|
Name |
Accession |
Description |
Interval |
E-value |
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
226-479 |
3.58e-34 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 136.73 E-value: 3.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 226 QLKESFQQLQLERDECAEHIEGERARWHQRMSKMSQEICTLKKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAVP-- 303
Cdd:pfam15070 1 QLMESLKQLQTERDQYAENLKEEGAVWQQKMQQLSEQVRTLREEKERSVSQVQELETSLAELKNQAAVPPAEEEQPPAgp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 304 SEVE------LQHLRKELERVAGELQSQVKNNQHISLLNRRQEERIREQEERLRKQEERLQE------------------ 359
Cdd:pfam15070 81 SEEEqrlqeeAEQLQKELEALAGQLQAQVQDNEQLSRLNQEQEQRLLELERAAERWGEQAEDrkqiledmqsdratisra 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 360 --QHEKLR-QLAKPQSVFEELNNEN---KSTLQLEQQVK--------ELQEKLGE------------------------- 400
Cdd:pfam15070 161 lsQNRELKeQLAELQNGFVKLTNENmelTSALQSEQHVKkelakklgQLQEELGElketlelksqeaqslqeqrdqylah 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 401 ------------------------------------------------------EHLEAASQQNQQLTAQLSLMALPGEG 426
Cdd:pfam15070 241 lqqyvaayqqlasekeelhkqyllqtqlmdrlqheevqgkvaaemarqelqetqERLEALTQQNQQLQAQLSLLANPGEG 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 472235303 427 HGGEHlDSEGEEAPRPMPSVPEDPESREAMSSFMDHL-----KEKADLSELVKKQELR 479
Cdd:pfam15070 321 DGLES-EEEEEEAPRPSLSIPEDFESREAMVAFFNSAlaqaeEERAELRRQLKEQKRR 377
|
|
| GM130_C |
pfam19046 |
GM130 C-terminal binding motif; This entry represents the C-terminal motif from the GM130 ... |
593-632 |
4.81e-15 |
|
GM130 C-terminal binding motif; This entry represents the C-terminal motif from the GM130 protein that is bound by the GRASP65 PDZ domain pfam04495.
Pssm-ID: 465957 Cd Length: 46 Bit Score: 69.33 E-value: 4.81e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 472235303 593 PLLDKPTAQPIV------QDHQEHPGLGSNCCVPLFCWAWLPRRRR 632
Cdd:pfam19046 1 SPPENPTAQQIMqllpeiQNPQEHPGLGSNPCIPFFYRADENDEVK 46
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
80-416 |
1.23e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.04 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 80 QERAVVLDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYF 159
Cdd:COG1196 228 ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 160 EEESKDLAVRLQHSLQckgELESALSAVIATEKKKANQLSscskahtewELEQSLQDQALLKAQLTQLKESFQQLQLERd 239
Cdd:COG1196 308 EERRRELEERLEELEE---ELAELEEELEELEEELEELEE---------ELEEAEEELEEAEAELAEAEEALLEAEAEL- 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 240 ecAEHIEGERARWHQRMSKMSQEIcTLKKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAVPSEVELQHLRKELERVA 319
Cdd:COG1196 375 --AEAEEELEELAEELLEALRAAA-ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 320 GELQSQVKNNQHISLLNRRQEERIREQEERLRKQEERLQEQHEKLRQLAK-----PQSVFEELNNENKS----TLQLEQQ 390
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAdyegfLEGVKAALLLAGLRglagAVAVLIG 531
|
330 340
....*....|....*....|....*.
gi 472235303 391 VKELQEKLGEEHLEAASQQNQQLTAQ 416
Cdd:COG1196 532 VEAAYEAALEAALAAALQNIVVEDDE 557
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
80-374 |
5.09e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.77 E-value: 5.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 80 QERAVVLDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYF 159
Cdd:TIGR02168 221 ELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 160 EEESKDLAVRLQHSLQCKGELEsalsAVIATEKKKANQLSScSKAHTEWELEQSLQDQALLKAQLTQLKESFQQLQLERD 239
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELE----AQLEELESKLDELAE-ELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 240 ECAEHIEGERARWHQRMSKMSQ---EICTLKKEKQQDMRRVEELERSLSKL-----KNQMAEPLPPEPPAVPSEVELQHL 311
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASlnnEIERLEARLERLEDRRERLQQEIEELlkkleEAELKELQAELEELEEELEELQEE 455
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 472235303 312 RKELERVAGELQSQVKNNQHISLLNRRQEERIREQEERLRKQEERLQEQHEKLRQLAKPQSVF 374
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGL 518
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
86-290 |
7.43e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.77 E-value: 7.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 86 LDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYFEEESKD 165
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 166 LAVRLQHSLQcKGELESALSAVIATEKKKA----NQLSSCSKAHTEwELEQSLQDQALLKAQLTQLKESFQQLQLERDEC 241
Cdd:COG4942 109 LLRALYRLGR-QPPLALLLSPEDFLDAVRRlqylKYLAPARREQAE-ELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 472235303 242 AEHIEGERARWHQRMSKMSQEICTLKKEKQQDMRRVEELERSLSKLKNQ 290
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
86-290 |
8.87e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.38 E-value: 8.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 86 LDSTSVKISRLKNTIKSLKQQKKQVEhqlEEEKKANNERQKAERE---LEVQIQTLIIQKEELNTDLYH----MERSLRY 158
Cdd:TIGR02169 296 IGELEAEIASLERSIAEKERELEDAE---ERLAKLEAEIDKLLAEieeLEREIEEERKRRDKLTEEYAElkeeLEDLRAE 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 159 FEEESKDLAVRLQHSLQCKGELESAlsaviateKKKANQLSSCSKAHTEwELEQSLQDQALLKAQLTQLKESFQQLQLER 238
Cdd:TIGR02169 373 LEEVDKEFAETRDELKDYREKLEKL--------KREINELKRELDRLQE-ELQRLSEELADLNAAIAGIEAKINELEEEK 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 472235303 239 DECAEHI---EGERARWHQRMSKMSQEICTLKKEKQQDMRRVEELERSLSKLKNQ 290
Cdd:TIGR02169 444 EDKALEIkkqEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQ 498
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
69-404 |
3.40e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 69 SATLKDLEspcqERAVVLDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELE------VQIQTLIIQK 142
Cdd:PRK03918 227 EKEVKELE----ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKelkekaEEYIKLSEFY 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 143 EELNTDLYHMERSLRYFEEESKDLAVRLQhslqckgELESALSAVIATEKKKANQLSSCSKAHTEWELeqsLQDQALLKA 222
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIK-------ELEEKEERLEELKKKLKELEKRLEELEERHEL---YEEAKAKKE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 223 QLTQLKESFQQLQLER-DECAEHIEGERARWHQRMSKMSQEICTLKKEKQQDMRRVEELERSLSK--------------- 286
Cdd:PRK03918 373 ELERLKKRLTGLTPEKlEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrelteehrke 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 287 -LKNQMAEPLPPEPPAVPSEVELQHLRKELERVAGELQSQ---VKNNQHISLLNRRQEERIREQEERLRKQEERLQEQHE 362
Cdd:PRK03918 453 lLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKEselIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKE 532
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 472235303 363 KLRQLAKPQSVF----EELNNENKSTLQLEQQVKELQEKLGEEHLE 404
Cdd:PRK03918 533 KLIKLKGEIKSLkkelEKLEELKKKLAELEKKLDELEEELAELLKE 578
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
70-318 |
9.34e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 9.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 70 ATLKDLESPCQERAVVLDST---SVKISRLKNTIKSLKQQKKQVE-HQLEEEKKANNERQKAERE---LEVQIQTL---I 139
Cdd:PRK03918 469 KEIEEKERKLRKELRELEKVlkkESELIKLKELAEQLKELEEKLKkYNLEELEKKAEEYEKLKEKlikLKGEIKSLkkeL 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 140 IQKEELNTDLYHMERSLRYFEEESKDLAVRLQH-SLQCKGELESALSAViatEK--KKANQLSSCSK---------AHTE 207
Cdd:PRK03918 549 EKLEELKKKLAELEKKLDELEEELAELLKELEElGFESVEELEERLKEL---EPfyNEYLELKDAEKelereekelKKLE 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 208 WELEQSLQDQALLKAQLTQLKESFQQLQLERDEcaehieGERARWHQRMSKMSQEICTLKKEKQQDMRRVEELERSLSKL 287
Cdd:PRK03918 626 EELDKAFEELAETEKRLEELRKELEELEKKYSE------EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKL 699
|
250 260 270
....*....|....*....|....*....|.
gi 472235303 288 KNQMAEPLPPEPpavpsevELQHLRKELERV 318
Cdd:PRK03918 700 KEELEEREKAKK-------ELEKLEKALERV 723
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
65-240 |
9.03e-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: 38.59 E-value: 9.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 65 GPTSSATLKDLESPCQERavvlDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQkaeRELEVQIQTLIIQKEE 144
Cdd:pfam09787 39 LDSSTALTLELEELRQER----DLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQL---QELEEQLATERSARRE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 145 LNTDLYHMERSLRYFEEESKDLAVRLQHSLQckgELESALSaviatekKKANQLSSCSKAHT-EWELEQSL--------Q 215
Cdd:pfam09787 112 AEAELERLQEELRYLEEELRRSKATLQSRIK---DREAEIE-------KLRNQLTSKSQSSSsQSELENRLhqltetliQ 181
|
170 180
....*....|....*....|....*
gi 472235303 216 DQALLKAqLTQLKESFqQLQLERDE 240
Cdd:pfam09787 182 KQTMLEA-LSTEKNSL-VLQLERME 204
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
226-479 |
3.58e-34 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 136.73 E-value: 3.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 226 QLKESFQQLQLERDECAEHIEGERARWHQRMSKMSQEICTLKKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAVP-- 303
Cdd:pfam15070 1 QLMESLKQLQTERDQYAENLKEEGAVWQQKMQQLSEQVRTLREEKERSVSQVQELETSLAELKNQAAVPPAEEEQPPAgp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 304 SEVE------LQHLRKELERVAGELQSQVKNNQHISLLNRRQEERIREQEERLRKQEERLQE------------------ 359
Cdd:pfam15070 81 SEEEqrlqeeAEQLQKELEALAGQLQAQVQDNEQLSRLNQEQEQRLLELERAAERWGEQAEDrkqiledmqsdratisra 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 360 --QHEKLR-QLAKPQSVFEELNNEN---KSTLQLEQQVK--------ELQEKLGE------------------------- 400
Cdd:pfam15070 161 lsQNRELKeQLAELQNGFVKLTNENmelTSALQSEQHVKkelakklgQLQEELGElketlelksqeaqslqeqrdqylah 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 401 ------------------------------------------------------EHLEAASQQNQQLTAQLSLMALPGEG 426
Cdd:pfam15070 241 lqqyvaayqqlasekeelhkqyllqtqlmdrlqheevqgkvaaemarqelqetqERLEALTQQNQQLQAQLSLLANPGEG 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 472235303 427 HGGEHlDSEGEEAPRPMPSVPEDPESREAMSSFMDHL-----KEKADLSELVKKQELR 479
Cdd:pfam15070 321 DGLES-EEEEEEAPRPSLSIPEDFESREAMVAFFNSAlaqaeEERAELRRQLKEQKRR 377
|
|
| GM130_C |
pfam19046 |
GM130 C-terminal binding motif; This entry represents the C-terminal motif from the GM130 ... |
593-632 |
4.81e-15 |
|
GM130 C-terminal binding motif; This entry represents the C-terminal motif from the GM130 protein that is bound by the GRASP65 PDZ domain pfam04495.
Pssm-ID: 465957 Cd Length: 46 Bit Score: 69.33 E-value: 4.81e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 472235303 593 PLLDKPTAQPIV------QDHQEHPGLGSNCCVPLFCWAWLPRRRR 632
Cdd:pfam19046 1 SPPENPTAQQIMqllpeiQNPQEHPGLGSNPCIPFFYRADENDEVK 46
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
80-416 |
1.23e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.04 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 80 QERAVVLDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYF 159
Cdd:COG1196 228 ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 160 EEESKDLAVRLQHSLQckgELESALSAVIATEKKKANQLSscskahtewELEQSLQDQALLKAQLTQLKESFQQLQLERd 239
Cdd:COG1196 308 EERRRELEERLEELEE---ELAELEEELEELEEELEELEE---------ELEEAEEELEEAEAELAEAEEALLEAEAEL- 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 240 ecAEHIEGERARWHQRMSKMSQEIcTLKKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAVPSEVELQHLRKELERVA 319
Cdd:COG1196 375 --AEAEEELEELAEELLEALRAAA-ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 320 GELQSQVKNNQHISLLNRRQEERIREQEERLRKQEERLQEQHEKLRQLAK-----PQSVFEELNNENKS----TLQLEQQ 390
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAdyegfLEGVKAALLLAGLRglagAVAVLIG 531
|
330 340
....*....|....*....|....*.
gi 472235303 391 VKELQEKLGEEHLEAASQQNQQLTAQ 416
Cdd:COG1196 532 VEAAYEAALEAALAAALQNIVVEDDE 557
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
96-406 |
2.20e-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: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 96 LKNTIKSLKQQKKQ----VEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYFE---EESKDLAV 168
Cdd:COG1196 198 LERQLEPLERQAEKaeryRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEaelEELRLELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 169 RLQHSLQCKGELESALSAVIAT-------EKKKANQLSScSKAHTEWELEQSLQDQALLKAQLTQLKESFQQLQLERDEC 241
Cdd:COG1196 278 ELELELEEAQAEEYELLAELARleqdiarLEERRRELEE-RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 242 AEHIEGERARWHQRMSKMSQEICTLKKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAVPSEVELQHLRKELERVAGE 321
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 322 L----QSQVKNNQHISLLNRRQEERIREQEERLRKQEERLQEQHEKLRQLAKPQSVFEELNNENKSTLQLEQQVKELQEK 397
Cdd:COG1196 437 EeeeeEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL 516
|
....*....
gi 472235303 398 LGEEHLEAA 406
Cdd:COG1196 517 AGLRGLAGA 525
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
80-374 |
5.09e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.77 E-value: 5.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 80 QERAVVLDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYF 159
Cdd:TIGR02168 221 ELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 160 EEESKDLAVRLQHSLQCKGELEsalsAVIATEKKKANQLSScSKAHTEWELEQSLQDQALLKAQLTQLKESFQQLQLERD 239
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELE----AQLEELESKLDELAE-ELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 240 ECAEHIEGERARWHQRMSKMSQ---EICTLKKEKQQDMRRVEELERSLSKL-----KNQMAEPLPPEPPAVPSEVELQHL 311
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASlnnEIERLEARLERLEDRRERLQQEIEELlkkleEAELKELQAELEELEEELEELQEE 455
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 472235303 312 RKELERVAGELQSQVKNNQHISLLNRRQEERIREQEERLRKQEERLQEQHEKLRQLAKPQSVF 374
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGL 518
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
92-401 |
4.42e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.61 E-value: 4.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 92 KISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYFEE-------ESK 164
Cdd:TIGR02169 682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQeienvksELK 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 165 DLAVRLQHSLQCKGELESALSAVIATE-----KKKANQLSSCSKAHTEWE-----LEQSLQDQALLKAQLTQLKesfQQL 234
Cdd:TIGR02169 762 ELEARIEELEEDLHKLEEALNDLEARLshsriPEIQAELSKLEEEVSRIEarlreIEQKLNRLTLEKEYLEKEI---QEL 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 235 QLERDECAEHIEGERARWHQ---RMSKMSQEICTLKKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAVPSEVELQHL 311
Cdd:TIGR02169 839 QEQRIDLKEQIKSIEKEIENlngKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKR 918
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 312 RKELERVAGELQSQVKnnqHIsLLNRRQEERIREQEERLRKQEERLQEQHEKLRQLakpqsvfEELNN----ENKSTLQL 387
Cdd:TIGR02169 919 LSELKAKLEALEEELS---EI-EDPKGEDEEIPEEELSLEDVQAELQRVEEEIRAL-------EPVNMlaiqEYEEVLKR 987
|
330
....*....|....
gi 472235303 388 EQQVKELQEKLGEE 401
Cdd:TIGR02169 988 LDELKEKRAKLEEE 1001
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
86-290 |
7.43e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.77 E-value: 7.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 86 LDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYFEEESKD 165
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 166 LAVRLQHSLQcKGELESALSAVIATEKKKA----NQLSSCSKAHTEwELEQSLQDQALLKAQLTQLKESFQQLQLERDEC 241
Cdd:COG4942 109 LLRALYRLGR-QPPLALLLSPEDFLDAVRRlqylKYLAPARREQAE-ELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 472235303 242 AEHIEGERARWHQRMSKMSQEICTLKKEKQQDMRRVEELERSLSKLKNQ 290
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
100-441 |
9.23e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.45 E-value: 9.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 100 IKSLKQQKKQVEHQLEEeKKANNER-QKAERELEVQIQTLIIQKE------ELNTDLYHMERSLryfeeeskdLAVRLQH 172
Cdd:TIGR02168 167 ISKYKERRKETERKLER-TRENLDRlEDILNELERQLKSLERQAEkaerykELKAELRELELAL---------LVLRLEE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 173 SLQCKGELESALSAVIATEKKKANQLSSCSKAHTEWELEQSLQDQALLKAQLTQLkeSFQQLQLERDECAEHIEGERARW 252
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELY--ALANEISRLEQQKQILRERLANL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 253 HQRMSKMSQEICTLKKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAVPSEVELQHLRKELERVAGELQSQVKN-NQH 331
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQlELQ 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 332 ISLLNRRQEErireqeerLRKQEERLQEQHEKLRQ----------LAKPQSVFEELNNENKSTLQLEQQVKELQEKLGEE 401
Cdd:TIGR02168 395 IASLNNEIER--------LEARLERLEDRRERLQQeieellkkleEAELKELQAELEELEEELEELQEELERLEEALEEL 466
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 472235303 402 HLEAASQQNQQLTAQLSLMALPGEGHGGEHLDSEGEEAPR 441
Cdd:TIGR02168 467 REELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSE 506
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
67-417 |
3.45e-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: 53.49 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 67 TSSATLKDLESPCQERAVvldstsvKISRLKNTIKSLKQQKKQVEHQLEEEK----KANNERQKAERE----------LE 132
Cdd:TIGR04523 51 NKEKELKNLDKNLNKDEE-------KINNSNNKIKILEQQIKDLNDKLKKNKdkinKLNSDLSKINSEikndkeqknkLE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 133 VQIQTLIIQKEELNTDLYHMERSLRYFEEESKDLAVRLQHSLQCKGELESALSAVIATEKKKANQLSSCSKAHTEWE--- 209
Cdd:TIGR04523 124 VELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLElll 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 210 --LEQSLQDQALLKAQLTQLKESFQQLQLERDECAEHIEGERArwhqRMSKMSQEICTLK----------KEKQQDM--- 274
Cdd:TIGR04523 204 snLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTT----EISNTQTQLNQLKdeqnkikkqlSEKQKELeqn 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 275 -RRVEELERSLSKLKNQMAEPLPPEPPAVPSEV--ELQHLRKELErvagELQSQV-KNNQHISLLNrrqeerirEQEERL 350
Cdd:TIGR04523 280 nKKIKELEKQLNQLKSEISDLNNQKEQDWNKELksELKNQEKKLE----EIQNQIsQNNKIISQLN--------EQISQL 347
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 472235303 351 RKQEERLQ-EQHEKLRQLAKPQSVFEELNNENKSTLQ----LEQQVKELQEKlgeehLEAASQQNQQLTAQL 417
Cdd:TIGR04523 348 KKELTNSEsENSEKQRELEEKQNEIEKLKKENQSYKQeiknLESQINDLESK-----IQNQEKLNQQKDEQI 414
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
86-290 |
8.87e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.38 E-value: 8.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 86 LDSTSVKISRLKNTIKSLKQQKKQVEhqlEEEKKANNERQKAERE---LEVQIQTLIIQKEELNTDLYH----MERSLRY 158
Cdd:TIGR02169 296 IGELEAEIASLERSIAEKERELEDAE---ERLAKLEAEIDKLLAEieeLEREIEEERKRRDKLTEEYAElkeeLEDLRAE 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 159 FEEESKDLAVRLQHSLQCKGELESAlsaviateKKKANQLSSCSKAHTEwELEQSLQDQALLKAQLTQLKESFQQLQLER 238
Cdd:TIGR02169 373 LEEVDKEFAETRDELKDYREKLEKL--------KREINELKRELDRLQE-ELQRLSEELADLNAAIAGIEAKINELEEEK 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 472235303 239 DECAEHI---EGERARWHQRMSKMSQEICTLKKEKQQDMRRVEELERSLSKLKNQ 290
Cdd:TIGR02169 444 EDKALEIkkqEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQ 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
114-455 |
9.43e-07 |
|
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: 52.37 E-value: 9.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 114 LEEEKKANNERQKAERELEVQIQTLIIQKEELntdlyhmerslryfEEESKDLAVRLQHSLQCKGELESALSAVIATEKK 193
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEEL--------------EEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 194 KANQLSSCSKAHTEWELEQSLQDQALLKAQlTQLKESFQQLQlERDECAEHIEGERARWHQRMSKMSQEICTLKKEKQQD 273
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAE-EELAEAEAEIE-ELEAQIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 274 MRRVEELERSLSKLKNQMAEPLPPEPPAVPSEVELQHLRKELERVAGELQSQVKnnqhiSLLNrrqeerireqeeRLRKQ 353
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE-----ALLN------------ERASL 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 354 EERLQEQHEKLRQLAkpqsvfEELNNENKSTLQLEQQVKELQEKLG--EEHLEAASQQNQQLTAQLSlmalpgeghggEH 431
Cdd:TIGR02168 886 EEALALLRSELEELS------EELRELESKRSELRRELEELREKLAqlELRLEGLEVRIDNLQERLS-----------EE 948
|
330 340
....*....|....*....|....
gi 472235303 432 LDSEGEEAPRPMPSVPEDPESREA 455
Cdd:TIGR02168 949 YSLTLEEAEALENKIEDDEEEARR 972
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
98-291 |
2.36e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 98 NTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYFEEESKDLAVRLQHSLQCK 177
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 178 GELESALSAVIATEKKKANQ------LSSCSKAHTEWELE------QSLQDQAL-LKAQLTQLKESFQQLQLERDECAEH 244
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQpplallLSPEDFLDAVRRLQylkylaPARREQAEeLRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 472235303 245 I---EGERARWHQRMSKMSQEICTLKKEKQQDMRRVEELERSLSKLKNQM 291
Cdd:COG4942 180 LaelEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
85-400 |
4.62e-06 |
|
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: 49.63 E-value: 4.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 85 VLDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYFEEESK 164
Cdd:TIGR04523 205 NLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIK 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 165 DLAVRLQhslqckgELESALSAViatEKKKANQLSSCSKAhtewELEQSLQDQALLKAQLTQLKESFQQL-----QLERD 239
Cdd:TIGR04523 285 ELEKQLN-------QLKSEISDL---NNQKEQDWNKELKS----ELKNQEKKLEEIQNQISQNNKIISQLneqisQLKKE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 240 ecAEHIEGERARWHQRMSKMSQEICTLKKEKQQDMRRVEELERSL----SKLKNQMAEPLPPEPPAVPSEVELQHLRKEL 315
Cdd:TIGR04523 351 --LTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIndleSKIQNQEKLNQQKDEQIKKLQQEKELLEKEI 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 316 ERVageLQSQVKNNQHISLLNRRQEERI------REQEERLRKQEERL--------QEQHEKLRQLAKPQSVFEELNNEN 381
Cdd:TIGR04523 429 ERL---KETIIKNNSEIKDLTNQDSVKEliiknlDNTRESLETQLKVLsrsinkikQNLEQKQKELKSKEKELKKLNEEK 505
|
330
....*....|....*....
gi 472235303 382 KstlQLEQQVKELQEKLGE 400
Cdd:TIGR04523 506 K---ELEEKVKDLTKKISS 521
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
69-404 |
3.40e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 69 SATLKDLEspcqERAVVLDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELE------VQIQTLIIQK 142
Cdd:PRK03918 227 EKEVKELE----ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKelkekaEEYIKLSEFY 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 143 EELNTDLYHMERSLRYFEEESKDLAVRLQhslqckgELESALSAVIATEKKKANQLSSCSKAHTEWELeqsLQDQALLKA 222
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIK-------ELEEKEERLEELKKKLKELEKRLEELEERHEL---YEEAKAKKE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 223 QLTQLKESFQQLQLER-DECAEHIEGERARWHQRMSKMSQEICTLKKEKQQDMRRVEELERSLSK--------------- 286
Cdd:PRK03918 373 ELERLKKRLTGLTPEKlEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrelteehrke 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 287 -LKNQMAEPLPPEPPAVPSEVELQHLRKELERVAGELQSQ---VKNNQHISLLNRRQEERIREQEERLRKQEERLQEQHE 362
Cdd:PRK03918 453 lLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKEselIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKE 532
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 472235303 363 KLRQLAKPQSVF----EELNNENKSTLQLEQQVKELQEKLGEEHLE 404
Cdd:PRK03918 533 KLIKLKGEIKSLkkelEKLEELKKKLAELEKKLDELEEELAELLKE 578
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
91-418 |
5.81e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.21 E-value: 5.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 91 VKISRLKNTIKSLKQQKKQVEhQLEEEKKANNERQKAERE------------LEVQIQTLIIQKEELNTDLYHMERSLRY 158
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLD-LIIDEKRQQLERLRREREkaeryqallkekREYEGYELLKEKEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 159 FEEESKDLAVRLQHSLQCKGELESALSAVIATEKKKANQLSSCSK---AHTEWELEQSLQDQALLKAQLTQLKESFQQLQ 235
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKekiGELEAEIASLERSIAEKERELEDAEERLAKLE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 236 LERDECAEHIEgerarwhqrmsKMSQEICTLKKEKQQDMRRVEELERSLSKLKNQMaepLPPEPPAVPSEVELQHLRKEL 315
Cdd:TIGR02169 329 AEIDKLLAEIE-----------ELEREIEEERKRRDKLTEEYAELKEELEDLRAEL---EEVDKEFAETRDELKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 316 ERVAGELQSqvknnqhisllnrrqeerireqeerLRKQEERLQEQHEKLRqlakpqSVFEELNNENKStlqLEQQVKELQ 395
Cdd:TIGR02169 395 EKLKREINE-------------------------LKRELDRLQEELQRLS------EELADLNAAIAG---IEAKINELE 440
|
330 340
....*....|....*....|....*
gi 472235303 396 EKLGE--EHLEAASQQNQQLTAQLS 418
Cdd:TIGR02169 441 EEKEDkaLEIKKQEWKLEQLAADLS 465
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
187-395 |
7.59e-05 |
|
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: 45.13 E-value: 7.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 187 VIATEKKKANQLSSCSKAHTEWELEQSLQDQALLKAQLTQLKESFQQLQLERDECAEHIEGErarwhqrMSKMSQEICTL 266
Cdd:pfam09787 26 LIASLKEGSGVEGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEE-------AESSREQLQEL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 267 KKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAVPSEVE-LQHLRKELERVAGELQSQVKNNQHISLLnrrqeerire 345
Cdd:pfam09787 99 EEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSrIKDREAEIEKLRNQLTSKSQSSSSQSEL---------- 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 472235303 346 qeerlrkqEERLQEQHEKLRQlakPQSVFEELNNENKSTL----QLEQQVKELQ 395
Cdd:pfam09787 169 --------ENRLHQLTETLIQ---KQTMLEALSTEKNSLVlqleRMEQQIKELQ 211
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
81-413 |
8.42e-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: 45.73 E-value: 8.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 81 ERAVVLDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYFE 160
Cdd:pfam02463 160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERI 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 161 EESKDLAVRLQHSLQCKGELESALSAVIATEKKKaNQLSSCSKAHTEWELEQSLQDQALLKAQLTQLKesfqQLQLERDE 240
Cdd:pfam02463 240 DLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKE-NKEEEKEKKLQEEELKLLAKEEEELKSELLKLE----RRKVDDEE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 241 CAEHIEGERARWHQRMSKMSQEICTLKKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAVPSEVELQHLRKELERVAG 320
Cdd:pfam02463 315 KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 321 ELQSQVKNNQHISLLNRRQEERIREQEERLRKQEERLQEQHEKLRQLAKPQSVFEELN-NENKSTLQLEQQVKELQEKLG 399
Cdd:pfam02463 395 EELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEElEKQELKLLKDELELKKSEDLL 474
|
330
....*....|....
gi 472235303 400 EEHLEAASQQNQQL 413
Cdd:pfam02463 475 KETQLVKLQEQLEL 488
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
92-505 |
9.16e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 9.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 92 KISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAErelEVQIQTLIIQK-EELNTDLYHMERSlryfeEESKDLAVRL 170
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD---ELKKAAAAKKKaDEAKKKAEEKKKA-----DEAKKKAEEA 1443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 171 QHSLQCKGELESALSA----VIATEKKKANQLSSCSKAHTEWELEQSLQDQALLKAQLTQLKESFQQLQLERDECAEHIE 246
Cdd:PTZ00121 1444 KKADEAKKKAEEAKKAeeakKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKK 1523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 247 GERARWHQRMSKMSQEICTLKKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAVPSEVELqhLRKELERVAGELQSQV 326
Cdd:PTZ00121 1524 ADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEE--AKKAEEARIEEVMKLY 1601
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 327 KNNQHISLLNRRQEERIREQEERLRKQEERLQEQHEKLRQLAKPQSVFEELNNENKSTLQLEQQVKELQEKLGEEHLEAA 406
Cdd:PTZ00121 1602 EEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAK 1681
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 407 SQQNQQLTAQLSLMALPGEGHGGEHLDSEGEEAPRPMPSVPEDPESREAMSsfmDHLKEKADlSELVKKQELRFiqywQE 486
Cdd:PTZ00121 1682 KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKA---EEAKKEAE-EDKKKAEEAKK----DE 1753
|
410
....*....|....*....
gi 472235303 487 RCHQKIHHLLSEPGGRAKD 505
Cdd:PTZ00121 1754 EEKKKIAHLKKEEEKKAEE 1772
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
70-318 |
9.34e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 9.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 70 ATLKDLESPCQERAVVLDST---SVKISRLKNTIKSLKQQKKQVE-HQLEEEKKANNERQKAERE---LEVQIQTL---I 139
Cdd:PRK03918 469 KEIEEKERKLRKELRELEKVlkkESELIKLKELAEQLKELEEKLKkYNLEELEKKAEEYEKLKEKlikLKGEIKSLkkeL 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 140 IQKEELNTDLYHMERSLRYFEEESKDLAVRLQH-SLQCKGELESALSAViatEK--KKANQLSSCSK---------AHTE 207
Cdd:PRK03918 549 EKLEELKKKLAELEKKLDELEEELAELLKELEElGFESVEELEERLKEL---EPfyNEYLELKDAEKelereekelKKLE 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 208 WELEQSLQDQALLKAQLTQLKESFQQLQLERDEcaehieGERARWHQRMSKMSQEICTLKKEKQQDMRRVEELERSLSKL 287
Cdd:PRK03918 626 EELDKAFEELAETEKRLEELRKELEELEKKYSE------EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKL 699
|
250 260 270
....*....|....*....|....*....|.
gi 472235303 288 KNQMAEPLPPEPpavpsevELQHLRKELERV 318
Cdd:PRK03918 700 KEELEEREKAKK-------ELEKLEKALERV 723
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
92-411 |
1.11e-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: 45.12 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 92 KISRLKNTIKSLKQQKKQVEhqlEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYFEEESKDLAVRLQ 171
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQME---LEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 172 HSLQCKGELESALSAVIATEKKkANQLSSCSK-----------------AHTEWELEQSLQDQALLKAQLTQLKESFQQL 234
Cdd:pfam05557 80 LKKKYLEALNKKLNEKESQLAD-AREVISCLKnelselrrqiqraelelQSTNSELEELQERLDLLKAKASEAEQLRQNL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 235 QLERDECAEHIegerarwhQRMSKMSQEICT------LKKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAVPSEVEL 308
Cdd:pfam05557 159 EKQQSSLAEAE--------QRIKELEFEIQSqeqdseIVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 309 QHLRKELERVAG---ELQSQVKNNQHISLLNRRQEERIREQEERLRKQE----ERLQEQHEKLRQLAKPQSVFEELNNEN 381
Cdd:pfam05557 231 EDLKRKLEREEKyreEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEdlsrRIEQLQQREIVLKEENSSLTSSARQLE 310
|
330 340 350
....*....|....*....|....*....|
gi 472235303 382 KSTLQLEQQVKELQEKLGEEHLEAASQQNQ 411
Cdd:pfam05557 311 KARRELEQELAQYLKKIEDLNKKLKRHKAL 340
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
94-438 |
1.56e-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: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 94 SRLKNTIKsLKQQKKQVEHQLEEEKKANNERQKaerelevQIQTLIIQKEELNTDLyhmeRSLRYFEEESKDLAVRLQHS 173
Cdd:pfam05483 209 ARLEMHFK-LKEDHEKIQHLEEEYKKEINDKEK-------QVSLLLIQITEKENKM----KDLTFLLEESRDKANQLEEK 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 174 LQCKGElesALSAVIATEKKKANQLSSCSKAhteweLEQSLQDQALLKAQLTQLKESFQQLQLERDECAEHIEGERARWH 253
Cdd:pfam05483 277 TKLQDE---NLKELIEKKDHLTKELEDIKMS-----LQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHS 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 254 QRMSKMSQEICTLKKEKQQDMRRVEELERSLS----KLKNQMAEPLPPEPPAVPSEVELQhlrkELERVAGELQSQVKNN 329
Cdd:pfam05483 349 FVVTEFEATTCSLEELLRTEQQRLEKNEDQLKiitmELQKKSSELEEMTKFKNNKEVELE----ELKKILAEDEKLLDEK 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 330 QHISLLNRRQEERIREQEERLRKQEERLQEQHEKLRQLAKPQSVFEELNNENKSTLQLEQqvkeLQEKLGEEHLEAASQQ 409
Cdd:pfam05483 425 KQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEK----LKNIELTAHCDKLLLE 500
|
330 340
....*....|....*....|....*....
gi 472235303 410 NQQLTAQLSLMALPGEGHGGEHLDSEGEE 438
Cdd:pfam05483 501 NKELTQEASDMTLELKKHQEDIINCKKQE 529
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
95-416 |
3.75e-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: 43.80 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 95 RLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQ----KEELNTDLYHMERSLRYFEEESK--DLAV 168
Cdd:TIGR00618 532 RGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCdnrsKEDIPNLQNITVRLQDLTEKLSEaeDMLA 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 169 RLQHSLQCKGELESALSAVIATEKKKANQLSSCSKAHTEWELEQSLQDQALLKAQLTQLKESFQQLQLERDECAEHIEGE 248
Cdd:TIGR00618 612 CEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQ 691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 249 RARWHQRMSkmsqeictlkkEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPA-VPSEVELQHLRKELERVAGE-LQSQV 326
Cdd:TIGR00618 692 LTYWKEMLA-----------QCQTLLRELETHIEEYDREFNEIENASSSLGSDlAAREDALNQSLKELMHQARTvLKART 760
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 327 KNNQHISLLNRRQEERIREQEERLRKQEERLQEQHEKLRQLAKPQSVFEELNNENKSTL------------QLEQQVKEL 394
Cdd:TIGR00618 761 EAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILnlqcetlvqeeeQFLSRLEEK 840
|
330 340
....*....|....*....|....*..
gi 472235303 395 QEKLGE-----EHLEAASQQNQQLTAQ 416
Cdd:TIGR00618 841 SATLGEithqlLKYEECSKQLAQLTQE 867
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
93-305 |
3.85e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 93 ISRLKNTIKSL-KQQKKQVEHQLEEEKKANNERQKAERELEvQIQTLIIQKEELNTDLYHMERSLRYFEEESKDLAVRLQ 171
Cdd:COG4717 48 LERLEKEADELfKPQGRKPELNLKELKELEEELKEAEEKEE-EYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 172 hslqckgelesaLSAVIATEKKKANQLSSCSKahtewELEQSLQDQALLKAQLTQLKESFQQLQLERDECAEHIEGERAR 251
Cdd:COG4717 127 ------------LLPLYQELEALEAELAELPE-----RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLA 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 472235303 252 WHQRMSKMSQEICTLKKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAVPSE 305
Cdd:COG4717 190 TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
86-401 |
6.66e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.70 E-value: 6.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 86 LDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYFEEESKD 165
Cdd:TIGR04523 330 ISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQ 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 166 LAVRLQHSLQCKGELESALSAVIATEKKKANQLSSCSKAHTEWELE--------QSLQDQ-ALLKAQLTQLKESFQQLQL 236
Cdd:TIGR04523 410 KDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIiknldntrESLETQlKVLSRSINKIKQNLEQKQK 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 237 ERDECAEHIEG---ERARWHQRMSKMSQEICTLKKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAVPsEVELQHLRK 313
Cdd:TIGR04523 490 ELKSKEKELKKlneEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENL-EKEIDEKNK 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 314 ELErvagelqsQVKNNQHiSLLNRRQEERIREQEERLRKQEERlQEQHEKLRQLAKPQSVFEELNNENKSTLQLEQQVKE 393
Cdd:TIGR04523 569 EIE--------ELKQTQK-SLKKKQEEKQELIDQKEKEKKDLI-KEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKS 638
|
....*...
gi 472235303 394 LQEKLGEE 401
Cdd:TIGR04523 639 KKNKLKQE 646
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
87-316 |
1.11e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 87 DSTSVKISRLKNTIKSLKQQKKQVEHQLEE-EKKANNERQKAE-RELEVQIQTLIIQKEELNTDLyhmerslryfeeesk 164
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEaEAALEEFRQKNGlVDLSEEAKLLLQQLSELESQL--------------- 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 165 dLAVRLQHSlqckgELESALSAVIATEKKKANQLSSCSKAHTEWELEQSLQDqalLKAQLTQLKESF-------QQLQLE 237
Cdd:COG3206 229 -AEARAELA-----EAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAE---LEAELAELSARYtpnhpdvIALRAQ 299
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 472235303 238 RDECAEHIEGERARwhqrmskmsqEICTLKKEKQQDMRRVEELERSLSKLKNQMAEPLPPeppavpsEVELQHLRKELE 316
Cdd:COG3206 300 IAALRAQLQQEAQR----------ILASLEAELEALQAREASLQAQLAQLEARLAELPEL-------EAELRRLEREVE 361
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
92-367 |
1.50e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.97 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 92 KISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELntdlyhmERSLRYFEEESKDLAVRLQ 171
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL-------REALDELRAELTLLNEEAA 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 172 HSLQCKGELESALSAviatekkkanqlsscskahTEWELEQSLQDQALLKAQLTQLKESFQQLQLERDEcaehIEGERAR 251
Cdd:TIGR02168 821 NLRERLESLERRIAA-------------------TERRLEDLEEQIEELSEDIESLAAEIEELEELIEE----LESELEA 877
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 252 WHQRMSKMSQEICTLKKEKQQDMRRVEELERSLSKLKNQMAeplppeppavpsevELQHLRKELERVAGELQSQVKNNQh 331
Cdd:TIGR02168 878 LLNERASLEEALALLRSELEELSEELRELESKRSELRRELE--------------ELREKLAQLELRLEGLEVRIDNLQ- 942
|
250 260 270
....*....|....*....|....*....|....*.
gi 472235303 332 iSLLNRRQEERIREQEERLRKQEERLQEQHEKLRQL 367
Cdd:TIGR02168 943 -ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRL 977
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
72-418 |
2.41e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 72 LKDLESPCQERAVVLDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYH 151
Cdd:TIGR04523 309 NKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKN 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 152 MERSLRyfeeeskdlavrlqhslqckgelesalsaviatekkkanqlsscskahtewELEQSLQDQallKAQLTQLKESF 231
Cdd:TIGR04523 389 LESQIN---------------------------------------------------DLESKIQNQ---EKLNQQKDEQI 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 232 QQLQLERDEcaehIEGERARWHQRMSKMSQEICTLKKEKQQDMRRVEELERSLSKLKNQMAEPlppeppavpsEVELQHL 311
Cdd:TIGR04523 415 KKLQQEKEL----LEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVL----------SRSINKI 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 312 RKELERVAGELQSQVKN----NQHISLLNRRQEERIREQEERLRKQEERLQEQHEKLRQLAKPQSVFEELNNENKSTlQL 387
Cdd:TIGR04523 481 KQNLEQKQKELKSKEKElkklNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKE-NL 559
|
330 340 350
....*....|....*....|....*....|....*.
gi 472235303 388 EQQVKELQEKLGEEH-----LEAASQQNQQLTAQLS 418
Cdd:TIGR04523 560 EKEIDEKNKEIEELKqtqksLKKKQEEKQELIDQKE 595
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
72-272 |
2.42e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.20 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 72 LKDLESPCQERAVVLDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYH 151
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 152 MERS-------LRYFEEESKDLAVRLQHSLQCKGELESALSaviatekKKANQLSSCSKAHTEWELEQSLQDQALLKAQL 224
Cdd:TIGR02168 391 LELQiaslnneIERLEARLERLEDRRERLQQEIEELLKKLE-------EAELKELQAELEELEEELEELQEELERLEEAL 463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 472235303 225 TQLKESFQQLQLERDECAEHIEGERARWH------QRMSKMSQEICTLKKEKQQ 272
Cdd:TIGR02168 464 EELREELEEAEQALDAAERELAQLQARLDslerlqENLEGFSEGVKALLKNQSG 517
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
103-416 |
3.02e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.88 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 103 LKQQKKQVEHQleeekKANNERQKAERELEVQIQTLIIQKEELntdLYHMERSlRYFEEESKDLAVRLQHSLQCKGELES 182
Cdd:pfam17380 271 LNQLLHIVQHQ-----KAVSERQQQEKFEKMEQERLRQEKEEK---AREVERR-RKLEEAEKARQAEMDRQAAIYAEQER 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 183 alsavIATEKKKanQLSSCSKAHTEWELEQSLQDQalLKAQLTQLKEsFQQLQLERDECAEHIEGERarwhqrmsKMSQE 262
Cdd:pfam17380 342 -----MAMERER--ELERIRQEERKRELERIRQEE--IAMEISRMRE-LERLQMERQQKNERVRQEL--------EAARK 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 263 ICTLKKEKQqdmRRVEELERSLSKLKNQMAEPLPPEPPAVPSEVElqhlrKELERVAgelQSQVKNNQHISLLNRRQEER 342
Cdd:pfam17380 404 VKILEEERQ---RKIQQQKVEMEQIRAEQEEARQREVRRLEEERA-----REMERVR---LEEQERQQQVERLRQQEEER 472
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 472235303 343 IreqeerlRKQEERLQEQHEKLRQLAKPQSVFEELNNENKSTLQLEQQVKELQEKLGEEHLEAASQQNQQLTAQ 416
Cdd:pfam17380 473 K-------RKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAE 539
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
219-422 |
3.26e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 219 LLKAQLTQLKESFQQLQLERDECAEHIEgERARWHQRMSKMSQEICTLKKEKQQ--DMRRVEELERSLSKLKNQMAEPLP 296
Cdd:COG4717 68 LNLKELKELEEELKEAEEKEEEYAELQE-ELEELEEELEELEAELEELREELEKleKLLQLLPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 297 PEPPAVPSEVELQHLRKELERVAGELQsqvKNNQHISLLNRRQEERIREQEERLRKQEERLQEQHEKLRQLakpqsvFEE 376
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELA---ELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEE------LEE 217
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 472235303 377 LNNENKstlQLEQQVKELQEKLGEEHLEAASQQNQQLTAQLSLMAL 422
Cdd:COG4717 218 AQEELE---ELEEELEQLENELEAAALEERLKEARLLLLIAAALLA 260
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
93-282 |
3.28e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.82 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 93 ISRLKNTIKSLKQ--QKKQVEHQLEEEKKANNERQKaeRELEVQIQTLIIQKEELNTDLYHMERSLRYFEEESKDLAVRL 170
Cdd:TIGR02169 807 VSRIEARLREIEQklNRLTLEKEYLEKEIQELQEQR--IDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL 884
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 171 QHSLQCKGELESALSAViateKKKANQLsscskahtEWELEQSLQDQALLKAQLTQLKE--------------------S 230
Cdd:TIGR02169 885 GDLKKERDELEAQLREL----ERKIEEL--------EAQIEKKRKRLSELKAKLEALEEelseiedpkgedeeipeeelS 952
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 472235303 231 FQQLQLERDECAEHIEG----------ERARWHQRMSKMSQEICTLKKEKQQDMRRVEELER 282
Cdd:TIGR02169 953 LEDVQAELQRVEEEIRAlepvnmlaiqEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
216-416 |
3.89e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.28 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 216 DQALLKAQLTQLKESFQQLQLERDEcAEHIEGERARWHQRMSKMSQEICTLKKEKQQDMRR------VEELERSLSKLKN 289
Cdd:PRK11281 57 EDKLVQQDLEQTLALLDKIDRQKEE-TEQLKQQLAQAPAKLRQAQAELEALKDDNDEETREtlstlsLRQLESRLAQTLD 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 290 QMAEPLPPEPPAVPSEVELQhlrKELERVAGELQSQVKNNQHI-SLLNRRQEERIRE---QEERLRKQEERLQEQHEKLR 365
Cdd:PRK11281 136 QLQNAQNDLAEYNSQLVSLQ---TQPERAQAALYANSQRLQQIrNLLKGGKVGGKALrpsQRVLLQAEQALLNAQNDLQR 212
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 472235303 366 QLAKPQSVFEELNNENKSTL-----QLEQQVKELQEKLGEEHLEAASQQNQQLTAQ 416
Cdd:PRK11281 213 KSLEGNTQLQDLLQKQRDYLtariqRLEHQLQLLQEAINSKRLTLSEKTVQEAQSQ 268
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
180-289 |
5.41e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.84 E-value: 5.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 180 LESALSAVIATEKKKANQLSSCSKAHTEWELEQSLQDQALLKAQLTQLKESFQQLQLERDECAEHIE------------- 246
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIErlerelsearsee 457
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 472235303 247 GERARWHQRMSKMSQEICTLKKEKQQDMRRVEELERSLSKLKN 289
Cdd:COG2433 458 RREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
91-437 |
5.69e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 39.66 E-value: 5.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 91 VKISRLKNTIKSLKQQKKQVEHQLeeeKKANNERQKAERELEVQIQTLIIQKEE---------LNTDLYHMERSLRYFEE 161
Cdd:pfam13166 96 EKIAKLKKEIKDHEEKLDAAEANL---QKLDKEKEKLEADFLDECWKKIKRKKNsalsealngFKYEANFKSRLLREIEK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 162 ESKDLAVRLQhslqcKGELESALSAVIATEKKKANQLSSCSKAHTEWELE--------------QSLQD----------- 216
Cdd:pfam13166 173 DNFNAGVLLS-----DEDRKAALATVFSDNKPEIAPLTFNVIDFDALEKAeiliqkvigkssaiEELIKnpdladwveqg 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 217 ------------------QALLKAQLTQ-LKESFQQLQLERDECAEHIEGERARWHQRMSKMSqeicTLKKEKQQDMRRV 277
Cdd:pfam13166 248 lelhkahldtcpfcgqplPAERKAALEAhFDDEFTEFQNRLQKLIEKVESAISSLLAQLPAVS----DLASLLSAFELDV 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 278 EELERSLSKLKNQMAEPLPPEPPAVP---SEVELQHLRKELERVAGELQSQV----KNNQHISLLNRRQEERIREQEERL 350
Cdd:pfam13166 324 EDIESEAEVLNSQLDGLRRALEAKRKdpfKSIELDSVDAKIESINDLVASINeliaKHNEITDNFEEEKNKAKKKLRLHL 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 351 RKQ-EERLQEQHEKLRQLAKPQSVFE-ELNNENKSTLQLEQQVKELQEKLGeEHLEAASQQNQQLTA----QLSLMALPG 424
Cdd:pfam13166 404 VEEfKSEIDEYKDKYAGLEKAINSLEkEIKNLEAEIKKLREEIKELEAQLR-DHKPGADEINKLLKAfgfgELELSFNEE 482
|
410 420
....*....|....*....|...
gi 472235303 425 EGH------GG----EHLdSEGE 437
Cdd:pfam13166 483 GKGyriirkGGsqaaETL-SEGE 504
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
105-381 |
6.31e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 105 QQKKQVEHQLEEEKKANNERQKAErELEVQIQTLIIQKEELNTDLYHMERSLRYFEEESKDLAVRLQHSLQCKGELESaL 184
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAE-EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQ-L 1638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 185 SAVIATEKKKANQLsscskahteweleQSLQDQALLKAQLTQLKESFQQLQLERDECAEHIEGERARWHQRMSKMSQEIC 264
Cdd:PTZ00121 1639 KKKEAEEKKKAEEL-------------KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE 1705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 265 TLKKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAVPSEVELQHLRKELERVAgelqsQVKNNQHISLLNRRQEERIR 344
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIA-----HLKKEEEKKAEEIRKEKEAV 1780
|
250 260 270
....*....|....*....|....*....|....*..
gi 472235303 345 EQEERLRKQEERLQEQHEKLRQLAKPQSVFEELNNEN 381
Cdd:PTZ00121 1781 IEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEG 1817
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
63-439 |
6.42e-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: 39.57 E-value: 6.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 63 REGPTSSATLKDLESPCQERAVVlDSTSVKISRLKNTIKSLKQQKkQVEHQLEEEKKANNERQKAERELevqiQTLIIQK 142
Cdd:TIGR00618 196 AELLTLRSQLLTLCTPCMPDTYH-ERKQVLEKELKHLREALQQTQ-QSHAYLTQKREAQEEQLKKQQLL----KQLRARI 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 143 EELNTDLYHME--RSLRYFEEESKDLAVRLQHSLQCKGELESALSAVIATEKKKANQLSSCSKAhteweleqsLQDQALL 220
Cdd:TIGR00618 270 EELRAQEAVLEetQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAH---------VKQQSSI 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 221 KAQLTQLKESFQQLQLERDEcaehiEGERARWHQRMSKMSQEICTLKKEkQQDMRRVEELERSLSKLKNQMAEPLPPEPP 300
Cdd:TIGR00618 341 EEQRRLLQTLHSQEIHIRDA-----HEVATSIREISCQQHTLTQHIHTL-QQQKTTLTQKLQSLCKELDILQREQATIDT 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 301 AVPSEVELQhlrKELERVAGELQSQVKNNQHISLLNRRQEERIREQEERLRKQEERLQEQHEKLRQLakpqsvfEELNNE 380
Cdd:TIGR00618 415 RTSAFRDLQ---GQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTK-------EQIHLQ 484
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 472235303 381 NKSTLQLEQQVKELQEKLGEEHLEAASQQNQQLTAQLSLMALPGEGHGGEHLDSEGEEA 439
Cdd:TIGR00618 485 ETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETS 543
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
161-418 |
6.75e-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: 39.36 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 161 EESKDLAVRLQHSLQCKGELESALSAVIATEKKKANQLSSCSK--AHTEWELEQSLQDQALLKAQLTQLKESFQQLQLER 238
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERriAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 239 DECAEHIeGERARWHQRMSKMSQEICTLKKEKQQDMRRVEELERSLSK-LKNQMAEPLPPEPPAVPSEVELQHLRKELER 317
Cdd:COG4942 100 EAQKEEL-AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPaRREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 318 VAGELQSQvknnqhisllnrrqeerireqeerLRKQEERLQEQHEKLRQLAKpqsvfeELNNENKSTLQLEQQVKELQEK 397
Cdd:COG4942 179 LLAELEEE------------------------RAALEALKAERQKLLARLEK------ELAELAAELAELQQEAEELEAL 228
|
250 260
....*....|....*....|.
gi 472235303 398 LGEEHLEAASQQNQQLTAQLS 418
Cdd:COG4942 229 IARLEAEAAAAAERTPAAGFA 249
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
86-269 |
8.86e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.04 E-value: 8.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 86 LDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNerqkaerELEVQIQTLIIQKEELNTDLYHMERSLRYFEEESKD 165
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYN-------ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 166 LAVRLQHSLQCKGELE---------------SALSAVIATEKKKANQLSSCSK--AHTEWELEQSLQDQALLKAQLTQLK 228
Cdd:COG3883 91 RARALYRSGGSVSYLDvllgsesfsdfldrlSALSKIADADADLLEELKADKAelEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 472235303 229 ESFQQLQLERDECAEHIEGERARWHQRMSKMSQEICTLKKE 269
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
65-240 |
9.03e-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: 38.59 E-value: 9.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 65 GPTSSATLKDLESPCQERavvlDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQkaeRELEVQIQTLIIQKEE 144
Cdd:pfam09787 39 LDSSTALTLELEELRQER----DLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQL---QELEEQLATERSARRE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472235303 145 LNTDLYHMERSLRYFEEESKDLAVRLQHSLQckgELESALSaviatekKKANQLSSCSKAHT-EWELEQSL--------Q 215
Cdd:pfam09787 112 AEAELERLQEELRYLEEELRRSKATLQSRIK---DREAEIE-------KLRNQLTSKSQSSSsQSELENRLhqltetliQ 181
|
170 180
....*....|....*....|....*
gi 472235303 216 DQALLKAqLTQLKESFqQLQLERDE 240
Cdd:pfam09787 182 KQTMLEA-LSTEKNSL-VLQLERME 204
|
|
| |
