|
Name |
Accession |
Description |
Interval |
E-value |
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
103-295 |
1.92e-73 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 235.57 E-value: 1.92e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 103 VTKRVLSARLLKINELQNEVSELQVKLAQLLKENKALKSLQYRQEKALNKFEDAENEISQLIHRHNNEITALKERLRKSQ 182
Cdd:pfam15619 1 VTQRVLSARLHKIKELQNELAELQSKLEELRKENRLLKRLQKRQEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 183 EKERATEKRVKETEGELFRTKFSLQKLKKISEARHLPERDDLAKKLVSAELKLDDTERKIKELSKNLELSTNSFQRQLLA 262
Cdd:pfam15619 81 EKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAA 160
|
170 180 190
....*....|....*....|....*....|...
gi 1907200902 263 ERKRAFEAYDENKVLQKELQRLHHKLKEKEKEL 295
Cdd:pfam15619 161 EKKKHKEAQEEVKILQEEIERLQQKLKEKEREL 193
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
107-319 |
6.73e-12 |
|
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: 67.87 E-value: 6.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 107 VLSARLLKINELQNEVSELQVKLAQLLKENKALKSLQYRQEKALNKFEDAENEISQLIHRHNNEITALKERLRKSQEKER 186
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 187 ATEKRVKETEGELFRTKFSLQKLKKISEARHLPERDDLAKKLVSAEL---KLDDTERKIKELSKNLELSTNSfQRQLLAE 263
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYlkyLAPARREQAEELRADLAELAAL-RAELEAE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907200902 264 RKRAFEAYDENKVLQKELQRLhhkLKEKEKELdikniyaNRLPKSSPKKEKEIERK 319
Cdd:COG4942 173 RAELEALLAELEEERAALEAL---KAERQKLL-------ARLEKELAELAAELAEL 218
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
112-296 |
1.54e-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: 58.14 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 112 LLKINELQNEVSELQVKLAQLLKENKALKSLQYRQEKALNKFEDAENEISQLIHR-------HNNEITALKERLRKSQEK 184
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEElqkelyaLANEISRLEQQKQILRER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 185 ERATEKRVKETEGELFRTKFSLQKLKKISEARHlPERDDLAKKLVSAELKLDdterKIKELSKNLELSTNSFQRQLLAER 264
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELE-EKLEELKEELESLEAELE----ELEAELEELESRLEELEEQLETLR 385
|
170 180 190
....*....|....*....|....*....|..
gi 1907200902 265 KRAFEAYDENKVLQKELQRLHHKLKEKEKELD 296
Cdd:TIGR02168 386 SKVAQLELQIASLNNEIERLEARLERLEDRRE 417
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
108-317 |
3.74e-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: 56.99 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 108 LSARLLKINELQNEVSELQVKLAQLLKENKALKSLQYRQEKALNKFEDAENEISQLIHRHNNEITALKERLRKSQEKERA 187
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 188 TEKRVKETEGELFRTKFSLQKLKKISEaRHLPERDDLAKKLVSAELKLDDTERKIKELSKNLE-LSTNSFQ--RQLLAER 264
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLE-ELKEELESLEAELEELEAELEELESRLEELEEQLEtLRSKVAQleLQIASLN 399
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907200902 265 KRAFEAYDENKVLQKELQRLHHKLKEKEKELDIKNIyaNRLPKSSPKKEKEIE 317
Cdd:TIGR02168 400 NEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL--KELQAELEELEEELE 450
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
114-295 |
1.25e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 114 KINELQNEVSELQVKLAQLLKENKALKSLQYRQEKALN----KFEDAENEISQLIhrhnNEITALKERLRKSQEKERATE 189
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEeaqaEEYELLAELARLE----QDIARLEERRRELEERLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 190 KRVKETEGELFRTKFSLQKLKKiSEARHLPERDDLAKKLVSAELKLDDTERKIKELSKNLElstnSFQRQLLAERKRAFE 269
Cdd:COG1196 323 EELAELEEELEELEEELEELEE-ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE----ELAEELLEALRAAAE 397
|
170 180
....*....|....*....|....*.
gi 1907200902 270 AYDENKVLQKELQRLHHKLKEKEKEL 295
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEEL 423
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
111-301 |
3.22e-07 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 53.78 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 111 RLLKINELQNEVSELQVKLAQLLKENKALKSLQYRQEK---------ALNKFEDAENEISQLIhrhnNEITALKERLRKS 181
Cdd:PRK05771 44 RLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVksleelikdVEEELEKIEKEIKELE----EEISELENEIKEL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 182 QEKERATE--KRVKETEGELFRTKFSLQKLKKISE--ARHLPERDDLAKKLVSAELKLDDT------ERKIKELSKnlEL 251
Cdd:PRK05771 120 EQEIERLEpwGNFDLDLSLLLGFKYVSVFVGTVPEdkLEELKLESDVENVEYISTDKGYVYvvvvvlKELSDEVEE--EL 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907200902 252 STNSFQRQLLAERKRAFEAY----DENKVLQKELQRLHHKLKEKEKEL--DIKNIY 301
Cdd:PRK05771 198 KKLGFERLELEEEGTPSELIreikEELEEIEKERESLLEELKELAKKYleELLALY 253
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
108-421 |
7.61e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 7.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 108 LSARLLKINELQNEVSELQVKLAQLLKENKALKSLQYRQEKALNKFEDAENEISQLIH---RHNNEITALKERLRKSQEK 184
Cdd:COG4913 656 YSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGeigRLEKELEQAEEELDELQDR 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 185 ERATEKRVKETEGELFRTKFSLQKLKKIsearhlpeRDDLAKKLVSaelKLDDTERKIKELSKNLELSTNSFQRQ---LL 261
Cdd:COG4913 736 LEAAEDLARLELRALLEERFAAALGDAV--------ERELRENLEE---RIDALRARLNRAEEELERAMRAFNREwpaET 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 262 AERKRAFEAYDenkvlqkELQRLHHKLKEkekeldikniyaNRLPKsspKKEKEIERKHVSCQSDFTDQCTK---GVQTA 338
Cdd:COG4913 805 ADLDADLESLP-------EYLALLDRLEE------------DGLPE---YEERFKELLNENSIEFVADLLSKlrrAIREI 862
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 339 ED------FELEDFPFTAQTVLCYENRWDEPEylsSYLEYQDlnkhgseMLSSVLGQEGKYDEDEdpcSAKQEA------ 406
Cdd:COG4913 863 KEridplnDSLKRIPFGPGRYLRLEARPRPDP---EVREFRQ-------ELRAVTSGASLFDEEL---SEARFAalkrli 929
|
330
....*....|....*...
gi 1907200902 407 ---RKPESEWAREELDKV 421
Cdd:COG4913 930 erlRSEEEESDRRWRARV 947
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
114-296 |
8.28e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 8.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 114 KINELQNEVSELQVKLAQLLKEnkaLKSLQYRQEKALNKFEDAENEISQLihrhNNEITALKERLRKSQEKERATEKRVK 193
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAE---LDALQAELEELNEEYNELQAELEAL----QAEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 194 ETEGELFRTKFSLQKLKKISEARHLperDDLAKKLVSAELKLDDTERKIKELsKNLELSTNSFQRQLLAERKRAFEAYDE 273
Cdd:COG3883 90 ERARALYRSGGSVSYLDVLLGSESF---SDFLDRLSALSKIADADADLLEEL-KADKAELEAKKAELEAKLAELEALKAE 165
|
170 180
....*....|....*....|...
gi 1907200902 274 NKVLQKELQRlhhKLKEKEKELD 296
Cdd:COG3883 166 LEAAKAELEA---QQAEQEALLA 185
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
114-478 |
8.99e-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: 8.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 114 KINELQNEVSELQVKLAQLLKENKALKSLQYRQEKALNKFEDAENEISQLIHRHNNEITALKERLRKSQEKERATEKRVK 193
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 194 ETEGELFRTKFSLQKLKKiSEARHLPERDDLAKKLVSAELKLDDTERKIKELSKNLELSTNSFQRQLLAERKRAFEAYDe 273
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEE-ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA- 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 274 nkvLQKELQRLHHKLKEKEKelDIKNIYANRLPKSSPKKEKEIERKHVSCQSDFTDQctkGVQTAEDfELEDFpftAQTV 353
Cdd:TIGR02168 836 ---TERRLEDLEEQIEELSE--DIESLAAEIEELEELIEELESELEALLNERASLEE---ALALLRS-ELEEL---SEEL 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 354 LCYENRWDEPEYlssylEYQDLNKHGSEMlssVLGQEG--------------KYDEDEDPCSAKQEARKPESEWAREELD 419
Cdd:TIGR02168 904 RELESKRSELRR-----ELEELREKLAQL---ELRLEGlevridnlqerlseEYSLTLEEAEALENKIEDDEEEARRRLK 975
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907200902 420 KVKGKSALLGRAEKLALE-----AGRFPTENYQ----AQSVDKFEDEAERLKTEM---LLAKLNEINKELQ 478
Cdd:TIGR02168 976 RLENKIKELGPVNLAAIEeyeelKERYDFLTAQkedlTEAKETLEEAIEEIDREArerFKDTFDQVNENFQ 1046
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
113-295 |
1.69e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 113 LKINELQNEVSELQVKLAQLLKENKALKSLQYRQEKALNKFEDAENEISQLIHRHNNEITALKERLRKSQEKERATEKRV 192
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 193 KETEGELfrtKFSLQKLKKISEARHlpERDDLAKKLVSAELKLDDTERKIKELSKNLELSTNSFQRQLLAERKRAFEAYD 272
Cdd:COG1196 354 EEAEAEL---AEAEEALLEAEAELA--EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
170 180
....*....|....*....|...
gi 1907200902 273 ENKVLQKELQRLHHKLKEKEKEL 295
Cdd:COG1196 429 ALAELEEEEEEEEEALEEAAEEE 451
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
114-318 |
3.78e-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: 50.40 E-value: 3.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 114 KINELQNEVSELQVKLAQLlkeNKALKSLQYRQEKALNKFEDAENEISQLIHRHNNEITALKErlrKSQEKERaTEKRVK 193
Cdd:TIGR04523 212 KNKSLESQISELKKQNNQL---KDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSE---KQKELEQ-NNKKIK 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 194 ETEGELFRTKFSLQKLKKISEARHLPE-RDDLA---KKLVSAELKLDDTERKIKEL----------SKNLELSTNSFQRQ 259
Cdd:TIGR04523 285 ELEKQLNQLKSEISDLNNQKEQDWNKElKSELKnqeKKLEEIQNQISQNNKIISQLneqisqlkkeLTNSESENSEKQRE 364
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907200902 260 lLAERKRAFEA--------YDENKVLQKELQRLHHKLKEKEKELDIKNIYANRLPKSSPKKEKEIER 318
Cdd:TIGR04523 365 -LEEKQNEIEKlkkenqsyKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIER 430
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
110-296 |
4.19e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 110 ARLLKINELQNEVSELQVKLAQLLKEnkaLKSLQYRQEKALNKFEDAENEISQL---IHRHNNEITALKERLRKSQEker 186
Cdd:COG1579 7 RALLDLQELDSELDRLEHRLKELPAE---LAELEDELAALEARLEAAKTELEDLekeIKRLELEIEEVEARIKKYEE--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 187 atekrvketegelfrtkfslqKLKKISEARhlpERDDLAKKLVSAELKLDDTERKIKELSKNLELSTNSFQ--RQLLAER 264
Cdd:COG1579 81 ---------------------QLGNVRNNK---EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAelEAELAEL 136
|
170 180 190
....*....|....*....|....*....|....*..
gi 1907200902 265 KRAFEAY-----DENKVLQKELQRLHHKLKEKEKELD 296
Cdd:COG1579 137 EAELEEKkaeldEELAELEAELEELEAEREELAAKIP 173
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
105-317 |
4.55e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 4.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 105 KRVLSARLLKINELQNEVSELQVKLAQLLKENKALKSLQYRQEKALNKFEDAE--NEISQLIHRHNneitalKERLRKSQ 182
Cdd:PRK03918 451 KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEqlKELEEKLKKYN------LEELEKKA 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 183 EKERATEKRVKETEGELFRTKFSLQKLKkisearhlperdDLAKKLVSAELKLDDTERKIKELSKNL-ELSTNSFQ--RQ 259
Cdd:PRK03918 525 EEYEKLKEKLIKLKGEIKSLKKELEKLE------------ELKKKLAELEKKLDELEEELAELLKELeELGFESVEelEE 592
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907200902 260 LLAERKRAFEAYDENKVLQKELQRLHHKLKEKEKELDIKNIYANRLPKSSPKKEKEIE 317
Cdd:PRK03918 593 RLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE 650
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
111-290 |
1.12e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 111 RLLKINELQNEVSELQVKLAQLlkenKALKSL--QYRQEKALNKFEDAENEISQLIHRHNNEITALKERLRKSQEKERAT 188
Cdd:COG4913 253 LLEPIRELAERYAAARERLAEL----EYLRAAlrLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 189 EKRVKETEGElfrtkfSLQKLKK-ISEA-----RHLPERDDLAKKLVSAELKLDDTERKIKELSKNLELSTNSFQRQLLA 262
Cdd:COG4913 329 EAQIRGNGGD------RLEQLEReIERLereleERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEA 402
|
170 180
....*....|....*....|....*...
gi 1907200902 263 ERKRAFEAYDENKVLQKELQRLHHKLKE 290
Cdd:COG4913 403 LEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
50-479 |
1.44e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 50 REKNPKRHLSDNQVHHPTVRKVSPKAVPSKKGIRVGFRSQSLNREPLRKDPDI-----VTKRVLSARllKINELQNEVSE 124
Cdd:PTZ00121 1249 RNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKkkadeAKKKAEEAK--KADEAKKKAEE 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 125 LQVKLAQLLKE----NKALKSLQYRQEKALNKFEDAENEISQLIHRHNNEITALKERLRKSQEKERATE--KRVKETEGE 198
Cdd:PTZ00121 1327 AKKKADAAKKKaeeaKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEakKKAEEDKKK 1406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 199 LFRTKFSLQKLKKISEARHLPE---RDDLAKKLVSAELKLDDTERKIKELSKNLELSTNSFQRQLLAERKRAFEAYDENK 275
Cdd:PTZ00121 1407 ADELKKAAAAKKKADEAKKKAEekkKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD 1486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 276 VLQKELQRLHHKLKEKEKELDIKNiYANRLPKSSPKKEKEIERKHVSCQSDFTDQCTKGVQTAEDFELEDFPFTAQTVLC 355
Cdd:PTZ00121 1487 EAKKKAEEAKKKADEAKKAAEAKK-KADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKK 1565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 356 YENRWDEPEYLSSYLEYQDLNKHGSEmlsSVLGQEGKYDEDEDPCSAKQEARKPESEWAREELDKVKGKSALLGRAEKLA 435
Cdd:PTZ00121 1566 AEEAKKAEEDKNMALRKAEEAKKAEE---ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKE 1642
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1907200902 436 LEAGRFPTENYQAQSVDKFEDEAERLKTEMLLAKLNEINKELQD 479
Cdd:PTZ00121 1643 AEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED 1686
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
109-296 |
1.92e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 109 SARLLKINelQNEVSELQVKLAQLLKENKALKSLQYRQEKALNKFEDAENEISQLIHRHNnEITALKERLRKSQEKERAT 188
Cdd:COG4717 62 QGRKPELN--LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELE-KLEKLLQLLPLYQELEALE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 189 EKRVKETEGelfrtkfsLQKLKkiseaRHLPERDDLAKKLVSAELKLDDTERKIKELSKNLELSTNSFQRQLLAERKRAF 268
Cdd:COG4717 139 AELAELPER--------LEELE-----ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ 205
|
170 180
....*....|....*....|....*...
gi 1907200902 269 EAYDEnkvLQKELQRLHHKLKEKEKELD 296
Cdd:COG4717 206 QRLAE---LEEELEEAQEELEELEEELE 230
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
115-305 |
2.24e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.81 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 115 INELQNEVSELQVKLAQLLKENKALKS-LQYRQEKALNKFEDaenEISQLIHRHNNEITALKERLRKSQEKERATEKRVk 193
Cdd:pfam15921 226 LRELDTEISYLKGRIFPVEDQLEALKSeSQNKIELLLQQHQD---RIEQLISEHEVEITGLTEKASSARSQANSIQSQL- 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 194 ETEGELFRTKFSLQklkkiseARHLPERDDLAKKLVSAELKLDDT-ERKIKELSKNLELSTNsfqrQLLAERKRAFEAYD 272
Cdd:pfam15921 302 EIIQEQARNQNSMY-------MRQLSDLESTVSQLRSELREAKRMyEDKIEELEKQLVLANS----ELTEARTERDQFSQ 370
|
170 180 190
....*....|....*....|....*....|...
gi 1907200902 273 ENKVLQKELQRLHHKLKEKEKELDIKNIYANRL 305
Cdd:pfam15921 371 ESGNLDDQLQKLLADLHKREKELSLEKEQNKRL 403
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
79-317 |
2.34e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 79 KKGIRVGFRSQSL-NREPLRKDPDIVTKRVLSARLLKINELQNEVSELQVKLAQLLKENKALKSLQYRQEKALNKFEDAE 157
Cdd:COG4372 3 RLGEKVGKARLSLfGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 158 NEISQLIHRHNNEITALKERLRKSQEKERATEKRVKETEGELFRTKFSLQKLKKisearhlpERDDLAKKLVSAELKLDD 237
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEA--------QIAELQSEIAEREEELKE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 238 TERKIKELSKNLELSTNSFQRQLLAERKRAFEAYDENKVLQKELQRLHHKLKEKEKELDIKNIYANRLPKSSPKKEKEIE 317
Cdd:COG4372 155 LEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLA 234
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
117-319 |
2.83e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 117 ELQNEVSELQVKLAQLLKEnkaLKSLQYRQEKALNKFEDAENEISQLiHRHNNEITALKERLRKSQEKERATEKRVKETE 196
Cdd:PRK03918 190 NIEELIKEKEKELEEVLRE---INEISSELPELREELEKLEKEVKEL-EELKEEIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 197 GELFRTKFSLQKL-KKISEARHLPERDDLAKKLVSAELKLDDTERKIKELSKNLELSTNSFQRQL--------------- 260
Cdd:PRK03918 266 ERIEELKKEIEELeEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIkeleekeerleelkk 345
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907200902 261 --------LAERKRAFEAYDENKVLQKELQRLHHKLKEKEKEldikniYANRLPKSSPKKEKEIERK 319
Cdd:PRK03918 346 klkelekrLEELEERHELYEEAKAKKEELERLKKRLTGLTPE------KLEKELEELEKAKEEIEEE 406
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
105-199 |
3.00e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.07 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 105 KRVLSARLLKINELQNEVSELQVKLAQLLKENKALKSLQYRQEKALNKFEDAENEISQLIHRHNNEITALKERLRKSQEK 184
Cdd:COG4942 142 KYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
90
....*....|....*
gi 1907200902 185 ERATEKRVKETEGEL 199
Cdd:COG4942 222 AEELEALIARLEAEA 236
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
147-295 |
3.33e-05 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 45.28 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 147 EKALNKFEDAENEIsqlIHRHNNEITALKERLRKSQEKERATEKRVKETEGELFRTKFSLQKLKKISEA--RHLPERDDL 224
Cdd:pfam13851 7 EKAFNEIKNYYNDI---TRNNLELIKSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEElrKQLENYEKD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 225 AKKLVSAELKLDDTERKIKELSKNLELSTNSFQrQLLAER---KRAFEA--YD-------ENKVLQKELQRLHHKLKEKE 292
Cdd:pfam13851 84 KQSLKNLKARLKVLEKELKDLKWEHEVLEQRFE-KVERERdelYDKFEAaiQDvqqktglKNLLLEKKLQALGETLEKKE 162
|
...
gi 1907200902 293 KEL 295
Cdd:pfam13851 163 AQL 165
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
115-315 |
3.80e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 115 INELQNEVSELQVKLAQLLKEnkaLKSLQYRQEKALNKFEDAENEISQLIHRHNNEITALKERLRKSQEKERATEKRVKE 194
Cdd:COG1196 325 LAELEEELEELEEELEELEEE---LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 195 TEGELFRTKFSLQKLkkiseARHLPERDDLAKKLVSAELKLDDTERKIKELSKNLElstNSFQRQLLAERKRAFEAYDEN 274
Cdd:COG1196 402 LEELEEAEEALLERL-----ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA---ELEEEEEALLELLAELLEEAA 473
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907200902 275 KVLQKELQRLHHKLKEKEKELDIKNIYANRLPKSSPKKEKE 315
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
117-317 |
6.53e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 6.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 117 ELQNEVSELQVKLAQLLKENKALKSLQYRQEKALNKFEDAENEISQLIHRhnneitaLKERLRKSQEKeraTEKRVKETE 196
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKE-------LEELGFESVEE---LEERLKELE 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 197 gELFRTKFSLQKLKKISEARhLPERDDLAKKLVSAELKLDDTERKIKELSKNLELSTNSFQRQllaERKRAFEAYDEnkv 276
Cdd:PRK03918 599 -PFYNEYLELKDAEKELERE-EKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE---EYEELREEYLE--- 670
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907200902 277 LQKELQRLHHKLKEKEKELD-----IKNIYANRlpKSSPKKEKEIE 317
Cdd:PRK03918 671 LSRELAGLRAELEELEKRREeikktLEKLKEEL--EEREKAKKELE 714
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
115-319 |
6.59e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 6.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 115 INELQNEVSELQVKLAQLlKENKALKSLQYRQEKALNKFEDAENEISQLIHRHNNEITALKERLRKSQEKER---ATEKR 191
Cdd:PRK03918 268 IEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEErleELKKK 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 192 VKETEGELFRTKFSLQKLKKI----SEARHLPER------DDLAKKLVSAELKLDDTERKIKEL-SKNLELstnsfqRQL 260
Cdd:PRK03918 347 LKELEKRLEELEERHELYEEAkakkEELERLKKRltgltpEKLEKELEELEKAKEEIEEEISKItARIGEL------KKE 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907200902 261 LAERKRAFEAYDENK----VLQKELQRLHHKLKEKEKELDIKNIyanrlpKSSPKKEKEIERK 319
Cdd:PRK03918 421 IKELKKAIEELKKAKgkcpVCGRELTEEHRKELLEEYTAELKRI------EKELKEIEEKERK 477
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
114-295 |
1.63e-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: 45.06 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 114 KINELQNEVSELQVKLAQLLKENKALKSLQYRQEKalnKFEDAENEISQLihrhNNEITALKERLRKSQEKERATEKRV- 192
Cdd:TIGR02169 682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASR---KIGEIEKEIEQL----EQEEEKLKERLEELEEDLSSLEQEIe 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 193 ------KETEGELFRTKFSLQKLKKIS---EARHLPER--------DDLAKKLVSAELKLDDTERKIKELSKNLELSTNS 255
Cdd:TIGR02169 755 nvkselKELEARIEELEEDLHKLEEALndlEARLSHSRipeiqaelSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907200902 256 FQ-----RQLLAERKRAFEAYDENkvLQKELQRLHHKLKEKEKEL 295
Cdd:TIGR02169 835 IQelqeqRIDLKEQIKSIEKEIEN--LNGKKEELEEELEELEAAL 877
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
114-267 |
3.37e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 114 KINELQNEVSELQVKLAQLLKENKALKSLQyrqekalnKFEDAENEISQLIHRHNNEITALKERLRKSQEKERAtEKRVK 193
Cdd:COG4717 103 ELEELEAELEELREELEKLEKLLQLLPLYQ--------ELEALEAELAELPERLEELEERLEELRELEEELEEL-EAELA 173
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907200902 194 ETEGELFR--TKFSLQKLKKISEArhLPERDDLAKKLVSAELKLDDTERKIKELSKNLELSTNSFQRQLLAERKRA 267
Cdd:COG4717 174 ELQEELEEllEQLSLATEEELQDL--AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKE 247
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
114-295 |
3.83e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 114 KINELQNEVSELQVKLAQLLKEnkaLKSLQYRQEKALNKFEDAENEISQLIHRHNNeitaLKERLRKSQEKERATEKRVK 193
Cdd:TIGR02169 834 EIQELQEQRIDLKEQIKSIEKE---IENLNGKKEELEEELEELEAALRDLESRLGD----LKKERDELEAQLRELERKIE 906
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 194 ETEGELFRTKFSLQKLK-KISEAR-HLPERDDLAKKLVS---AELKLDDTERKIKELSKNLelstnsfqRQLLAERKRAF 268
Cdd:TIGR02169 907 ELEAQIEKKRKRLSELKaKLEALEeELSEIEDPKGEDEEipeEELSLEDVQAELQRVEEEI--------RALEPVNMLAI 978
|
170 180
....*....|....*....|....*..
gi 1907200902 269 EAYDENKVLQKELQRLHHKLKEKEKEL 295
Cdd:TIGR02169 979 QEYEEVLKRLDELKEKRAKLEEERKAI 1005
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
86-249 |
4.13e-04 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 43.50 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 86 FRSQSLNREPLRKDPdiVTKRVLSARLLKINELQnevsELQvklaqLLKENKalKSLQYRQEKALNKFEDAENEISQLIH 165
Cdd:pfam10168 544 FREEYLKKHDLAREE--IQKRVKLLKLQKEQQLQ----ELQ-----SLEEER--KSLSERAEKLAEKYEEIKDKQEKLMR 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 166 RHNNEITALKERLRKSQEKERATEKRVKETEGELFRTKFSLQKLK-KISEARHLPERDDLAKKLVSAELKlDDTERKIKE 244
Cdd:pfam10168 611 RCKKVLQRLNSQLPVLSDAEREMKKELETINEQLKHLANAIKQAKkKMNYQRYQIAKSQSIRKKSSLSLS-EKQRKTIKE 689
|
....*
gi 1907200902 245 LSKNL 249
Cdd:pfam10168 690 ILKQL 694
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
122-296 |
5.22e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 122 VSELQVKLAQLLKENKALKSLQyrqekaLNKFEDAENEISQLIHRHnNEITALKERLRKSQEKERATEKRVKETEGELFR 201
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELN------LKELKELEEELKEAEEKE-EEYAELQEELEELEEELEELEAELEELREELEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 202 TKFSLQKLKKISEARHLPER-DDLAKKLVSAELKLD---DTERKIKELSKNLELSTNSFQRQL----LAERKRAFEAYDE 273
Cdd:COG4717 121 LEKLLQLLPLYQELEALEAElAELPERLEELEERLEelrELEEELEELEAELAELQEELEELLeqlsLATEEELQDLAEE 200
|
170 180
....*....|....*....|...
gi 1907200902 274 NKVLQKELQRLHHKLKEKEKELD 296
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELE 223
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
87-318 |
5.42e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 5.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 87 RSQSLNREPLRKdpdivTKRVLSARLlkiNELQNEVSELQVKLAqllkenkalkslQYRQEkalNKFEDAENEISQLIhr 166
Cdd:COG3206 164 QNLELRREEARK-----ALEFLEEQL---PELRKELEEAEAALE------------EFRQK---NGLVDLSEEAKLLL-- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 167 hnNEITALKERLRKSQEKERATEKRVKETEGELFRTKFSLQKLKKISEARHLPER-DDLAKKLVSAELKLDDTERKIKEL 245
Cdd:COG3206 219 --QQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQlAELEAELAELSARYTPNHPDVIAL 296
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907200902 246 SKNLElstnSFQRQLLAERKRAFEAYD-ENKVLQKELQRLHHKLKEKEKELdikniyanrlpKSSPKKEKEIER 318
Cdd:COG3206 297 RAQIA----ALRAQLQQEAQRILASLEaELEALQAREASLQAQLAQLEARL-----------AELPELEAELRR 355
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
109-294 |
8.70e-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: 42.65 E-value: 8.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 109 SARLLKINELQNEV-SELQVKLAQLLKENKALKSLQ------YRQEKALNKFEDAENEISQ------LIHRHNNEITALK 175
Cdd:TIGR00618 299 IKAVTQIEQQAQRIhTELQSKMRSRAKLLMKRAAHVkqqssiEEQRRLLQTLHSQEIHIRDahevatSIREISCQQHTLT 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 176 ERLRKSQE-KERATEKrvketEGELFRTKFSLQKLKKISEARHLPERDDLAKKLVS-AELKLDDTERKIKELSknlelST 253
Cdd:TIGR00618 379 QHIHTLQQqKTTLTQK-----LQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAkKQQELQQRYAELCAAA-----IT 448
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907200902 254 NSFQRQLLAER--KRAFEAYDENKVLQKELQRLHHKLKEKEKE 294
Cdd:TIGR00618 449 CTAQCEKLEKIhlQESAQSLKEREQQLQTKEQIHLQETRKKAV 491
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
114-319 |
1.93e-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: 41.54 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 114 KINELQNEVSELQVKLAQLLKENKALKSLQYRQEKALNKFEDAENEISQLIHRHNNEITALKERLRKSQEKERATEKRVK 193
Cdd:TIGR04523 90 KLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 194 ETEGELfrTKFSLQKLKKISEArhlperDDLAKKLVSAELKLDDTERKIKElSKNLELSTNSFQRQllaerkrafeayde 273
Cdd:TIGR04523 170 ELENEL--NLLEKEKLNIQKNI------DKIKNKLLKLELLLSNLKKKIQK-NKSLESQISELKKQ-------------- 226
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907200902 274 NKVLQKELQRLHHKLKEKEKELDIKNIYANRLPKSSPKKEKEIERK 319
Cdd:TIGR04523 227 NNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK 272
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
114-321 |
2.10e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 114 KINELQNEVSELQVKLAQLLKENKALKSLQYRQEKALNKFEDAENEISQLIHRHNNEITalkerlrkSQEKERATEKRVK 193
Cdd:COG1340 72 KVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVL--------SPEEEKELVEKIK 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 194 ETEGELFRTKFSLQKLKKISEARhlperddlaKKLVSAELKLDDTERKIKELSK---NLELSTNSFQRQLLAERKRAFEA 270
Cdd:COG1340 144 ELEKELEKAKKALEKNEKLKELR---------AELKELRKEAEEIHKKIKELAEeaqELHEEMIELYKEADELRKEADEL 214
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907200902 271 YDENKVLQKELQRLHHKLKEKEKELD-----IKNIYANRLPKSSPKKEKEIERKHV 321
Cdd:COG1340 215 HKEIVEAQEKADELHEEIIELQKELRelrkeLKKLRKKQRALKREKEKEELEEKAE 270
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
114-330 |
2.11e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 114 KINELQNEVSELQVKLAQLLKENKALKSLQYRQEKALNKFEDAENEISQLIHRHNNEITALKERLRKSQEKERATEKRVK 193
Cdd:COG4372 67 ELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 194 ETEGELFRTKfslQKLKKISEARHLPERDDLAKKLVSAELKLDDTERKIKELSKNLELSTNSFQRQLLAERKRAFEAYDE 273
Cdd:COG4372 147 EREEELKELE---EQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEA 223
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907200902 274 NKVLQKELQRLHHKLKEKEKELDIKNIYANRLPKSSPKKEKEIERKHVSCQSDFTDQ 330
Cdd:COG4372 224 KDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEI 280
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
137-319 |
2.48e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 137 KALKSLQYRQEkALNKFEDAENEISQLIHRHNNEITALKERLRKSQEKERATEKRVKETEGELFR---TKFSLQKLKKIS 213
Cdd:PRK03918 169 EVIKEIKRRIE-RLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEleeLKEEIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 214 EARhLPERDDLAKKLVSAELKLDDTERKIKELSKNLELSTNSFQRQLLAERKRAF--EAYDENKVLQKELQRLHHKLKEK 291
Cdd:PRK03918 248 ESL-EGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFyeEYLDELREIEKRLSRLEEEINGI 326
|
170 180
....*....|....*....|....*...
gi 1907200902 292 EKELDIKNIYANRLPKSSpKKEKEIERK 319
Cdd:PRK03918 327 EERIKELEEKEERLEELK-KKLKELEKR 353
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
114-328 |
3.01e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 41.19 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 114 KINELQNEVSELQVKLAQLLK---ENKALKSLQyRQEKALNKFEDAENEISQLIHRHNNEITALKERLRKSQEKERATEK 190
Cdd:PTZ00108 1103 KVEKLNAELEKKEKELEKLKNttpKDMWLEDLD-KFEEALEEQEEVEEKEIAKEQRLKSKTKGKASKLRKPKLKKKEKKK 1181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 191 RVKETEGELFRTKFSLQKLKKISEARHLPERDDLAKKLVSAELKLDDTERKIKELSKNLELSTNSfqrqllaerkrafEA 270
Cdd:PTZ00108 1182 KKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSK-------------KN 1248
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907200902 271 YDENKVLQKELQRLHHKLKEKEKELDIKNIYANRLPKSSPKKEKEIERKHVSCQSDFT 328
Cdd:PTZ00108 1249 NSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKPSSPT 1306
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
94-319 |
3.10e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 94 EPLRKDPDIvtKRVLSAR----LLKINELQNEVSELQVKLAQLLKENKALKSLQYRQEKALNKFEDAENEISQLIHRHNN 169
Cdd:PTZ00121 1191 EELRKAEDA--RKAEAARkaeeERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARR 1268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 170 EITALKERLRKSQEKERATEKRVKETEGELFRTKFSLQKLKKISEARhlpERDDLAKKLVSAELKLDDTERKIKELSKNL 249
Cdd:PTZ00121 1269 QAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAK---KADEAKKKAEEAKKKADAAKKKAEEAKKAA 1345
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907200902 250 ELS---TNSFQRQLLAERKRAFEAYDENKVLQKELQRLHHKLKEKEKELDIKNIYANRLPKSSPKKEKEIERK 319
Cdd:PTZ00121 1346 EAAkaeAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK 1418
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
112-290 |
3.32e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.86 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 112 LLKINELQNEVSELQVKLAQLL--------KENKALKSLQYRQEKALNKFEDAENEISQLIHRHNNeitaLKERLRKSQE 183
Cdd:pfam05483 498 LLENKELTQEASDMTLELKKHQediinckkQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDE----VKCKLDKSEE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 184 KERATEKRVKETEGELFRTKFSLQKLKKISEARH-----LPERDDLAKKLVSA--------ELKLDDTERKIKELSKNLE 250
Cdd:pfam05483 574 NARSIEYEVLKKEKQMKILENKCNNLKKQIENKNknieeLHQENKALKKKGSAenkqlnayEIKVNKLELELASAKQKFE 653
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1907200902 251 LSTNSFQRQ----------LLAERKRAFEAYDENKVLQKEL-QRLHHKLKE 290
Cdd:pfam05483 654 EIIDNYQKEiedkkiseekLLEEVEKAKAIADEAVKLQKEIdKRCQHKIAE 704
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
142-303 |
3.75e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.46 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 142 LQYRQEKALNKFEDAENEISQLIHRHNNEITALKERLRKSQEKERATEKRVKEtegELFRTKFSLQKLKKISEARHLpER 221
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRERE---ELQREEERLVQKEEQLDARAE-KL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 222 DDLAKKLVSAELKLDDTERKIKELSKNLELS-------TNSFQRQLLAERKRAFeaydenkvLQKELQRLHHKLKEK--- 291
Cdd:PRK12705 101 DNLENQLEEREKALSARELELEELEKQLDNElyrvaglTPEQARKLLLKLLDAE--------LEEEKAQRVKKIEEEadl 172
|
170
....*....|..
gi 1907200902 292 EKELDIKNIYAN 303
Cdd:PRK12705 173 EAERKAQNILAQ 184
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
114-319 |
4.07e-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: 40.39 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 114 KINELQNEVSELQVKLAQLLKENKALKSLQYRQEKALNKFEDAENEISQLIHRHNNEITALKERLRKSQEKERATEKRVK 193
Cdd:TIGR04523 336 IISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIK 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 194 ETEGELFRTKFSLQKLKKISEARHlPERDDLAKKLVSAELKLDDTERKIKELSKNLE---LSTNSFQRQLLAERKRAFEA 270
Cdd:TIGR04523 416 KLQQEKELLEKEIERLKETIIKNN-SEIKDLTNQDSVKELIIKNLDNTRESLETQLKvlsRSINKIKQNLEQKQKELKSK 494
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1907200902 271 YDENKVLQKELQRLHHKLKEKEKELDIKNIYANRLPKSSPKKEKEIERK 319
Cdd:TIGR04523 495 EKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDL 543
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
99-226 |
5.93e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 39.33 E-value: 5.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 99 DPDIVTKRVLSA----------RLLKINELQNEVSELQVKLAQLLKENKALKSlqyRQEKALNKFEDAENEISQLihrhN 168
Cdd:COG4026 104 DVELVRKEIKNAiiraglkslqNIPEYNELREELLELKEKIDEIAKEKEKLTK---ENEELESELEELREEYKKL----R 176
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907200902 169 NEITALKERLRKSQEKERATEKRVKETEGELFRTKFSLQKLKKISEARHLPERDDLAK 226
Cdd:COG4026 177 EENSILEEEFDNIKSEYSDLKSRFEELLKKRLLEVFSLEELWKELFPEELPEEDFIYF 234
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
178-319 |
8.23e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 8.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 178 LRKSQEKERATEKRVKET-EGELFRTKFSLQKLKKISEAR----HLPERDDLAKKLVSAELKLDDTERKIKELSKNLE-- 250
Cdd:PTZ00121 1580 LRKAEEAKKAEEARIEEVmKLYEEEKKMKAEEAKKAEEAKikaeELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEen 1659
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 251 -LSTNSFQRQLLAERKRAFEAYDENKVLQKELQRLHHKLKEKEKELDIKNIYANRLPKSSPKKEKEIERK 319
Cdd:PTZ00121 1660 kIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENK 1729
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
209-320 |
9.89e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.99 E-value: 9.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 209 LKKISEARHLperddLAKKLvsAELKLDDTERKIKELSKNLELS--------TNSFQRQLlAERKRAFEAYdENKVLQKE 280
Cdd:PRK12704 25 RKKIAEAKIK-----EAEEE--AKRILEEAKKEAEAIKKEALLEakeeihklRNEFEKEL-RERRNELQKL-EKRLLQKE 95
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1907200902 281 lQRLHHK---LKEKEKELDIKNIYANRLPKSSPKKEKEIERKH 320
Cdd:PRK12704 96 -ENLDRKlelLEKREEELEKKEKELEQKQQELEKKEEELEELI 137
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
51-330 |
9.99e-03 |
|
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: 39.18 E-value: 9.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 51 EKNPKRHLSDNQVHHPTVRKVSPKAVPSKKGIRVGFRSQSLNREPLRKDPDIVTKRVLSARLLKINELQNEVSELQVKLA 130
Cdd:pfam02463 587 LKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKA 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 131 QLLKENKALKSLQYRQEKalNKFEDAENEISQlihrhNNEITALKERLRKSQEKERATEKRvketegelfrtkfsLQKLK 210
Cdd:pfam02463 667 SLSELTKELLEIQELQEK--AESELAKEEILR-----RQLEIKKKEQREKEELKKLKLEAE--------------ELLAD 725
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200902 211 KISEARHLPERDDLAKKLVSAELKLDDTERKIKELSKNLELSTNSFQRQLLAERKrafeaydENKVLQKELQRLHHKLKE 290
Cdd:pfam02463 726 RVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEER-------EKTEKLKVEEEKEEKLKA 798
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1907200902 291 KEKELDIK-----------NIYANRLPKSSPKKEKEIERKHVSCQSDFTDQ 330
Cdd:pfam02463 799 QEEELRALeeelkeeaellEEEQLLIEQEEKIKEEELEELALELKEEQKLE 849
|
|
| |
