|
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 |
6.80e-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: 135.96 E-value: 6.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 226 QLKESFQQLQLERDECAEHIEGERARWHQRMSKMLQEICTLKKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAVP-- 303
Cdd:pfam15070 1 QLMESLKQLQTERDQYAENLKEEGAVWQQKMQQLSEQVRTLREEKERSVSQVQELETSLAELKNQAAVPPAEEEQPPAgp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 304 SEVE------LQHLRKELERVAGELQSQVKNNQHISLLNRRQEERIREQEERLRKQEERLQE------------------ 359
Cdd:pfam15070 81 SEEEqrlqeeAEQLQKELEALAGQLQAQVQDNEQLSRLNQEQEQRLLELERAAERWGEQAEDrkqiledmqsdratisra 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 360 --QHEKLR-QLAKPQSVFEELNNEN---KSTLQLEQQVK--------ELQEKLGE------------------------- 400
Cdd:pfam15070 161 lsQNRELKeQLAELQNGFVKLTNENmelTSALQSEQHVKkelakklgQLQEELGElketlelksqeaqslqeqrdqylah 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 401 ------------------------------------------------------EHLEAASQQNQQLTAQLNLMALPGEG 426
Cdd:pfam15070 241 lqqyvaayqqlasekeelhkqyllqtqlmdrlqheevqgkvaaemarqelqetqERLEALTQQNQQLQAQLSLLANPGEG 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1243057543 427 HGGEHlDSEGEEAPQPMPSVPEDLESREAMSSFMDHL-----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 1243057543 593 PLLDKPTAQPIV------QDHQEHPGLGSNCCVPLFCWAWLPRRRR 632
Cdd:pfam19046 1 SPPENPTAQQIMqllpeiQNPQEHPGLGSNPCIPFFYRADENDEVK 46
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
80-416 |
1.02e-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: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 80 QERAVVLDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYF 159
Cdd:COG1196 228 ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 160 EEESKDLAVRLQHSLQckgELERALSAVIATEKKKANQLSscskahtewELEQSLQDQALLKAQLTQLKESFQQLQLERD 239
Cdd:COG1196 308 EERRRELEERLEELEE---ELAELEEELEELEEELEELEE---------ELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 240 ECAEHIEGERarwhQRMSKMLQEICTLKKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAVPSEVELQHLRKELERVA 319
Cdd:COG1196 376 EAEEELEELA----EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 320 GELQSQVKNNQHISLLNRRQEERIREQEERLRKQEERLQEQHEKLRQLAK-----PQSVFEELNNENKS----TLQLEQQ 390
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAdyegfLEGVKAALLLAGLRglagAVAVLIG 531
|
330 340
....*....|....*....|....*.
gi 1243057543 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 |
6.25e-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: 62.38 E-value: 6.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 80 QERAVVLDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYF 159
Cdd:TIGR02168 221 ELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 160 EEESKDLAVRLQHSLQCKGELERALsaviaTEKKKANQLSSCSKAHTEWELEQSLQDQALLKAQLTQLKESFQQLQLERD 239
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQL-----EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 240 ECAEHIEGERARWHQRMSKMLQ---EICTLKKEKQQDMRRVEELERSLSKL-----KNQMAEPLPPEPPAVPSEVELQHL 311
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASlnnEIERLEARLERLEDRRERLQQEIEELlkkleEAELKELQAELEELEEELEELQEE 455
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1243057543 312 RKELERVAGELQSQVKNNQHISLLNRRQEERIREQEERLRKQEERLQEQHEKLRQLAKPQSVF 374
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGL 518
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
86-291 |
3.63e-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: 52.84 E-value: 3.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 86 LDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYFEEESKD 165
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 166 LAVRLQHSLQcKGELERALSAVIATEKKKANQLSSCSKAHTEWELEQSLQDQALLKAQLTQLKESFQQLQLERDEcaehI 245
Cdd:COG4942 109 LLRALYRLGR-QPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE----L 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1243057543 246 EGERARWHQRMSKMLQEICTLKKEKQQDMRRVEELERSLSKLKNQM 291
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
86-290 |
3.25e-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: 50.45 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 86 LDSTSVKISRLKNTIKSLKQQKKQVEhqlEEEKKANNERQKAERE---LEVQIQTLIIQKEELNTDLYH----MERSLRY 158
Cdd:TIGR02169 296 IGELEAEIASLERSIAEKERELEDAE---ERLAKLEAEIDKLLAEieeLEREIEEERKRRDKLTEEYAElkeeLEDLRAE 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 159 FEEESKDLAVRLQHSLQCKGELERAlsaviateKKKANQLSSCSKAHTEwELEQSLQDQALLKAQLTQLKESFQQLQLER 238
Cdd:TIGR02169 373 LEEVDKEFAETRDELKDYREKLEKL--------KREINELKRELDRLQE-ELQRLSEELADLNAAIAGIEAKINELEEEK 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1243057543 239 DECAEHI---EGERARWHQRMSKMLQEICTLKKEKQQDMRRVEELERSLSKLKNQ 290
Cdd:TIGR02169 444 EDKALEIkkqEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQ 498
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
69-404 |
4.36e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 69 SATLKDLEspcqERAVVLDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELE------VQIQTLIIQK 142
Cdd:PRK03918 227 EKEVKELE----ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKelkekaEEYIKLSEFY 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 143 EELNTDLYHMERSLRYFEEESKDLAVRLQHSLQCKGELERALSAVIATEKKKAnqlsscskahtewELEQS---LQDQAL 219
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLE-------------ELEERhelYEEAKA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 220 LKAQLTQLKESFQQLQLER-DECAEHIEGERARWHQRMSKMLQEICTLKKEKQQDMRRVEELERSLSK------------ 286
Cdd:PRK03918 370 KKEELERLKKRLTGLTPEKlEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrelteeh 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 287 ----LKNQMAEPLPPEPPAVPSEVELQHLRKELERVAGELQSQ---VKNNQHISLLNRRQEERIREQEERLRKQEERLQE 359
Cdd:PRK03918 450 rkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKEselIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEK 529
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1243057543 360 QHEKLRQLAKPQSVF----EELNNENKSTLQLEQQVKELQEKLGEEHLE 404
Cdd:PRK03918 530 LKEKLIKLKGEIKSLkkelEKLEELKKKLAELEKKLDELEEELAELLKE 578
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
70-318 |
8.48e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 8.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 70 ATLKDLESPCQERAVVLDST---SVKISRLKNTIKSLKQQKKQVE-HQLEEEKKANNERQKAERE---LEVQIQTL---I 139
Cdd:PRK03918 469 KEIEEKERKLRKELRELEKVlkkESELIKLKELAEQLKELEEKLKkYNLEELEKKAEEYEKLKEKlikLKGEIKSLkkeL 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 140 IQKEELNTDLYHMERSLRYFEEESKDLAVRLQH-SLQCKGELERALSAViatEK--KKANQLSSCSK---------AHTE 207
Cdd:PRK03918 549 EKLEELKKKLAELEKKLDELEEELAELLKELEElGFESVEELEERLKEL---EPfyNEYLELKDAEKelereekelKKLE 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 208 WELEQSLQDQALLKAQLTQLKESFQQLQLERDEcaehieGERARWHQRMSKMLQEICTLKKEKQQDMRRVEELERSLSKL 287
Cdd:PRK03918 626 EELDKAFEELAETEKRLEELRKELEELEKKYSE------EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKL 699
|
250 260 270
....*....|....*....|....*....|.
gi 1243057543 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 |
7.71e-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: 38.97 E-value: 7.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 65 GPTSSATLKDLESPCQERavvlDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQkaeRELEVQIQTLIIQKEE 144
Cdd:pfam09787 39 LDSSTALTLELEELRQER----DLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQL---QELEEQLATERSARRE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 145 LNTDLYHMERSLRYFEEESKDLAVRLQHSLQCKG-ELERALSAViatekkKANQLSSCSKAHTEWEL----EQSLQDQAL 219
Cdd:pfam09787 112 AEAELERLQEELRYLEEELRRSKATLQSRIKDREaEIEKLRNQL------TSKSQSSSSQSELENRLhqltETLIQKQTM 185
|
170 180
....*....|....*....|.
gi 1243057543 220 LKAqLTQLKESFqQLQLERDE 240
Cdd:pfam09787 186 LEA-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 |
6.80e-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: 135.96 E-value: 6.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 226 QLKESFQQLQLERDECAEHIEGERARWHQRMSKMLQEICTLKKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAVP-- 303
Cdd:pfam15070 1 QLMESLKQLQTERDQYAENLKEEGAVWQQKMQQLSEQVRTLREEKERSVSQVQELETSLAELKNQAAVPPAEEEQPPAgp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 304 SEVE------LQHLRKELERVAGELQSQVKNNQHISLLNRRQEERIREQEERLRKQEERLQE------------------ 359
Cdd:pfam15070 81 SEEEqrlqeeAEQLQKELEALAGQLQAQVQDNEQLSRLNQEQEQRLLELERAAERWGEQAEDrkqiledmqsdratisra 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 360 --QHEKLR-QLAKPQSVFEELNNEN---KSTLQLEQQVK--------ELQEKLGE------------------------- 400
Cdd:pfam15070 161 lsQNRELKeQLAELQNGFVKLTNENmelTSALQSEQHVKkelakklgQLQEELGElketlelksqeaqslqeqrdqylah 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 401 ------------------------------------------------------EHLEAASQQNQQLTAQLNLMALPGEG 426
Cdd:pfam15070 241 lqqyvaayqqlasekeelhkqyllqtqlmdrlqheevqgkvaaemarqelqetqERLEALTQQNQQLQAQLSLLANPGEG 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1243057543 427 HGGEHlDSEGEEAPQPMPSVPEDLESREAMSSFMDHL-----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 1243057543 593 PLLDKPTAQPIV------QDHQEHPGLGSNCCVPLFCWAWLPRRRR 632
Cdd:pfam19046 1 SPPENPTAQQIMqllpeiQNPQEHPGLGSNPCIPFFYRADENDEVK 46
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
80-416 |
1.02e-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: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 80 QERAVVLDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYF 159
Cdd:COG1196 228 ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 160 EEESKDLAVRLQHSLQckgELERALSAVIATEKKKANQLSscskahtewELEQSLQDQALLKAQLTQLKESFQQLQLERD 239
Cdd:COG1196 308 EERRRELEERLEELEE---ELAELEEELEELEEELEELEE---------ELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 240 ECAEHIEGERarwhQRMSKMLQEICTLKKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAVPSEVELQHLRKELERVA 319
Cdd:COG1196 376 EAEEELEELA----EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 320 GELQSQVKNNQHISLLNRRQEERIREQEERLRKQEERLQEQHEKLRQLAK-----PQSVFEELNNENKS----TLQLEQQ 390
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAdyegfLEGVKAALLLAGLRglagAVAVLIG 531
|
330 340
....*....|....*....|....*.
gi 1243057543 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 |
6.25e-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: 62.38 E-value: 6.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 80 QERAVVLDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYF 159
Cdd:TIGR02168 221 ELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 160 EEESKDLAVRLQHSLQCKGELERALsaviaTEKKKANQLSSCSKAHTEWELEQSLQDQALLKAQLTQLKESFQQLQLERD 239
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQL-----EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 240 ECAEHIEGERARWHQRMSKMLQ---EICTLKKEKQQDMRRVEELERSLSKL-----KNQMAEPLPPEPPAVPSEVELQHL 311
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASlnnEIERLEARLERLEDRRERLQQEIEELlkkleEAELKELQAELEELEEELEELQEE 455
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1243057543 312 RKELERVAGELQSQVKNNQHISLLNRRQEERIREQEERLRKQEERLQEQHEKLRQLAKPQSVF 374
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGL 518
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
97-441 |
1.17e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.61 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 97 KNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYFEEESKDLAVRLQHSLQC 176
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 177 KGELEralsAVIATEKKKANQLSScskahtewELEQSLQDQALLKAQLTQLKESFQQLQLERDEcaehiegerarwhqrm 256
Cdd:TIGR02168 756 LTELE----AEIEELEERLEEAEE--------ELAEAEAEIEELEAQIEQLKEELKALREALDE---------------- 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 257 skmLQEICTLKKEKQQDMR-RVEELERSLSKLKNQMAEPLPPEPPAVPSEVELQHLRKELERVAGELQSQVKnnqhiSLL 335
Cdd:TIGR02168 808 ---LRAELTLLNEEAANLReRLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE-----ALL 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 336 NRrqeerireqeerLRKQEERLQEQHEKLRQLAkpqsvfEELNNENKSTLQLEQQVKELQEKLG--EEHLEAASQQNQQL 413
Cdd:TIGR02168 880 NE------------RASLEEALALLRSELEELS------EELRELESKRSELRRELEELREKLAqlELRLEGLEVRIDNL 941
|
330 340
....*....|....*....|....*....
gi 1243057543 414 TAQLN-LMALPGEGHGGEHLDSEGEEAPQ 441
Cdd:TIGR02168 942 QERLSeEYSLTLEEAEALENKIEDDEEEA 970
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
96-419 |
2.96e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 2.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 96 LKNTIKSLKQQKKQ----VEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRyfEEESKDLAVRLQ 171
Cdd:COG1196 198 LERQLEPLERQAEKaeryRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELA--ELEAELEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 172 HSlqckgELERALSAVIATEKKKANqlsscskahtewELEQSLQDQALLKAQLTQLKESFQQLQLERDECAEHIEGERAR 251
Cdd:COG1196 276 LE-----ELELELEEAQAEEYELLA------------ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 252 whqrmskmLQEictLKKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAVPSEVELQHLRKELERVAGELQSQVKNNQh 331
Cdd:COG1196 339 --------LEE---LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE- 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 332 isllnrRQEERIREQEERLRKQEERLQEQHEKLRQLAKPQSvfEELNNENKSTLQLEQQVKELQEKLGEEHLEAASQQNQ 411
Cdd:COG1196 407 ------EAEEALLERLERLEEELEELEEALAELEEEEEEEE--EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
....*...
gi 1243057543 412 QLTAQLNL 419
Cdd:COG1196 479 LAELLEEL 486
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
54-418 |
1.25e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.16 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 54 PGDSATGFHREGPTSSATLKDLESPCQERAVVLDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEV 133
Cdd:TIGR02169 651 KSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQ 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 134 QIQTLIIQKEELNTDLYHMERSLRYFEEESKDLAVRLQhslqckgELERALSAVIATE------------KKKANQLSSC 201
Cdd:TIGR02169 731 EEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIE-------ELEEDLHKLEEALndlearlshsriPEIQAELSKL 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 202 SKAHTEWE-----LEQSLQDQALLKAQLTQLKesfQQLQLERDECAEHIEGERARWHQ---RMSKMLQEICTLKKEKQQD 273
Cdd:TIGR02169 804 EEEVSRIEarlreIEQKLNRLTLEKEYLEKEI---QELQEQRIDLKEQIKSIEKEIENlngKKEELEEELEELEAALRDL 880
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 274 MRRVEELERSLSKLKNQMAEPLPPEPPAVPSEVELQHLRKELERVAGELQSQVKnnqHIsLLNRRQEERIREQEERLRKQ 353
Cdd:TIGR02169 881 ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS---EI-EDPKGEDEEIPEEELSLEDV 956
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1243057543 354 EERLQEQHEKLRQLakpqsvfEELNN----ENKSTlqlEQQVKELQEKLgeEHLEAASQQNQQLTAQLN 418
Cdd:TIGR02169 957 QAELQRVEEEIRAL-------EPVNMlaiqEYEEV---LKRLDELKEKR--AKLEEERKAILERIEEYE 1013
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
86-418 |
1.45e-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: 54.68 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 86 LDSTSVKISRLKNTIKSLKQQKKQVEHQLEeekKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYFEEESKD 165
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQLKSLERQAE---KAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 166 LAVRLQhslQCKGELERALSAVIATEKKKANQLSscskahtewELEQSLQDQALLKAQLTQLKESFQQLQLERDEcaehI 245
Cdd:TIGR02168 258 LTAELQ---ELEEKLEELRLEVSELEEEIEELQK---------ELYALANEISRLEQQKQILRERLANLERQLEE----L 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 246 EGERARWHQRMSKMLQEICTLKKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAvpsEVELQHLRKElerVAGELQSQ 325
Cdd:TIGR02168 322 EAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL---EEQLETLRSK---VAQLELQI 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 326 VKNNQHISLLnrrqeerireqeerlRKQEERLQEQHEKLRQ----------LAKPQSVFEELNNENKSTLQLEQQVKELQ 395
Cdd:TIGR02168 396 ASLNNEIERL---------------EARLERLEDRRERLQQeieellkkleEAELKELQAELEELEEELEELQEELERLE 460
|
330 340
....*....|....*....|....*
gi 1243057543 396 EKLG--EEHLEAASQQNQQLTAQLN 418
Cdd:TIGR02168 461 EALEelREELEEAEQALDAAERELA 485
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
86-291 |
3.63e-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: 52.84 E-value: 3.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 86 LDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYFEEESKD 165
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 166 LAVRLQHSLQcKGELERALSAVIATEKKKANQLSSCSKAHTEWELEQSLQDQALLKAQLTQLKESFQQLQLERDEcaehI 245
Cdd:COG4942 109 LLRALYRLGR-QPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE----L 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1243057543 246 EGERARWHQRMSKMLQEICTLKKEKQQDMRRVEELERSLSKLKNQM 291
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
67-417 |
1.86e-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: 51.17 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 67 TSSATLKDLESPCQERAVvldstsvKISRLKNTIKSLKQQKKQVEHQLEEEK----KANNERQKAERE----------LE 132
Cdd:TIGR04523 51 NKEKELKNLDKNLNKDEE-------KINNSNNKIKILEQQIKDLNDKLKKNKdkinKLNSDLSKINSEikndkeqknkLE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 133 VQIQTLIIQKEELNTDLYHMERSLRYFEEESKDLAVRLQHSLQCKGELERALSAVIATEKKKANQLSSCSKAHTEWE--- 209
Cdd:TIGR04523 124 VELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLElll 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 210 --LEQSLQDQALLKAQLTQLKESFQQLQLERDECAEHIEGERARWHQRMSKMLQEICTLKKEK----------QQDMRRV 277
Cdd:TIGR04523 204 snLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKkqlsekqkelEQNNKKI 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 278 EELERSLSKLKNQMAEPLPPEPPAVPSEV--ELQHLRKELErvagELQSQV-KNNQHISLLNrrqeerirEQEERLRKQE 354
Cdd:TIGR04523 284 KELEKQLNQLKSEISDLNNQKEQDWNKELksELKNQEKKLE----EIQNQIsQNNKIISQLN--------EQISQLKKEL 351
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1243057543 355 ERLQ-EQHEKLRQLAKPQSVFEELNNENKSTLQ----LEQQVKELQEKlgeehLEAASQQNQQLTAQL 417
Cdd:TIGR04523 352 TNSEsENSEKQRELEEKQNEIEKLKKENQSYKQeiknLESQINDLESK-----IQNQEKLNQQKDEQI 414
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
86-290 |
3.25e-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: 50.45 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 86 LDSTSVKISRLKNTIKSLKQQKKQVEhqlEEEKKANNERQKAERE---LEVQIQTLIIQKEELNTDLYH----MERSLRY 158
Cdd:TIGR02169 296 IGELEAEIASLERSIAEKERELEDAE---ERLAKLEAEIDKLLAEieeLEREIEEERKRRDKLTEEYAElkeeLEDLRAE 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 159 FEEESKDLAVRLQHSLQCKGELERAlsaviateKKKANQLSSCSKAHTEwELEQSLQDQALLKAQLTQLKESFQQLQLER 238
Cdd:TIGR02169 373 LEEVDKEFAETRDELKDYREKLEKL--------KREINELKRELDRLQE-ELQRLSEELADLNAAIAGIEAKINELEEEK 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1243057543 239 DECAEHI---EGERARWHQRMSKMLQEICTLKKEKQQDMRRVEELERSLSKLKNQ 290
Cdd:TIGR02169 444 EDKALEIkkqEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQ 498
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
85-400 |
1.40e-05 |
|
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: 48.09 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 85 VLDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYFEEESK 164
Cdd:TIGR04523 205 NLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIK 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 165 DLAVRLQhslQCKGELEralsaviATEKKKANQLSSCSKAhtewELEQSLQDQALLKAQLTQLKESFQQL-----QLERD 239
Cdd:TIGR04523 285 ELEKQLN---QLKSEIS-------DLNNQKEQDWNKELKS----ELKNQEKKLEEIQNQISQNNKIISQLneqisQLKKE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 240 ecAEHIEGERARWHQRMSKMLQEICTLKKEKQQDMRRVEELERSLS----KLKNQMAEPLPPEPPAVPSEVELQHLRKEL 315
Cdd:TIGR04523 351 --LTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINdlesKIQNQEKLNQQKDEQIKKLQQEKELLEKEI 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 316 ERVageLQSQVKNNQHISLLNRRQEERI------REQEERLRKQEERL--------QEQHEKLRQLAKPQSVFEELNNEN 381
Cdd:TIGR04523 429 ERL---KETIIKNNSEIKDLTNQDSVKEliiknlDNTRESLETQLKVLsrsinkikQNLEQKQKELKSKEKELKKLNEEK 505
|
330
....*....|....*....
gi 1243057543 382 KstlQLEQQVKELQEKLGE 400
Cdd:TIGR04523 506 K---ELEEKVKDLTKKISS 521
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
69-404 |
4.36e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 69 SATLKDLEspcqERAVVLDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELE------VQIQTLIIQK 142
Cdd:PRK03918 227 EKEVKELE----ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKelkekaEEYIKLSEFY 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 143 EELNTDLYHMERSLRYFEEESKDLAVRLQHSLQCKGELERALSAVIATEKKKAnqlsscskahtewELEQS---LQDQAL 219
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLE-------------ELEERhelYEEAKA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 220 LKAQLTQLKESFQQLQLER-DECAEHIEGERARWHQRMSKMLQEICTLKKEKQQDMRRVEELERSLSK------------ 286
Cdd:PRK03918 370 KKEELERLKKRLTGLTPEKlEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrelteeh 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 287 ----LKNQMAEPLPPEPPAVPSEVELQHLRKELERVAGELQSQ---VKNNQHISLLNRRQEERIREQEERLRKQEERLQE 359
Cdd:PRK03918 450 rkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKEselIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEK 529
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1243057543 360 QHEKLRQLAKPQSVF----EELNNENKSTLQLEQQVKELQEKLGEEHLE 404
Cdd:PRK03918 530 LKEKLIKLKGEIKSLkkelEKLEELKKKLAELEKKLDELEEELAELLKE 578
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
187-395 |
1.15e-04 |
|
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: 44.36 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 187 VIATEKKKANQLSSCSKAHTEWELEQSLQDQALLKAQLTQLKESFQQLQLERDECAEHIEGERARWHQRMSKmlqeictL 266
Cdd:pfam09787 26 LIASLKEGSGVEGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQE-------L 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 267 KKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAVPSEVE-LQHLRKELERVAGELQSQVKNNQHISLLnrrqeerire 345
Cdd:pfam09787 99 EEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSrIKDREAEIEKLRNQLTSKSQSSSSQSEL---------- 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1243057543 346 qeerlrkqEERLQEQHEKLRQlakPQSVFEELNNENKSTL----QLEQQVKELQ 395
Cdd:pfam09787 169 --------ENRLHQLTETLIQ---KQTMLEALSTEKNSLVlqleRMEQQIKELQ 211
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
91-412 |
1.18e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.44 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 91 VKISRLKNTIKSLKQQKKQVEhQLEEEKKANNERQKAERE------------LEVQIQTLIIQKEELNTDLYHMERSLRY 158
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLD-LIIDEKRQQLERLRREREkaeryqallkekREYEGYELLKEKEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 159 FEEESKDLAVRLQHSLQCKGELERALSAVIATEKKKANQLSSCSK---AHTEWELEQSLQDQALLKAQLTQLKESFQQLQ 235
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKekiGELEAEIASLERSIAEKERELEDAEERLAKLE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 236 LERDECAEHIE---GERARWHQRMSKMLQEICTLKKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAVPsevELQHLR 312
Cdd:TIGR02169 329 AEIDKLLAEIEeleREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKR---EINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 313 KELERVAGELQSQVKNNQHISLLNRRQEERIREQEERLRKQEERLQEQHEKLRQLAKPQSVFEELNNENKSTL-QLEQQV 391
Cdd:TIGR02169 406 RELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYdRVEKEL 485
|
330 340
....*....|....*....|.
gi 1243057543 392 KELQEKLGEehLEAASQQNQQ 412
Cdd:TIGR02169 486 SKLQRELAE--AEAQARASEE 504
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
103-416 |
1.23e-04 |
|
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: 45.11 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 103 LKQQKKQVEHQleeekKANNERQKAERELEVQIQTLIIQKEELntdLYHMERSlRYFEEESKDLAVRLQHSLQCKGELER 182
Cdd:pfam17380 271 LNQLLHIVQHQ-----KAVSERQQQEKFEKMEQERLRQEKEEK---AREVERR-RKLEEAEKARQAEMDRQAAIYAEQER 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 183 alsavIATEKKKanqlsscskahtewELEQSLQDQAllKAQLTQLKESFQQLQLERDECAEHIEGERARWHQRMSKMLQE 262
Cdd:pfam17380 342 -----MAMERER--------------ELERIRQEER--KRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 263 ICTLKKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAVPSEVElqhlrKELERVAgelQSQVKNNQHISLLNRRQEER 342
Cdd:pfam17380 401 ARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERA-----REMERVR---LEEQERQQQVERLRQQEEER 472
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1243057543 343 IreqeerlRKQEERLQEQHEKLRQLAKPQSVFEELNNENKSTLQLEQQVKELQEKLGEEHLEAASQQNQQLTAQ 416
Cdd:pfam17380 473 K-------RKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAE 539
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
81-413 |
1.71e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 44.96 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 81 ERAVVLDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYFE 160
Cdd:pfam02463 160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERI 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 161 EES-KDLAVRLQHSLQCKGELERALSavIATEKKKANQLSSCSKAHTEWELEQSLQDQALLKAQLTQLKesfqQLQLERD 239
Cdd:pfam02463 240 DLLqELLRDEQEEIESSKQEIEKEEE--KLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLE----RRKVDDE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 240 ECAEHIEGERARWHQRMSKMLQEICTLKKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAVPSEVELQHLRKELERVA 319
Cdd:pfam02463 314 EKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLK 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 320 GELQSQVKNNQHISLLNRRQEERIREQEERLRKQEERLQEQHEKLRQLAKPQSVFEELN-NENKSTLQLEQQVKELQEKL 398
Cdd:pfam02463 394 EEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEElEKQELKLLKDELELKKSEDL 473
|
330
....*....|....*
gi 1243057543 399 GEEHLEAASQQNQQL 413
Cdd:pfam02463 474 LKETQLVKLQEQLEL 488
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
92-411 |
2.15e-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: 44.35 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 92 KISRLKNTIKSLKQQKKQVEhqlEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYFEEESKDLAVRLQ 171
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQME---LEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 172 HSLQCKGELERALSAVIATEKKkANQLSSCSK-----------------AHTEWELEQSLQDQALLKAQLTQLKESFQQL 234
Cdd:pfam05557 80 LKKKYLEALNKKLNEKESQLAD-AREVISCLKnelselrrqiqraelelQSTNSELEELQERLDLLKAKASEAEQLRQNL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 235 QLERDECAEHIegerarwhQRMSKMLQEICT------LKKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAVPSEVEL 308
Cdd:pfam05557 159 EKQQSSLAEAE--------QRIKELEFEIQSqeqdseIVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 309 QHLRKELERVAG---ELQSQVKNNQHISLLNRRQEERIREQEERLRKQE----ERLQEQHEKLRQLAKPQSVFEELNNEN 381
Cdd:pfam05557 231 EDLKRKLEREEKyreEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEdlsrRIEQLQQREIVLKEENSSLTSSARQLE 310
|
330 340 350
....*....|....*....|....*....|
gi 1243057543 382 KSTLQLEQQVKELQEKLGEEHLEAASQQNQ 411
Cdd:pfam05557 311 KARRELEQELAQYLKKIEDLNKKLKRHKAL 340
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
86-400 |
2.42e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.24 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 86 LDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYFEEESKD 165
Cdd:TIGR04523 330 ISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQ 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 166 LAVRLQHSLQCKGELERALSAVIATEKKKANQLSSCSKAHTEWELE--------QSLQDQ-ALLKAQLTQLKESFQQLQL 236
Cdd:TIGR04523 410 KDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIiknldntrESLETQlKVLSRSINKIKQNLEQKQK 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 237 ERDECAEHI----------EGERARWHQRMSKMLQEICTLKKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAVPSE- 305
Cdd:TIGR04523 490 ELKSKEKELkklneekkelEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKe 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 306 -VELQHLRKELERVAGELQSQVKNNQHISLLNRRQEERIREQEERLRKQEERLQEQHEKLRQLAKpqSVFEELNNENKST 384
Cdd:TIGR04523 570 iEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIK--NIKSKKNKLKQEV 647
|
330
....*....|....*.
gi 1243057543 385 LQLEQQVKELQEKLGE 400
Cdd:TIGR04523 648 KQIKETIKEIRNKWPE 663
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
93-305 |
2.48e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 93 ISRLKNTIKSL-KQQKKQVEHQLEEEKKANNERQKAERELEvQIQTLIIQKEELNTDLYHMERSLRYFEEESKDL--AVR 169
Cdd:COG4717 48 LERLEKEADELfKPQGRKPELNLKELKELEEELKEAEEKEE-EYAELQEELEELEEELEELEAELEELREELEKLekLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 170 LQHSLQCKGELERALSAVIAtekkkanqlsscskahtewELEQSLQDQALLKAQLTQLKESFQQLQLERDECAEHIEGER 249
Cdd:COG4717 127 LLPLYQELEALEAELAELPE-------------------RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLS 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1243057543 250 ARWHQRMSKMLQEICTLKKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAVPSE 305
Cdd:COG4717 188 LATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| 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 1243057543 95 RLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQ----KEELNTDLYHMERSLRYFEEESK--DLAV 168
Cdd:TIGR00618 532 RGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCdnrsKEDIPNLQNITVRLQDLTEKLSEaeDMLA 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 169 RLQHSLQCKGELERALSAVIATEKKKANQLSSCSKAHTEWELEQSLQDQALLKAQLTQLKESFQQLQLERDECAEHIEGE 248
Cdd:TIGR00618 612 CEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQ 691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 249 RARWHQRMSKMLQEICTLKKEKQQDMRRVEELERSLSKLKNQMaepLPPEPPAVPSEVELQHLRKELERvAGELQSQVKN 328
Cdd:TIGR00618 692 LTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDL---AAREDALNQSLKELMHQARTVLK-ARTEAHFNNN 767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 329 NQHISLLNRRQEERIREQEERLRKQ--EERLQEQHEKLRQLAKPQSVFEELNNENKSTL-----QLEQQVKELQEKLGE- 400
Cdd:TIGR00618 768 EEVTAALQTGAELSHLAAEIQFFNRlrEEDTHLLKTLEAEIGQEIPSDEDILNLQCETLvqeeeQFLSRLEEKSATLGEi 847
|
330 340
....*....|....*....|
gi 1243057543 401 ----EHLEAASQQNQQLTAQ 416
Cdd:TIGR00618 848 thqlLKYEECSKQLAQLTQE 867
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
70-318 |
8.48e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 8.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 70 ATLKDLESPCQERAVVLDST---SVKISRLKNTIKSLKQQKKQVE-HQLEEEKKANNERQKAERE---LEVQIQTL---I 139
Cdd:PRK03918 469 KEIEEKERKLRKELRELEKVlkkESELIKLKELAEQLKELEEKLKkYNLEELEKKAEEYEKLKEKlikLKGEIKSLkkeL 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 140 IQKEELNTDLYHMERSLRYFEEESKDLAVRLQH-SLQCKGELERALSAViatEK--KKANQLSSCSK---------AHTE 207
Cdd:PRK03918 549 EKLEELKKKLAELEKKLDELEEELAELLKELEElGFESVEELEERLKEL---EPfyNEYLELKDAEKelereekelKKLE 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 208 WELEQSLQDQALLKAQLTQLKESFQQLQLERDEcaehieGERARWHQRMSKMLQEICTLKKEKQQDMRRVEELERSLSKL 287
Cdd:PRK03918 626 EELDKAFEELAETEKRLEELRKELEELEKKYSE------EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKL 699
|
250 260 270
....*....|....*....|....*....|.
gi 1243057543 288 KNQMAEPLPPEPpavpsevELQHLRKELERV 318
Cdd:PRK03918 700 KEELEEREKAKK-------ELEKLEKALERV 723
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
92-505 |
1.20e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 92 KISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAErelEVQIQTLIIQK-EELNTDLYHMERSlryfeEESKDLAVRL 170
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD---ELKKAAAAKKKaDEAKKKAEEKKKA-----DEAKKKAEEA 1443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 171 QHSLQCKGELERALSA----VIATEKKKANQLSSCSKAHTEWELEQSLQDQALLKAQLTQLKESFQQLQLERDECAEHIE 246
Cdd:PTZ00121 1444 KKADEAKKKAEEAKKAeeakKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKK 1523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 247 GERARWHQRMSKMLQEICTLKKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAVPSEVELqhLRKELERVAGELQSQV 326
Cdd:PTZ00121 1524 ADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEE--AKKAEEARIEEVMKLY 1601
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 327 KNNQHISLLNRRQEERIREQEERLRKQEERLQEQHEKLRQLAKPQSVFEELNNENKSTLQLEQQVKELQEKLGEEHLEAA 406
Cdd:PTZ00121 1602 EEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAK 1681
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 407 SQQNQQLTAQLNLMALPGEGHGGEHLDSEGEEAPQPMPSVPEDLESREAMSsfmDHLKEKADlSELVKKQELRFiqywQE 486
Cdd:PTZ00121 1682 KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKA---EEAKKEAE-EDKKKAEEAKK----DE 1753
|
410
....*....|....*....
gi 1243057543 487 RCHQKIHHLLSEPGGRAKD 505
Cdd:PTZ00121 1754 EEKKKIAHLKKEEEKKAEE 1772
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
92-418 |
1.57e-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: 41.58 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 92 KISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELntdlyhmERSLRYFEEESKDLAVRLQ 171
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL-------REALDELRAELTLLNEEAA 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 172 HSLQCKGELERALSAviatekkkanqlsscskahTEWELEQSLQDQALLKAQLTQLKESFQQLQLERDEcaehIEGERAR 251
Cdd:TIGR02168 821 NLRERLESLERRIAA-------------------TERRLEDLEEQIEELSEDIESLAAEIEELEELIEE----LESELEA 877
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 252 WHQRMSKMLQEICTLKKEKQQDMRRVEELERSLSKLKNQMAeplppeppavpsevELQHLRKELERVAGELQSQVKNNQh 331
Cdd:TIGR02168 878 LLNERASLEEALALLRSELEELSEELRELESKRSELRRELE--------------ELREKLAQLELRLEGLEVRIDNLQ- 942
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 332 iSLLNRRQEERIREQEERLRKQEERLQEQHEKLRQLakpQSVFEELNNENKSTLQLEQQVKELQEKLGEEH--LEAASQQ 409
Cdd:TIGR02168 943 -ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRL---ENKIKELGPVNLAAIEEYEELKERYDFLTAQKedLTEAKET 1018
|
....*....
gi 1243057543 410 NQQLTAQLN 418
Cdd:TIGR02168 1019 LEEAIEEID 1027
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
72-251 |
3.15e-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: 40.81 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 72 LKDLESPCQERAVVLDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYH 151
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 152 MERS-------LRYFEEESKDLAVRLQHSLQCKGELERALSaviatekKKANQLSSCSKAHTEWELEQSLQDQALLKAQL 224
Cdd:TIGR02168 391 LELQiaslnneIERLEARLERLEDRRERLQQEIEELLKKLE-------EAELKELQAELEELEEELEELQEELERLEEAL 463
|
170 180
....*....|....*....|....*..
gi 1243057543 225 TQLKESFQQLQLERDECAEHIEGERAR 251
Cdd:TIGR02168 464 EELREELEEAEQALDAAERELAQLQAR 490
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
87-316 |
3.18e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 87 DSTSVKISRLKNTIKSLKQQKKQVEHQLEE-EKKANNERQKAE-RELEVQIQTLIIQKEELNTDLyhmerslryfeeesk 164
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEaEAALEEFRQKNGlVDLSEEAKLLLQQLSELESQL--------------- 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 165 dLAVRLQHSlqckgELERALSAVIATEKKKANQLSSCSKAHTEWELEQSLQDqalLKAQLTQLKESFQ----QLQLERDE 240
Cdd:COG3206 229 -AEARAELA-----EAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAE---LEAELAELSARYTpnhpDVIALRAQ 299
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1243057543 241 caehIEGERARWHQRMSKMLQEictLKKEKQQDMRRVEELERSLSKLKNQMAEPLPPeppavpsEVELQHLRKELE 316
Cdd:COG3206 300 ----IAALRAQLQQEAQRILAS---LEAELEALQAREASLQAQLAQLEARLAELPEL-------EAELRRLEREVE 361
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
92-280 |
4.32e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 92 KISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTL-IIQKEELNTDLYHMERSLryfeEESKDLAVRL 170
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLEREL----EERERRRARL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 171 QHSLqckgeleRALSAVIATEKKKANQLSSCSKAHteweLEQSLQDQALLKAQLTQLKESFQQLQLERDECAEHIEGERA 250
Cdd:COG4913 365 EALL-------AALGLPLPASAEEFAALRAEAAAL----LEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
170 180 190
....*....|....*....|....*....|...
gi 1243057543 251 R---WHQRMSKMLQEICTLKKEKQQDMRRVEEL 280
Cdd:COG4913 434 RksnIPARLLALRDALAEALGLDEAELPFVGEL 466
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
92-475 |
4.57e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 92 KISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIqkEELNTDLYHMERSLRYFEEESKDLAVRLQ 171
Cdd:PRK03918 406 EISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELL--EEYTAELKRIEKELKEIEEKERKLRKELR 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 172 hslqcKGELERALSAVIATEKKKANQLSscskahtewELEQSLQDQALLKaqLTQLKESFQQLQLERDECAEHIEGerar 251
Cdd:PRK03918 484 -----ELEKVLKKESELIKLKELAEQLK---------ELEEKLKKYNLEE--LEKKAEEYEKLKEKLIKLKGEIKS---- 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 252 whqrMSKMLQEICTLKKEKQQDMRRVEELERSLSKLKNQMAEPLPPeppavpSEVELQHLRKELERVagelqsqvkNNQH 331
Cdd:PRK03918 544 ----LKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFE------SVEELEERLKELEPF---------YNEY 604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 332 ISLLNRRQEerireqeerLRKQEERLQEQHEKLRQlakpqsVFEELNNENKSTLQLEQQVKELQEKLGEEHLEAASQQNQ 411
Cdd:PRK03918 605 LELKDAEKE---------LEREEKELKKLEEELDK------AFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYL 669
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1243057543 412 QLTaqlnlMALPGEGHGGEHLDSEGEEAPQPMPSVPEDLESREAMSSFMDHL-KEKADLSELVKK 475
Cdd:PRK03918 670 ELS-----RELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLeKALERVEELREK 729
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
65-240 |
7.71e-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: 38.97 E-value: 7.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 65 GPTSSATLKDLESPCQERavvlDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQkaeRELEVQIQTLIIQKEE 144
Cdd:pfam09787 39 LDSSTALTLELEELRQER----DLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQL---QELEEQLATERSARRE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 145 LNTDLYHMERSLRYFEEESKDLAVRLQHSLQCKG-ELERALSAViatekkKANQLSSCSKAHTEWEL----EQSLQDQAL 219
Cdd:pfam09787 112 AEAELERLQEELRYLEEELRRSKATLQSRIKDREaEIEKLRNQL------TSKSQSSSSQSELENRLhqltETLIQKQTM 185
|
170 180
....*....|....*....|.
gi 1243057543 220 LKAqLTQLKESFqQLQLERDE 240
Cdd:pfam09787 186 LEA-LSTEKNSL-VLQLERME 204
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
216-416 |
8.89e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.12 E-value: 8.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 216 DQALLKAQLTQLKESFQQLQLERDEcAEHIEGERARWHQRMSKMLQEICTLKKEKQQDMRR------VEELERSLSKLKN 289
Cdd:PRK11281 57 EDKLVQQDLEQTLALLDKIDRQKEE-TEQLKQQLAQAPAKLRQAQAELEALKDDNDEETREtlstlsLRQLESRLAQTLD 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 290 QMAEPLPPEPPAVPSEVELQhlrKELERVAGELQSQVKNNQHI-SLLNRRQEERIRE---QEERLRKQEERLQEQHEKLR 365
Cdd:PRK11281 136 QLQNAQNDLAEYNSQLVSLQ---TQPERAQAALYANSQRLQQIrNLLKGGKVGGKALrpsQRVLLQAEQALLNAQNDLQR 212
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1243057543 366 QLAKPQSVFEELNNENKSTL-----QLEQQVKELQEKLGEEHLEAASQQNQQLTAQ 416
Cdd:PRK11281 213 KSLEGNTQLQDLLQKQRDYLtariqRLEHQLQLLQEAINSKRLTLSEKTVQEAQSQ 268
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
92-421 |
8.90e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.98 E-value: 8.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 92 KISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEvqiqtliiqkEELNTDLYHMERSLRYFEEESKDLAVRLQ 171
Cdd:COG4717 140 ELAELPERLEELEERLEELRELEEELEELEAELAELQEELE----------ELLEQLSLATEEELQDLAEELEELQQRLA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 172 hslqckgELERALSAVIATEKKKANQLSSCSKAHTEWELEQSLQDQALLKAQLTQLkESFQQLQLERDECAEHIEGERAR 251
Cdd:COG4717 210 -------ELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAAL-LALLGLGGSLLSLILTIAGVLFL 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 252 WHQRMSKMLQEICTLKKEKQQDMRRVEEL-------ERSLSKLKNQMAEPLPPEPPAVPSEVELQHLRKELERVAGELQS 324
Cdd:COG4717 282 VLGLLALLFLLLAREKASLGKEAEELQALpaleeleEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 325 QVKNNQHISLLNRRQEERIREQEERLRKQEERLQEQHEKLRQLAKPQSVFEELNNENKSTL------QLEQQVKELQEKL 398
Cdd:COG4717 362 ELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLealdeeELEEELEELEEEL 441
|
330 340
....*....|....*....|....*
gi 1243057543 399 --GEEHLEAASQQNQQLTAQLNLMA 421
Cdd:COG4717 442 eeLEEELEELREELAELEAELEQLE 466
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
97-411 |
9.21e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.98 E-value: 9.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 97 KNTIKSLKQQKKQVEhQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYF---------EEESKDLA 167
Cdd:COG4717 67 ELNLKELKELEEELK-EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLplyqelealEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 168 VRLQHSLQCKGELE------RALSAVIATEKKKANQLSSCSKAHTEWELEQSLQDQALLKAQLTQLKESFQQLQLERDEC 241
Cdd:COG4717 146 ERLEELEERLEELReleeelEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 242 AEHIEG-ERARWHQRMSKMLQEICTL---------------------------------------------KKEKQQDMR 275
Cdd:COG4717 226 EEELEQlENELEAAALEERLKEARLLlliaaallallglggsllsliltiagvlflvlgllallflllareKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057543 276 RVEEL-------ERSLSKLKNQMAEPLPPEPPAVPSEVELQHLRKELERVAGELQSQVKNNQHISLLNRRQEERIREQEE 348
Cdd:COG4717 306 ELQALpaleeleEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEE 385
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1243057543 349 RLRKQEERLQEQHEKLRQLAKPQSVFEELNNENKSTL-------------QLEQQVKELQEKLGEEHLEAASQQNQ 411
Cdd:COG4717 386 ELRAALEQAEEYQELKEELEELEEQLEELLGELEELLealdeeeleeeleELEEELEELEEELEELREELAELEAE 461
|
|
| |
