|
Name |
Accession |
Description |
Interval |
E-value |
| CUT |
pfam02376 |
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ... |
1132-1209 |
1.24e-29 |
|
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.
Pssm-ID: 460543 Cd Length: 78 Bit Score: 113.07 E-value: 1.24e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528492582 1132 MSAELDTYVITKKVKEVLTDNNLGQRLFGESILGLTQGSVSDLLARPKPWHKLSLKGREpFVRMQLWLSDPRNVEKLM 1209
Cdd:pfam02376 1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERMEI 77
|
|
| CUT |
pfam02376 |
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ... |
978-1046 |
5.44e-27 |
|
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.
Pssm-ID: 460543 Cd Length: 78 Bit Score: 105.37 E-value: 5.44e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528492582 978 MYQEVDTVDLTQQVKEKLAKNGICQRIFGEKVLGLSQGSVSDMLSRPKHWSKLTQKGREpFIRMQLWLN 1046
Cdd:pfam02376 1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLS 68
|
|
| CUT |
pfam02376 |
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ... |
580-656 |
5.78e-26 |
|
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.
Pssm-ID: 460543 Cd Length: 78 Bit Score: 102.29 E-value: 5.78e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528492582 580 EGEEMDTAEIARQVKEQLIKHNIGQRVFGHYVLGLSQGSVSEILARPKPWSKLTIRGKEpFHKMKHFLSDEQNILAL 656
Cdd:pfam02376 1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
|
|
| Homeodomain |
pfam00046 |
Homeodomain; |
1270-1326 |
2.97e-16 |
|
Homeodomain;
Pssm-ID: 459649 [Multi-domain] Cd Length: 57 Bit Score: 74.07 E-value: 2.97e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 528492582 1270 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELASQLNLKTSTVINWFHNYRSRIRR 1326
Cdd:pfam00046 1 RRKRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
58-363 |
1.13e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.60 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 58 EDLRKQIAPLLKgfQAEI----DALSKRSKESEAAFLSVYKRlidvpdpvsalEAAQQLQVTVRKMHDLETENQRLKDTL 133
Cdd:COG1196 196 GELERQLEPLER--QAEKaeryRELKEELKELEAELLLLKLR-----------ELEAELEELEAELEELEAELEELEAEL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 134 QEYEREISEVKNQevtIKALKEKLEQYERSLQAKNTEEAVEPNLDSSEREERQSKGENLpnnyaDKESQPEQSQESRTED 213
Cdd:COG1196 263 AELEAELEELRLE---LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL-----EELEEELAELEEELEE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 214 SDVKTQSLQTALEATQAELHELKtkyDEESTAKANEIEAVMTDLERANQRAETAEREAGTLREQLTSAGKTMQSSNQIQN 293
Cdd:COG1196 335 LEEELEELEEELEEAEEELEEAE---AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 294 APEMDKSLEAELGAKEREVERLAEDVQRLQASLAQLSETSTNQISQLEQQLSSKEALLKQLEEKLQDQSD 363
Cdd:COG1196 412 LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
|
| homeodomain |
cd00086 |
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ... |
1270-1327 |
7.24e-14 |
|
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic developmental processes; may bind to DNA as monomers or as homo- and/or heterodimers, in a sequence-specific manner.
Pssm-ID: 238039 [Multi-domain] Cd Length: 59 Bit Score: 67.27 E-value: 7.24e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 528492582 1270 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELASQLNLKTSTVINWFHNYRSRIRRE 1327
Cdd:cd00086 1 RRKRTRFTPEQLEELEKEFEKNPYPSREEREELAKELGLTERQVKIWFQNRRAKLKRS 58
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
16-371 |
9.96e-14 |
|
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: 76.63 E-value: 9.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 16 DLQQLQKELDATATALANRQDESEQSRKKLIDQSREFKkntpeDLRKQIAPLLKGFQ---AEIDALSKRSKESEAAFLSV 92
Cdd:TIGR02168 692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQIS-----ALRKDLARLEAEVEqleERIAQLSKELTELEAEIEEL 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 93 YKRLIdvpdpvsalEAAQQLQVTVRKMHDLETENQRLKDTLQEYEREISEVKNQevtIKALKEKLeqyersLQAKNTEEA 172
Cdd:TIGR02168 767 EERLE---------EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE---LTLLNEEA------ANLRERLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 173 VEPNLDSSER--EERQSKGENLPNNYADKESQPEQSQESRTEDSDvKTQSLQTALEATQAELHELKTKYDEEStAKANEI 250
Cdd:TIGR02168 829 LERRIAATERrlEDLEEQIEELSEDIESLAAEIEELEELIEELES-ELEALLNERASLEEALALLRSELEELS-EELREL 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 251 EAVMTDLERANQRAETaerEAGTLREQLTSAgkTMQSSNQIQNAPEMDKSLEAELGAKEREVE----RLAEDVQRLQASL 326
Cdd:TIGR02168 907 ESKRSELRRELEELRE---KLAQLELRLEGL--EVRIDNLQERLSEEYSLTLEEAEALENKIEddeeEARRRLKRLENKI 981
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 528492582 327 AQLSETSTNQISQLEQQLSSKEALLKQLEEKLQDQSDYEEIKREL 371
Cdd:TIGR02168 982 KELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| HOX |
smart00389 |
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ... |
1270-1325 |
3.32e-13 |
|
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key developmental processes
Pssm-ID: 197696 [Multi-domain] Cd Length: 57 Bit Score: 65.35 E-value: 3.32e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 528492582 1270 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELASQLNLKTSTVINWFHNYRSRIR 1325
Cdd:smart00389 2 RRKRTSFTPEQLEELEKEFQKNPYPSREEREELAKKLGLSERQVKVWFQNRRAKWK 57
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
107-389 |
5.84e-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: 73.94 E-value: 5.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 107 EAA------QQLQVTVRKMHDLETENQRLKDTLQEYEREISEVKNQ-EVTIK--ALKEKLEQYERSLQAKNTEEAVEpNL 177
Cdd:TIGR02168 163 EAAgiskykERRKETERKLERTRENLDRLEDILNELERQLKSLERQaEKAERykELKAELRELELALLVLRLEELRE-EL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 178 DS--SEREERQSKGENLPNNYADKESQPEQSQESRTEDSDvKTQSLQTALEATQAELHELKTK---YDEESTAKANEIEA 252
Cdd:TIGR02168 242 EElqEELKEAEEELEELTAELQELEEKLEELRLEVSELEE-EIEELQKELYALANEISRLEQQkqiLRERLANLERQLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 253 VMTDLERANQRAETAEREAGTLREQLTSAgktmqsSNQIQNAPEMDKSLEAELGAKEREVERLAEDVQRLQASLAQLSE- 331
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEEL------KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELq 394
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528492582 332 --TSTNQISQLEQQLSSKEALLKQLEEKLQDQ------SDYEEIKRELCTLKSVEHNSSDHHSSAQ 389
Cdd:TIGR02168 395 iaSLNNEIERLEARLERLEDRRERLQQEIEELlkkleeAELKELQAELEELEEELEELQEELERLE 460
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
18-371 |
1.80e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.40 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 18 QQLQKELDATATALANRQD---ESEQSRKKLIDQSRE-----FKKNTPEDLRKQIAPL-LKGFQAEIDALSKRSKESEAA 88
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDilnELERQLKSLERQAEKaerykELKAELRELELALLVLrLEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 89 FLSvYKRLIDvpdpvsalEAAQQLQVTVRKMHDLETENQRLKDTLQEYEREISEVKNQevtIKALKEKLEQYERSLQAKN 168
Cdd:TIGR02168 255 LEE-LTAELQ--------ELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ---KQILRERLANLERQLEELE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 169 TEEAVEPNLDSSEREERQSKGENLPNNYADKESQPEQSQESRTEDSDVKTQS--LQTALEATQAELHELKtkydEESTAK 246
Cdd:TIGR02168 323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLeeLEEQLETLRSKVAQLE----LQIASL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 247 ANEIEAVMTDLERANQRAETAEREAGTLREQLTSAGKtmqssnqiqnapemdKSLEAELGAKEREVERLAEDVQRLQASL 326
Cdd:TIGR02168 399 NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL---------------KELQAELEELEEELEELQEELERLEEAL 463
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 528492582 327 AQLS---ETSTNQISQLEQQLSSKEALLKQLEEKLQDQSDYEEIKREL 371
Cdd:TIGR02168 464 EELReelEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAL 511
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
133-363 |
7.46e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.47 E-value: 7.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 133 LQEYEREISEVKNQ----EVTIKALKEKLEQYERSLQAKNTEEAvepnlDSSEREERQSKGENLPNNYADKESQPEQSQE 208
Cdd:TIGR02168 672 ILERRREIEELEEKieelEEKIAELEKALAELRKELEELEEELE-----QLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 209 SRTedsdvktQSLQTALEATQAELHELKTKYDEESTAKAnEIEAVMTDLEranQRAETAEREAGTLREQLTSAGKTMQSS 288
Cdd:TIGR02168 747 ERI-------AQLSKELTELEAEIEELEERLEEAEEELA-EAEAEIEELE---AQIEQLKEELKALREALDELRAELTLL 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 289 NQ-IQNAPEMDKSLEAELGAKEREVERLA-------EDVQRLQASLAQLSETSTNQISQLE---QQLSSKEALLKQLEEK 357
Cdd:TIGR02168 816 NEeAANLRERLESLERRIAATERRLEDLEeqieelsEDIESLAAEIEELEELIEELESELEallNERASLEEALALLRSE 895
|
....*.
gi 528492582 358 LQDQSD 363
Cdd:TIGR02168 896 LEELSE 901
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
107-359 |
1.19e-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: 69.70 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 107 EAAQQLQVTVRKMHDLETENQRLKD-------TLQEYEREISEVKNQEVTIKALKEKLEQYERSLQAKNTEEAVEPNLDS 179
Cdd:TIGR02168 688 ELEEKIAELEKALAELRKELEELEEeleqlrkELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 180 SEREERQSKGENLPNNYADKESQPEQSQESrtedsdvkTQSLQTALEATQAELHELKtkydEESTAKANEIEAVMTDLER 259
Cdd:TIGR02168 768 ERLEEAEEELAEAEAEIEELEAQIEQLKEE--------LKALREALDELRAELTLLN----EEAANLRERLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 260 ANQRAETAEREAGTLREQLTSAGKTMQSSNQIQNApemdksLEAELGAKEREVERLAEDVQRLQASLAQLSET---STNQ 336
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEE------LESELEALLNERASLEEALALLRSELEELSEElreLESK 909
|
250 260
....*....|....*....|...
gi 528492582 337 ISQLEQQLSSKEALLKQLEEKLQ 359
Cdd:TIGR02168 910 RSELRRELEELREKLAQLELRLE 932
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
18-356 |
9.14e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 9.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 18 QQLQKELDATATALANRQDESEQSRKKLIDQSREFKKNTPEDLRKQIAPL---LKGFQAEIDALSKRSKESEAAFLSVYK 94
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELeaeLEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 95 RLIdvpdpvsalEAAQQLQVTVRKMHDLETENQRLKDTLQEYEREISEVKNQEVTIKALKEKLEQYERSLQAKNTEEAVE 174
Cdd:COG1196 296 ELA---------RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 175 PNLDSSEREERQSKGENLpnnyADKESQPEQSQESRTEDSDVKTQSLQTALEATQAELHELKTKYDEESTAKANEIEAVM 254
Cdd:COG1196 367 LLEAEAELAEAEEELEEL----AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 255 TDLERANQRAETAEREAGTLREQLTSAGKTMQSSNQIQNApemDKSLEAELGAKEREVERLAEDVQRLQASLAQLSETST 334
Cdd:COG1196 443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL---LEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
|
330 340
....*....|....*....|..
gi 528492582 335 NQISQLEQQLSSKEALLKQLEE 356
Cdd:COG1196 520 RGLAGAVAVLIGVEAAYEAALE 541
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
22-376 |
1.40e-10 |
|
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: 66.20 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 22 KELDATATALANRQDESEQSRKKLIDQSREFKKNtpEDLRKQIAPLLKgfqAEIDALSKRSKESEaaflsvyKRLIDVPD 101
Cdd:TIGR04523 78 KILEQQIKDLNDKLKKNKDKINKLNSDLSKINSE--IKNDKEQKNKLE---VELNKLEKQKKENK-------KNIDKFLT 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 102 PVSALEaaQQLQVTVRKMHDLETENQRLKDTLQEYEREISEVKNQEVTIKALKEKLEQYERSLQAKNTEEavepNLDSSE 181
Cdd:TIGR04523 146 EIKKKE--KELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKN----KSLESQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 182 REERQSKGENLPNNyadKESQPEQSQESRTEDSDVKTQSLQTA---------LEATQAELHELKTKYDEeSTAKANEIEA 252
Cdd:TIGR04523 220 ISELKKQNNQLKDN---IEKKQQEINEKTTEISNTQTQLNQLKdeqnkikkqLSEKQKELEQNNKKIKE-LEKQLNQLKS 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 253 VMTDLEraNQRAE-----------TAEREAGTLREQLTSAGKTMQSSNQ--------IQNAPEMDKSLEAELGAKEREVE 313
Cdd:TIGR04523 296 EISDLN--NQKEQdwnkelkselkNQEKKLEEIQNQISQNNKIISQLNEqisqlkkeLTNSESENSEKQRELEEKQNEIE 373
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528492582 314 RLAEDVQRLQASLAQLsetsTNQISQLEQQLSSKEALLKQLEEKLQD-QSDYEEIKRELCTLKS 376
Cdd:TIGR04523 374 KLKKENQSYKQEIKNL----ESQINDLESKIQNQEKLNQQKDEQIKKlQQEKELLEKEIERLKE 433
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
115-371 |
5.85e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.19 E-value: 5.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 115 TVRKMHDLEtEN-QRLKDTLQEYEREISEVKNQ-EVTIK--ALKEKLEQYERSLQAKNTEEAvepnldSSEREERQSKGE 190
Cdd:COG1196 177 AERKLEATE-ENlERLEDILGELERQLEPLERQaEKAERyrELKEELKELEAELLLLKLREL------EAELEELEAELE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 191 NLPNNYADKESQpEQSQESRTEDSDVKTQSLQTALEATQAELHELKTK----------YDEESTAKANEIEAVMTDLERA 260
Cdd:COG1196 250 ELEAELEELEAE-LAELEAELEELRLELEELELELEEAQAEEYELLAElarleqdiarLEERRRELEERLEELEEELAEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 261 NQRAETAEREAGTLREQLTSAGKTMQSS-NQIQNAPEMDKSLEAELGAKEREVERLAEDVQRLQASLAQLsetsTNQISQ 339
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAeAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL----AAQLEE 404
|
250 260 270
....*....|....*....|....*....|..
gi 528492582 340 LEQQLSSKEALLKQLEEKLQDQSDYEEIKREL 371
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEE 436
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
131-373 |
7.73e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.78 E-value: 7.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 131 DTLQEYEREISEVKNQevtIKALKEKLEQYERSLQAKNTEEAVEPNLDSSEREERQSKGENLPNNYADKESQPEQSQESR 210
Cdd:COG4913 235 DDLERAHEALEDAREQ---IELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAEL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 211 TEdsdvktqsLQTALEATQAELHELKTKYDEESTAKANEIEAvmtDLERANQRAETAEREAGTLREQLTSAGKTMQSSnq 290
Cdd:COG4913 312 ER--------LEARLDALREELDELEAQIRGNGGDRLEQLER---EIERLERELEERERRRARLEALLAALGLPLPAS-- 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 291 iqnapemdkslEAELGAKEREVERLAEDVQRLQASLAQLSETSTNQISQLEQQLSSKEALLKQLEEKlqdQSDY----EE 366
Cdd:COG4913 379 -----------AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR---KSNIparlLA 444
|
....*..
gi 528492582 367 IKRELCT 373
Cdd:COG4913 445 LRDALAE 451
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
123-371 |
8.79e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.80 E-value: 8.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 123 ETENqRLKDTLQEYERE---ISEVKNQevtIKALKEKLEQYERSLQAKNTEEAVEPNLDSSEREERQSKGENLPNNYADK 199
Cdd:COG1196 176 EAER-KLEATEENLERLediLGELERQ---LEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEEL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 200 ESQpEQSQESRTEDSDVKTQSLQTALEATQAELHELKTKYDEESTAKANEIEAVMTDLERANQRAETAEREAGTLREQLt 279
Cdd:COG1196 252 EAE-LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 280 sagktmqssNQIQNAPEMDKSLEAELGAKEREVERLAEDVQRLQASLAQLSETSTNQISQLEQQLSSKEALLKQLEEKLQ 359
Cdd:COG1196 330 ---------EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
250
....*....|..
gi 528492582 360 DQSDYEEIKREL 371
Cdd:COG1196 401 QLEELEEAEEAL 412
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
16-357 |
1.24e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.86 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 16 DLQQLQKELDATATALANRQDESEQSRKKL-----------IDQSREFKKNTPEDLRKQIAPLlKGFQAEIDALSKRSKE 84
Cdd:COG4717 96 ELEELEEELEELEAELEELREELEKLEKLLqllplyqeleaLEAELAELPERLEELEERLEEL-RELEEELEELEAELAE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 85 SEAAfLSVYKRLIDVPDPVSALEAAQQLQVTVRKMHDLETENQRLKDTLQEYEREISEVKNqEVTIKALKEKLEQYERSL 164
Cdd:COG4717 175 LQEE-LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN-ELEAAALEERLKEARLLL 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 165 QA---------------------------------------KNTEEAVEPNLDSSEREERQSKGENLP-NNYADKESQPE 204
Cdd:COG4717 253 LIaaallallglggsllsliltiagvlflvlgllallflllAREKASLGKEAEELQALPALEELEEEElEELLAALGLPP 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 205 QSQESRTEDSDVKTQSLQTALEATQAELHELKTKYDEES------TAKANEIEAVMTDLERANQRAETAEREAgTLREQL 278
Cdd:COG4717 333 DLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEiaallaEAGVEDEEELRAALEQAEEYQELKEELE-ELEEQL 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 279 TSAGKTMQSSNQIQNAPEMDK---SLEAELGAKEREVERLAEDVQRLQASLAQLSEtsTNQISQLEQQLSSKEALLKQLE 355
Cdd:COG4717 412 EELLGELEELLEALDEEELEEeleELEEELEELEEELEELREELAELEAELEQLEE--DGELAELLQELEELKAELRELA 489
|
..
gi 528492582 356 EK 357
Cdd:COG4717 490 EE 491
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
96-371 |
2.08e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 62.34 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 96 LIDVPDPVSALEAAQQLQVTVRkmhDLETENQRLK---------DTLQEYEREISEVKNQEVTIKALKEKLeqyerSLQA 166
Cdd:COG3206 60 LVEPQSSDVLLSGLSSLSASDS---PLETQIEILKsrpvlervvDKLNLDEDPLGEEASREAAIERLRKNL-----TVEP 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 167 KNTEEAVEPNLDSSEREerqsKGENLPNNYAD---KESQPEQSQESRTEDSDVKTQ--SLQTALEATQAELHELKTKY-- 239
Cdd:COG3206 132 VKGSNVIEISYTSPDPE----LAAAVANALAEaylEQNLELRREEARKALEFLEEQlpELRKELEEAEAALEEFRQKNgl 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 240 ---DEESTAKANEIEAVMTDLERANQRAETAEREAGTLREQLtsaGKTMQSSNQIQNAPEMDkSLEAELGAKEREVERLA 316
Cdd:COG3206 208 vdlSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL---GSGPDALPELLQSPVIQ-QLRAQLAELEAELAELS 283
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528492582 317 E-------DVQRLQASLAQLSE-----------TSTNQISQLEQQLSSKEALLKQLEEKLQD----QSDYEEIKREL 371
Cdd:COG3206 284 ArytpnhpDVIALRAQIAALRAqlqqeaqrilaSLEAELEALQAREASLQAQLAQLEARLAElpelEAELRRLEREV 360
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
32-418 |
5.36e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.31 E-value: 5.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 32 ANRQDESEQSRKKLIDQSREFKKntPEDLRKQIAPLLKGFQAEIDALSKRSKESEAAFLSVYKRLIDVPDPVSALEAAQQ 111
Cdd:PTZ00121 1449 AKKKAEEAKKAEEAKKKAEEAKK--ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE 1526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 112 LQVT--VRKMHDL-ETENQRLKDTLQEYE--REISEVKNQEVTIKALKEKLEQYERSLQAKNTEEAVEPNLDSSEREERQ 186
Cdd:PTZ00121 1527 AKKAeeAKKADEAkKAEEKKKADELKKAEelKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKK 1606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 187 SKGENLPN-----------NYADKESQPEQSQESRTEDSDVKTQSLQTALEATQAELHELKTKyDEESTAKANEIEAVMT 255
Cdd:PTZ00121 1607 MKAEEAKKaeeakikaeelKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK-AEEDKKKAEEAKKAEE 1685
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 256 DLERANQRAETAEREAGTLREQLTSAGKTMQSSNQIQNAPEMDKSLEAELGAKEREVERLAEDvqrlqaslAQLSETSTN 335
Cdd:PTZ00121 1686 DEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEE--------AKKDEEEKK 1757
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 336 QISQLEQQLSSK-EALLKQLEEKLQDQSDYEEIKRELCTLKSVEhNSSDHHSSAQDSSKplEMLLTGKDHSQLSESALKR 414
Cdd:PTZ00121 1758 KIAHLKKEEEKKaEEIRKEKEAVIEEELDEEDEKRRMEVDKKIK-DIFDNFANIIEGGK--EGNLVINDSKEMEDSAIKE 1834
|
....
gi 528492582 415 LANS 418
Cdd:PTZ00121 1835 VADS 1838
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
17-429 |
2.57e-08 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 58.91 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 17 LQQLQKELDATATALANRQDES--------EQSRKKLIDQSREFKKNTPEDLRKQIAPLLKGFqaeidalskRSKESEAA 88
Cdd:TIGR01612 698 LDDLKSKIDKEYDKIQNMETATvelhlsniENKKNELLDIIVEIKKHIHGEINKDLNKILEDF---------KNKEKELS 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 89 flsvykrlidvpdpvsaleaaqqlqvtvRKMHDLETENqrlkDTLQEYEREISEVKNQ---EVTIKALKEK--LEQYERS 163
Cdd:TIGR01612 769 ----------------------------NKINDYAKEK----DELNKYKSKISEIKNHyndQINIDNIKDEdaKQNYDKS 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 164 LQAKNTEEAVEPNLDSSEREERQSKGE---------NLPNNYADK-----ESQPEQSQESRTEDSDVKTQSLQTALEATQ 229
Cdd:TIGR01612 817 KEYIKTISIKEDEIFKIINEMKFMKDDflnkvdkfiNFENNCKEKidsehEQFAELTNKIKAEISDDKLNDYEKKFNDSK 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 230 AELHELkTKYDEESTAKANEIEAVMTDLERANQRAETAER---EAGTLREQLTSAGKTMQSSNQIQNA------------ 294
Cdd:TIGR01612 897 SLINEI-NKSIEEEYQNINTLKKVDEYIKICENTKESIEKfhnKQNILKEILNKNIDTIKESNLIEKSykdkfdntlidk 975
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 295 -PEMDKSL-EAELGAKEREVERLAEDVQRLQASLAqlsetsTNQISQLEQQLSSKEALLKQLEEKLQDQSdyeeikrelc 372
Cdd:TIGR01612 976 iNELDKAFkDASLNDYEAKNNELIKYFNDLKANLG------KNKENMLYHQFDEKEKATNDIEQKIEDAN---------- 1039
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 528492582 373 tlKSVEHNSSDHHSSAQDSSKPLEMLLtGKDHSQLSESALKRlANSDFT--GAVGRKLK 429
Cdd:TIGR01612 1040 --KNIPNIEIAIHTSIYNIIDEIEKEI-GKNIELLNKEILEE-AEINITnfNEIKEKLK 1094
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
134-360 |
2.75e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 58.49 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 134 QEYEREISEVKNQEV--TIKALKEKLEQYERSLQAKntEEAVEpnldssereerqskgenlpnNYadKESQPEQSQESRT 211
Cdd:COG3206 159 EAYLEQNLELRREEArkALEFLEEQLPELRKELEEA--EAALE--------------------EF--RQKNGLVDLSEEA 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 212 EDSDVKTQSLQTALEATQAELHELKTKYD---EESTAKANEIEAVMTD--LERANQRAETAEREAGTLREQLTSAGKTMQ 286
Cdd:COG3206 215 KLLLQQLSELESQLAEARAELAEAEARLAalrAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVI 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 287 S-SNQIQNA-PEMDKSLEAELGAKEREVERLAEDVQRLQASLAQLSETSTN------QISQLEQQLSSKEALLKQLEEKL 358
Cdd:COG3206 295 AlRAQIAALrAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAElpeleaELRRLEREVEVARELYESLLQRL 374
|
..
gi 528492582 359 QD 360
Cdd:COG3206 375 EE 376
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
142-382 |
3.46e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 3.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 142 EVKNQEVTIKALKEKLEQYERslqaknTEEAVEpnldssEREERQSKGENLPNNYADKESQPEQSQESRTEDSDVKTQSL 221
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLER------AHEALE------DAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 222 QTALEATQAELHELKTkydeestakanEIEAVMTDLERANQRAETAEREAGTLREQLTSAGktmqsSNQIQnapemdkSL 301
Cdd:COG4913 287 QRRLELLEAELEELRA-----------ELARLEAELERLEARLDALREELDELEAQIRGNG-----GDRLE-------QL 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 302 EAELGAKEREVERLAEDVQRLQASLAQLSETS-------TNQISQLEQQLSSKEALLKQLEEKL--------QDQSDYEE 366
Cdd:COG4913 344 EREIERLERELEERERRRARLEALLAALGLPLpasaeefAALRAEAAALLEALEEELEALEEALaeaeaalrDLRRELRE 423
|
250
....*....|....*.
gi 528492582 367 IKRElctLKSVEHNSS 382
Cdd:COG4913 424 LEAE---IASLERRKS 436
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
12-372 |
3.63e-08 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 58.55 E-value: 3.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 12 WKRFDLQQLQKELDATATALANRQDESEQSRKKLIdqsrEFKKNTPEDLRKQIapllkgfqaeidalskrskESEAAFLS 91
Cdd:COG5022 875 QRVELAERQLQELKIDVKSISSLKLVNLELESEII----ELKKSLSSDLIENL-------------------EFKTELIA 931
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 92 VYKRLIDVPDPVSALEAAQQLQVTVRKMHdleTENQRLKDTLQEYEREISEVKNQEVTIKALKEKLEQYERSLQAKNTEE 171
Cdd:COG5022 932 RLKKLLNNIDLEEGPSIEYVKLPELNKLH---EVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQY 1008
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 172 AVEPNlDSSEREERQSKGENLPNNYADKESQPEQSQeSRTEDSDVKTQSLQtALEATQAELHELKTKYDEESTAKANE-- 249
Cdd:COG5022 1009 GALQE-STKQLKELPVEVAELQSASKIISSESTELS-ILKPLQKLKGLLLL-ENNQLQARYKALKLRRENSLLDDKQLyq 1085
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 250 IEAVMTDLERAN-QRAETAEREAGTLREQLTSAGKTMQSSNQIQnapEMDKSLEAELGAKEREVERLAEDVQRLQASLAQ 328
Cdd:COG5022 1086 LESTENLLKTINvKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQ---EISKFLSQLVNTLEPVFQKLSVLQLELDGLFWE 1162
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 528492582 329 LSetstnqisqlEQQLSSKEALLKQLEEKLQDQSDYEEIKRELC 372
Cdd:COG5022 1163 AN----------LEALPSPPPFAALSEKRLYQSALYDEKSKLSS 1196
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
117-360 |
8.68e-08 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 57.14 E-value: 8.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 117 RKMHDLETENQRLKDT--LQEYEREiSEVKNQEVT---IKALKEKLEQYERSLQAKNteeavepnldsSEREERQSKGEN 191
Cdd:pfam10174 247 RNIRDLEDEVQMLKTNglLHTEDRE-EEIKQMEVYkshSKFMKNKIDQLKQELSKKE-----------SELLALQTKLET 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 192 LPNNYAD--------KESQPEQSQESRTEDSDVktQSLQTALEATQAELHElKTKY----DEESTAKANEIEAVMTDLER 259
Cdd:pfam10174 315 LTNQNSDckqhievlKESLTAKEQRAAILQTEV--DALRLRLEEKESFLNK-KTKQlqdlTEEKSTLAGEIRDLKDMLDV 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 260 ANQRAETAEREAGTLREQLTSAGKTMQSSNQIQNAPEMDKS--------LEAELGAKEREVERLAEDVQRLQASLAQLSE 331
Cdd:pfam10174 392 KERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSntdtalttLEEALSEKERIIERLKEQREREDRERLEELE 471
|
250 260
....*....|....*....|....*....
gi 528492582 332 TSTNQISQLEQQLSSKEALLKQLEEKLQD 360
Cdd:pfam10174 472 SLKKENKDLKEKVSALQPELTEKESSLID 500
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
17-371 |
1.84e-07 |
|
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: 56.13 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 17 LQQLQKELDATATALANR------QDESEQSRKKLIDQSREFKKNTPEDLRKQIAPLLKGFQAEIDALSKRSKESEAAFL 90
Cdd:TIGR00618 540 LETSEEDVYHQLTSERKQraslkeQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLR 619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 91 SVYKRLIDVPDPVSALEAAQQLQVTVRKMHDLETEnqRLKDTLQEYEREISEVKNQEVTIKALKEKLEQYERSLQAKNTE 170
Cdd:TIGR00618 620 KLQPEQDLQDVRLHLQQCSQELALKLTALHALQLT--LTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKE 697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 171 EAvePNLDSSEREERQSKGENlpnnyaDKESQpEQSQESRTEDSDVKtQSLQTALEATQAELHELKTKYDEESTAKANEI 250
Cdd:TIGR00618 698 ML--AQCQTLLRELETHIEEY------DREFN-EIENASSSLGSDLA-AREDALNQSLKELMHQARTVLKARTEAHFNNN 767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 251 EAVMTDLERANQRAETAEREAGTLREQLTSAGKTMQSSNQIQnapemdKSLEAELGAKEREVERLAedvQRLQASLAQLS 330
Cdd:TIGR00618 768 EEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIG------QEIPSDEDILNLQCETLV---QEEEQFLSRLE 838
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 528492582 331 ETSTNQIsQLEQQLSSKEALLKQLEEKLQDQSDYEEIKREL 371
Cdd:TIGR00618 839 EKSATLG-EITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
16-344 |
3.13e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 16 DLQQLQKELDATATALANRQDESEQSRKKLIDQSREFKKNTPEDLRKQIAPLLKGFQAEidALSKRSKESEaaflSVYKR 95
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLE--ELEKKAEEYE----KLKEK 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 96 LIDVPDPVSALEAaqqlqvTVRKMHDLETENQRLKDTLQEYEREISEVKNQEV-----TIKALKEKLEQ----YERSLQA 166
Cdd:PRK03918 534 LIKLKGEIKSLKK------ELEKLEELKKKLAELEKKLDELEEELAELLKELEelgfeSVEELEERLKElepfYNEYLEL 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 167 KNTEEAVEpnldssEREERQSKgenlpnnyadkesqpeqsQESRTEDSDVKTQSLQTALEATQAELHELKTKYDEES--- 243
Cdd:PRK03918 608 KDAEKELE------REEKELKK------------------LEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyee 663
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 244 -----TAKANEIEAVMTDLERANQRAETAEREAGTLREQLtsagktmqssNQIQNAPEMDKSLEAelgAKEReVERLAED 318
Cdd:PRK03918 664 lreeyLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL----------EEREKAKKELEKLEK---ALER-VEELREK 729
|
330 340
....*....|....*....|....*.
gi 528492582 319 VQRLQASLAqlsETSTNQISQLEQQL 344
Cdd:PRK03918 730 VKKYKALLK---ERALSKVGEIASEI 752
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
18-383 |
3.16e-07 |
|
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: 55.03 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 18 QQLQKELDATATALANRQDESEQSRKKLIDQSREFK--KNTPEDLRKQIAPLLKGFQAEIDALSKRSKESeaaflsvykr 95
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINnsNNKIKILEQQIKDLNDKLKKNKDKINKLNSDL---------- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 96 lidvpdpvsaLEAAQQLQVTVRKMHDLETENQRLKDTLQEYEREI----SEVKNQEVTIKALKEKLEQYERSLQAKNTEE 171
Cdd:TIGR04523 106 ----------SKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIdkflTEIKKKEKELEKLNNKYNDLKKQKEELENEL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 172 avepNLDSSEREERQSKGENLPNNYADKE---------SQPEQSQESRTEDSDVKTQSLQTALEATQAELHELKTKY--- 239
Cdd:TIGR04523 176 ----NLLEKEKLNIQKNIDKIKNKLLKLElllsnlkkkIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEIsnt 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 240 DEESTAKANEIEAVMTDLERANQRAETAEREAGTLREQLTSAGKTMQSSNQiQNAPEMDKSLEAELGAKEREVERLAEDV 319
Cdd:TIGR04523 252 QTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNN-QKEQDWNKELKSELKNQEKKLEEIQNQI 330
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528492582 320 QRLQASLAQLsetsTNQISQLEQQLSSKEA----LLKQLEEKlqdQSDYEEIKRE----LCTLKSVEHNSSD 383
Cdd:TIGR04523 331 SQNNKIISQL----NEQISQLKKELTNSESenseKQRELEEK---QNEIEKLKKEnqsyKQEIKNLESQIND 395
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
146-370 |
4.09e-07 |
|
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: 54.00 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 146 QEVTIKALKEKLEQYERSLQAKNTEeavepnLDSSEREERQSKGEnlpnnyadkesqpEQSQESRTEDSDVKTQSLQTAL 225
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKE------LAALKKEEKALLKQ-------------LAALERRIAALARRIRALEQEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 226 EATQAELHELKTKYdEESTAKANEIEAVMTDLERANQRAETAEREAGTLR-EQLTSAGKTMQSSNQIQNApemDKSLEAE 304
Cdd:COG4942 79 AALEAELAELEKEI-AELRAELEAQKEELAELLRALYRLGRQPPLALLLSpEDFLDAVRRLQYLKYLAPA---RREQAEE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528492582 305 LGAKEREVERLAEDVQRLQASLAQLSETSTNQISQLEQQLSSKEALLKQLEEKLQDQSDYEEIKRE 370
Cdd:COG4942 155 LRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
100-339 |
5.07e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.25 E-value: 5.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 100 PDPVSALEAAQQL-QVTVRkmHDLETENQRLKDTLQEYEREISEVKNQevtIKALKEKLEQYERSLQAKNTEEAVEPNLD 178
Cdd:COG3206 145 PDPELAAAVANALaEAYLE--QNLELRREEARKALEFLEEQLPELRKE---LEEAEAALEEFRQKNGLVDLSEEAKLLLQ 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 179 -----SSEREERQSKGENLPNNYADKESQPEQSQESRTEDS-DVKTQSLQTALEATQAELHELKTKYDEES---TAKANE 249
Cdd:COG3206 220 qlselESQLAEARAELAEAEARLAALRAQLGSGPDALPELLqSPVIQQLRAQLAELEAELAELSARYTPNHpdvIALRAQ 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 250 IEAVMTDLERANQRA-ETAEREAGTLREQLTSAGKTMQS-SNQIQNAPEmdksLEAELGAKEREVERLAEDVQRLQASLA 327
Cdd:COG3206 300 IAALRAQLQQEAQRIlASLEAELEALQAREASLQAQLAQlEARLAELPE----LEAELRRLEREVEVARELYESLLQRLE 375
|
250
....*....|..
gi 528492582 328 QLSETSTNQISQ 339
Cdd:COG3206 376 EARLAEALTVGN 387
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
102-333 |
5.60e-07 |
|
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: 53.61 E-value: 5.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 102 PVSALEAAQQLQVTVRKMHDLETENQRLKDTLQEYEREI----SEVKNQEVTIKALKEKLEQYERSLQAKNTE----EAV 173
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEkallKQLAALERRIAALARRIRALEQELAALEAElaelEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 174 EPNLDSSEREERQSKGENLPNNYADKESQPEQ---SQESrTEDSDVKTQSLQTALEATQAELHELKtkydeestAKANEI 250
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQPPLAlllSPED-FLDAVRRLQYLKYLAPARREQAEELR--------ADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 251 EAVMTDLERANQRAETAEREAGTLREQLTSAGKTMQSsnQIQNAPEMDKSLEAELGAKEREVERLAEDVQRLQASLAQLS 330
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQK--LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
...
gi 528492582 331 ETS 333
Cdd:COG4942 241 ERT 243
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
16-370 |
6.30e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.38 E-value: 6.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 16 DLQQLQKELDATATALANRQDESEQSRKKLIDQSREFKKNTPEDLRKQIAPLLKGFQAE--IDALSKRSKESEAAFLSVY 93
Cdd:PTZ00121 1319 EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKkkADAAKKKAEEKKKADEAKK 1398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 94 KRLIDV--PDPVSALEAAQQLQVTVRKMHDLETENQRLKDTLQEYEREISEVKNQEVTIKA--LKEKLEQYERSLQAKN- 168
Cdd:PTZ00121 1399 KAEEDKkkADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAeeAKKKAEEAKKADEAKKk 1478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 169 TEEAVEPNLDSSEREERQSKGENLPNnyadKESQPEQSQESRTEDSDVKTQSLQTALEATQAE---LHELKTKYDE---- 241
Cdd:PTZ00121 1479 AEEAKKADEAKKKAEEAKKKADEAKK----AAEAKKKADEAKKAEEAKKADEAKKAEEAKKADeakKAEEKKKADElkka 1554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 242 ESTAKANEIEAVmTDLERANQRAETAEREAGTLR---EQLTSAGKTMQSSNQIQNAPEMDKSLEAELGA----KEREVER 314
Cdd:PTZ00121 1555 EELKKAEEKKKA-EEAKKAEEDKNMALRKAEEAKkaeEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAeelkKAEEEKK 1633
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 528492582 315 LAEDVQRLQASLAQLSEtstnQISQLEQQLSSKEALLKQLEEklQDQSDYEEIKRE 370
Cdd:PTZ00121 1634 KVEQLKKKEAEEKKKAE----ELKKAEEENKIKAAEEAKKAE--EDKKKAEEAKKA 1683
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
67-371 |
6.92e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.19 E-value: 6.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 67 LLKGFQAEIDALSKRSKESEA-------------AFLSVYKRLIDVPDPVSALEAA-QQLQVTVRKMHDLETENQR---- 128
Cdd:PRK04863 787 RIEQLRAEREELAERYATLSFdvqklqrlhqafsRFIGSHLAVAFEADPEAELRQLnRRRVELERALADHESQEQQqrsq 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 129 ---LKDTLQEYEREISEVK--NQEVTIKALKEKLEQYERSLQAK-------NTEEAVEPNLdSSEREErqskgenlPNNY 196
Cdd:PRK04863 867 leqAKEGLSALNRLLPRLNllADETLADRVEEIREQLDEAEEAKrfvqqhgNALAQLEPIV-SVLQSD--------PEQF 937
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 197 ADKESQPEQSQESRtedSDVKTQSLqtALeatqAELHELKTKYDEESTAKANEIEAVMTDLERanQRAETAEREAGTLRE 276
Cdd:PRK04863 938 EQLKQDYQQAQQTQ---RDAKQQAF--AL----TEVVQRRAHFSYEDAAEMLAKNSDLNEKLR--QRLEQAEQERTRARE 1006
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 277 QLTSAGKTMQSSNQ--------IQNAPEMDKSLEAELG-----AKEREVERLAEDVQRLQAslaQLSETSTnQISQLEQQ 343
Cdd:PRK04863 1007 QLRQAQAQLAQYNQvlaslkssYDAKRQMLQELKQELQdlgvpADSGAEERARARRDELHA---RLSANRS-RRNQLEKQ 1082
|
330 340
....*....|....*....|....*....
gi 528492582 344 LSSKEALLKQLEEKLQD-QSDYEEIKREL 371
Cdd:PRK04863 1083 LTFCEAEMDNLTKKLRKlERDYHEMREQV 1111
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
12-414 |
8.32e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.99 E-value: 8.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 12 WKRFDLQQLQKeldatatalaNRQDESEQSRKKLIDQSREFKKNTPEDLRKQIAPLLKGFQAEIDALSKRSKESEAAFLS 91
Cdd:PTZ00121 1076 YKDFDFDAKED----------NRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEA 1145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 92 VYKRLIDVPDPVSALEAAQQLQVTVRKMHDLETENQRLKDTLQEYE--REISEVKNQEVTIKALKEKLEQYERSLQAKNT 169
Cdd:PTZ00121 1146 RKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEelRKAEDARKAEAARKAEEERKAEEARKAEDAKK 1225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 170 EEAVEPNLDSSEREERQSKGENLPNN------------YADKESQPEQSQESRTEDSDVKTQSLQTALEATQAE----LH 233
Cdd:PTZ00121 1226 AEAVKKAEEAKKDAEEAKKAEEERNNeeirkfeearmaHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEekkkAD 1305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 234 ELKTKYDEEStaKANEI----EAVMTDLERANQRAETAEREAGTLREQLTSAGKTMQSSNQIQNAPEMDKSleaELGAKE 309
Cdd:PTZ00121 1306 EAKKKAEEAK--KADEAkkkaEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKE---EAKKKA 1380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 310 REVERLAEDVQRlqaslAQLSETSTNQISQLEQQLSSKEALLKQLEE---KLQDQSDYEEIKRelctlKSVEHNSSDHHS 386
Cdd:PTZ00121 1381 DAAKKKAEEKKK-----ADEAKKKAEEDKKKADELKKAAAAKKKADEakkKAEEKKKADEAKK-----KAEEAKKADEAK 1450
|
410 420
....*....|....*....|....*...
gi 528492582 387 SAQDSSKPLEMLLTGKDHSQLSESALKR 414
Cdd:PTZ00121 1451 KKAEEAKKAEEAKKKAEEAKKADEAKKK 1478
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
17-437 |
1.09e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.58 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 17 LQQLQKELDATATALANRQDESEQSRKKLIDQSREFKKNTPEDLRKQIAPLLKGFQAEIDALSKRSKESEAAFLSVYKRL 96
Cdd:pfam15921 222 ISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQL 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 97 IDVPDpvsalEAAQQLQVTVRKMHDLETENQRLKDTLQEYEReisevknqevtikALKEKLEQYERSLQAKNTE--EAve 174
Cdd:pfam15921 302 EIIQE-----QARNQNSMYMRQLSDLESTVSQLRSELREAKR-------------MYEDKIEELEKQLVLANSEltEA-- 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 175 pnldSSEREERQSKGENLPNNYA---------DKESQPEQSQESRTEDSDVktqslqtaleATQAELHELKTKYDEESTa 245
Cdd:pfam15921 362 ----RTERDQFSQESGNLDDQLQklladlhkrEKELSLEKEQNKRLWDRDT----------GNSITIDHLRRELDDRNM- 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 246 KANEIEAVMTDLERANQraETAEREAGTLREQLTSAGKTMQSSNQIQNAPEMDKSLEAELGAKEREVERLAEDVQRLQAS 325
Cdd:pfam15921 427 EVQRLEALLKAMKSECQ--GQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTAS 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 326 LAQLS---ETSTNQISQLEQqlsskeallkQLEEKLQdqsdyeeikrELCTLKsvehNSSDHHSSAQDSSKPLEMLLTGK 402
Cdd:pfam15921 505 LQEKEraiEATNAEITKLRS----------RVDLKLQ----------ELQHLK----NEGDHLRNVQTECEALKLQMAEK 560
|
410 420 430
....*....|....*....|....*....|....*.
gi 528492582 403 DhsQLSESALKRLAN-SDFTGAVGRKLKETTVENPQ 437
Cdd:pfam15921 561 D--KVIEILRQQIENmTQLVGQHGRTAGAMQVEKAQ 594
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
121-374 |
1.23e-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: 53.53 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 121 DLETENQRLKdtlqEYEREISEVKNQEVTIKALKEKLEQYeRSLQAKNTEeaVEPNLDSSEREERQSKGENLPNNYADKE 200
Cdd:TIGR02169 178 ELEEVEENIE----RLDLIIDEKRQQLERLRREREKAERY-QALLKEKRE--YEGYELLKEKEALERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 201 SQPEQSQESRTEdsdvktqsLQTALEATQAELHELKTKYDEESTAKANEIEAVMTDLERANQRAETAEREAgtLREQLTS 280
Cdd:TIGR02169 251 EELEKLTEEISE--------LEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEK--ERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 281 AGKTMQSSNQIQNAPEMDKSLEAELGAKEREVERLAEDVQRLQASLaqlsETSTNQISQLEQQLSSKEALLKQLEEKLQD 360
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL----EDLRAELEEVDKEFAETRDELKDYREKLEK 396
|
250
....*....|....*
gi 528492582 361 -QSDYEEIKRELCTL 374
Cdd:TIGR02169 397 lKREINELKRELDRL 411
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
123-358 |
1.37e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.12 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 123 ETENQRLKDTLQEYEREISEVKNQ-----------EVTIKALKEKLEQYERSLQAKNT-EEAVEpnlDSSER-EERQSKG 189
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEieryeeqreqaRETRDEADEVLEEHEERREELETlEAEIE---DLRETiAETERER 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 190 ENLPNNYADKESQPEQSQESRTE---DSDVKTQSlQTALEATQAELHELKTKYDEESTAKANEIEAVMTDLERANQRAET 266
Cdd:PRK02224 275 EELAEEVRDLRERLEELEEERDDllaEAGLDDAD-AEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADD 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 267 AEREAGTLREQLTSAGKTMQSS-NQIQNAPEMDKSLEAELGAKEREVERLAEDVQRLQASLAQLSETstnqISQLEQQLS 345
Cdd:PRK02224 354 LEERAEELREEAAELESELEEArEAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREE----RDELREREA 429
|
250
....*....|...
gi 528492582 346 SKEALLKQLEEKL 358
Cdd:PRK02224 430 ELEATLRTARERV 442
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
16-247 |
1.48e-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: 52.07 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 16 DLQQLQKELDATATALANRQDESEQSRKKLIDQSREFKKNTPE--DLRKQIAPL---LKGFQAEIDALSKRSKESEAAfl 90
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRirALEQELAALeaeLAELEKEIAELRAELEAQKEE-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 91 svYKRLIDV------PDPVSALEAAQQLQVTVRKMHDLETENQRLKDTLQEYEREISEvknqevtIKALKEKLEQYERSL 164
Cdd:COG4942 106 --LAELLRAlyrlgrQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE-------LAALRAELEAERAEL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 165 QAKNTEEAVEPNLDSSEREERQSKGENLPNNYADKESQPEQSQESRtedsdvktQSLQTALEATQAELHELKTKYDEEST 244
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA--------EELEALIARLEAEAAAAAERTPAAGF 248
|
...
gi 528492582 245 AKA 247
Cdd:COG4942 249 AAL 251
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
217-359 |
1.82e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.83 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 217 KTQSLQTALEATQAELHELKTKYDEESTAKANEIEAVMTDLERANQRAETAEREAGTLREQLTsagktmQSSNQIQNAPE 296
Cdd:COG4372 21 KTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE------ELNEQLQAAQA 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528492582 297 MDKSLEAELGAKEREVERLAEDVQRLQASLAQLSETSTN---QISQLEQQLSSKEALLKQLEEKLQ 359
Cdd:COG4372 95 ELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQleaQIAELQSEIAEREEELKELEEQLE 160
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
196-503 |
2.04e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 196 YADKESQPEQSQESRTEDsdvKTQSLQTALEATQAELHELKTKYDEestaKANEIEAVMTDLERANQRAETAEREAGTLR 275
Cdd:COG3883 13 FADPQIQAKQKELSELQA---ELEAAQAELDALQAELEELNEEYNE----LQAELEALQAEIDKLQAEIAEAEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 276 EQLTSAGKTMQSSNQIQNapemdkSLEAELGAKEreverLAEDVQRLQAsLAQLSETSTNQISQLEQQLSSKEALLKQLE 355
Cdd:COG3883 86 EELGERARALYRSGGSVS------YLDVLLGSES-----FSDFLDRLSA-LSKIADADADLLEELKADKAELEAKKAELE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 356 EKLQD----QSDYEEIKRELCTLKS-----VEHNSSDHHSSAQDSSKPLEMLLTGKDHSQLSESALKRLANSDFTGAVGR 426
Cdd:COG3883 154 AKLAElealKAELEAAKAELEAQQAeqealLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528492582 427 KLKETTVENPQRLPATPVPTTLQGSPPPPSPQLLMRTGTATSESAASANGTHPFSPTGIGPDFFTPGMASVGATFPP 503
Cdd:COG3883 234 AAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGA 310
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
128-376 |
2.75e-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: 52.38 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 128 RLKDTLQEYEREISEVKNQEVTIKALKEKLEQYERSLQAKNTEEavepnldSSEREERQSKGENLpnnyadkeSQPEQSQ 207
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDA-------SRKIGEIEKEIEQL--------EQEEEKL 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 208 ESRTEDSDVKTQSLQTALEATQAELHELKTKYdEESTAKANEIEAVMTDLER--ANQRAETAEREAGTLREQLTSAGKTM 285
Cdd:TIGR02169 736 KERLEELEEDLSSLEQEIENVKSELKELEARI-EELEEDLHKLEEALNDLEArlSHSRIPEIQAELSKLEEEVSRIEARL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 286 QSsnqiqnapemdksLEAELGAKEREVERLAEDVQRLQaslaqlsetstNQISQLEQQLSSKEALLKQLEEKLQD-QSDY 364
Cdd:TIGR02169 815 RE-------------IEQKLNRLTLEKEYLEKEIQELQ-----------EQRIDLKEQIKSIEKEIENLNGKKEElEEEL 870
|
250
....*....|..
gi 528492582 365 EEIKRELCTLKS 376
Cdd:TIGR02169 871 EELEAALRDLES 882
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
122-359 |
2.75e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.04 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 122 LETENQRLKDTLQEYEREISEVKNQEVTIKALKEKLEQYERSLQAKNTEEA---VEPNLDSSEREERQSKGENLPNNYAD 198
Cdd:pfam15921 470 LESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITklrSRVDLKLQELQHLKNEGDHLRNVQTE 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 199 KESQPEQ----------------------SQESRTEDS-DVKTQSLQTALEATQAELHELKTKYDEEStAKANEIEAVMT 255
Cdd:pfam15921 550 CEALKLQmaekdkvieilrqqienmtqlvGQHGRTAGAmQVEKAQLEKEINDRRLELQEFKILKDKKD-AKIRELEARVS 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 256 DLERANQRAETAEreagtlREQLTSAGKTMQSSNQIQNapemdksleaELGAKEREVERLAEDVQRLQASLAQLSETSTN 335
Cdd:pfam15921 629 DLELEKVKLVNAG------SERLRAVKDIKQERDQLLN----------EVKTSRNELNSLSEDYEVLKRNFRNKSEEMET 692
|
250 260
....*....|....*....|....
gi 528492582 336 QISQLEQQLSSKEALLKQLEEKLQ 359
Cdd:pfam15921 693 TTNKLKMQLKSAQSELEQTRNTLK 716
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
108-371 |
3.50e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.06 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 108 AAQQLQVTVRKMHDLETENQRLKDTLQEYEREISEVKNQevtIKALKEKLEQYERSLQAKNTEeavepnLDSSEREERQS 187
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEE---LEQARSELEQLEEELEELNEQ------LQAAQAELAQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 188 KgenlpnnyadKESQPEQSQESRTEDSDVKTQSLQTALEATQAELHELKTKYDEESTAKANEIEAVMTDLERANQRAETA 267
Cdd:COG4372 100 Q----------EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 268 EREAGTLREQLTSAGKTMQSSNQIQNAPEMDKSLEAELGAKEREVERLAEDVQRLQASLAQLSETSTNQISQLEQQLSSK 347
Cdd:COG4372 170 EQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKE 249
|
250 260
....*....|....*....|....
gi 528492582 348 EALLKQLEEKLQDQSDYEEIKREL 371
Cdd:COG4372 250 ELLEEVILKEIEELELAILVEKDT 273
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
17-371 |
6.03e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 6.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 17 LQQLQKELDATATALANRQDESEQSRKKLIDQSREFK-----KNTPEDLRKQIAPL---LKGFQAEIDALSKRSKESEAA 88
Cdd:PRK03918 195 IKEKEKELEEVLREINEISSELPELREELEKLEKEVKeleelKEEIEELEKELESLegsKRKLEEKIRELEERIEELKKE 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 89 FLSVYKRLIDV----PDPVSALEAAQQLQVTVRKMHDLETENQRLKDTLQEYEREISEVKNQEVTIKALKEKLEQYERSL 164
Cdd:PRK03918 275 IEELEEKVKELkelkEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 165 -------QAKNTEEAVEPNLDSSEREERQSKGENLPNNYADKESQPEQSQESRTEDSDVKTQ------SLQTALEA---- 227
Cdd:PRK03918 355 eeleerhELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGElkkeikELKKAIEElkka 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 228 -----------TQAELHELKTKYdeesTAKANEIEAVMTDLERANQRAETAEREAGTLREQLTSAGKTMQSSNQIQNAPE 296
Cdd:PRK03918 435 kgkcpvcgrelTEEHRKELLEEY----TAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEE 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 297 MDKSLEAE-LGAKEREVERLAEDVQRLQAslaqlsetstnQISQLEQQLSSKEAL---LKQLEEKLQD-QSDYEEIKREL 371
Cdd:PRK03918 511 KLKKYNLEeLEKKAEEYEKLKEKLIKLKG-----------EIKSLKKELEKLEELkkkLAELEKKLDElEEELAELLKEL 579
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
7-376 |
7.84e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 7.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 7 SMFQYWKRFDLQQLQKELDATATALANRQDESEQSRKKLIDQSREFKKNTPEdlrkqiaplLKGFQAEIDALSKRSKESE 86
Cdd:COG4717 45 AMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEE---------LEELEEELEELEAELEELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 87 AAfLSVYKRLIDVPDPVSALEAAQQlqvtvrKMHDLETENQRLKDTLQEYEREISEVKNQEVTIKALKEKLEQYERSLQA 166
Cdd:COG4717 116 EE-LEKLEKLLQLLPLYQELEALEA------ELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 167 KnTEEAVEPNLD-----SSEREERQSKGENLPNNYADKESQPEQSQESRTEDSDVK------------------------ 217
Cdd:COG4717 189 A-TEEELQDLAEeleelQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEErlkearlllliaaallallglggs 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 218 -------------------------TQSLQTALEATQAELHELKTKYDEESTAKANEIEAVMTDLERANQRAETAEREAG 272
Cdd:COG4717 268 llsliltiagvlflvlgllallfllLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 273 TLREQLTSAGKTMQSSNQIQNAPEMDKSLEA----------ELGAKEREVERLAEDVQRLQASLAQLSETSTNQIS---- 338
Cdd:COG4717 348 ELQELLREAEELEEELQLEELEQEIAALLAEagvedeeelrAALEQAEEYQELKEELEELEEQLEELLGELEELLEalde 427
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 528492582 339 -QLEQQLSSKEALLKQLEEKLQD-QSDYEEIKRELCTLKS 376
Cdd:COG4717 428 eELEEELEELEEELEELEEELEElREELAELEAELEQLEE 467
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
17-371 |
1.06e-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: 50.35 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 17 LQQLQKELDATATALANRQDESEQSRKK----------LIDQSREFKKNTPE-DLRKQIAPLLKGFQAEIDALSKRSKES 85
Cdd:TIGR00618 461 LQESAQSLKEREQQLQTKEQIHLQETRKkavvlarlleLQEEPCPLCGSCIHpNPARQDIDNPGPLTRRMQRGEQTYAQL 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 86 EAAFLSVYKRLIdvpdpvsalEAAQQLQVTVRKMHDLETENQRLKDTLQEYEREISEVKNQEVTIKALKEKLEQYERSLQ 165
Cdd:TIGR00618 541 ETSEEDVYHQLT---------SERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLA 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 166 AKNTEEAVEPNLDSSEREERQSKGeNLPNNYADKESQPEQSQESRTEDSDVKTQSLQTALEATQAELHELKTKYDEesta 245
Cdd:TIGR00618 612 CEQHALLRKLQPEQDLQDVRLHLQ-QCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQ---- 686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 246 kaNEIEAVMTDLERANQR------AETAEREAGTLREQLTSAGKTMQSS--------NQIQNA--PEMDKSLEAELGAKE 309
Cdd:TIGR00618 687 --SEKEQLTYWKEMLAQCqtllreLETHIEEYDREFNEIENASSSLGSDlaaredalNQSLKElmHQARTVLKARTEAHF 764
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528492582 310 REVERLAEDVQRLQaSLAQLSETSTNQISQLEQQLSSKEALLKQLEEKLQDQSDYEEIKREL 371
Cdd:TIGR00618 765 NNNEEVTAALQTGA-ELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCET 825
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
215-369 |
1.26e-05 |
|
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: 48.38 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 215 DVKTQSLQTALEATQAELHELKTKYDEESTAKAN---EIEAVMTDLERANQRAETAEREAGTLREQLTSAG--KTMQS-S 288
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAaktELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnKEYEAlQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 289 NQIQNAPEMDKSLEAELGAKEREVERLAEDVQRLQASLAQLSETSTNQISQLEQQLSSKEALLKQLEEKLQDQSD----- 363
Cdd:COG1579 96 KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAkippe 175
|
170
....*....|
gi 528492582 364 ----YEEIKR 369
Cdd:COG1579 176 llalYERIRK 185
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
16-366 |
1.46e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 16 DLQQLQKELDATATALANRQDESEQSRKKLIDQSREFKKNTPEDLRKQIAPL----------LKGFQAEIDALSKRSKES 85
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLereleererrRARLEALLAALGLPLPAS 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 86 EAAFLSVYKRLIDVPDPVSALEAAQQLQVTvrkmhDLETENQRLKDTLQEYEREISEVKNQEVTI-KALKEKLEQYERSL 164
Cdd:COG4913 379 AEEFAALRAEAAALLEALEEELEALEEALA-----EAEAALRDLRRELRELEAEIASLERRKSNIpARLLALRDALAEAL 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 165 QAKNTE-----EAVEPNLDSSERE---ER--QSKGENL---PNNYAD-------------------KESQPEQSQESRTE 212
Cdd:COG4913 454 GLDEAElpfvgELIEVRPEEERWRgaiERvlGGFALTLlvpPEHYAAalrwvnrlhlrgrlvyervRTGLPDPERPRLDP 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 213 DS-----DVKTQSLQTALEA------------TQAEL-------------------HELKTKYDEEST------------ 244
Cdd:COG4913 534 DSlagklDFKPHPFRAWLEAelgrrfdyvcvdSPEELrrhpraitragqvkgngtrHEKDDRRRIRSRyvlgfdnrakla 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 245 AKANEIEAVMTDLERANQRAETAEREAGTLREQLTSAGKTMQSSNQIQNAPemdkSLEAELGAKEREVERLAE---DVQR 321
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA----SAEREIAELEAELERLDAssdDLAA 689
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 528492582 322 LQASLAQL----------SETSTNQISQLEQQLSSKEALLKQLEEKLQDQSDYEE 366
Cdd:COG4913 690 LEEQLEELeaeleeleeeLDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR 744
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
105-320 |
1.62e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 105 ALEAAQQLQVTVRKMHDL---ETENQRLKDTLQEYEREISEVKNQEVTIKALKEKLEQYERSLqaknteeavepnldssE 181
Cdd:COG4913 266 AARERLAELEYLRAALRLwfaQRRLELLEAELEELRAELARLEAELERLEARLDALREELDEL----------------E 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 182 REERQSKG---ENLPNNYADKESQPEQSQESRTEDSDvKTQSLQTALEATQAELHELKTKYDEESTAKANEIEAVMTDLE 258
Cdd:COG4913 330 AQIRGNGGdrlEQLEREIERLERELEERERRRARLEA-LLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALA 408
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528492582 259 RANQRAETAEREAGTLREQLTSAGKtmQSSNQIQNAPEMDKSLEAELGAKEREVERLAEDVQ 320
Cdd:COG4913 409 EAEAALRDLRRELRELEAEIASLER--RKSNIPARLLALRDALAEALGLDEAELPFVGELIE 468
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
127-371 |
1.75e-05 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 47.72 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 127 QRLKDTLQEYEREISEVKNQevtIKALKEKLEQYERSLQAKNTE-EAVEPNLDSSErEERQSKGENLPNNY--ADKESQP 203
Cdd:pfam00261 4 QQIKEELDEAEERLKEAMKK---LEEAEKRAEKAEAEVAALNRRiQLLEEELERTE-ERLAEALEKLEEAEkaADESERG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 204 EQSQESRTEDSDVKTQSLQTALEATQAELHELKTKYdEESTAKANEIEAvmtDLERANQRAETAEREAGTLREQLTSAGK 283
Cdd:pfam00261 80 RKVLENRALKDEEKMEILEAQLKEAKEIAEEADRKY-EEVARKLVVVEG---DLERAEERAELAESKIVELEEELKVVGN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 284 TMQSSnQIQNAPEMDKSLEAELGAKEREvERLAEDVQRLQASlaqlsetstnqisqlEQQLSSKEALLKQLEEKLQDQ-S 362
Cdd:pfam00261 156 NLKSL-EASEEKASEREDKYEEQIRFLT-EKLKEAETRAEFA---------------ERSVQKLEKEVDRLEDELEAEkE 218
|
....*....
gi 528492582 363 DYEEIKREL 371
Cdd:pfam00261 219 KYKAISEEL 227
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
109-371 |
2.30e-05 |
|
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: 49.18 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 109 AQQLQVTVRKmhDLETENQRLKDTLQEYEREISEVKNQEV----TIKALKEKLEQYER-----SLQAKNTE----EAVEP 175
Cdd:COG3096 823 GGHLAVAFAP--DPEAELAALRQRRSELERELAQHRAQEQqlrqQLDQLKEQLQLLNKllpqaNLLADETLadrlEELRE 900
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 176 NLDSSEREER--QSKGEN---LPNNYADKESQPEQSQEsrtedsdvktqsLQTALEATQAELHELKTKYD--EE------ 242
Cdd:COG3096 901 ELDAAQEAQAfiQQHGKAlaqLEPLVAVLQSDPEQFEQ------------LQADYLQAKEQQRRLKQQIFalSEvvqrrp 968
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 243 --STAKANEIEAVMTDL-ERANQRAETAEREAGTLREQLTSAGKTMQSSNQI--------QNAPEMDKSLEAELG----- 306
Cdd:COG3096 969 hfSYEDAVGLLGENSDLnEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVlaslkssrDAKQQTLQELEQELEelgvq 1048
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528492582 307 AKEREVERLAEDVQRLQASLAQlsetSTNQISQLEQQLSSKEALLKQLEEKL-QDQSDYEEIKREL 371
Cdd:COG3096 1049 ADAEAEERARIRRDELHEELSQ----NRSRRSQLEKQLTRCEAEMDSLQKRLrKAERDYKQEREQV 1110
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
104-439 |
2.68e-05 |
|
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: 49.07 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 104 SALEAAQQLQVTVRKmhDLETENQRLKDTLQEYEREISEVKNQEVTIKALKEKLEQYERSLQaknteEAVEPNLDSSERE 183
Cdd:pfam12128 611 EALQSAREKQAAAEE--QLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKN-----KALAERKDSANER 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 184 ERQSKGE---NLPNNYADKESQPEQSQESRTE----------DSDVKTQSLQTALEATQ----AELHELKTKYDEESTAK 246
Cdd:pfam12128 684 LNSLEAQlkqLDKKHQAWLEEQKEQKREARTEkqaywqvvegALDAQLALLKAAIAARRsgakAELKALETWYKRDLASL 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 247 ANEiEAVMTDLERANQRAETAEREAGTLREQLTSAGKTMQSSNQIQNApemdksleaELGAKEREVERlaeDVQRLQASL 326
Cdd:pfam12128 764 GVD-PDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRP---------RLATQLSNIER---AISELQQQL 830
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 327 AQLSETSTNQISQLEQQLSSKEALLKQLEEKLQDQSDYEeikRELCTLKSVEHNSSDHHSSAQDSSKPLEMLLTgkdHSQ 406
Cdd:pfam12128 831 ARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEM---SKLATLKEDANSEQAQGSIGERLAQLEDLKLK---RDY 904
|
330 340 350
....*....|....*....|....*....|...
gi 528492582 407 LSESALKRlaNSDFTGAVGRKLKETTVENPQRL 439
Cdd:pfam12128 905 LSESVKKY--VEHFKNVIADHSGSGLAETWESL 935
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
28-374 |
3.02e-05 |
|
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: 48.35 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 28 ATALANRQDESEQSRKKLI------DQSREFKKNTPEDLRKQIAPLLKGFQAEIDALS---KRSKESEAAFLSVYKRLID 98
Cdd:pfam07888 29 AELLQNRLEECLQERAELLqaqeaaNRQREKEKERYKRDREQWERQRRELESRVAELKeelRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 99 VPDPVSA----------------LEAAQQLQVTVRKMHDLETENQRLKDTLqeyEREISEVKNQEVTIKALKEKLEQYER 162
Cdd:pfam07888 109 SSEELSEekdallaqraaheariRELEEDIKTLTQRVLERETELERMKERA---KKAGAQRKEEEAERKQLQAKLQQTEE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 163 SLQAKNTEEAVepnldssereerqskgenLPNNYADKESQPEQSQESRTEDSDVKTQSLQ--TALEATQAELHELKTKY- 239
Cdd:pfam07888 186 ELRSLSKEFQE------------------LRNSLAQRDTQVLQLQDTITTLTQKLTTAHRkeAENEALLEELRSLQERLn 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 240 --DEESTAKANEIEAVMTDLERANQRAETAEREAGTLREQLTSAGKTM--------QSSNQIQNAPEMDK----SLEAEL 305
Cdd:pfam07888 248 asERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALregrarwaQERETLQQSAEADKdrieKLSAEL 327
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 306 GAKEREVERLAEDVQRLQASLAQLSETSTNQISQLEQQLSSKEALLKQLE-EKLQDQSDYEEIKRELCTL 374
Cdd:pfam07888 328 QRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQkEKEQLQAEKQELLEYIRQL 397
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
133-344 |
3.29e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 133 LQEYEREISEVKNQEVTIKALKEKLEQYERSLQaknteeavepnldssereERQSKGENLpnnyadkesqpeqsqeSRTE 212
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQ------------------ERREALQRL----------------AEYS 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 213 DSDVKTQSLQTALEATQAELHELKTKYDEESTAKAnEIEAVMTDLERANQRAETAEREAGTLREQLTSAGKTMQSSNQIQ 292
Cdd:COG4913 658 WDEIDVASAEREIAELEAELERLDASSDDLAALEE-QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 528492582 293 NAPEMDKSLEAELGAKER-EVERLAEDVQRLQASLAQLSETSTNQISQLEQQL 344
Cdd:COG4913 737 EAAEDLARLELRALLEERfAAALGDAVERELRENLEERIDALRARLNRAEEEL 789
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
16-190 |
3.65e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 16 DLQQLQKELDATATALANRQDESEQSRKKLIDQSREFKKNTPEdlRKQIAPLLKGFQAEIDALSKRSKESEAAFLSVYKR 95
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEK--LEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 96 LIDVPDPVSALE-----AAQQLQVTVRKMHDLETENQRLKDTLQEYEREISEVKNQEV-----TIKALKEKLEQYERSLQ 165
Cdd:TIGR02168 381 LETLRSKVAQLElqiasLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELqaeleELEEELEELQEELERLE 460
|
170 180 190
....*....|....*....|....*....|
gi 528492582 166 A-----KNTEEAVEPNLDSSEREERQSKGE 190
Cdd:TIGR02168 461 EaleelREELEEAEQALDAAERELAQLQAR 490
|
|
| COG5576 |
COG5576 |
Homeodomain-containing transcription factor [Transcription]; |
1270-1327 |
3.69e-05 |
|
Homeodomain-containing transcription factor [Transcription];
Pssm-ID: 227863 [Multi-domain] Cd Length: 156 Bit Score: 45.51 E-value: 3.69e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 528492582 1270 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELASQLNLKTSTVINWFHNYRSRIRRE 1327
Cdd:COG5576 52 KSKRRRTTDEQLMVLEREFEINPYPSSITRIKLSLLLNMPPKSVQIWFQNKRAKEKKK 109
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
15-284 |
3.75e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 15 FDLQQLQKELDATATALANRQDESEQSRKKLIDQSREFkkntpEDLRKQiaplLKGFQAEIDALSKRSKESEAAFLSVYK 94
Cdd:COG4372 38 FELDKLQEELEQLREELEQAREELEQLEEELEQARSEL-----EQLEEE----LEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 95 RLIDVPDPVSALEAAQQLQVTVRKmhDLETENQRLKDTLQEYEREISEVKNQEVTIKALKEKLEQYERSLQAKNTEEAVE 174
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRK--QLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 175 PNLDSSEREERQSKGENLPNNYADKESQPEQSQESRTEDSDVKTQSLQTALEATQAELHELKTKYDEESTAKANEIEAVM 254
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270
....*....|....*....|....*....|
gi 528492582 255 TDLERANQRAETAEREAGTLREQLTSAGKT 284
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELK 296
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
225-370 |
4.18e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.85 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 225 LEAtQAELHELKTKYDEESTAKANEIEAVmtdLERANQRAETAEREAGTLREQltsagktmqssnqiqnapemdkslEAE 304
Cdd:PRK12704 60 LEA-KEEIHKLRNEFEKELRERRNELQKL---EKRLLQKEENLDRKLELLEKR------------------------EEE 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528492582 305 LGAKEREVERLAEDVQRLQASLAQLSEtstNQISQLEQ--QLSSKEA---LLKQLEEKLQDQS-----DYEEIKRE 370
Cdd:PRK12704 112 LEKKEKELEQKQQELEKKEEELEELIE---EQLQELERisGLTAEEAkeiLLEKVEEEARHEAavlikEIEEEAKE 184
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
17-358 |
4.78e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 17 LQQLQKELDATATALANRQD--ESEQSR-------KKLIDQSREFKkntpedlrkQIAPL-LKGFQAEIDALSKRSKESE 86
Cdd:PRK04863 385 AEAAEEEVDELKSQLADYQQalDVQQTRaiqyqqaVQALERAKQLC---------GLPDLtADNAEDWLEEFQAKEQEAT 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 87 AAFLSVYKRLIDVPDPVSALEAAQQLqvtVRKMHDlETENQRLKDTLQEYEREISEVKNQEVTIKALKEKLEQYERSLQA 166
Cdd:PRK04863 456 EELLSLEQKLSVAQAAHSQFEQAYQL---VRKIAG-EVSRSEAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQ 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 167 KNTEEAVepnldSSEREERQSKGENLPNNYADKESQPEQSQESRtedSDVKTQSLQTALEaTQAELHELKTKYdEESTAK 246
Cdd:PRK04863 532 QQRAERL-----LAEFCKRLGKNLDDEDELEQLQEELEARLESL---SESVSEARERRMA-LRQQLEQLQARI-QRLAAR 601
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 247 ANEIEAVMTDLERanqraetaereagtLREQltsAGKTMQSSNQIQNApeMDKSLEAELGAkEREVERLAEDVQRLQAsl 326
Cdd:PRK04863 602 APAWLAAQDALAR--------------LREQ---SGEEFEDSQDVTEY--MQQLLEREREL-TVERDELAARKQALDE-- 659
|
330 340 350
....*....|....*....|....*....|..
gi 528492582 327 aqlsetstnQISQLEQQLSSKEALLKQLEEKL 358
Cdd:PRK04863 660 ---------EIERLSQPGGSEDPRLNALAERF 682
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
13-231 |
5.81e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 5.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 13 KRFDLQQLQKELDATATALANRQDESEQSRKKLIDQSREFKKNTPE--DLRKQIAPLlkgfQAEIDALSKRSKEseaaFL 90
Cdd:COG3883 21 KQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEidKLQAEIAEA----EAEIEERREELGE----RA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 91 SVYKRLIDVPDPVSALEAAQQLQVTVRKMHDLETENQRLKDTLQEYEREISEVKNQE-------VTIKALKEKLEQYERS 163
Cdd:COG3883 93 RALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKaeleaklAELEALKAELEAAKAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528492582 164 LQAKNTEEAVEPNLDSSEREERQSKGENLPNNYADKESQPEQSQESRTEDSDVKTQSLQTALEATQAE 231
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
13-375 |
6.25e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 6.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 13 KRFDLQQLQKELDATATALAnrqdESEQSRKKLIDQSREfKKNTPEDLRKQIAPLLKGF---QAEIDALSKRSKESEAAF 89
Cdd:PRK02224 249 RREELETLEAEIEDLRETIA----ETEREREELAEEVRD-LRERLEELEEERDDLLAEAgldDADAEAVEARREELEDRD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 90 LSVYKRLIDVPdpVSALEAAQQLQVTVRKMHDLETENQRLKDTLQEYEreiSEVKNQEVTIKALKEKLEQYE---RSLQA 166
Cdd:PRK02224 324 EELRDRLEECR--VAAQAHNEEAESLREDADDLEERAEELREEAAELE---SELEEAREAVEDRREEIEELEeeiEELRE 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 167 KNTEEAVEPNLDSSEREERQSKGENLPNNYADKESQPEQSQESRTED-------------SDVKTQSLQTALEATQAELH 233
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAealleagkcpecgQPVEGSPHVETIEEDRERVE 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 234 ELktkyDEESTAKANEIEAVMTDLERANQRAEtAEREAGTLREQLTSAGKTMQssnQIQNAPEMDKSLEAELGAKEREVE 313
Cdd:PRK02224 479 EL----EAELEDLEEEVEEVEERLERAEDLVE-AEDRIERLEERREDLEELIA---ERRETIEEKRERAEELRERAAELE 550
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528492582 314 RLAEDVQRLQASLAQLSETSTNQISQLEQQLSSKEALLKQLEEKLQDQSDYEEIKRELCTLK 375
Cdd:PRK02224 551 AEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLR 612
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
14-357 |
6.70e-05 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 47.38 E-value: 6.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 14 RFDLQQLQKELDATATALANRQDESEQSRKKLID-QSREfkkntpEDLRK--QIAPLLKGfqaEIDAL---SKRSKESEA 87
Cdd:pfam05622 65 QKQLEQLQEENFRLETARDDYRIKCEELEKEVLElQHRN------EELTSlaEEAQALKD---EMDILresSDKVKKLEA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 88 AFLSVYKRLIDVPD---PVSALE--AAQQLQVTVrkmhDLETENQR---LKDTLQEYEREISEV--KNQEVTIKAlkEKL 157
Cdd:pfam05622 136 TVETYKKKLEDLGDlrrQVKLLEerNAEYMQRTL----QLEEELKKanaLRGQLETYKRQVQELhgKLSEESKKA--DKL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 158 EQYERSLQAKNteEAVEPNLDS--SEREERQSKGENLPNNYA--DKESQPEQSQESRTEDSDVKTQSLQTA-----LEAT 228
Cdd:pfam05622 210 EFEYKKLEEKL--EALQKEKERliIERDTLRETNEELRCAQLqqAELSQADALLSPSSDPGDNLAAEIMPAeirekLIRL 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 229 QAELHELKTKYDEESTAKANEIEAVMTDLERANQRAETAEREAGTLREQLTSAGKTMQSSNQIQNAPEMDKS-LEAELGA 307
Cdd:pfam05622 288 QHENKMLRLGQEGSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKAEDSSlLKQKLEE 367
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 528492582 308 KEREVERLAEDVQRLQASLAQLSETSTNQ----ISQLEQQLSSKEALLKQLEEK 357
Cdd:pfam05622 368 HLEKLHEAQSELQKKKEQIEELEPKQDSNlaqkIDELQEALRKKDEDMKAMEER 421
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
103-376 |
6.87e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.64 E-value: 6.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 103 VSALEAAQQLQVTVRKmhDLETENQRLKDTLQEYErEISEVKNQEVTIKALKEKLEQYERSLQAKnTEEAVEPNLDSSER 182
Cdd:PRK04863 299 RRQLAAEQYRLVEMAR--ELAELNEAESDLEQDYQ-AASDHLNLVQTALRQQEKIERYQADLEEL-EERLEEQNEVVEEA 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 183 EERQSKGENlpnnyadKESQPEQSQES-RTEDSDVKT----------------QSLQTA--------LEATQAE--LHEL 235
Cdd:PRK04863 375 DEQQEENEA-------RAEAAEEEVDElKSQLADYQQaldvqqtraiqyqqavQALERAkqlcglpdLTADNAEdwLEEF 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 236 KTKyDEESTAKANEIEAVMTDLERANQRAETA-----------EREAG--TLREQLTSAGKTMQSSNQIQnapemdkSLE 302
Cdd:PRK04863 448 QAK-EQEATEELLSLEQKLSVAQAAHSQFEQAyqlvrkiagevSRSEAwdVARELLRRLREQRHLAEQLQ-------QLR 519
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528492582 303 AELGAKEREVeRLAEDVQRLQASLAQLSETSTNQISQLEQQLSSKEALLKQLEEKL-QDQSDYEEIKRELCTLKS 376
Cdd:PRK04863 520 MRLSELEQRL-RQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVsEARERRMALRQQLEQLQA 593
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
228-375 |
8.69e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 47.16 E-value: 8.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 228 TQAELHELKTKYDEESTAKANEIEAVMTDLERANQ--RAETAEREAGTLREQLTSAGKTMQSSNQiqnapEMDKSLEAEl 305
Cdd:pfam06160 43 TQEKFEEWRKKWDDIVTKSLPDIEELLFEAEELNDkyRFKKAKKALDEIEELLDDIEEDIKQILE-----ELDELLESE- 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528492582 306 gAKER-EVERLAEDVQRLQASLAQLSETSTNQISQLEQQLSSKEALLKQLEEkLQDQSDYEEIKRELCTLK 375
Cdd:pfam06160 117 -EKNReEVEELKDKYRELRKTLLANRFSYGPAIDELEKQLAEIEEEFSQFEE-LTESGDYLEAREVLEKLE 185
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
13-341 |
9.00e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 9.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 13 KRFDLQQLQKELDATATALANRQDESEQSRKKLIDQSREFKkNTPEDLRKqIAPLLKGFQAEIDALSKRSKESEAAFLSV 92
Cdd:PRK02224 361 LREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFG-DAPVDLGN-AEDFLEELREERDELREREAELEATLRTA 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 93 YKRLidvpdpvsalEAAQQLqvtvRKMHDLETENQRLKD-----TLQEYEREISEVKNQEVTIKALKEKLEQ-YERSLQA 166
Cdd:PRK02224 439 RERV----------EEAEAL----LEAGKCPECGQPVEGsphveTIEEDRERVEELEAELEDLEEEVEEVEErLERAEDL 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 167 KNTEEAVEpnldsSEREERQSKGENLPNNYADKESQPEQSQESRTE------DSDVKTQSLQTALEATQAELHELKTkYD 240
Cdd:PRK02224 505 VEAEDRIE-----RLEERREDLEELIAERRETIEEKRERAEELRERaaeleaEAEEKREAAAEAEEEAEEAREEVAE-LN 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 241 EESTAKANEIEAVMTDLERANQRAEtAEREAGTLREQLTS-AGKTMQSSNQIQNAPEMDKSLEAEL-------------- 305
Cdd:PRK02224 579 SKLAELKERIESLERIRTLLAAIAD-AEDEIERLREKREAlAELNDERRERLAEKRERKRELEAEFdearieearedker 657
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528492582 306 --------------------------GAKEREVERLAEDVQRLQASLAQLS--ETSTNQISQLE 341
Cdd:PRK02224 658 aeeyleqveekldelreerddlqaeiGAVENELEELEELRERREALENRVEalEALYDEAEELE 721
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
106-376 |
9.84e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 46.87 E-value: 9.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 106 LEAAQQLQVTVRKMHDLETENQRLKDtLQEYEREISEV--KNQEVTIKALKEKLEQYERSLQAK--------NTEEAVEP 175
Cdd:COG5185 222 LEKAKEIINIEEALKGFQDPESELED-LAQTSDKLEKLveQNTDLRLEKLGENAESSKRLNENAnnlikqfeNTKEKIAE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 176 NLDSSEREERQSKGENLpnnyaDKESQPEQSQESRTEDSDVKTQSLQTALEATQAELHELKTKYDEESTAKANEIEavmt 255
Cdd:COG5185 301 YTKSIDIKKATESLEEQ-----LAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVE---- 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 256 dLERANQRAETAEREAGTLREQLTSAGKtmqssNQIQNAPEMDKSLEAELGAKEREVERLAEDVQRLQASLAQLSETSTN 335
Cdd:COG5185 372 -LSKSSEELDSFKDTIESTKESLDEIPQ-----NQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNE 445
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 528492582 336 QISQLEQQL-SSKEALLKQLEEKLQ-----DQSDYEEIKRELCTLKS 376
Cdd:COG5185 446 LISELNKVMrEADEESQSRLEEAYDeinrsVRSKKEDLNEELTQIES 492
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
119-371 |
9.99e-05 |
|
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: 47.27 E-value: 9.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 119 MHDLETENQRLKDTLQEYEREISEVKnqevtiKALKEKLEQYERSLQaKNTEEAVEPNLDSSEREERQSKGENLPNNYAD 198
Cdd:pfam02463 190 IDLEELKLQELKLKEQAKKALEYYQL------KEKLELEEEYLLYLD-YLKLNEERIDLLQELLRDEQEEIESSKQEIEK 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 199 KESQPEQSQESRTEDSDVK--TQSLQTALEATQAELHELKTKYDEESTAKANEIEAVMTDLERAnQRAETAEREAGTLRE 276
Cdd:pfam02463 263 EEEKLAQVLKENKEEEKEKklQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKA-EKELKKEKEEIEELE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 277 QLtsagKTMQSSNQIQNAPEMDKSLEAELGAKEREverlaedvQRLQASLAQLSETSTNQISQLEQQLSSKEALLKQLEE 356
Cdd:pfam02463 342 KE----LKELEIKREAEEEEEEELEKLQEKLEQLE--------EELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQL 409
|
250
....*....|....*
gi 528492582 357 KLQDQSDYEEIKREL 371
Cdd:pfam02463 410 LLELARQLEDLLKEE 424
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
72-355 |
1.14e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 46.21 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 72 QAEIDALSKRSKESEAAFLSVYKRLIDVPDPVSALEAaqQLQVTVRKMHDLETENQRLKDTLQEYEREISEVKNQEVTIK 151
Cdd:pfam19220 89 VARLAKLEAALREAEAAKEELRIELRDKTAQAEALER--QLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATAR 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 152 ALKEKLEQYERSLQAKNTEEAVEpnldssereerqskGENLPNNYADKESQPEQSQEsrtedsdvKTQSLQTALEATQAE 231
Cdd:pfam19220 167 ERLALLEQENRRLQALSEEQAAE--------------LAELTRRLAELETQLDATRA--------RLRALEGQLAAEQAE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 232 LHELKTKYDEESTAKANEIEAVMTDLERANQRAETAEREAGTLREQL----------------TSAGKTM---------- 285
Cdd:pfam19220 225 RERAEAQLEEAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLrdrdeairaaerrlkeASIERDTlerrlaglea 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 286 QSSNQIQNAPEMDKS-LEAE---------LGAKEREVERLAEDVQRLQASLAQLSETSTNQISQLEQQlssKEALLKQLE 355
Cdd:pfam19220 305 DLERRTQQFQEMQRArAELEeraemltkaLAAKDAALERAEERIASLSDRIAELTKRFEVERAALEQA---NRRLKEELQ 381
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
101-371 |
1.18e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.83 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 101 DPVSALEAAQQLQvTVRKMHDLETENQRLKDTLQEYEREISEVKNQEVTIKALKEKLEQYERSLQAKNTEEAvepNLDSS 180
Cdd:PRK11281 34 DLPTEADVQAQLD-ALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELE---ALKDD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 181 EREERQSKGENLPNnyadkeSQPEQSQESRTED--------SDVKTQ--SLQTALEATQAELHELKTKYDEESTAKAN-- 248
Cdd:PRK11281 110 NDEETRETLSTLSL------RQLESRLAQTLDQlqnaqndlAEYNSQlvSLQTQPERAQAALYANSQRLQQIRNLLKGgk 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 249 EIEAVMTDLERANQRAETAEREAGTLREQltsagKTMQSSNQIQnapemdksleaELGAKEREVerLAEDVQRLQASLAQ 328
Cdd:PRK11281 184 VGGKALRPSQRVLLQAEQALLNAQNDLQR-----KSLEGNTQLQ-----------DLLQKQRDY--LTARIQRLEHQLQL 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 528492582 329 LSET-STNQISQLEQQLssKEALLKQLEEKLQDQSdyeEIKREL 371
Cdd:PRK11281 246 LQEAiNSKRLTLSEKTV--QEAQSQDEAARIQANP---LVAQEL 284
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
13-360 |
1.20e-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: 46.71 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 13 KRFDlqQLQKELDATATALANRQDESE-QSRKK---LIDQSREFKKNTpeDLRKQIAPLLKGFQAEIDALSKrSKEseaa 88
Cdd:pfam01576 604 KKFD--QMLAEEKAISARYAEERDRAEaEAREKetrALSLARALEEAL--EAKEELERTNKQLRAEMEDLVS-SKD---- 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 89 flsvykrliDVPDPVSALEAAQQLqvtvrkmhdLETENQRLKDTLQEYEREISEVKNQ----EVTIKALKEkleQYERSL 164
Cdd:pfam01576 675 ---------DVGKNVHELERSKRA---------LEQQVEEMKTQLEELEDELQATEDAklrlEVNMQALKA---QFERDL 733
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 165 QAKntEEAVEP----------NLDSSEREERQSKG------ENLPNNYADKESQPEQSQESRtEDSDVKTQSLQTALEAT 228
Cdd:pfam01576 734 QAR--DEQGEEkrrqlvkqvrELEAELEDERKQRAqavaakKKLELDLKELEAQIDAANKGR-EEAVKQLKKLQAQMKDL 810
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 229 QAELHELKTKYDE------ESTAKANEIEAVMTDLERANQRAETAEREAGTLREQLTsagKTMQSSNQIQNAPEMDK--- 299
Cdd:pfam01576 811 QRELEEARASRDEilaqskESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELA---DEIASGASGKSALQDEKrrl 887
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528492582 300 -----SLEAELGAKEREVERLAEDVQRLQASLAQLSETSTNQISQLEQQLSSKEALLKQ---LEEKLQD 360
Cdd:pfam01576 888 eariaQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQnkeLKAKLQE 956
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
205-360 |
1.30e-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: 45.88 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 205 QSQESRTEDSDVKTQSLQTALEATQAELHELKTkydeESTAKANEIEAVMTDLERANQRAETAEREAGTLREQLTS---- 280
Cdd:pfam00529 57 QAALDSAEAQLAKAQAQVARLQAELDRLQALES----ELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARrrvl 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 281 AGKTMQSSNQIQNAPEMDKSLEAELGAKEREVERLAEDVQRLQASLAQLSEtstNQISQLEQQLSSKEALLKQLEEKLQD 360
Cdd:pfam00529 133 APIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVR---SELSGAQLQIAEAEAELKLAKLDLER 209
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
17-357 |
1.34e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 46.65 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 17 LQQLQkELDATATALANRQDESEQSRKKLIDqsrefKKNTPEDLRKQIAPLLK----------GFQAEIDALSKRSKESE 86
Cdd:pfam15921 530 LQELQ-HLKNEGDHLRNVQTECEALKLQMAE-----KDKVIEILRQQIENMTQlvgqhgrtagAMQVEKAQLEKEINDRR 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 87 AAfLSVYKRLIDVPDP-VSALEA-AQQLQVTVRKMHDLETENQR-LKDTLQEYEREISEVKNQEVTIKALKEKLEQYERS 163
Cdd:pfam15921 604 LE-LQEFKILKDKKDAkIRELEArVSDLELEKVKLVNAGSERLRaVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRN 682
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 164 LQAKNteeavepnldsserEERQSKGENLPNNYADKESQPEQsqesrtedsdvkTQSLQTALEATQAELHELKTKYDEES 243
Cdd:pfam15921 683 FRNKS--------------EEMETTTNKLKMQLKSAQSELEQ------------TRNTLKSMEGSDGHAMKVAMGMQKQI 736
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 244 TAKANEIEAVMTDLERANQRAETAEREAGTLREQLTSAGKTMQSSNQIQNapEMDKSLEAeLGAKEReveRLAEDVQRLQ 323
Cdd:pfam15921 737 TAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKN--KMAGELEV-LRSQER---RLKEKVANME 810
|
330 340 350
....*....|....*....|....*....|....*.
gi 528492582 324 ASL--AQLSETSTNQISQLEQQLSSKEALLKQLEEK 357
Cdd:pfam15921 811 VALdkASLQFAECQDIIQRQEQESVRLKLQHTLDVK 846
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
13-359 |
1.42e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 46.35 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 13 KRFDLQQLQKELDAtataLANRQDESEQSrkklIDQSREfkKNTPEDLRKQIapllkgFQAEIDALSKRSKESEAAFLSV 92
Cdd:pfam10174 301 KESELLALQTKLET----LTNQNSDCKQH----IEVLKE--SLTAKEQRAAI------LQTEVDALRLRLEEKESFLNKK 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 93 YKRLIDVPDPVSALEAA-----QQLQVTVRKMHDLETENQRLKDTLQEYEREISEVKN---------------------- 145
Cdd:pfam10174 365 TKQLQDLTEEKSTLAGEirdlkDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKErvkslqtdssntdtalttleea 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 146 ---QEVTIKALKEKLEQYERSL-----QAKNTEEAVEPNLDSSERE--ERQSKGENLPNNYADKESQP----------EQ 205
Cdd:pfam10174 445 lseKERIIERLKEQREREDRERleeleSLKKENKDLKEKVSALQPEltEKESSLIDLKEHASSLASSGlkkdsklkslEI 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 206 SQESRTEDSDVKTQSLQTALEATQAE------------LHELKTKYDEESTAKANEIEAVMTDLERANQRAETAEREAGT 273
Cdd:pfam10174 525 AVEQKKEECSKLENQLKKAHNAEEAVrtnpeindrirlLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAE 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 274 LREQLTSAGK--TMQSSNQIQNAPEMDKSLEAELGAKEREVERLAEDVQRLQAS--LAQLSET-----STNQ-ISQLEQQ 343
Cdd:pfam10174 605 LESLTLRQMKeqNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEelMGALEKTrqeldATKArLSSTQQS 684
|
410 420
....*....|....*....|....
gi 528492582 344 LSSKEALL--------KQLEEKLQ 359
Cdd:pfam10174 685 LAEKDGHLtnlraerrKQLEEILE 708
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
42-375 |
1.44e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.43 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 42 RKKLIDQSREFK---------KNTPEDLRKQIAPL------LKGFQAEIDALSKRSKESEAAfLSVYKRLIDVPDPV--S 104
Cdd:PRK01156 151 RKKILDEILEINslernydklKDVIDMLRAEISNIdyleekLKSSNLELENIKKQIADDEKS-HSITLKEIERLSIEynN 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 105 ALEAAQQLQVTVRKMHDLETENQRLKDTLQEYEREISEVKNQEVTIKALKEKLEQYERSLQAKNTEEAVE---------- 174
Cdd:PRK01156 230 AMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDyfkykndien 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 175 -----PNLDS--SEREERQSKGENLPNNYADKESQPEQSQESRTEDSDVKT-----QSLQTALEATQAELHELKTKYDEE 242
Cdd:PRK01156 310 kkqilSNIDAeiNKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGyemdyNSYLKSIESLKKKIEEYSKNIERM 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 243 ST----------AKANEIEAVMTDLERANQRAETA----EREAGTLREQLTSAGKTM------------------QSSNQ 290
Cdd:PRK01156 390 SAfiseilkiqeIDPDAIKKELNEINVKLQDISSKvsslNQRIRALRENLDELSRNMemlngqsvcpvcgttlgeEKSNH 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 291 IQNAPEMDKS-LEAELGAKEREVERLAEDVQRLQASLAQLSETSTNQISQLEQQLSSKEALLKQLEEKLQDQSD----YE 365
Cdd:PRK01156 470 IINHYNEKKSrLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDkhdkYE 549
|
410
....*....|
gi 528492582 366 EIKRELCTLK 375
Cdd:PRK01156 550 EIKNRYKSLK 559
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
17-269 |
1.66e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.59 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 17 LQQLQKELDATATALANRQDESEQSRKKLIDQSREFK--KNTPEDLRKQIAPLlkgfQAEIDALSKRSKESEAAFLSVYK 94
Cdd:TIGR02168 805 LDELRAELTLLNEEAANLRERLESLERRIAATERRLEdlEEQIEELSEDIESL----AAEIEELEELIEELESELEALLN 880
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 95 RLIDVPDPVSALEAaqQLQVTVRKMHDLETENQRLKDTLQEYEREISEVKNQevtikalKEKLEQYERSLQAKNTEEAve 174
Cdd:TIGR02168 881 ERASLEEALALLRS--ELEELSEELRELESKRSELRRELEELREKLAQLELR-------LEGLEVRIDNLQERLSEEY-- 949
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 175 pnldssereerQSKGENLPNNYADKESQPEQSQESRTEdsdvktqsLQTALE-------ATQAELHELKTKYDEESTAKA 247
Cdd:TIGR02168 950 -----------SLTLEEAEALENKIEDDEEEARRRLKR--------LENKIKelgpvnlAAIEEYEELKERYDFLTAQKE 1010
|
250 260
....*....|....*....|....
gi 528492582 248 NEIEAVmTDLERANQR--AETAER 269
Cdd:TIGR02168 1011 DLTEAK-ETLEEAIEEidREARER 1033
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
109-413 |
3.16e-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: 45.42 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 109 AQQLQVTVRKMHDLETENQRLKDTLQEYEREISEvknQEVTIKALKEKLEQYERSLQAKNTEEAVEPNLDSSEREERQ-- 186
Cdd:TIGR00606 736 QSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEE---QETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQqa 812
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 187 --SKGENLPNNYADKESQPEQSQEsRTEDSDVKTQSLQTALEATQAELHELKTKYDEESTAKAneieavmtdleranQRA 264
Cdd:TIGR00606 813 akLQGSDLDRTVQQVNQEKQEKQH-ELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKL--------------QIG 877
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 265 ETAEReAGTLREQLTSAGKTMQSSN-QIQNAPEMDKSLEAelgAKEREVERLAEDVQRLQASlaqlSETSTNQISQLEQQ 343
Cdd:TIGR00606 878 TNLQR-RQQFEEQLVELSTEVQSLIrEIKDAKEQDSPLET---FLEKDQQEKEELISSKETS----NKKAQDKVNDIKEK 949
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 344 LSSKEALLKQLEEKLQDQSDYEEIKRElCTLKSVEHNSSDHHSSAQDSSKPLEMLLTGKDHSQLSESALK 413
Cdd:TIGR00606 950 VKNIHGYMKDIENKIQDGKDDYLKQKE-TELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQ 1018
|
|
| mS26_Tt |
cd23695 |
Tetrahymena thermophila ribosomal protein mS26 and similar proteins; Ribosomal protein mS26 is ... |
118-368 |
3.19e-04 |
|
Tetrahymena thermophila ribosomal protein mS26 and similar proteins; Ribosomal protein mS26 is a component of small subunit (SSU) in Tetrahymena thermophila mitochondrial ribosome (mitoribosome). The structure of the mitoribosome reveals an assembly of 94-ribosomal proteins and four-rRNAs with an additional protein mass of ~700 kDa on the small subunit; the large mitoribosomal subunit (LSU) lacks 5S rRNA.
Pssm-ID: 467909 [Multi-domain] Cd Length: 496 Bit Score: 45.20 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 118 KMHDLETENQRL----KDTLQEYEREISEVKNQEVTIKALKEKLEQY-------ERSLQAKNTEEAVEPNLDSSER--EE 184
Cdd:cd23695 221 KLEKLEKAFATLlknyKEELEEPEKQLEFMQKRLLDLYNLLRLWGQYitivkmpDSVVRDIMNKTQARPEVAKLNSkqEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 185 RQSKGENLPNNYADKESQPEQSQESRTEDSDVKTQSLQTALEATQAELHELKTKY-----DEESTAKANEIEAVM----- 254
Cdd:cd23695 301 EDAKNRKRDTEENEFDDDYESADEGETSDEEDEIEEENFQLQKEKKKEEELNAEFniaknSLYKFSPQNDKNVVDdrdfy 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 255 --TDLERANQRAetaereagTLREQLTSAGKTMQSSNQIQNAPEMDKSLEAELGAKEREverLAEDVQRLQASLaqLSET 332
Cdd:cd23695 381 sgVDLENVFPRA--------LLNNLNDFTGLDFQNVKEILNNEEKLKIIQGEDDQNDQE---DFNNPRKFQTSL--IVQT 447
|
250 260 270
....*....|....*....|....*....|....*..
gi 528492582 333 STNQISQLEQ-QLSSKEALLKQLEEKLQDQSDyeEIK 368
Cdd:cd23695 448 YKQKINNLDAeSLTRATQEKKNDIQKLLDLIG--EIK 482
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
105-372 |
3.25e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.34 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 105 ALEAAQQLQVT---VRKMHDLETENQRLKDTLQEYEREISEVKNQEVTIKALKEKLEQYERSLQAKNTEEAVEPNLDSSE 181
Cdd:TIGR00618 231 LREALQQTQQShayLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQ 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 182 R--EERQSKGENLPNNYADKESQPEQSQESRTEDSDVKTQSLQTALEATQAELHELKTKYDEESTAKANEIEAVMTDLER 259
Cdd:TIGR00618 311 RihTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTT 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 260 ANQRAETAEREAGTLR-EQLTSAGKTMQSSNQIQNAPEMDKSLEAELGAKEREVERLAEDVQRLQASLAQLSEtSTNQIS 338
Cdd:TIGR00618 391 LTQKLQSLCKELDILQrEQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQE-SAQSLK 469
|
250 260 270
....*....|....*....|....*....|....*...
gi 528492582 339 QLEQQLSSKEALLKQLEEK----LQDQSDYEEIKRELC 372
Cdd:TIGR00618 470 EREQQLQTKEQIHLQETRKkavvLARLLELQEEPCPLC 507
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
84-378 |
3.52e-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: 45.42 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 84 ESEAAFLSVYK-RLIDVPDPVSALEAAQQLQVTVRKMHDLETEnqRLKDTLQEYEREISEVKNQEVTIKALKEKLEQYER 162
Cdd:TIGR00606 206 QMELKYLKQYKeKACEIRDQITSKEAQLESSREIVKSYENELD--PLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEK 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 163 sLQAKNTEEAVEPNLDSSER-----EERQSKGENLPNNYADKESQPEQSQESRTEDSDVKT------------------- 218
Cdd:TIGR00606 284 -DNSELELKMEKVFQGTDEQlndlyHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTellveqgrlqlqadrhqeh 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 219 --------QSLQTALEATQAE-----------LHELKTKYDEESTAKANEIEAVMTDLERanqraeTAEREAGTLREQLT 279
Cdd:TIGR00606 363 irardsliQSLATRLELDGFErgpfserqiknFHTLVIERQEDEAKTAAQLCADLQSKER------LKQEQADEIRDEKK 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 280 SAGKTMQSSNQI-QNAPEMDKSLEAELGAKEREVERLAEDVQRLQASLAQLSETSTNQISQ--LEQQLSSKEALLKQLEE 356
Cdd:TIGR00606 437 GLGRTIELKKEIlEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTEtlKKEVKSLQNEKADLDRK 516
|
330 340
....*....|....*....|..
gi 528492582 357 KLQDQSDYEEIKRELCTLKSVE 378
Cdd:TIGR00606 517 LRKLDQEMEQLNHHTTTRTQME 538
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
13-366 |
4.35e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 13 KRFDLQQLQKEldATATALANRQDESEQSRKKLidqsrEFKKNTPEDLRKQIApllkGFQAEIDALSKRSKESEAAFLSV 92
Cdd:PRK02224 223 ERYEEQREQAR--ETRDEADEVLEEHEERREEL-----ETLEAEIEDLRETIA----ETEREREELAEEVRDLRERLEEL 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 93 YKRLIDVPDPvSALEAAQQLQVTVRKmHDLETENQRLKDTLQEYEREISEVKNQevtIKALKEKLEQYE-RSLQAKNTEE 171
Cdd:PRK02224 292 EEERDDLLAE-AGLDDADAEAVEARR-EELEDRDEELRDRLEECRVAAQAHNEE---AESLREDADDLEeRAEELREEAA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 172 AVEPNLDS--SEREERQSKGENLpnnyadkESQPEqSQESRTEDSDVKTQSLQTALEATQAELHELKtkydeestAKANE 249
Cdd:PRK02224 367 ELESELEEarEAVEDRREEIEEL-------EEEIE-ELRERFGDAPVDLGNAEDFLEELREERDELR--------EREAE 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 250 IEAvmtDLERANQRAETAEReagtlreqLTSAGKTMQSSNQIQNAPEMD---------KSLEAELG-------------- 306
Cdd:PRK02224 431 LEA---TLRTARERVEEAEA--------LLEAGKCPECGQPVEGSPHVEtieedrervEELEAELEdleeeveeveerle 499
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528492582 307 ------AKEREVERLAEDVQRLQASLAQLSETSTNQISQLEQQLSSKEALLKQLEEKLQDQSDYEE 366
Cdd:PRK02224 500 raedlvEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEE 565
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
17-371 |
4.71e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 17 LQQLQKELDATATALANRQDESEQSRKKLIDQSREFKKNTPEDLRKQiapllkgfqAEIDALSKRSKESEAAFLSVYKRL 96
Cdd:COG1196 409 EEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE---------EEEEALLELLAELLEEAALLEAAL 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 97 IDVPDPVSALEAAQQLQVTVRKMHDLETENQRLKDTLQEYEREISEVKNQEVTIKALKEKLEQYE-RSLQAKNTE-EAVE 174
Cdd:COG1196 480 AELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALaAALQNIVVEdDEVA 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 175 PNLDSSEREERQSKGENLPNNYADKESQPEQSQESRTEDSDV-------------KTQSLQTALEATQAELHELKTKYde 241
Cdd:COG1196 560 AAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVdlvasdlreadarYYVLGDTLLGRTLVAARLEAALR-- 637
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 242 ESTAKANEIEAVMTDLERANQRAETAEREAGTLREQLTSAGKTMQSSNQIQNAPEMD-KSLEAELGAKEREVERLAEDVQ 320
Cdd:COG1196 638 RAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELElEEALLAEEEEERELAEAEEERL 717
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 528492582 321 RLQASLAQLSETSTNQISQ-LEQQLSSKEALLKQLEEKLQDQSDYEEIKREL 371
Cdd:COG1196 718 EEELEEEALEEQLEAEREElLEELLEEEELLEEEALEELPEPPDLEELEREL 769
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
94-268 |
5.20e-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: 43.37 E-value: 5.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 94 KRLIDVPDPVSALEAAQQlqvtvrkmhDLETENQRLKDTLQEYEREISEVKNQevtIKALKEKLEQYERSL-QAKNTEE- 171
Cdd:COG1579 24 HRLKELPAELAELEDELA---------ALEARLEAAKTELEDLEKEIKRLELE---IEEVEARIKKYEEQLgNVRNNKEy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 172 -AVEPNLDSSEREERQSkgenlpnnyadkesqpeqsqESRTEDSDVKTQSLQTALEATQAELHELKTKYDEESTAKANEI 250
Cdd:COG1579 92 eALQKEIESLKRRISDL--------------------EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL 151
|
170
....*....|....*...
gi 528492582 251 EAVMTDLERANQRAETAE 268
Cdd:COG1579 152 AELEAELEELEAEREELA 169
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
111-375 |
5.31e-04 |
|
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: 44.71 E-value: 5.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 111 QLQVTVRKMHDL-ETENQRLKDT----------LQEYEREISEV----KNQEVTIKALKEKLEQYERSLQAKNTEEAVEP 175
Cdd:pfam05483 353 EFEATTCSLEELlRTEQQRLEKNedqlkiitmeLQKKSSELEEMtkfkNNKEVELEELKKILAEDEKLLDEKKQFEKIAE 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 176 NLDSSEREerqskgenlpnnyadkESQPEQSQESRTEDSDVKTQSLQTALEATQAELHELKTKYDEESTaKANEIEAVMT 255
Cdd:pfam05483 433 ELKGKEQE----------------LIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKL-KNIELTAHCD 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 256 DLERAN----QRAETAEREAGTLREQLTSAGKTMQSS-NQIQNAPEMDKSLEAELGAKEREVERLAEDVQRLQASLAQLS 330
Cdd:pfam05483 496 KLLLENkeltQEASDMTLELKKHQEDIINCKKQEERMlKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENA 575
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 528492582 331 ETSTNQISQLEQQLSSKEALLKQLEEKLQDQSDY-EEIKRELCTLK 375
Cdd:pfam05483 576 RSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNiEELHQENKALK 621
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
299-375 |
7.47e-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: 42.99 E-value: 7.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 299 KSLEAELGAKEREVERLAEDVQRLQASLAQLsetsTNQISQLEQQLSSKEALLKQLEEKL---QDQSDYEEIKRELCTLK 375
Cdd:COG1579 27 KELPAELAELEDELAALEARLEAAKTELEDL----EKEIKRLELEIEEVEARIKKYEEQLgnvRNNKEYEALQKEIESLK 102
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
23-330 |
9.27e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.58 E-value: 9.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 23 ELDATATALA-NRQDESEQSRKKLID----QSREFKKNtpEDLRKQIApLLKGFQAEIDALSKRSKESEAAFLSVYKRLI 97
Cdd:pfam05557 31 ELEKKASALKrQLDRESDRNQELQKRirllEKREAEAE--EALREQAE-LNRLKKKYLEALNKKLNEKESQLADAREVIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 98 DVPDPVSALE-----AAQQLQVTVRKMHDLETENQRLKDTLQEYEREISEVKNQEVTIKALKEKLEQYERSLQAKNTEEA 172
Cdd:pfam05557 108 CLKNELSELRrqiqrAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 173 VEPNLDSS-------EREERQSKGEN--LPNNYADKESQPEQSQE-----SRTEDSDVKTQSLQTALEATQAELHELKtK 238
Cdd:pfam05557 188 IVKNSKSElaripelEKELERLREHNkhLNENIENKLLLKEEVEDlkrklEREEKYREEAATLELEKEKLEQELQSWV-K 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 239 YDEESTAKANEIEAVMTDLERANQRAETAEREAGTLREQLTSAGKTMQS-----SNQIQNAPEMDKSLeaelgakerevE 313
Cdd:pfam05557 267 LAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARREleqelAQYLKKIEDLNKKL-----------K 335
|
330
....*....|....*..
gi 528492582 314 RLAEDVQRLQASLAQLS 330
Cdd:pfam05557 336 RHKALVRRLQRRVLLLT 352
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
70-344 |
9.44e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 9.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 70 GFQAE--IDALSKRSKESEAAFLSVYKRLIDVPDPVSALEAAQQLQVTVRKMHDLETENQRLKDTLQEYEREISEVKNQE 147
Cdd:COG4913 605 GFDNRakLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 148 VTIKALKEKLEQYERSLQAknTEEavepnldssEREERQSKGENLPNNYADKESQPEQSQESRTEDSDVKTQSLQTALEA 227
Cdd:COG4913 685 DDLAALEEQLEELEAELEE--LEE---------ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 228 TQAELHelktkyDEESTAKAneieavmtdLERANQRAETAEREAGTLREQLTsagKTMQSSNQIQNAP--EMDKSLEAeL 305
Cdd:COG4913 754 RFAAAL------GDAVEREL---------RENLEERIDALRARLNRAEEELE---RAMRAFNREWPAEtaDLDADLES-L 814
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 528492582 306 GAKEREVERLAED--VQRLQASLAQLSETSTNQISQLEQQL 344
Cdd:COG4913 815 PEYLALLDRLEEDglPEYEERFKELLNENSIEFVADLLSKL 855
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
194-370 |
1.01e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 42.82 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 194 NNYADKESQPEQSQE----SRTEDSDVKTQSLQTALEATQAELHELKTKYDEESTAKANEIEAVMTDLERANQRAETaer 269
Cdd:pfam09787 10 ADYKQKAARILQSKEkliaSLKEGSGVEGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQE--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 270 EAGTLREQLTSAGKTMQSSNQIQnapemdKSLEAELGAKEREVERLAEDVQRLQASLAQLSETSTNQISQLEQQLSSK-- 347
Cdd:pfam09787 87 EAESSREQLQELEEQLATERSAR------REAEAELERLQEELRYLEEELRRSKATLQSRIKDREAEIEKLRNQLTSKsq 160
|
170 180 190
....*....|....*....|....*....|..
gi 528492582 348 --------EALLKQLEEKL-QDQSDYEEIKRE 370
Cdd:pfam09787 161 ssssqselENRLHQLTETLiQKQTMLEALSTE 192
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
17-356 |
1.02e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.63 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 17 LQQLQKELDATATALANRQDESEQSRKKLIDQSREF--KKNTPEDLRKQIAPLLKGFQAEIDALSKRSKESEaaflsvyK 94
Cdd:pfam01576 382 LESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELqaRLSESERQRAELAEKLSKLQSELESVSSLLNEAE-------G 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 95 RLIDVPDPVSALEAaqQLQVTvrkmHDLETENQRLKDTLQEYEREISEVKNqevtikALKEKLEQYERSlqakntEEAVE 174
Cdd:pfam01576 455 KNIKLSKDVSSLES--QLQDT----QELLQEETRQKLNLSTRLRQLEDERN------SLQEQLEEEEEA------KRNVE 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 175 PNLDSSEREERQSKgenlpNNYADKESQPEQSQESRtedsdvktQSLQTALEATQAELHELKTKYDEESTAKA---NEIE 251
Cdd:pfam01576 517 RQLSTLQAQLSDMK-----KKLEEDAGTLEALEEGK--------KRLQRELEALTQQLEEKAAAYDKLEKTKNrlqQELD 583
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 252 AVMTDLERANQRAETAEREAGTLrEQLTSAGKTMQSsnqiQNAPEMDKSlEAELGAKEREVERLAEDVQRLQASLAQLSE 331
Cdd:pfam01576 584 DLLVDLDHQRQLVSNLEKKQKKF-DQMLAEEKAISA----RYAEERDRA-EAEAREKETRALSLARALEEALEAKEELER 657
|
330 340
....*....|....*....|....*
gi 528492582 332 TSTNQISQLEQQLSSKEALLKQLEE 356
Cdd:pfam01576 658 TNKQLRAEMEDLVSSKDDVGKNVHE 682
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
33-371 |
1.09e-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: 43.88 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 33 NRQDESEQSRKKLIDQSREFKKNTPE--DLRKQIAPLL-----KGFQAEIDALSKRSKESEAAFLSVYKRLIDVP-DPVS 104
Cdd:TIGR00606 309 NHQRTVREKERELVDCQRELEKLNKErrLLNQEKTELLveqgrLQLQADRHQEHIRARDSLIQSLATRLELDGFErGPFS 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 105 ALEAAQQLQVTVRKMHD-LETENQRLKD------TLQEYEREIS-EVKNQEVTIKALKEKLEQYERSLQAKNTE----EA 172
Cdd:TIGR00606 389 ERQIKNFHTLVIERQEDeAKTAAQLCADlqskerLKQEQADEIRdEKKGLGRTIELKKEILEKKQEELKFVIKElqqlEG 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 173 VEPNLDSSEREERQSKGEnlpnnyadkesQPEQSQESRTEDSDVKTQSLQTAleatQAELHELKTKYDEESTAKANEIEA 252
Cdd:TIGR00606 469 SSDRILELDQELRKAERE-----------LSKAEKNSLTETLKKEVKSLQNE----KADLDRKLRKLDQEMEQLNHHTTT 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 253 VMTDLERANQRAETAEReagtlreqlTSAGKTMQSSNQIQNAPEM--DKSLEAELGAKEREVERLAEDVQRLQASLAQLs 330
Cdd:TIGR00606 534 RTQMEMLTKDKMDKDEQ---------IRKIKSRHSDELTSLLGYFpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASL- 603
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 528492582 331 ETSTNQISQleqQLSSKEALLKQLEEKLQD-------QSDYEEIKREL 371
Cdd:TIGR00606 604 EQNKNHINN---ELESKEEQLSSYEDKLFDvcgsqdeESDLERLKEEI 648
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
14-278 |
1.13e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 14 RFDLQQLQKELD-ATATALANRQDESEQSRKKLIDQSREFKKNTPEDLRKQIAPLlkgfQAEIDALSKRSKESEAAflsv 92
Cdd:PRK02224 488 EEEVEEVEERLErAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEEL----RERAAELEAEAEEKREA---- 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 93 ykrlidvpdpvsALEAAQQLQVTVRKMHDLETENQRLKDTLQEYER---EISEVKNQEVTIKALKEKLEQyersLQAKNT 169
Cdd:PRK02224 560 ------------AAEAEEEAEEAREEVAELNSKLAELKERIESLERirtLLAAIADAEDEIERLREKREA----LAELND 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 170 EEavEPNLdsSEREERQSK------GENLPNNYADKEsQPEQSQESRTEDSDVKTQ---SLQTALEATQAELHELKTKYD 240
Cdd:PRK02224 624 ER--RERL--AEKRERKREleaefdEARIEEAREDKE-RAEEYLEQVEEKLDELREerdDLQAEIGAVENELEELEELRE 698
|
250 260 270
....*....|....*....|....*....|....*...
gi 528492582 241 EEstakaNEIEAVMTDLERANQRAETAEREAGTLREQL 278
Cdd:PRK02224 699 RR-----EALENRVEALEALYDEAEELESMYGDLRAEL 731
|
|
| Homeobox_KN |
pfam05920 |
Homeobox KN domain; This is a homeobox transcription factor KN domain conserved from fungi to ... |
1289-1323 |
1.19e-03 |
|
Homeobox KN domain; This is a homeobox transcription factor KN domain conserved from fungi to human and plants. They were first identified as TALE homeobox genes in eukaryotes, (including KNOX and MEIS genes). They have been recently classified.
Pssm-ID: 428673 Cd Length: 39 Bit Score: 37.88 E-value: 1.19e-03
10 20 30
....*....|....*....|....*....|....*
gi 528492582 1289 QQKPYPSPKTIEELASQLNLKTSTVINWFHNYRSR 1323
Cdd:pfam05920 5 LHNPYPSEEEKAELAKETGLSRKQISNWFINARRR 39
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
126-345 |
1.30e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 42.66 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 126 NQRLK---DTLQEY-------EREISEV--------KNQEVtIKALKEKLEQYERSLQAKNTEEAVEPNLD-----SSER 182
Cdd:pfam02841 57 AQKVKlptETLQELldlhrdcEKEAIAVfmkrsfkdENQEF-QKELVELLEAKKDDFLKQNEEASSKYCSAllqdlSEPL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 183 EERQSKGENL-PNNYAD-KESQPEQSQESRTE-DSDVKT-QSLQTALEAtQAELHELKTKYDEESTAKANEIEAvmtdlE 258
Cdd:pfam02841 136 EEKISQGTFSkPGGYKLfLEERDKLEAKYNQVpRKGVKAeEVLQEFLQS-KEAVEEAILQTDQALTAKEKAIEA-----E 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 259 RAnqRAETAEREAGTLREQLTSAGKTMQS---SNQIqNAPEMDKSLEAELGAKEREVERLAEdvQRLQASLAQLSETSTN 335
Cdd:pfam02841 210 RA--KAEAAEAEQELLREKQKEEEQMMEAqerSYQE-HVKQLIEKMEAEREQLLAEQERMLE--HKLQEQEELLKEGFKT 284
|
250
....*....|
gi 528492582 336 QISQLEQQLS 345
Cdd:pfam02841 285 EAESLQKEIQ 294
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
107-375 |
1.38e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 43.50 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 107 EAAQQLQVTVRKMHDLETENQRLkdtlQEYEREISEVKNQEVTIKALKEKLEQYERSLQAKNTEEAVEPNL--DSSE--R 182
Cdd:PRK10929 45 EIVEALQSALNWLEERKGSLERA----KQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPNMSTDALEQEIlqVSSQllE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 183 EERQSKGE-NLPNNYADKESQ-PEQSQESRTEDSDV--KTQSL--------QTALEATQAELHELKTKYDEESTAK--AN 248
Cdd:PRK10929 121 KSRQAQQEqDRAREISDSLSQlPQQQTEARRQLNEIerRLQTLgtpntplaQAQLTALQAESAALKALVDELELAQlsAN 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 249 ---EIEAVMTDLerANQRAETAEREAGTLREQLTS-----AGKTMQSSNQI-QNAPEMDKSLEAELgAKEREVER-LAED 318
Cdd:PRK10929 201 nrqELARLRSEL--AKKRSQQLDAYLQALRNQLNSqrqreAERALESTELLaEQSGDLPKSIVAQF-KINRELSQaLNQQ 277
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528492582 319 VQRLQASLAQlSETSTNQISQLEQQLSS--------------KEALLKQLeEKLQDQSDYEEIKRELCTLK 375
Cdd:PRK10929 278 AQRMDLIASQ-QRQAASQTLQVRQALNTlreqsqwlgvsnalGEALRAQV-ARLPEMPKPQQLDTEMAQLR 346
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
16-371 |
1.44e-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: 43.09 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 16 DLQQLQKELDATATALANRQDESEQSRKKLIDQSRE--FKKNTPEDLRKQIAPLlkgfQAEIDALSKRSKESEaaflsvy 93
Cdd:TIGR04523 343 QISQLKKELTNSESENSEKQRELEEKQNEIEKLKKEnqSYKQEIKNLESQINDL----ESKIQNQEKLNQQKD------- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 94 krlidvpdpvsaleaaQQLQVTVRKMHDLETENQRLKDTLQEYEREISEVKNQEVTIKALKEKLEQYERSLQAKnteeav 173
Cdd:TIGR04523 412 ----------------EQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQ------ 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 174 epnLDSSERE--ERQSKGENLPNNYADKESQ----PEQSQESRTEDSDVKTQslQTALEATQAELHELKTKYDEESTAKA 247
Cdd:TIGR04523 470 ---LKVLSRSinKIKQNLEQKQKELKSKEKElkklNEEKKELEEKVKDLTKK--ISSLKEKIEKLESEKKEKESKISDLE 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 248 NEIEAVMTDLERANqraetaereagtLREQLTSAGKTMQSSNQIQnapemdKSLEAELGAKEREVERLAEDVQRLQASLa 327
Cdd:TIGR04523 545 DELNKDDFELKKEN------------LEKEIDEKNKEIEELKQTQ------KSLKKKQEEKQELIDQKEKEKKDLIKEI- 605
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 528492582 328 qlsETSTNQISQLEQQLSSKEALLKQLEEKLQD-QSDYEEIKREL 371
Cdd:TIGR04523 606 ---EEKEKKISSLEKELEKAKKENEKLSSIIKNiKSKKNKLKQEV 647
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
228-375 |
1.50e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.90 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 228 TQAELHELKTKYDEESTAKANEIEAVMTDLERANQ--RAETAEREAGTLREQLTSAGKTMQSSNQiqnapEMDKSLEAEl 305
Cdd:PRK04778 62 SEEKFEEWRQKWDEIVTNSLPDIEEQLFEAEELNDkfRFRKAKHEINEIESLLDLIEEDIEQILE-----ELQELLESE- 135
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528492582 306 gAKER-EVERLAEDVQRLQASLAQLSETSTNQISQLEQQLSSKEALLKQLEEkLQDQSDYEEIKRELCTLK 375
Cdd:PRK04778 136 -EKNReEVEQLKDLYRELRKSLLANRFSFGPALDELEKQLENLEEEFSQFVE-LTESGDYVEAREILDQLE 204
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
102-379 |
1.63e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 42.49 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 102 PVSALEAAQQLQVTVRKMHDLETENQRLKDTLQEYEREISEVKNQEVTIKALKEKLEQYERSLQAKNTEE-AVEPNLDSS 180
Cdd:pfam15905 48 STPATARKVKSLELKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKtSLSASVASL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 181 EREERQSK--GENLPNNYADKESQP-------------------EQSQESRTEDSDVKTQSLQTALEATQAELHELKTKY 239
Cdd:pfam15905 128 EKQLLELTrvNELLKAKFSEDGTQKkmsslsmelmklrnkleakMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 240 deestakaneieaVMTDLERANQRAETAEREAGTLREQltsagktmQSSNQIQNAPEMDKSLEAELGAKEREVERLAedv 319
Cdd:pfam15905 208 -------------VSTEKEKIEEKSETEKLLEYITELS--------CVSEQVEKYKLDIAQLEELLKEKNDEIESLK--- 263
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 320 QRLQASLAQLSETSTNQISQLEQQLSSKEALLKQLEEKLQDQSDYEEIKRELCTLKSVEH 379
Cdd:pfam15905 264 QSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEH 323
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
72-376 |
1.73e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 72 QAEIDALSKRSKESEaaflSVYKRLIDVPDPVSALEAAQQLQVTV-RKMHDLE-----TEN--QRLKDTLQEYEREISEV 143
Cdd:PRK03918 134 QGEIDAILESDESRE----KVVRQILGLDDYENAYKNLGEVIKEIkRRIERLEkfikrTENieELIKEKEKELEEVLREI 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 144 KNQEVTIKALKEKLEQYERSLQaknteeavepnldssEREERQSKGENLpnnyaDKEsqpEQSQESRTEDSDVKTQSLQT 223
Cdd:PRK03918 210 NEISSELPELREELEKLEKEVK---------------ELEELKEEIEEL-----EKE---LESLEGSKRKLEEKIRELEE 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 224 ALEATQAELHELKTKYDE--ESTAKANEIEAVMTDLERANQRAETAEREAGTLREQLTSAGKTMQSSNQIQNAPEMDKSL 301
Cdd:PRK03918 267 RIEELKKEIEELEEKVKElkELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKK 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 302 EAELgakEREVERLAEDVQRLQASLAQLsetstNQISQLEQQLS--SKEALLKQLEE----KLQDQSDYEEIKRELCTLK 375
Cdd:PRK03918 347 LKEL---EKRLEELEERHELYEEAKAKK-----EELERLKKRLTglTPEKLEKELEElekaKEEIEEEISKITARIGELK 418
|
.
gi 528492582 376 S 376
Cdd:PRK03918 419 K 419
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
243-378 |
1.92e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 243 STAKANEIEavmtdlERANQRAETAEREAGTLREQLTSAGKTM---------QSSNQIQNapEMDKsLEAELGAKEREVE 313
Cdd:PRK12704 29 AEAKIKEAE------EEAKRILEEAKKEAEAIKKEALLEAKEEihklrnefeKELRERRN--ELQK-LEKRLLQKEENLD 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528492582 314 RLAEDVQRLQASLAQLSETSTNQISQLEQQLSSKEALLKQLEEKLQDQSDY--EEIKRELctLKSVE 378
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLtaEEAKEIL--LEKVE 164
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
16-363 |
2.05e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 16 DLQQLQKELDATATALANRQDESEQSRKKLIDQSREFKKntpedlrkqiapLLKGFQAEIDALSKRSKESEAAflSVYKR 95
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQR------------LAEYSWDEIDVASAEREIAELE--AELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 96 LIDVPDPVSALEaaQQLQvtvrkmhDLETENQRLKDTLQEYEREISEVKNQevtIKALKEKLEQYERSLQAKNTEEAVEP 175
Cdd:COG4913 680 LDASSDDLAALE--EQLE-------ELEAELEELEEELDELKGEIGRLEKE---LEQAEEELDELQDRLEAAEDLARLEL 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 176 NLDSSEREERQSKGENlpnnyadkESQPEQSQESRTEDSDVKTQSLQTALEATqaeLHELKTKYDEE------STAKANE 249
Cdd:COG4913 748 RALLEERFAAALGDAV--------ERELRENLEERIDALRARLNRAEEELERA---MRAFNREWPAEtadldaDLESLPE 816
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 250 IEAVMTDLER----------ANQRAETAEREAGTLREQLTSAGKTMQssNQIQnapEMDKSLEA---------ELGAKER 310
Cdd:COG4913 817 YLALLDRLEEdglpeyeerfKELLNENSIEFVADLLSKLRRAIREIK--ERID---PLNDSLKRipfgpgrylRLEARPR 891
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 528492582 311 EVerlaEDVQRLQASLAQLSETSTNQISQLEQQlssKEALLKQLEEKLQDQSD 363
Cdd:COG4913 892 PD----PEVREFRQELRAVTSGASLFDEELSEA---RFAALKRLIERLRSEEE 937
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
17-168 |
2.15e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 17 LQQLQKELDATATALANRQDESEQSRKKLIDQSREFkkntpEDLRKQIAPL------------LKGFQAEIDALSKRSKE 84
Cdd:COG1579 33 LAELEDELAALEARLEAAKTELEDLEKEIKRLELEI-----EEVEARIKKYeeqlgnvrnnkeYEALQKEIESLKRRISD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 85 SEAAFLSVYKRlidvpdpvsaLEAAQQLQVTVRKmhDLETENQRLKDTLQEYEREISEVKNQEVTIKALKEK-------- 156
Cdd:COG1579 108 LEDEILELMER----------IEELEEELAELEA--ELAELEAELEEKKAELDEELAELEAELEELEAEREElaakippe 175
|
170
....*....|...
gi 528492582 157 -LEQYERSLQAKN 168
Cdd:COG1579 176 lLALYERIRKRKN 188
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
67-354 |
2.42e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.52 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 67 LLKGFQA---EIDALSKRSKESEAAFLSVYKRLIDVPDPVSALEAAQQLQVTVRKmhDLETENQRLKDTLQEYEREIsev 143
Cdd:pfam12128 232 AIAGIMKirpEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSA--ELNQLLRTLDDQWKEKRDEL--- 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 144 kNQEvtIKALKEKLEQYERSLQAKnteEAVEPNLDSSEREERQSKGENLPNNYADKESQPEQ------SQESRTEDSDVK 217
Cdd:pfam12128 307 -NGE--LSAADAAVAKDRSELEAL---EDQHGAFLDADIETAAADQEQLPSWQSELENLEERlkaltgKHQDVTAKYNRR 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 218 TQSLQTALEATQAELHELKTKYDEESTAKANEIEAVMTDLE------------RANQRAETAEREAGTLREQLTSAGKTM 285
Cdd:pfam12128 381 RSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALEselreqleagklEFNEEEYRLKSRLGELKLRLNQATATP 460
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 286 QSSNQIQNAPEMDKSLEAELGAKEREVERLAEDVQRLQASLAQLSEtSTNQISQ-LEQQLSSKEALLKQL 354
Cdd:pfam12128 461 ELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASE-ALRQASRrLEERQSALDELELQL 529
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
278-371 |
2.43e-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: 42.06 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 278 LTSAGKTMQSSNQIQNAPEMDKSLEAELGAKEREVERLAEDVQRLQASLAQLSE---TSTNQISQLEQQLSSKEALLKQL 354
Cdd:COG4942 9 LLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERriaALARRIRALEQELAALEAELAEL 88
|
90
....*....|....*...
gi 528492582 355 EEKLQD-QSDYEEIKREL 371
Cdd:COG4942 89 EKEIAElRAELEAQKEEL 106
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
216-378 |
2.87e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 216 VKTQSLQTALE-ATQAELHELKTKYDEESTAKANEIEAVMTDLERANQRAETAEREAGTLREQLTSAGKTMQSSNQIQNa 294
Cdd:COG2433 373 IRGLSIEEALEeLIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELS- 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 295 pEMDKSLEAELGaKEREVERLAEDVQRLQASLAQLSETStnqisqleQQLSSKEALLKQLEEKlqdqsdyeEIKRELCTL 374
Cdd:COG2433 452 -EARSEERREIR-KDREISRLDREIERLERELEEERERI--------EELKRKLERLKELWKL--------EHSGELVPV 513
|
....
gi 528492582 375 KSVE 378
Cdd:COG2433 514 KVVE 517
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
18-253 |
2.90e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 18 QQLQKELDATATALANRQDESEQSRKKLiDQS----REFKKNT----PEDLRKQIAPLLKGFQAEIDALSKRSKESEAAF 89
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKEL-EEAeaalEEFRQKNglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 90 LSVYKRLIDVPDPVSALEAAQQLQVTVRKMHDLETENQRLKDTLQEyereisevknQEVTIKALKEKLEQYERSLQ--AK 167
Cdd:COG3206 243 AALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTP----------NHPDVIALRAQIAALRAQLQqeAQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 168 NTEEAVEPNLDSSEREERQskgenLPNNYADKESQpeQSQESRTEdsdVKTQSLQTALEATQAELHELKTKYDEESTAKA 247
Cdd:COG3206 313 RILASLEAELEALQAREAS-----LQAQLAQLEAR--LAELPELE---AELRRLEREVEVARELYESLLQRLEEARLAEA 382
|
....*.
gi 528492582 248 NEIEAV 253
Cdd:COG3206 383 LTVGNV 388
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
16-363 |
2.90e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 16 DLQQLQKELDATATALaNRQDESEQSRKKLIDQSREfkkntPEDLRKQIAPLLK-----GFQAEIDALSKRSKESE--AA 88
Cdd:PRK04863 838 ELRQLNRRRVELERAL-ADHESQEQQQRSQLEQAKE-----GLSALNRLLPRLNlladeTLADRVEEIREQLDEAEeaKR 911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 89 FLSVYKRLIDVPDP-VSALEAAQQlqvtvrkmhdletENQRLKDTLQEYEREISEVKNQevtIKALKEKLEQ-----YER 162
Cdd:PRK04863 912 FVQQHGNALAQLEPiVSVLQSDPE-------------QFEQLKQDYQQAQQTQRDAKQQ---AFALTEVVQRrahfsYED 975
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 163 S--LQAKNTE--EAVEPNLDSSEREERQSKgENLpNNYADKESQPEQSQESRTEDSDVKTQSLQtalEATQaELHELKTK 238
Cdd:PRK04863 976 AaeMLAKNSDlnEKLRQRLEQAEQERTRAR-EQL-RQAQAQLAQYNQVLASLKSSYDAKRQMLQ---ELKQ-ELQDLGVP 1049
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 239 YDEESTAKA------------------NEIEAVMTDLERA----NQRAETAEREAGTLREQLTSAGKTMQS------SNQ 290
Cdd:PRK04863 1050 ADSGAEERArarrdelharlsanrsrrNQLEKQLTFCEAEmdnlTKKLRKLERDYHEMREQVVNAKAGWCAvlrlvkDNG 1129
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 291 I-----------QNAPEM----DKSLEA---ELGAKE--REVERLAEDVQRLQASL---------------AQLSETS-- 333
Cdd:PRK04863 1130 VerrlhrrelayLSADELrsmsDKALGAlrlAVADNEhlRDVLRLSEDPKRPERKVqfyiavyqhlrerirQDIIRTDdp 1209
|
410 420 430
....*....|....*....|....*....|
gi 528492582 334 TNQISQLEQQLSSKEALLKQLEEKLQDQSD 363
Cdd:PRK04863 1210 VEAIEQMEIELSRLTEELTSREQKLAISSE 1239
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
103-357 |
3.14e-03 |
|
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: 42.25 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 103 VSALEAAQQLQVTVRKmhDLETENQRLKDTLQEYEREISEVKNQ----EVTIKALKEKLEQYERSLQAKNTEEAV--EPN 176
Cdd:COG3096 356 LEELTERLEEQEEVVE--EAAEQLAEAEARLEAAEEEVDSLKSQladyQQALDVQQTRAIQYQQAVQALEKARALcgLPD 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 177 LDSSEREERQSKgenlpnnYADKESQPEQS---QESRTEDSDVKTQSLQTALEATQAELHELKTkydEESTAKANEIeav 253
Cdd:COG3096 434 LTPENAEDYLAA-------FRAKEQQATEEvleLEQKLSVADAARRQFEKAYELVCKIAGEVER---SQAWQTAREL--- 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 254 mtdLERANQRAETAEREAgTLREQLTSAGKTMQSSNQIQN-APEMDKSLEAELGAKErEVERLAEDVQRLQASLAQLSET 332
Cdd:COG3096 501 ---LRRYRSQQALAQRLQ-QLRAQLAELEQRLRQQQNAERlLEEFCQRIGQQLDAAE-ELEELLAELEAQLEELEEQAAE 575
|
250 260
....*....|....*....|....*
gi 528492582 333 STNQISQLEQQLSSKEALLKQLEEK 357
Cdd:COG3096 576 AVEQRSELRQQLEQLRARIKELAAR 600
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
291-361 |
3.47e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 39.48 E-value: 3.47e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528492582 291 IQNAPE---MDKSLEAELGAKEREVERLAEDVQRLQASLAQLSETSTNQISQLEQQLSSKEALLKQLEEKLQDQ 361
Cdd:pfam03938 11 LEESPEgkaAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQE 84
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
138-363 |
3.50e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.20 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 138 REISEVKNQEVTiKALKEKLEQYERSLQAKNTEEAVEPNLD---SSEREERQSKGENLPN----NYADK--ESQPEQSQE 208
Cdd:PLN02939 40 RGFSSQQKKKRG-KNIAPKQRSSNSKLQSNTDENGQLENTSlrtVMELPQKSTSSDDDHNrasmQRDEAiaAIDNEQQTN 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 209 SRTED--SDVKTQSLQTALEAT--------QAELHELK--TKYDEESTAKANEIEAVMTDLERANQRAETAERE---AGT 273
Cdd:PLN02939 119 SKDGEqlSDFQLEDLVGMIQNAeknilllnQARLQALEdlEKILTEKEALQGKINILEMRLSETDARIKLAAQEkihVEI 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 274 LREQLTSAGKTMQSSNQIQNAPEMDKSLEAELgAKEREVErLAEDVQRLQASLAQLSETStNQISQLEQQLSSKEALLKQ 353
Cdd:PLN02939 199 LEEQLEKLRNELLIRGATEGLCVHSLSKELDV-LKEENML-LKDDIQFLKAELIEVAETE-ERVFKLEKERSLLDASLRE 275
|
250
....*....|.
gi 528492582 354 LEEKLQD-QSD 363
Cdd:PLN02939 276 LESKFIVaQED 286
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
16-359 |
3.53e-03 |
|
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: 42.25 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 16 DLQQLQKELDATATALANRQDESEQSRKKLIDQSREFKkntpeDLRKQIApllkGFQAEIDALSKRSKESEAAflsvykr 95
Cdd:COG3096 355 DLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVD-----SLKSQLA----DYQQALDVQQTRAIQYQQA------- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 96 lidvpdpVSALEAAQQLQvtvrKMHDLETENqrLKDTLQEYEReisevKNQEVT--IKALKEKL-------EQYERSLQA 166
Cdd:COG3096 419 -------VQALEKARALC----GLPDLTPEN--AEDYLAAFRA-----KEQQATeeVLELEQKLsvadaarRQFEKAYEL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 167 knteeaVEPNLDSSEREERQSKGENLPNNYADKESQPEQSQESRTEDSDVKTqslqtaLEATQAELHELKTKYDEESTAK 246
Cdd:COG3096 481 ------VCKIAGEVERSQAWQTARELLRRYRSQQALAQRLQQLRAQLAELEQ------RLRQQQNAERLLEEFCQRIGQQ 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 247 ANEIEAVMTDLERANQRAETAEREAGTLREQLtsagktMQSSNQIQNAPEMDKSLEAE----LGAKEReVERLAE----- 317
Cdd:COG3096 549 LDAAEELEELLAELEAQLEELEEQAAEAVEQR------SELRQQLEQLRARIKELAARapawLAAQDA-LERLREqsgea 621
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 528492582 318 --DVQRLQASLAQLSETSTnQISQLEQQLSS-KEALLKQLEEKLQ 359
Cdd:COG3096 622 laDSQEVTAAMQQLLERER-EATVERDELAArKQALESQIERLSQ 665
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
283-369 |
3.90e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 39.10 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 283 KTMQSSNQIQNApemDKSLEAELGAKEREVERLAEDVQRLQASLAQLSET-STNQISQLEQQLSSKEALLKQLEEKLQD- 360
Cdd:smart00935 8 KILQESPAGKAA---QKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATlSEAAREKKEKELQKKVQEFQRKQQKLQQd 84
|
90
....*....|.
gi 528492582 361 --QSDYEEIKR 369
Cdd:smart00935 85 lqKRQQEELQK 95
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
111-271 |
3.97e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 111 QLQVTVRKMHDLETENQRLKDTLQEYEREISEVKNQevtIKALKEKLEQYERSLQAKNTEEAvepnlDSSEREER-QSKG 189
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEAR---LEAAKTELEDLEKEIKRLELEIE-----EVEARIKKyEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 190 ENLPNN--YADKESQpEQSQESRTEDSDVKTQSLQTALEATQAELHELKTKYDE---ESTAKANEIEAVMTDLErANQRA 264
Cdd:COG1579 83 GNVRNNkeYEALQKE-IESLKRRISDLEDEILELMERIEELEEELAELEAELAEleaELEEKKAELDEELAELE-AELEE 160
|
....*..
gi 528492582 265 ETAEREA 271
Cdd:COG1579 161 LEAEREE 167
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
217-376 |
4.08e-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: 41.29 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 217 KTQSLQTALEATQAELHELKTKYDEEstakANEIEAVMTDLERANQRAETAEREAGTLREQLTSAGKTMQSSNQIQNApe 296
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAAL----KKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 297 mdksLEAELGAKEREVERL------------------AEDVQRLQASLA---QLSETSTNQISQLEQQLSSKEALLKQLE 355
Cdd:COG4942 95 ----LRAELEAQKEELAELlralyrlgrqpplalllsPEDFLDAVRRLQylkYLAPARREQAEELRADLAELAALRAELE 170
|
170 180
....*....|....*....|..
gi 528492582 356 EKLQD-QSDYEEIKRELCTLKS 376
Cdd:COG4942 171 AERAElEALLAELEEERAALEA 192
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
16-380 |
4.48e-03 |
|
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: 41.49 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 16 DLQQLQKELDATATALANRQDESEQSRKKLIDQSREFKKNTPE-----------DLRKQIAPLLKGFQA------EIDAL 78
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQeavleetqeriNRARKAAPLAAHIKAvtqieqQAQRI 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 79 SKRSKESEAAFLSVYKRLIDVPDPVSALEAAQQLQVTVRKMHD-LETENQRLKDTLQEYEREISE---VKNQEVTIKALK 154
Cdd:TIGR00618 313 HTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIhIRDAHEVATSIREISCQQHTLtqhIHTLQQQKTTLT 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 155 EKLEQYERSLQAKNTEEAVEPNLDSSEREERQSKGenlpnnYADKESQPEQSqesRTEDSDVKTQSLQTALEATQAELHE 234
Cdd:TIGR00618 393 QKLQSLCKELDILQREQATIDTRTSAFRDLQGQLA------HAKKQQELQQR---YAELCAAAITCTAQCEKLEKIHLQE 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 235 LKTKYDEESTAKAN----------------------------------EIEAVMTD----------LERANQRAETAERE 270
Cdd:TIGR00618 464 SAQSLKEREQQLQTkeqihlqetrkkavvlarllelqeepcplcgsciHPNPARQDidnpgpltrrMQRGEQTYAQLETS 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 271 AGTLREQLTSAGKTMQS-SNQIQNAPEMDKSLEAELGAKEREVERLAEDVQRLQASLAQLSETSTNQISQLEQQLSSKEA 349
Cdd:TIGR00618 544 EEDVYHQLTSERKQRASlKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQP 623
|
410 420 430
....*....|....*....|....*....|.
gi 528492582 350 LLKQLEEKLQDQSDYEEIKRELCTLKSVEHN 380
Cdd:TIGR00618 624 EQDLQDVRLHLQQCSQELALKLTALHALQLT 654
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
16-184 |
4.93e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 16 DLQQLQKELDATATALANRQDESEQSRKKLIDQSREFK--KNTPEDLRKQIapllKGFQAEIDALSKRSKESEaaflsvy 93
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEaaKTELEDLEKEI----KRLELEIEEVEARIKKYE------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 94 KRLIDVPDP--VSALEaaQQLQVTVRKMHDLETENQRLKDTLQEYEREISEVKNQevtIKALKEKLEQYERSLQAKNTEE 171
Cdd:COG1579 80 EQLGNVRNNkeYEALQ--KEIESLKRRISDLEDEILELMERIEELEEELAELEAE---LAELEAELEEKKAELDEELAEL 154
|
170
....*....|...
gi 528492582 172 AVEPNLDSSEREE 184
Cdd:COG1579 155 EAELEELEAEREE 167
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
110-359 |
6.17e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 41.32 E-value: 6.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 110 QQLQVTVRKMHdleTENQRLKDTLQEyEREISEVKNQEVT-IKALKEkLEQYERSLQaknteeavepnldsSEREERQSk 188
Cdd:PRK10246 443 AQLQVAIQNVT---QEQTQRNAALNE-MRQRYKEKTQQLAdVKTICE-QEARIKDLE--------------AQRAQLQA- 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 189 GENLPNNYADKESQPEQSQESRTEDSdvktqslQTALEATQAELHELKtkydEESTAKANEIEAVMTDLERanqraetAE 268
Cdd:PRK10246 503 GQPCPLCGSTSHPAVEAYQALEPGVN-------QSRLDALEKEVKKLG----EEGAALRGQLDALTKQLQR-------DE 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 269 REAGTLREQ---LTSAGKTMQSSNQIQNAPEMDksLEAELGAKEREVERLAEDVQR--LQASLAQlsetSTNQISQLEQQ 343
Cdd:PRK10246 565 SEAQSLRQEeqaLTQQWQAVCASLNITLQPQDD--IQPWLDAQEEHERQLRLLSQRheLQGQIAA----HNQQIIQYQQQ 638
|
250
....*....|....*.
gi 528492582 344 LSSKEAllkQLEEKLQ 359
Cdd:PRK10246 639 IEQRQQ---QLLTALA 651
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
110-326 |
6.38e-03 |
|
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: 40.19 E-value: 6.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 110 QQLQVTVRKMHDLETENQRLkdtLQEYEREISEVKNQEVTIKALKEKLEQY---ERSLQAKNTEEavepnlDSSEREERQ 186
Cdd:pfam17045 56 KEIGLLRQQLEELEKGKQEL---VAKYEQQLQKLQEELSKLKRSYEKLQRKqlkEAREEAKSREE------DRSELSRLN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 187 SKGENLPNNYADKESQPEQSQESRTE-DSDVKTQSLQTALEATQAELHELKTKyDEESTAKANEIEAVMTDLERANQRAE 265
Cdd:pfam17045 127 GKLEEFRQKSLEWEQQRLQYQQQVASlEAQRKALAEQSSLIQSAAYQVQLEGR-KQCLEASQSEIQRLRSKLERAQDSLC 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528492582 266 TAEREAGTLR---EQLTSAGKTMQSSNQiqnapemdkSLEAELGAKEREVERLAEDVQRLQASL 326
Cdd:pfam17045 206 AQELELERLRmrvSELGDSNRKLLEEQQ---------RLLEELRMSQRQLQVLQNELMELKATL 260
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
137-343 |
6.64e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 41.35 E-value: 6.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 137 EREISEVKNQevTIKALKEKLEQYERsLQAKNTEEAVE--PNLDSSEREERQSKGENLPNNYADKE---SQPEQS----- 206
Cdd:NF041483 93 ERELRDARAQ--TQRILQEHAEHQAR-LQAELHTEAVQrrQQLDQELAERRQTVESHVNENVAWAEqlrARTESQarrll 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 207 QESRTEdsdvKTQSLQTALEATQAELHELKTKYDEESTAKANEIEAVM----TDLERANQRAETAEREAGTLREQLTSAg 282
Cdd:NF041483 170 DESRAE----AEQALAAARAEAERLAEEARQRLGSEAESARAEAEAILrrarKDAERLLNAASTQAQEATDHAEQLRSS- 244
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528492582 283 KTMQSSNQIQNAPEMDKSLEAELGAKErevERLAEDVQRLQASLAQLSETSTNQISQLEQQ 343
Cdd:NF041483 245 TAAESDQARRQAAELSRAAEQRMQEAE---EALREARAEAEKVVAEAKEAAAKQLASAESA 302
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
16-362 |
8.19e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 8.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 16 DLQQLQKELDATATALANRQDESEQSRKKLIDQSREFKkntpeDLRKQIApllkGFQAEIDALSKRSKESEAAflsvykr 95
Cdd:PRK04863 356 DLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVD-----ELKSQLA----DYQQALDVQQTRAIQYQQA------- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 96 lidvpdpVSALEAAQQLQvtvrKMHDLETENqrLKDTLQEYereisevKNQEvtiKALKEKLEQYERSLQaknteeavep 175
Cdd:PRK04863 420 -------VQALERAKQLC----GLPDLTADN--AEDWLEEF-------QAKE---QEATEELLSLEQKLS---------- 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 176 nlDSSEREERQSKGENLPNNYADKESQPEQSQESRTEDSDVKTQSLQTA-LEATQAELHELKTKYDEESTAkaneiEAVM 254
Cdd:PRK04863 467 --VAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVARELLRRLREQRHLAEqLQQLRMRLSELEQRLRQQQRA-----ERLL 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 255 TDLERANQRAETAEREAGTLREQLtsagktmqssnqiqnapemdkslEAELGAKEREVERLAEDVQRLQASLAQLSEtst 334
Cdd:PRK04863 540 AEFCKRLGKNLDDEDELEQLQEEL-----------------------EARLESLSESVSEARERRMALRQQLEQLQA--- 593
|
330 340 350
....*....|....*....|....*....|..
gi 528492582 335 nQISQLEQQ----LSSKEALlkqleEKLQDQS 362
Cdd:PRK04863 594 -RIQRLAARapawLAAQDAL-----ARLREQS 619
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
221-398 |
8.52e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.66 E-value: 8.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 221 LQTALEATQAELHELKTKYDEEstakaneiEAVMTDLERANQRAETAEREAGTLREQLTSAGKTMQSSNQIQNAPEMD-K 299
Cdd:PRK01156 188 LEEKLKSSNLELENIKKQIADD--------EKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEiK 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 300 SLEAELGAKEREVERLAEDVQRLQASLAQLSETSTNQI-----------------SQLEQQLSSKEALLKQLEEKLQDQS 362
Cdd:PRK01156 260 TAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYIndyfkykndienkkqilSNIDAEINKYHAIIKKLSVLQKDYN 339
|
170 180 190
....*....|....*....|....*....|....*.
gi 528492582 363 DYEEIKRELCTLKSVEHNSSDHHSSAQDSSKPLEML 398
Cdd:PRK01156 340 DYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESL 375
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
16-361 |
9.87e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.67 E-value: 9.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 16 DLQQLQKELDATATALANRQDESEQSRKKL------IDQSREFKKNTPEDLRKQIAPLLKGFQAEIDALSKRSKeseaaf 89
Cdd:PRK11281 136 QLQNAQNDLAEYNSQLVSLQTQPERAQAALyansqrLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQND------ 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 90 lsvYKRLidvpdpvsALEAAQQLQVTVRKMHDLETENQRLkdtLQEYEREISEVKNQevtikalkEKLEQYErslqaKNT 169
Cdd:PRK11281 210 ---LQRK--------SLEGNTQLQDLLQKQRDYLTARIQR---LEHQLQLLQEAINS--------KRLTLSE-----KTV 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 170 EEAVEPnldsserEERQSKGENlpnnyadkesqPEQSQEsrtedSDVKTQSLQTALEATQA--EL--HELKTKydeesta 245
Cdd:PRK11281 263 QEAQSQ-------DEAARIQAN-----------PLVAQE-----LEINLQLSQRLLKATEKlnTLtqQNLRVK------- 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492582 246 kaneieavmTDLERANQraetAEReagTLREQLTSAGKTMQSS----NQIQNAP--EMDKSLE---AELGAKEREVERLA 316
Cdd:PRK11281 313 ---------NWLDRLTQ----SER---NIKEQISVLKGSLLLSrilyQQQQALPsaDLIEGLAdriADLRLEQFEINQQR 376
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 528492582 317 EDVQRLQASLAQLSETSTNQIS-----QLEQQLSSKEALLKQLEEKLQDQ 361
Cdd:PRK11281 377 DALFQPDAYIDKLEAGHKSEVTdevrdALLQLLDERRELLDQLNKQLNNQ 426
|
|
| |
