGDLDSVLSQLNFTHTSEDL----LQAEVTCLEgsLESVS---------ATCKQLSQELM 372
Cdd:pfam15921 583 ----RTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAkireLEARVSDLE--LEKVKlvnagserlRAVKDIKQERD 656
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530375321 373 EKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSALEGMKMEISHLTQELHQRDITIASTKGS 437
Cdd:pfam15921 657 QLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGS 721
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
110-528 |
9.26e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 9.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 110 LKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKsldwEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLV 189
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAEL----QEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 190 NRKQKLESVELssQSEIQHLSSKLERAndticanELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLR----ESEKLLEAL 265
Cdd:COG4717 127 LLPLYQELEAL--EAELAELPERLEEL-------EERLEELRELEEELEELEAELAELQEELEELLEqlslATEEELQDL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 266 QEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAIrprEESLAEKKYTSQGQGDLDSVLSQLNFTHTSEDL 345
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL---EERLKEARLLLLIAAALLALLGLGGSLLSLILT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 346 LQAEVTCLEGSLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQI-LQGEQSYSSALEGMKmEISHLTQEL 424
Cdd:COG4717 275 IAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALgLPPDLSPEELLELLD-RIEELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 425 HQRDITIASTKGSSSDMEKRLRAEMQKAEDKA--VEHKEILDQLESLKLENRHLSEMVMKLELGLHEAKEISLADLQENY 502
Cdd:COG4717 354 REAEELEEELQLEELEQEIAALLAEAGVEDEEelRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEE 433
|
410 420 430
....*....|....*....|....*....|
gi 530375321 503 IEALNKLVSENQ----QLQKDLMNTKSQLE 528
Cdd:COG4717 434 LEELEEELEELEeeleELREELAELEAELE 463
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
164-392 |
9.89e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 9.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 164 QQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVElssqsEIQHLSSKLERANDTicanELEIERLTMRvndlvgtsmt 243
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQ-----ERREALQRLAEYSWD----EIDVASAERE---------- 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 244 vLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQhaVEAIRPREESlAEKKYTS 323
Cdd:COG4913 670 -IAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE--LDELQDRLEA-AEDLARL 745
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530375321 324 QGQGDLDSVLSQLNFTHTSEDLLQAevtcLEGSLESVSATCKQLSQELMEKyeelkrMEAHNNEYKAEI 392
Cdd:COG4913 746 ELRALLEERFAAALGDAVERELREN----LEERIDALRARLNRAEEELERA------MRAFNREWPAET 804
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
95-323 |
1.29e-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: 51.30 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 95 EYKQELKKLHEELCILKRSYEKLQKKQmrefrgntknhREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQR 174
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEE-----------KALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 175 KALAEQSEIIQAQLVNRKQKLESVE-------LSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVgtsmtvlQE 247
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGrqpplalLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA-------AL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 248 QQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVK-----ATNTQHAVEAIRPREESLAEKKYT 322
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAelqqeAEELEALIARLEAEAAAAAERTPA 245
|
.
gi 530375321 323 S 323
Cdd:COG4942 246 A 246
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
136-296 |
2.37e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.79 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 136 RSEIERLTAKIEEFRQKS--LDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESV-----ELSSQSEIQH 208
Cdd:COG3206 188 RKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGpdalpELLQSPVIQQ 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 209 LSSKLERAndticanELEIERLTMRVNDLvGTSMTVLQEQQQ--KEEKLRESEKLLEALQEEKRELKAALQSQENLIHEA 286
Cdd:COG3206 268 LRAQLAEL-------EAELAELSARYTPN-HPDVIALRAQIAalRAQLQQEAQRILASLEAELEALQAREASLQAQLAQL 339
|
170
....*....|
gi 530375321 287 RIQKEKLQEK 296
Cdd:COG3206 340 EARLAELPEL 349
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
133-308 |
4.90e-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: 49.38 E-value: 4.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 133 REDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVelssQSEIQHLSSK 212
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL----EKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 213 LERANDTI---------------------CANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRE 271
Cdd:COG4942 99 LEAQKEELaellralyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190
....*....|....*....|....*....|....*..
gi 530375321 272 LKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEA 308
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAEL 215
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
270-528 |
6.15e-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: 49.67 E-value: 6.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 270 RELKAALQSQENLIHEARIQKEKLQEKvkATNTQHAVEAIRPREESLAEKkyTSQGQGDLDSVLSQLNFTHTSEDLLQAE 349
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEK--IAELEKALAELRKELEELEEE--LEQLRKELEELSRQISALRKDLARLEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 350 VTCLEGSLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQgeqsYSSALEGMKMEISHLTQELHQRDI 429
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ----LKEELKALREALDELRAELTLLNE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 430 TIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEILDQLESLKLENRHLSEMVMKLELGLHEAKEI---------SLADLQE 500
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNErasleealaLLRSELE 897
|
250 260
....*....|....*....|....*...
gi 530375321 501 NYIEALNKLVSENQQLQKDLMNTKSQLE 528
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKLA 925
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
246-533 |
6.48e-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: 6.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 246 QEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQhaVEAIRPREESLAEKKytsqg 325
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE--LARLEQDIARLEERR----- 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 326 qgdldsvlsqlnfthtsEDLLQAEVTcLEGSLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQS 405
Cdd:COG1196 312 -----------------RELEERLEE-LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 406 YSSALEgmkmEISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEILDQLESL--KLENRHLSEMVMKL 483
Cdd:COG1196 374 LAEAEE----ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELeeEEEEEEEALEEAAE 449
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 530375321 484 ELGLHEAKEISLADLQENYIEALNKLVSENQQLQKDLMNTKSQLEISTQM 533
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
157-485 |
8.95e-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: 8.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 157 EKQRLIYQQQVSSLEAQRKALAEQseiiqaqlvnrKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVND 236
Cdd:TIGR02168 224 ELELALLVLRLEELREELEELQEE-----------LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 237 LVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHaveairprEESL 316
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL--------EELE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 317 AEKKYTSQGQGDLDSVLSQLNfthtsedllqAEVTCLEGSLESVSAtckqlsqelmekyeELKRMEAHNNEYKAEIKKLK 396
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLR----------SKVAQLELQIASLNN--------------EIERLEARLERLEDRRERLQ 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 397 EQILQGEQSYSSA-LEGMKMEISHLTQELHQ---RDITIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEILDQLESLKLE 472
Cdd:TIGR02168 421 QEIEELLKKLEEAeLKELQAELEELEEELEElqeELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN 500
|
330
....*....|...
gi 530375321 473 NRHLSEMVMKLEL 485
Cdd:TIGR02168 501 LEGFSEGVKALLK 513
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
211-541 |
9.73e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.30 E-value: 9.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 211 SKLERANDTICANELEIERLTmrvndlvgtsmTVLQEQQQKEEKLR-ESEKLLE--ALQEEKRELKAALQSQENLIHEAR 287
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLD-----------LIIDEKRQQLERLRrEREKAERyqALLKEKREYEGYELLKEKEALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 288 IQKEKLQEKVKATNTQHAVEAIRPREESLAEKkytsqgQGDLDSVLSQLNFTHTSEDL-LQAEVTCLEGSLESVSATCKQ 366
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEI------EQLLEELNKKIKDLGEEEQLrVKEKIGELEAEIASLERSIAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 367 LSQELMEKYEELKRMEAHNNEYKAEIKKLKEQI--LQGEQ-SYSSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEK 443
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLAEIEELEREIeeERKRRdKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 444 RLraemqkaEDKAVEHKEILDQLESLKLENRHLSEMV--MKLELGLHEAKEISLADLQENYIEALNKLVSENQQLQKDLM 521
Cdd:TIGR02169 393 KL-------EKLKREINELKRELDRLQEELQRLSEELadLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465
|
330 340
....*....|....*....|
gi 530375321 522 NTKSQLEISTQMCKKQNDRI 541
Cdd:TIGR02169 466 KYEQELYDLKEEYDRVEKEL 485
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
54-398 |
2.92e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 54 LKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEELcilkrsyEKLQKKQMREFRGNTKNHR 133
Cdd:PRK03918 343 LKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEEL-------EKAKEEIEEEISKITARIG 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 134 EDRSEIERLTAKIEEFRQKSL----------DWEKQRLI--YQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLE----- 196
Cdd:PRK03918 416 ELKKEIKELKKAIEELKKAKGkcpvcgreltEEHRKELLeeYTAELKRIEKELKEIEEKERKLRKELRELEKVLKkesel 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 197 SVELSSQSEIQHLSSKLERAN-DTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAA 275
Cdd:PRK03918 496 IKLKELAEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAEL 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 276 LQSQENLIHEARIQ-KEKLQEKVKATNtqHAVEAIRPREESLAEKKYTSQGQGDLDSVLSQLNFTHTSEDLLQAEVTCLE 354
Cdd:PRK03918 576 LKELEELGFESVEElEERLKELEPFYN--EYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELE 653
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 530375321 355 GSL-----ESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQ 398
Cdd:PRK03918 654 KKYseeeyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE 702
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
57-301 |
3.41e-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: 46.68 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 57 REQELKSLRSQLDVTHKEVGMLHQQVEEHEKikqemtmeykqELKKLHEELCILKRSYEKLQKKQmrefrgntknhREDR 136
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLK-----------QLAALERRIAALARRIRALEQEL-----------AALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 137 SEIERLTAKIEEFRQKSLDWEKQ--RLIYQQQVSSLEAQRKALAEQSEIiqAQLVNRKQKLESVELSSQSEIQHLSSKLE 214
Cdd:COG4942 83 AELAELEKEIAELRAELEAQKEElaELLRALYRLGRQPPLALLLSPEDF--LDAVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 215 RANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQ 294
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
....*..
gi 530375321 295 EKVKATN 301
Cdd:COG4942 241 ERTPAAG 247
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
131-319 |
4.11e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 131 NHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQ--VSSLEAQRKALAEQSEIIQAQLVNRKQKLESVelssQSEIQH 208
Cdd:COG3206 169 RREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEA----EARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 209 LSSKLERANDTICA--NELEIERLTMRVNDLVgtsmtvlQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQ-ENLIHE 285
Cdd:COG3206 245 LRAQLGSGPDALPEllQSPVIQQLRAQLAELE-------AELAELSARYTPNHPDVIALRAQIAALRAQLQQEaQRILAS 317
|
170 180 190
....*....|....*....|....*....|....
gi 530375321 286 ARIQKEKLQEKVKATNTQhaVEAIRPREESLAEK 319
Cdd:COG3206 318 LEAELEALQAREASLQAQ--LAQLEARLAELPEL 349
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
98-289 |
7.20e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 7.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 98 QELKKLHEELCILKRSYEKLQkkQMREFRGNTKNHREDRSEIERLTAKIE-EFRQKSLDWEKQRLI-YQQQVSSLEAQRK 175
Cdd:COG4913 235 DDLERAHEALEDAREQIELLE--PIRELAERYAAARERLAELEYLRAALRlWFAQRRLELLEAELEeLRAELARLEAELE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 176 ALAEQSEIIQAQLVNRKQKLESVELSS----QSEIQHLSSKLERANDTICANELEIERLTMRVND-----------LVGT 240
Cdd:COG4913 313 RLEARLDALREELDELEAQIRGNGGDRleqlEREIERLERELEERERRRARLEALLAALGLPLPAsaeefaalraeAAAL 392
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 530375321 241 SMTVLQEQQQKEEKLRESEKLLEALQEEKRELK---AALQSQENLIHEARIQ 289
Cdd:COG4913 393 LEALEEELEALEEALAEAEAALRDLRRELRELEaeiASLERRKSNIPARLLA 444
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
73-528 |
8.27e-05 |
|
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: 46.12 E-value: 8.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 73 KEVGMLHQQVEEHEKIKQEMTMEYKQElKKLHEELCILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQk 152
Cdd:TIGR00618 163 KEKKELLMNLFPLDQYTQLALMEFAKK-KSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQ- 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 153 SLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVELSSQSE--------IQHLSSKLERANDTICANE 224
Cdd:TIGR00618 241 SHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAplaahikaVTQIEQQAQRIHTELQSKM 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 225 LEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEK--RELKAALQSQENLIHEARIQKEKLQEKVKA--- 299
Cdd:TIGR00618 321 RSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATsiREISCQQHTLTQHIHTLQQQKTTLTQKLQSlck 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 300 -----TNTQHAVEAIRPREESLAEKKYTSQGQGDLDSVLSQLNFTHTSEDL--LQAEVTCLEGSLESVSATCKQLS--QE 370
Cdd:TIGR00618 401 eldilQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAqcEKLEKIHLQESAQSLKEREQQLQtkEQ 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 371 LMEKYEELKRMEAHN-NEYKAEIKKLKEQILQGEQSYSSALE----------GMKMEISHLTQELHQRDITIASTKGSSS 439
Cdd:TIGR00618 481 IHLQETRKKAVVLARlLELQEEPCPLCGSCIHPNPARQDIDNpgpltrrmqrGEQTYAQLETSEEDVYHQLTSERKQRAS 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 440 DMEK--RLRAEMQKAEDKAVEHKEILDQLESLKLENRHLSEMVMKLELGLHEAKEISLADLQENyiEALNKLVSENQQLQ 517
Cdd:TIGR00618 561 LKEQmqEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPE--QDLQDVRLHLQQCS 638
|
490
....*....|.
gi 530375321 518 KDLMNTKSQLE 528
Cdd:TIGR00618 639 QELALKLTALH 649
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
58-453 |
1.10e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 58 EQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQemTMEYKQELKKLHEELCILKRSYEKLqKKQMREFRGNTKNHREDRS 137
Cdd:COG4717 94 QEELEELEEELEELEAELEELREELEKLEKLLQ--LLPLYQELEALEAELAELPERLEEL-EERLEELRELEEELEELEA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 138 EIERLTAKIEE-FRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLEsvELSSQSEIQHLSSKLERA 216
Cdd:COG4717 171 ELAELQEELEElLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE--QLENELEAAALEERLKEA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 217 N------DTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELkAALQSQENLIHEARIQK 290
Cdd:COG4717 249 RlllliaAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQAL-PALEELEEEELEELLAA 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 291 EKLQEKVKATNTQHAVEAIRPREESLAEKKytsqgqgDLDSVLSQLNFTHTSEDLLQAevtCLEGSLESVSATCKQLS-- 368
Cdd:COG4717 328 LGLPPDLSPEELLELLDRIEELQELLREAE-------ELEEELQLEELEQEIAALLAE---AGVEDEEELRAALEQAEey 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 369 QELMEKYEELK-RMEAHNNEYKAEIKKLKEQILQGE-QSYSSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLR 446
Cdd:COG4717 398 QELKEELEELEeQLEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQE 477
|
....*..
gi 530375321 447 AEMQKAE 453
Cdd:COG4717 478 LEELKAE 484
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
81-471 |
1.26e-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: 45.35 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 81 QVEEHEKIKQEMTMEYKQELKKLHEELCILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQR 160
Cdd:pfam02463 180 EETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 161 liyQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGT 240
Cdd:pfam02463 260 ---IEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 241 SmtvLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAIRPREESLAEKK 320
Cdd:pfam02463 337 I---EELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLEL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 321 ytsqgqgdLDSVLSQLNFTHTSEDLLQAEVTCLEGSLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQIL 400
Cdd:pfam02463 414 --------ARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQ 485
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530375321 401 QGEQSYSSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEILDQLESLKL 471
Cdd:pfam02463 486 LELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSAT 556
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
163-322 |
1.69e-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: 44.34 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 163 YQQQVSSLEAQRKALAEQSEIIQAQlVNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDlvgtsM 242
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAE-LDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLAR-----R 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 243 TVLQEQQ-QKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAIRPREESLAEKKY 321
Cdd:pfam00529 130 RVLAPIGgISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLER 209
|
.
gi 530375321 322 T 322
Cdd:pfam00529 210 T 210
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
18-455 |
2.11e-04 |
|
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: 44.65 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 18 LTSCEAELQELMKQIDIMVahkkseweGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYK 97
Cdd:TIGR00606 711 LKSTESELKKKEKRRDEML--------GLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEE 782
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 98 QE---------LKKLHEELCILKRSYEKLQKKQ-----MREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIY 163
Cdd:TIGR00606 783 SAkvcltdvtiMERFQMELKDVERKIAQQAAKLqgsdlDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHL 862
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 164 QQQVSSLEAQRKALAEQSEiiqaqlvnRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVgtsmt 243
Cdd:TIGR00606 863 KSKTNELKSEKLQIGTNLQ--------RRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELI----- 929
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 244 vlqeqQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARiQKEKLQEKVKATNTQHAVEAIRPREESLAEkkyts 323
Cdd:TIGR00606 930 -----SSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGK-DDYLKQKETELNTVNAQLEECEKHQEKINE----- 998
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 324 qgqgDLDSVLSQLNFTHTSEDLLQAEVTclegsLESVSATCKQLSQELMEKYEELKRMEAhnNEYKAEIKKLKEQILQGE 403
Cdd:TIGR00606 999 ----DMRLMRQDIDTQKIQERWLQDNLT-----LRKRENELKEVEEELKQHLKEMGQMQV--LQMKQEHQKLEENIDLIK 1067
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 530375321 404 QSYSSALEGMK---MEISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDK 455
Cdd:TIGR00606 1068 RNHVLALGRQKgyeKEIKHFKKELREPQFRDAEEKYREMMIVMRTTELVNKDLDI 1122
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
38-525 |
2.28e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.63 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 38 HKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTmEYKQELKKLHEELCILKRSYEKL 117
Cdd:TIGR04523 159 NKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNK-SLESQISELKKQNNQLKDNIEKK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 118 QKKQmrefrgntknhREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVN-RKQKLE 196
Cdd:TIGR04523 238 QQEI-----------NEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDlNNQKEQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 197 SVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAAL 276
Cdd:TIGR04523 307 DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 277 QSQENLIH--EARIQKEK-----LQEKVKATNTQHAV---EAIRPREESLAEKKYTSQGQGDLDSVLSQLNFTHTSEDLL 346
Cdd:TIGR04523 387 KNLESQINdlESKIQNQEklnqqKDEQIKKLQQEKELlekEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESL 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 347 QAEVTCLEGSLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQI---LQGEQSYSSALEGMKMEISHLTQE 423
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKIsslKEKIEKLESEKKEKESKISDLEDE 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 424 LHQRDITIASTKGSSSDMEK-----RLRAEMQKAEDKAVEHKEILDQLESLKLENRHLSEMVMKL------ELGLHEAKE 492
Cdd:TIGR04523 547 LNKDDFELKKENLEKEIDEKnkeieELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKisslekELEKAKKEN 626
|
490 500 510
....*....|....*....|....*....|...
gi 530375321 493 ISLADLQENYIEALNKLVSENQQLQKDLMNTKS 525
Cdd:TIGR04523 627 EKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRN 659
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
136-305 |
2.37e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 136 RSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEI---------IQAQLVNRKQKLESVELSSqSEI 206
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYswdeidvasAEREIAELEAELERLDASS-DDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 207 QHLSSKLERAndticanELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKR-ELKAALQSQ-ENLIH 284
Cdd:COG4913 688 AALEEQLEEL-------EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlELRALLEERfAAALG 760
|
170 180
....*....|....*....|...
gi 530375321 285 EARIQK--EKLQEKVKATNTQHA 305
Cdd:COG4913 761 DAVERElrENLEERIDALRARLN 783
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
24-458 |
2.80e-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: 44.44 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 24 ELQELMKQIDIMVAHKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKL 103
Cdd:pfam12128 280 ERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 104 HEELCILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLdwEKQRLIYQQQVSSL----EAQRKALAE 179
Cdd:pfam12128 360 EERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQL--AVAEDDLQALESELreqlEAGKLEFNE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 180 QSEIIQAQLVNRKQKLESVELSS---------QSEIQHLSSKLERANDTICANELEIERLTMR---VNDLVGTSMTVLQE 247
Cdd:pfam12128 438 EEYRLKSRLGELKLRLNQATATPelllqlenfDERIERAREEQEAANAEVERLQSELRQARKRrdqASEALRQASRRLEE 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 248 QQQKEEKLRE-----SEKLLEALQEEK---RELKAALQSQEnLIHEARIQKEKLQEKVKATNTQHAV------------- 306
Cdd:pfam12128 518 RQSALDELELqlfpqAGTLLHFLRKEApdwEQSIGKVISPE-LLHRTDLDPEVWDGSVGGELNLYGVkldlkridvpewa 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 307 ---EAIRpREESLAEKKYTSQG--QGDLDSVLSQLNfthTSEDLLQAEVTCLEGSLESVSATCKQLS----QELMEKYEE 377
Cdd:pfam12128 597 aseEELR-ERLDKAEEALQSARekQAAAEEQLVQAN---GELEKASREETFARTALKNARLDLRRLFdekqSEKDKKNKA 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 378 LKRMEAHNNEYKAEIKKLKEQILQGEQSYSSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDKAV 457
Cdd:pfam12128 673 LAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKAL 752
|
.
gi 530375321 458 E 458
Cdd:pfam12128 753 E 753
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
226-492 |
3.29e-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: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 226 EIERLTMRVNDLVGTSMTVLQEQqqkeeklrESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATN---- 301
Cdd:COG3096 810 KLQRLHQAFSQFVGGHLAVAFAP--------DPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNkllp 881
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 302 -------TQHA--VEAIRPREESLAEKKYTSQGQGD----LDSVLSQLNFTHTSEDLLQAEVTCLEGSLESVSATCKQLS 368
Cdd:COG3096 882 qanlladETLAdrLEELREELDAAQEAQAFIQQHGKalaqLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALS 961
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 369 qELMEK-----YEELKRMEAHNNEYKaeiKKLKEQILQGEQSYSSALEGMKMEISHLTQeLHQRditIASTKGS------ 437
Cdd:COG3096 962 -EVVQRrphfsYEDAVGLLGENSDLN---EKLRARLEQAEEARREAREQLRQAQAQYSQ-YNQV---LASLKSSrdakqq 1033
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530375321 438 ----------------SSDMEKRLRAEMQKAEDKAVEHKEILDQLE----SLKLENRHLSEMVMKLELGLHEAKE 492
Cdd:COG3096 1034 tlqeleqeleelgvqaDAEAEERARIRRDELHEELSQNRSRRSQLEkqltRCEAEMDSLQKRLRKAERDYKQERE 1108
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
20-220 |
3.63e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 20 SCEAELQELMKQIDIMVAhKKSEWEgrthALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQE--MTMEYK 97
Cdd:COG4913 665 SAEREIAELEAELERLDA-SSDDLA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDElqDRLEAA 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 98 QELKKLHEELCILKRSYEKLQKKQMREFRGNTKNHRED-RSEIERLTAKIEE-FRQKSLDWekqRLIYQQQVSSLEAQRK 175
Cdd:COG4913 740 EDLARLELRALLEERFAAALGDAVERELRENLEERIDAlRARLNRAEEELERaMRAFNREW---PAETADLDADLESLPE 816
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 530375321 176 ALAEQSEIIQAQLVNRKQKL-ESVELSSQSEIQHLSSKLERANDTI 220
Cdd:COG4913 817 YLALLDRLEEDGLPEYEERFkELLNENSIEFVADLLSKLRRAIREI 862
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
58-336 |
3.70e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 58 EQELKSLRSQL-------DVTHKEVGMLHQQVEEHEKIKQ-------------EMTMEYKQELKKLHEELCILKRsyeKL 117
Cdd:PRK04863 389 EEEVDELKSQLadyqqalDVQQTRAIQYQQAVQALERAKQlcglpdltadnaeDWLEEFQAKEQEATEELLSLEQ---KL 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 118 QKKQM--REFRGNTKNHREDRSEIERLTAKiEEFRQKSLDWEKQRlIYQQQVSSLEAQRKALAEQSEIIQA--QLVNRKQ 193
Cdd:PRK04863 466 SVAQAahSQFEQAYQLVRKIAGEVSRSEAW-DVARELLRRLREQR-HLAEQLQQLRMRLSELEQRLRQQQRaeRLLAEFC 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 194 KLESVELSSQSEIQHLSSKLERandticanelEIERLTMRVNDLVGTSMTVLQEQQQKEEKLREseklLEALQEEKRELK 273
Cdd:PRK04863 544 KRLGKNLDDEDELEQLQEELEA----------RLESLSESVSEARERRMALRQQLEQLQARIQR----LAARAPAWLAAQ 609
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530375321 274 AAL-----QSQENLIHEARI--QKEKLQEKVKAtnTQHAVEAIRPREESL-AEKKYTSQGQGDLDSVLSQL 336
Cdd:PRK04863 610 DALarlreQSGEEFEDSQDVteYMQQLLERERE--LTVERDELAARKQALdEEIERLSQPGGSEDPRLNAL 678
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
22-528 |
4.01e-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: 44.01 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 22 EAELQELMKQIDIMVAHKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTME---YKQ 98
Cdd:pfam01576 52 ETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEkvtTEA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 99 ELKKLHEELCILKRSYEKLQKkqmrefrgnTKNHREDRseIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKala 178
Cdd:pfam01576 132 KIKKLEEDILLLEDQNSKLSK---------ERKLLEER--ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLK--- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 179 eQSEIIQAQLVNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLREs 258
Cdd:pfam01576 198 -KEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISE- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 259 ekLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAIRPREESLAEKKYTSQGQGDlDSVLSQLNF 338
Cdd:pfam01576 276 --LQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSH-EAQLQEMRQ 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 339 THTSE-DLLQAEVTCLEGSLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQiLQGEQSYSSALEGMKMEI 417
Cdd:pfam01576 353 KHTQAlEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQ-LQELQARLSESERQRAEL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 418 SHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEILDQLESLKLEnrhLSEMVMKLelglhEAKEISLAD 497
Cdd:pfam01576 432 AEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLN---LSTRLRQL-----EDERNSLQE 503
|
490 500 510
....*....|....*....|....*....|.
gi 530375321 498 LQENYIEALNKLVSENQQLQKDLMNTKSQLE 528
Cdd:pfam01576 504 QLEEEEEAKRNVERQLSTLQAQLSDMKKKLE 534
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
247-456 |
4.35e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 247 EQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQ--HAVEAIRPREESLAEKKYTSQ 324
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 325 GQGDLDSVLSQLnFTHTS-EDLLQAEVTclegsLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGE 403
Cdd:COG3883 97 RSGGSVSYLDVL-LGSESfSDFLDRLSA-----LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 530375321 404 QSYSSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDKA 456
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
58-303 |
4.52e-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: 43.63 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 58 EQELKSLRSQldvthkEVGMLHQQVEE----HEKIKQEMTMEYKQELKKLHEELCILKRSYEKLQK-KQMREfrgntKNH 132
Cdd:pfam01576 318 QQELRSKREQ------EVTELKKALEEetrsHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKaKQALE-----SEN 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 133 REDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVE---LSSQSEIQHL 209
Cdd:pfam01576 387 AELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEgknIKLSKDVSSL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 210 SSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQ 289
Cdd:pfam01576 467 ESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEG 546
|
250
....*....|....
gi 530375321 290 KEKLQEKVKATNTQ 303
Cdd:pfam01576 547 KKRLQRELEALTQQ 560
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
61-540 |
4.67e-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: 43.67 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 61 LKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEELcilkrsyeklqKKQMREFRGNTKNHRED----R 136
Cdd:pfam12128 253 LESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQW-----------KEKRDELNGELSAADAAvakdR 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 137 SEIERLTAKIEEFRQKSLDWEKQRL----IYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKlesVELSSQSEIQHLSSK 212
Cdd:pfam12128 322 SELEALEDQHGAFLDADIETAAADQeqlpSWQSELENLEERLKALTGKHQDVTAKYNRRRSK---IKEQNNRDIAGIKDK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 213 LERANDTI----CANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARI 288
Cdd:pfam12128 399 LAKIREARdrqlAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERARE 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 289 QKEKLQEKVKATNTQHAVEAIRPREESLA---EKKYTSQGQGDLDSVLSQLN-FTHTSEDLLQAEVTCLEGSLESVSATC 364
Cdd:pfam12128 479 EQEAANAEVERLQSELRQARKRRDQASEAlrqASRRLEERQSALDELELQLFpQAGTLLHFLRKEAPDWEQSIGKVISPE 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 365 KQLSQELMEKYEE---------------LKRMEAhnNEYKAEIKKLKEQILQGEQSYSSALEGMKMEISHLTQ-----EL 424
Cdd:pfam12128 559 LLHRTDLDPEVWDgsvggelnlygvkldLKRIDV--PEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQangelEK 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 425 HQRDITIASTKGSSSDME-KRLRAEMQKAEDKAveHKEILDQLESLKLENRHLSEMVMKLELGLHEAKEISLADLQENYI 503
Cdd:pfam12128 637 ASREETFARTALKNARLDlRRLFDEKQSEKDKK--NKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREART 714
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 530375321 504 EALNKL--VSENQQLQKDLMNT-----KSQLEISTQMCKKQNDR 540
Cdd:pfam12128 715 EKQAYWqvVEGALDAQLALLKAaiaarRSGAKAELKALETWYKR 758
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
136-320 |
4.78e-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: 4.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 136 RSEIERLTAKIEEFRQksldwEKQRLiyQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVeLSSQSEIQHLSSKLER 215
Cdd:COG3883 36 QAELDALQAELEELNE-----EYNEL--QAELEALQAEIDKLQAEIAEAEAEIEERREELGER-ARALYRSGGSVSYLDV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 216 ---ANDTicaNELeIERLTMrVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEK 292
Cdd:COG3883 108 llgSESF---SDF-LDRLSA-LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEA 182
|
170 180
....*....|....*....|....*...
gi 530375321 293 LQEKVKAtNTQHAVEAIRPREESLAEKK 320
Cdd:COG3883 183 LLAQLSA-EEAAAEAQLAELEAELAAAE 209
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
133-299 |
5.97e-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: 41.83 E-value: 5.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 133 REDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVelSSQSEIQHLSSK 212
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV--RNNKEYEALQKE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 213 LERANDTICANELEIERLTMRVNDLvgtsmtvlqeQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEK 292
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEEL----------EEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
....*..
gi 530375321 293 LQEKVKA 299
Cdd:COG1579 168 LAAKIPP 174
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
22-286 |
6.87e-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: 43.13 E-value: 6.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 22 EAELQELMKQIdimvahkkSEWEGRTHALETCLKIREQELKSLRSQLdvthkevgmlhqqveEHEKIKQEMTMEYKQELK 101
Cdd:TIGR02169 797 QAELSKLEEEV--------SRIEARLREIEQKLNRLTLEKEYLEKEI---------------QELQEQRIDLKEQIKSIE 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 102 KLHEELCILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQS 181
Cdd:TIGR02169 854 KEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 182 EIIQAQLvnRKQKLESVELSSQSEIQhlssklerandticaneLEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKL 261
Cdd:TIGR02169 934 SEIEDPK--GEDEEIPEEELSLEDVQ-----------------AELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEK 994
|
250 260
....*....|....*....|....*
gi 530375321 262 LEALQEEKRELKAALQSQENLIHEA 286
Cdd:TIGR02169 995 RAKLEEERKAILERIEEYEKKKREV 1019
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
89-500 |
8.25e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.97 E-value: 8.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 89 KQEMTMEYKQELKKLHEELCILKRSYEKLqKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQrliYQQQVS 168
Cdd:PRK01156 323 KYHAIIKKLSVLQKDYNDYIKKKSRYDDL-NNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAF---ISEILK 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 169 SLEAQRKALAEQSEIIQAQLVNRKQKLESVELSSQSEIQHLSSKLERAND-------TICANELEIERLTMRVNDLVgts 241
Cdd:PRK01156 399 IQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMlngqsvcPVCGTTLGEEKSNHIINHYN--- 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 242 mtvlQEQQQKEEKLRESEKLLEALQEEKRELKAAlqsqenlihEARIQKEKLQEKVKATN----TQHAVEAIRPREESLA 317
Cdd:PRK01156 476 ----EKKSRLEEKIREIEIEVKDIDEKIVDLKKR---------KEYLESEEINKSINEYNkiesARADLEDIKIKINELK 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 318 EK---------KYTSQGQGDLDSVLSQLNFTHTSEDLLQAEVtcLEGSLESVSATCKQLSQELMEKYEELKRMEAHNNEY 388
Cdd:PRK01156 543 DKhdkyeeiknRYKSLKLEDLDSKRTSWLNALAVISLIDIET--NRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKS 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 389 kaeIKKLKEQILQGEQSYS------SALEGMKMEISHLTQELHQRDITIASTKGSSS---DMEKRLRAEMQKAEDKAVEH 459
Cdd:PRK01156 621 ---IREIENEANNLNNKYNeiqenkILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSrinDIEDNLKKSRKALDDAKANR 697
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 530375321 460 KEILDQLESLKLENRHLSEMVMKLELGLHEAKEI--SLADLQE 500
Cdd:PRK01156 698 ARLESTIEILRTRINELSDRINDINETLESMKKIkkAIGDLKR 740
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
233-337 |
1.26e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.12 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 233 RVNDLVGTSMTVLQEQQQKEE----KLRESEKLLEALQEEKRELKAAlqsQENLIHEariQKEKLQEKVKAtnTQHAVEA 308
Cdd:PRK00409 517 KLNELIASLEELERELEQKAEeaeaLLKEAEKLKEELEEKKEKLQEE---EDKLLEE---AEKEAQQAIKE--AKKEADE 588
|
90 100
....*....|....*....|....*....
gi 530375321 309 IRPREESLAEKKYTSQGQGDLDSVLSQLN 337
Cdd:PRK00409 589 IIKELRQLQKGGYASVKAHELIEARKRLN 617
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
58-209 |
1.30e-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: 40.66 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 58 EQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMtMEYKQELKKLHEELCILKRSYEKLQKKqmrefrgNTKNHREDRS 137
Cdd:pfam13851 53 QQENKRLTEPLQKAQEEVEELRKQLENYEKDKQSL-KNLKARLKVLEKELKDLKWEHEVLEQR-------FEKVERERDE 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530375321 138 EIERLTAKIEEFRQKSldwEKQRLIYQQQVSSL-------EAQRKALAEQSEIIQAQLVNRKQKLESVELSSQSEIQHL 209
Cdd:pfam13851 125 LYDKFEAAIQDVQQKT---GLKNLLLEKKLQALgetlekkEAQLNEVLAAANLDPDALQAVTEKLEDVLESKNQLIKDL 200
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
95-512 |
1.32e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 95 EYKQELKKLHEELCILKRSYEKLQkkQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQR 174
Cdd:COG4717 92 ELQEELEELEEELEELEAELEELR--EELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 175 KALAEQSEIIQaqlvnrkQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDlvgtsmtvLQEQQQKEEK 254
Cdd:COG4717 170 AELAELQEELE-------ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE--------LEEELEQLEN 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 255 LRESEKLLEALQEEKRELKAA------------LQSQENLIHEARI---------------QKEKLQEKVKATNTQHAVE 307
Cdd:COG4717 235 ELEAAALEERLKEARLLLLIAaallallglggsLLSLILTIAGVLFlvlgllallflllarEKASLGKEAEELQALPALE 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 308 AIRPRE-ESLAEKKYTSQGQ-----GDLDSVLSQLNFTHTSEDLLQAEVTcLEGSLESVSATCKQLSQELMEKYEELKRM 381
Cdd:COG4717 315 ELEEEElEELLAALGLPPDLspeelLELLDRIEELQELLREAEELEEELQ-LEELEQEIAALLAEAGVEDEEELRAALEQ 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 382 EAHNNEYKAEIKKLKEQILQGEQSYSSALEGMKMEisHLTQELHQRDITIASTKGSSSDMEKR---LRAEMQKAEDKAvE 458
Cdd:COG4717 394 AEEYQELKEELEELEEQLEELLGELEELLEALDEE--ELEEELEELEEELEELEEELEELREElaeLEAELEQLEEDG-E 470
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 530375321 459 HKEILDQLESLKLENRHLSEMVMKLELGLHEAKEIsLADLQENYIEALNKLVSE 512
Cdd:COG4717 471 LAELLQELEELKAELRELAEEWAALKLALELLEEA-REEYREERLPPVLERASE 523
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
55-518 |
1.96e-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: 41.57 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 55 KIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEmtmeYKQELKKLHEELCILKRSYEKLQKKQMREfrgntknhre 134
Cdd:TIGR00606 573 KQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNH----INNELESKEEQLSSYEDKLFDVCGSQDEE---------- 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 135 drSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSeiiqaqlvnrkQKLESVELSSQSEIQHLSSKLE 214
Cdd:TIGR00606 639 --SDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVC-----------QRVFQTEAELQEFISDLQSKLR 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 215 RANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIhEARIQKEKLQ 294
Cdd:TIGR00606 706 LAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLL-GTIMPEEESA 784
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 295 E--KVKATNTQHAVEAIRPREESLAEKKYTSQGQgDLDSVLSQLNfthtsedllqAEVTCLEGSLESVSATCKQLSQELM 372
Cdd:TIGR00606 785 KvcLTDVTIMERFQMELKDVERKIAQQAAKLQGS-DLDRTVQQVN----------QEKQEKQHELDTVVSKIELNRKLIQ 853
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 373 EKYEELKRMEAHNNEYKAEIKKLKEQiLQGEQSYSSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKA 452
Cdd:TIGR00606 854 DQQEQIQHLKSKTNELKSEKLQIGTN-LQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSK 932
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530375321 453 EDkavEHKEILDQLESLKLENRHLSEMVMKLELGLHEAKEISLADlQENYIEALNKLVSENQQLQK 518
Cdd:TIGR00606 933 ET---SNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQ-KETELNTVNAQLEECEKHQE 994
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
95-341 |
2.00e-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: 41.42 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 95 EYKQELKKLHEELCILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQR 174
Cdd:pfam07888 38 ECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 175 KALAEQSEiiqaqlvnrkqklesvelSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEK 254
Cdd:pfam07888 118 DALLAQRA------------------AHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 255 LRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHA-VEAIRPREESLAEKKYTSQGQ-----GD 328
Cdd:pfam07888 180 LQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAeNEALLEELRSLQERLNASERKveglgEE 259
|
250
....*....|...
gi 530375321 329 LDSVLSQLNFTHT 341
Cdd:pfam07888 260 LSSMAAQRDRTQA 272
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
253-456 |
2.11e-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: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 253 EKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAV-----------------------EAI 309
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAleqelaaleaelaelekeiaelrAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 310 RPREESLAEKKYTSQGQGDLDSVLSQLNfthtSEDLLQAEVTclEGSLESVSATCKQLSQELMEKYEELKRMEAHNNEYK 389
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLLS----PEDFLDAVRR--LQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530375321 390 AEIKKLKEQILQGEQSYSSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDKA 456
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
97-299 |
2.27e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.21 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 97 KQELKKLHEELCILKRSYEKLQKKQmrefrgntknhREDRSEIERLTAKIEEFRQ--------KSLDWEKQRLIYQQQV- 167
Cdd:COG0497 157 LEEYREAYRAWRALKKELEELRADE-----------AERARELDLLRFQLEELEAaalqpgeeEELEEERRRLSNAEKLr 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 168 SSLEAQRKALAEQSEIIQAQLVNRKQKLESVE-------------LSSQSEIQHLSSKLERANDTICANELEIERLTMRV 234
Cdd:COG0497 226 EALQEALEALSGGEGGALDLLGQALRALERLAeydpslaelaerlESALIELEEAASELRRYLDSLEFDPERLEEVEERL 305
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530375321 235 NDLVGTS----------MTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQK-EKLQEKVKA 299
Cdd:COG0497 306 ALLRRLArkygvtveelLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKKAaKKLEKAVTA 381
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
54-539 |
2.35e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 54 LKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMT---MEYKQELKKLHEELCILKrSYEKLQKKQM-------- 122
Cdd:TIGR04523 49 LKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNdklKKNKDKINKLNSDLSKIN-SEIKNDKEQKnkleveln 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 123 ---REFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLiyqqqvsSLEAQRKALAEQSEIIQAQLVNRKQKLesve 199
Cdd:TIGR04523 128 kleKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKE-------ELENELNLLEKEKLNIQKNIDKIKNKL---- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 200 lssqSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQ 279
Cdd:TIGR04523 197 ----LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 280 ENLIHEARIQKEKLQEKVKATNTQHAVEAIRPREESLAE-KKYTSQGQGDLDSVLSQLNFTHTSEDLLQAEVTCLEGSLE 358
Cdd:TIGR04523 273 QKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKElKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELT 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 359 SVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQIlqgeqsyssalEGMKMEISHLTQELHQRDITIASTKGSS 438
Cdd:TIGR04523 353 NSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI-----------NDLESKIQNQEKLNQQKDEQIKKLQQEK 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 439 SDMEKrlraemqkaedkavEHKEILDQLESLKLENRHLSEMVMKLELGLHEAKeiSLADLQENYIEALNKLVSENQQlqk 518
Cdd:TIGR04523 422 ELLEK--------------EIERLKETIIKNNSEIKDLTNQDSVKELIIKNLD--NTRESLETQLKVLSRSINKIKQ--- 482
|
490 500
....*....|....*....|.
gi 530375321 519 DLMNTKSQLEISTQMCKKQND 539
Cdd:TIGR04523 483 NLEQKQKELKSKEKELKKLNE 503
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
193-303 |
2.46e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 193 QKLESVELSSQ-SEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRE 271
Cdd:PRK09039 41 QFFLSREISGKdSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGE 120
|
90 100 110
....*....|....*....|....*....|..
gi 530375321 272 LKAALQSQENLIHEARIQKEKLQEKVKATNTQ 303
Cdd:PRK09039 121 LAQELDSEKQVSARALAQVELLNQQIAALRRQ 152
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
191-512 |
2.56e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 191 RKQKLESVELSSQSEIQHLSSKLERANDTICAnELEIERLTMRVNDLVgtsmtvlQEQQQKEEKLRESEKLLEALQEEKR 270
Cdd:PRK02224 476 RVEELEAELEDLEEEVEEVEERLERAEDLVEA-EDRIERLEERREDLE-------ELIAERRETIEEKRERAEELRERAA 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 271 ELKAALQSQENLIHEARIQKEKLQEKVKATNTQhaveairpreeslaekkytsqgQGDLDSVLSQLNFTHTSEDLLqaev 350
Cdd:PRK02224 548 ELEAEAEEKREAAAEAEEEAEEAREEVAELNSK----------------------LAELKERIESLERIRTLLAAI---- 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 351 tclegslesvsATCKQLSQELMEKYEELKRMeahNNEYKAEIKKLKEQILQGEQSY-SSALEGMKMEISHLTQELHQRDI 429
Cdd:PRK02224 602 -----------ADAEDEIERLREKREALAEL---NDERRERLAEKRERKRELEAEFdEARIEEAREDKERAEEYLEQVEE 667
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 430 TIASTKGSSSDMEKRLraemqkaedKAVEHKeiLDQLESLKLENRHLSEMVMKLELGLHEAKEIS------LADLQENYI 503
Cdd:PRK02224 668 KLDELREERDDLQAEI---------GAVENE--LEELEELRERREALENRVEALEALYDEAEELEsmygdlRAELRQRNV 736
|
....*....
gi 530375321 504 EALNKLVSE 512
Cdd:PRK02224 737 ETLERMLNE 745
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
57-492 |
3.29e-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: 40.86 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 57 REQELKSLRSQLDVTHKEVgmlhQQVEEHEKIKQEMTMEYKQELKKLHEELCILKRSYEKLQKKQmrefrgntKNHREDR 136
Cdd:pfam05483 252 KENKMKDLTFLLEESRDKA----NQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQ--------KALEEDL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 137 SEIERLTAKIEEFRQKSLD-WEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVELssqsEIQHLSSKLER 215
Cdd:pfam05483 320 QIATKTICQLTEEKEAQMEeLNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITM----ELQKKSSELEE 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 216 ANDTICANELEIERLTmrvndlvgtsmTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKeklqe 295
Cdd:pfam05483 396 MTKFKNNKEVELEELK-----------KILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQL----- 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 296 KVKATNTQHAVEAIRPREESLAEKKYTSQGQGDLDSVLSQLNFTHTSEdllQAEVTCLEGSLESVSATCKQLSQELMEKY 375
Cdd:pfam05483 460 TAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQE---ASDMTLELKKHQEDIINCKKQEERMLKQI 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 376 EELKRMEAhnnEYKAEIKKLKEQILQGEQSYSSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDK 455
Cdd:pfam05483 537 ENLEEKEM---NLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEEL 613
|
410 420 430
....*....|....*....|....*....|....*..
gi 530375321 456 AVEHKEILDQLESLKLENRHLSEMVMKLELGLHEAKE 492
Cdd:pfam05483 614 HQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQ 650
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
140-469 |
4.04e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.80 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 140 ERLTAKIEEFRQKSLDWEKQRLIYQQ-QVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVELSS-QSEIQHLSSKLERAN 217
Cdd:TIGR00606 189 ETLRQVRQTQGQKVQEHQMELKYLKQyKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNrLKEIEHNLSKIMKLD 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 218 DTICA---NELEIERLTMRVNDLVGTSMTVLQEQ------------QQKEEKLRESEKLLEALQEEKRELKAALQSQENL 282
Cdd:TIGR00606 269 NEIKAlksRKKQMEKDNSELELKMEKVFQGTDEQlndlyhnhqrtvREKERELVDCQRELEKLNKERRLLNQEKTELLVE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 283 IHEARIQKEKLQEKVKATNTQHAVEAIRPREESLAEKKYTS-----------QGQGDLDSVLSQL-NFTHTSEDLLQAEV 350
Cdd:TIGR00606 349 QGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSErqiknfhtlviERQEDEAKTAAQLcADLQSKERLKQEQA 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 351 TCLEGSLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKlkeqILQGEQSYSSALEGM-KMEISHLTQELHQRDI 429
Cdd:TIGR00606 429 DEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDR----ILELDQELRKAERELsKAEKNSLTETLKKEVK 504
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 530375321 430 tiaSTKGSSSDMEKRLRAEMQKAEDKAvEHKEILDQLESL 469
Cdd:TIGR00606 505 ---SLQNEKADLDRKLRKLDQEMEQLN-HHTTTRTQMEML 540
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
18-409 |
6.47e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 18 LTSCEAELQELMKQID-IMVAHKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEY 96
Cdd:COG4717 104 LEELEAELEELREELEkLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 97 KQELKKLHEELCILKRSYEKLQKKQMREfrgnTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQ--------VS 168
Cdd:COG4717 184 EQLSLATEEELQDLAEELEELQQRLAEL----EEELEEAQEELEELEEELEQLENELEAAALEERLKEARlllliaaaLL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 169 SLEAQRKALAEQSEIIQAQLVNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQ 248
Cdd:COG4717 260 ALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEEL 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 249 QQKEEKLRESEKLLEALQEEKRELKaalqsqenlIHEARIQKEKLQEKVKATNTQ---HAVEAIRPREESLAE-KKYTSQ 324
Cdd:COG4717 340 LELLDRIEELQELLREAEELEEELQ---------LEELEQEIAALLAEAGVEDEEelrAALEQAEEYQELKEElEELEEQ 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 325 GQGDLDSVLSQLNftHTSEDLLQAEVTCLEGSLESVSATCKQLSQELMEKYEELKRMEAHNN--EYKAEIKKLKEQILQG 402
Cdd:COG4717 411 LEELLGELEELLE--ALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGElaELLQELEELKAELREL 488
|
....*..
gi 530375321 403 EQSYSSA 409
Cdd:COG4717 489 AEEWAAL 495
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
55-554 |
7.30e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 7.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 55 KIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQ---ELKKLHEelcilKRSYEKLQKK--QMREFRGNT 129
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKkadEAKKAEE-----KKKADEAKKKaeEAKKADEAK 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 130 KNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLEsvELSSQSEIQHL 209
Cdd:PTZ00121 1322 KKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE--EKKKADEAKKK 1399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 210 SSKLERANDTICANELEIERltmrvndlvgtsmtvLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENliHEARIQ 289
Cdd:PTZ00121 1400 AEEDKKKADELKKAAAAKKK---------------ADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA--KKAEEA 1462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 290 KEKLQEKVKATNTQHAVEAIRPREESlaeKKYTSQGQGDLDSVLSQLNFTHTSEDLLQAEVTclEGSLESVSATCKQLSQ 369
Cdd:PTZ00121 1463 KKKAEEAKKADEAKKKAEEAKKADEA---KKKAEEAKKKADEAKKAAEAKKKADEAKKAEEA--KKADEAKKAEEAKKAD 1537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 370 ELMEKYEELKRMEAHNNE--YKAEIKKLKEQILQGEQSYSSALEgmKMEISHLTQELHQRDITIASTKGSSSDMEKRLRA 447
Cdd:PTZ00121 1538 EAKKAEEKKKADELKKAEelKKAEEKKKAEEAKKAEEDKNMALR--KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA 1615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 448 EMQ--KAED--KAVEHKEILDQLESLKLENRHLSEMVMKLE--LGLHEAKEISLADLQENYIEALNKLVSENQQLQKDLM 521
Cdd:PTZ00121 1616 EEAkiKAEElkKAEEEKKKVEQLKKKEAEEKKKAEELKKAEeeNKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALK 1695
|
490 500 510
....*....|....*....|....*....|...
gi 530375321 522 NTKSQLEISTQMCKKQNDRIFKPTHSRTTEFKN 554
Cdd:PTZ00121 1696 KEAEEAKKAEELKKKEAEEKKKAEELKKAEEEN 1728
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
54-424 |
8.68e-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: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 54 LKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEY-------KQELKKLHEELCILKRSYEKLQKKQMREFR 126
Cdd:TIGR00606 250 LKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMekvfqgtDEQLNDLYHNHQRTVREKERELVDCQRELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 127 GNTKNHR-------EDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQK----- 194
Cdd:TIGR00606 330 KLNKERRllnqektELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEdeakt 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 195 -------LESVELSSQSEIQHLSSKLERANDTIcanELEIERLTMRVNDLvgtsMTVLQEQQQKEEKLRESEKLLEALQE 267
Cdd:TIGR00606 410 aaqlcadLQSKERLKQEQADEIRDEKKGLGRTI---ELKKEILEKKQEEL----KFVIKELQQLEGSSDRILELDQELRK 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 268 EKRELKAALQS---QENLIHEARIQKEKLQEKVKATNTQHAVEAIRPREESLAEKKYTSQGQGDLDSVLSQLNFTHTSED 344
Cdd:TIGR00606 483 AERELSKAEKNsltETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDEL 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375321 345 LLQA----EVTCLEGSLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQ---------GEQSYSSALE 411
Cdd:TIGR00606 563 TSLLgyfpNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSyedklfdvcGSQDEESDLE 642
|
410
....*....|...
gi 530375321 412 GMKMEISHLTQEL 424
Cdd:TIGR00606 643 RLKEEIEKSSKQR 655
|
|
| |
