|
Name |
Accession |
Description |
Interval |
E-value |
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
10-222 |
5.54e-35 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 134.19 E-value: 5.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 10 VALPSAAFADeydTKIQQQDQKINALTSQMSDAEAKVAAIENDMVETAKQIDTLTAKKNKLSSEVSKLYSEISDLNVRIQ 89
Cdd:COG3883 6 LAAPTPAFAD---PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 90 KREVQMTKQARDVQVNGQSDSIIDAVLDADSVADAIGRVQAVSTMMSANNELLEQQKEDKATVEKKTKNVEKQIAELEAA 169
Cdd:COG3883 83 ERREELGERARALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 642976529 170 TKELNDKTESLKTLKIQQEVAKNDLEAQRSEEQGKKDGFIKQKKEAEKRLAEE 222
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1-221 |
8.97e-20 |
|
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: 90.59 E-value: 8.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 1 MVCSITLTSVALPSAAFADEYDTKIQQQDQKINALTSQMSDAEAKVAAIENDMVETAKQIDTLTAKKNKLSSEVSKLYSE 80
Cdd:COG4942 5 LLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 81 ISDLNVRIQK-------REVQMTKQARDVQVNGQSDSiIDAVLDADSVADAIGRVQAVSTMMSANNELLEQQKEDKATVE 153
Cdd:COG4942 85 LAELEKEIAElraeleaQKEELAELLRALYRLGRQPP-LALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 642976529 154 KKTKNVEKQIAELEAATKELNDKTESLKTLKIQQEVAKNDLEAQRSEEQGKKDGFIKQKKEAEKRLAE 221
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
24-222 |
1.47e-10 |
|
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: 61.09 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 24 KIQQQDQKINALTSQMSDAEAKVAAIENDMVETAKQIDTLTAKKNKLSSEVSKLYSEISDLNVRIQKREVQMT--KQARD 101
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGnvRNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 102 VQvngqsdsiidavldadsvadaigrvqavstmmSANNElLEQQKEDKATVEKKTKNVEKQIAELEAATKELNDKTESLK 181
Cdd:COG1579 91 YE--------------------------------ALQKE-IESLKRRISDLEDEILELMERIEELEEELAELEAELAELE 137
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 642976529 182 TlkiQQEVAKNDLEAQRSEEQGKKDGFIKQKKEAEKRLAEE 222
Cdd:COG1579 138 A---ELEEKKAELDEELAELEAELEELEAEREELAAKIPPE 175
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
19-221 |
1.79e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 63.12 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 19 DEYDTKIQQQDQKINALTSQMSDAEAKVAAIEND-------MVETAKQIDTLTAKKNKLSSEVSKLYSEISDLNVRIQKR 91
Cdd:TIGR04523 324 EEIQNQISQNNKIISQLNEQISQLKKELTNSESEnsekqreLEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQ 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 92 EvqmtkqardvQVNGQSDSIIDavldadsvadaigrvqavsTMMSANNELLEQQKEDKATVEKKT---KNVEKQIAELEA 168
Cdd:TIGR04523 404 E----------KLNQQKDEQIK-------------------KLQQEKELLEKEIERLKETIIKNNseiKDLTNQDSVKEL 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 169 ATKELNDKTESLKT----LKIQQEVAKNDLEAQRSEEQGKK---DGFIKQKKEAEKRLAE 221
Cdd:TIGR04523 455 IIKNLDNTRESLETqlkvLSRSINKIKQNLEQKQKELKSKEkelKKLNEEKKELEEKVKD 514
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
24-221 |
5.00e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.93 E-value: 5.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 24 KIQQQDQKINALTSQMSDAEAKVAAIENDMVETAKQIDTLTAKKNKLSSEVSKLY-------SEISDLNVRIQKREVQMT 96
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEqeienvkSELKELEARIEELEEDLH 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 97 K-------------QARDVQVNGQSDSIIDAVLDADSVADAI-GRVQAVSTMM----SANNELLEQQ---KEDKATVEKK 155
Cdd:TIGR02169 776 KleealndlearlsHSRIPEIQAELSKLEEEVSRIEARLREIeQKLNRLTLEKeyleKEIQELQEQRidlKEQIKSIEKE 855
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 642976529 156 TKNVEKQIAELEAATKELndkteslktlkiqqEVAKNDLEAQRSEEQGKKDGFIKQKKEAEKRLAE 221
Cdd:TIGR02169 856 IENLNGKKEELEEELEEL--------------EAALRDLESRLGDLKKERDELEAQLRELERKIEE 907
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
24-222 |
2.74e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 24 KIQQQDQKINALTSQMSDAEAKVAAIENDMVETAKQIDTLTAKKNKLSSEVSKLYSEISDLNVRIQKrevqmtKQARDVQ 103
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEE------AQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 104 VNGQsdsiidavldadsVADAIGRVQAVSTMMSANNELLEQQKEDKATVEKKTKNVEKQIAELEAATKELNDKTESLKTL 183
Cdd:COG1196 293 LLAE-------------LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
|
170 180 190
....*....|....*....|....*....|....*....
gi 642976529 184 KIQQEVAKNDLEAQRSEEQGKKDGFIKQKKEAEKRLAEE 222
Cdd:COG1196 360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
25-195 |
1.63e-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: 53.91 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 25 IQQQDQKINALTSQMSDAEAKVAAIENDMVETAKQIDTLTAKKNKLSSEVSKLYSEISDLNVRIQK---REVQMTKQARD 101
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANlreRLESLERRIAA 835
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 102 VQVNGQ--SDSIIDAVLDADSVADAIGR-----------VQAVSTMMSANNELLEQQKEDKATVEKKTKNVEKQIAELEA 168
Cdd:TIGR02168 836 TERRLEdlEEQIEELSEDIESLAAEIEEleelieeleseLEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915
|
170 180
....*....|....*....|....*..
gi 642976529 169 ATKELNDKtesLKTLKIQQEVAKNDLE 195
Cdd:TIGR02168 916 ELEELREK---LAQLELRLEGLEVRID 939
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
19-213 |
2.87e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.10 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 19 DEYDTKIQQQDQKINALTSQMSDAEAKVAAIENDMVETAKQIDTLTAKKNKLSSEVSKLYSEISDLNVRIQKREVQMTKq 98
Cdd:TIGR04523 457 KNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE- 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 99 aRDVQVNGQSDSII--DAVLDADSVADAI-GRVQAVSTMMSANNELLEQQKEDKATVEKKTKNVEKQIAELEAATKELND 175
Cdd:TIGR04523 536 -KESKISDLEDELNkdDFELKKENLEKEIdEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISS 614
|
170 180 190
....*....|....*....|....*....|....*...
gi 642976529 176 KTESLKTLKIQQEvaknDLEAQRSEEQGKKDGFIKQKK 213
Cdd:TIGR04523 615 LEKELEKAKKENE----KLSSIIKNIKSKKNKLKQEVK 648
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
20-221 |
3.34e-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: 53.14 E-value: 3.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 20 EYDTKIQQQDQKINALTSQMSDAEAKVAAIENDMVETAKQIDTLTAKKNKLSSEVSKLYSEISDLNVRIQKREVQMTKQA 99
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 100 RDVqvngqsdsiidavldadsvADAIGRVQAVSTMMSANNELLEQQKEDKATVEKKTKNVEKQIAELEAATKELNDKTES 179
Cdd:TIGR02168 754 KEL-------------------TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL 814
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 642976529 180 LKTLKIQQEVAKNDLEAQRSEEQGKKDGFIKQKKEAEKRLAE 221
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES 856
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
37-222 |
6.13e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 6.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 37 SQMSDAEAKVAAIENDMVETAKQIDTLTAKKNKLSSEVSKLYSEISDL--------NVRIQKREVQMTKQARDVQVNGQS 108
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELeelkeeieELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 109 DSIIDAVLDADSVADAIGRV---QAVSTMMSANNELLEQQKEDKATVEKKTKNVEKQIAELEAATKELNDKTESLKTLKI 185
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELkelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKK 345
|
170 180 190
....*....|....*....|....*....|....*..
gi 642976529 186 QQEVAKNDLEaqRSEEQGKKDGFIKQKKEAEKRLAEE 222
Cdd:PRK03918 346 KLKELEKRLE--ELEERHELYEEAKAKKEELERLKKR 380
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
18-168 |
1.99e-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: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 18 ADEYDTKIQQQDQKINALTSQMSDAEAKVAAIENDMVETAKQIDTLTAKKNKLSSEVSKLYSEISDLNV---RIQKREVQ 94
Cdd:TIGR02169 338 IEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKReldRLQEELQR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 95 MTKQARDVqvNGQSDSIIDAVLDADSVADAI--------GRVQAVSTMMSANNELLEQQKEDKATVEKKTKNVEKQIAEL 166
Cdd:TIGR02169 418 LSEELADL--NAAIAGIEAKINELEEEKEDKaleikkqeWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEA 495
|
..
gi 642976529 167 EA 168
Cdd:TIGR02169 496 EA 497
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
30-217 |
4.22e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 48.37 E-value: 4.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 30 QKINALTSQMSDAEAKVAAIEndmvetaKQIDTLTAKKNKLSSEVSKLYSEISDLNVRI-----------QKR-----EV 93
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELR-------EEIEELKEKRDELNEELKELAEKRDELNAQVkelreeaqelrEKRdelneKV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 94 QMTKQARDvQVNGQSDSIIDAVLDADSVADAIGRV-QAVSTMMSANNELLEQQ-------KEDKATVEkKTKNVEKQIAE 165
Cdd:COG1340 74 KELKEERD-ELNEKLNELREELDELRKELAELNKAgGSIDKLRKEIERLEWRQqtevlspEEEKELVE-KIKELEKELEK 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 642976529 166 LEAA---TKELNDKTESLKTLKIQQEVAKNDLEAQRSEEQGKKDGFIKQKKEAEK 217
Cdd:COG1340 152 AKKAlekNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADE 206
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
19-244 |
6.15e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.90 E-value: 6.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 19 DEYDTKIQQQDQKINALTSQMSDAEAKVAAIENDMVETAKQIDTLTAKKNKLSSEVSKLYSEISDLNVRIQ------KRE 92
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQilrerlANL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 93 VQMTKQARDVQVNGQSDSIIDAvLDADSVADAIGRVQAVSTMMSA-NNELLEQQKEDKATVEKKTKNVEKQ---IAELEA 168
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELA-EELAELEEKLEELKEELESLEAeLEELEAELEELESRLEELEEQLETLrskVAQLEL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 169 ATKELNDKTESLKTLKIQQEVAKNDLEAQRSEEQGKKDGfiKQKKEAEKRLAE---------EQARQRAAAKKAEEQAAA 239
Cdd:TIGR02168 394 QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEEleeeleelqEELERLEEALEELREELE 471
|
....*
gi 642976529 240 QAQAA 244
Cdd:TIGR02168 472 EAEQA 476
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
24-222 |
9.24e-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: 48.09 E-value: 9.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 24 KIQQQDQKINALTSQMSDAEAKVAAIENDMVETAKQIDTLTAKKNKLSSEVSKLYSEISDLNvriQKREVQMTKqardvQ 103
Cdd:TIGR04523 240 EINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLN---NQKEQDWNK-----E 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 104 VNGQSDSIIDAVLDADSVADaigrvQAVSTMMSANNEL--LEQQKEDKATV-EKKTKNVEKQIAELEAATKELNDKTESL 180
Cdd:TIGR04523 312 LKSELKNQEKKLEEIQNQIS-----QNNKIISQLNEQIsqLKKELTNSESEnSEKQRELEEKQNEIEKLKKENQSYKQEI 386
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 642976529 181 KTLKIQQEVAKNDLEAQRSEEQgKKDGFIKqKKEAEKRLAEE 222
Cdd:TIGR04523 387 KNLESQINDLESKIQNQEKLNQ-QKDEQIK-KLQQEKELLEK 426
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
23-206 |
1.50e-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: 47.71 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 23 TKIQQQDQKINALTSQMSDAEAKVAAIENdmvetakQIDTLTAKKNKLSSEVSKLYSEISDLNVRIQKREVQMT-KQARD 101
Cdd:TIGR04523 204 SNLKKKIQKNKSLESQISELKKQNNQLKD-------NIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSeKQKEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 102 VQVNGQSDSIIDAVLDADSVADAIGRvQAVSTMMSANNELLEQQKEDKATVEKKTKNVEKQIAEL----EAATKELNDKT 177
Cdd:TIGR04523 277 EQNNKKIKELEKQLNQLKSEISDLNN-QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLneqiSQLKKELTNSE 355
|
170 180
....*....|....*....|....*....
gi 642976529 178 ESLKTLKIQQEVAKNDLEAQRSEEQGKKD 206
Cdd:TIGR04523 356 SENSEKQRELEEKQNEIEKLKKENQSYKQ 384
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
24-221 |
1.55e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.60 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 24 KIQQQDQKINALTSQMSDAEAK-------VAAIENDMVETAKQ------IDTLTAKKNKLSSEVSKLYSEISDLNVRI-- 88
Cdd:PRK11281 74 KIDRQKEETEQLKQQLAQAPAKlrqaqaeLEALKDDNDEETREtlstlsLRQLESRLAQTLDQLQNAQNDLAEYNSQLvs 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 89 ---QKREVQ---MTKQARDVQVNGQSDSIIDAvlDADSVADAIGRVQAVSTMMSANNEL-------------LEQQKEDK 149
Cdd:PRK11281 154 lqtQPERAQaalYANSQRLQQIRNLLKGGKVG--GKALRPSQRVLLQAEQALLNAQNDLqrkslegntqlqdLLQKQRDY 231
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 642976529 150 ATVekKTKNVEKQIAELEAAtkeLNDkteslKTLKIQQEVAKndlEAQRSEEQGKKDG--FIKQKKEAEKRLAE 221
Cdd:PRK11281 232 LTA--RIQRLEHQLQLLQEA---INS-----KRLTLSEKTVQ---EAQSQDEAARIQAnpLVAQELEINLQLSQ 292
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
57-222 |
1.57e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 57 AKQIDTLTAKKNKLSSEVSKLYSEISDLNVRIQkrevQMTKQARDVQvngQSDSIIDAVLDADSVADAIGRVQAVSTMMS 136
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELD----ALQERREALQ---RLAEYSWDEIDVASAEREIAELEAELERLD 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 137 ANNELLEQQKEDKATVEKKTKNVEKQIAELEAATKELNDKtesLKTLKIQQEVAKNDLEAQRSEEQgkkdgfIKQKKEAE 216
Cdd:COG4913 682 ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE---LEQAEEELDELQDRLEAAEDLAR------LELRALLE 752
|
....*.
gi 642976529 217 KRLAEE 222
Cdd:COG4913 753 ERFAAA 758
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
31-184 |
1.64e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.37 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 31 KINALTSQMSDAEAKVAAIENDMVETAKQIDTLTAKKNKLSSEVSKLYSEISDLNVRIQKREVQMTKQARDV----QVNG 106
Cdd:TIGR02169 862 KKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELseieDPKG 941
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 642976529 107 QSDSIIDAVLDADSVADAIGRVQA-VSTMMSANNELLEQQKEdkatVEKKTKNVEKQIAELEAATKELNDKTESLKTLK 184
Cdd:TIGR02169 942 EDEEIPEEELSLEDVQAELQRVEEeIRALEPVNMLAIQEYEE----VLKRLDELKEKRAKLEEERKAILERIEEYEKKK 1016
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
14-206 |
1.97e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.93 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 14 SAAFADEYDTKIQQQDQKINALTSQMSDAEAKVAAIENDMVETAKQIDTLTAKKNKLSSEVS------KLYSE------- 80
Cdd:PHA02562 211 NGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEqfqkviKMYEKggvcptc 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 81 ---ISDLNVRIQK---REVQMTKQARDVQvngqsDSIIDAVLDADSVADAIGRVQAVstmmsaNNELlEQQKEDKATVEK 154
Cdd:PHA02562 291 tqqISEGPDRITKikdKLKELQHSLEKLD-----TAIDELEEIMDEFNEQSKKLLEL------KNKI-STNKQSLITLVD 358
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 642976529 155 KTKNVEKQIAELEAATKelnDKTESLKTLkiQQEvaKNDLEAQRSEEQGKKD 206
Cdd:PHA02562 359 KAKKVKAAIEELQAEFV---DNAEELAKL--QDE--LDKIVKTKSELVKEKY 403
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
19-216 |
2.27e-05 |
|
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: 47.02 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 19 DEYDTKIQQQDQKINALTSQMSDAEAKVAAIENDMVETAKQIDTLTaKKNKLSSEVSK--------LYSEISDLNVRIQK 90
Cdd:pfam05483 229 EEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLE-EKTKLQDENLKeliekkdhLTKELEDIKMSLQR 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 91 REVQMTKQARDVQVngQSDSIIDAVLDADSVADAIGRVQAVSTMMSAN--------NELL--EQQKEDKATVEKK--TKN 158
Cdd:pfam05483 308 SMSTQKALEEDLQI--ATKTICQLTEEKEAQMEELNKAKAAHSFVVTEfeattcslEELLrtEQQRLEKNEDQLKiiTME 385
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 642976529 159 VEKQIAELEAATKELNDKT---ESLKTLKIQQEV---AKNDLEAQRSEEQGKKDG--FIKQKKEAE 216
Cdd:pfam05483 386 LQKKSSELEEMTKFKNNKEvelEELKKILAEDEKlldEKKQFEKIAEELKGKEQEliFLLQAREKE 451
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
19-206 |
3.83e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 19 DEYDTKIQQQDQKINALTSQMSDAEAKVAAIENDMVETAKQIDTLTAKKNKLSSEVSKLYSEISDLNVRIQKREVQMTKQ 98
Cdd:COG4372 76 EQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKEL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 99 ARDVQVNGQSDSIIDAVLDADSVADAIGRVQAVSTMMSANNELLEQQKEDKATVEKKTKNVEKQIAELEAATKELNDKTE 178
Cdd:COG4372 156 EEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLAL 235
|
170 180
....*....|....*....|....*...
gi 642976529 179 SLKTLKIQQEVAKNDLEAQRSEEQGKKD 206
Cdd:COG4372 236 SALLDALELEEDKEELLEEVILKEIEEL 263
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
16-201 |
4.72e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 4.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 16 AFADEY-----DTKIQQQDQKINALTSQMSDAEAKVAAIE---------NDMVETAKQIDTLTAKKNKLSSEVSKLYSEI 81
Cdd:COG3206 156 ALAEAYleqnlELRREEARKALEFLEEQLPELRKELEEAEaaleefrqkNGLVDLSEEAKLLLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 82 SDLNVR---IQKREVQMTKQARDVQVNGQSDSIIDAVLDADS-VADAIGR-------VQAVSTMMSANNELLEQQKE--- 147
Cdd:COG3206 236 AEAEARlaaLRAQLGSGPDALPELLQSPVIQQLRAQLAELEAeLAELSARytpnhpdVIALRAQIAALRAQLQQEAQril 315
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 642976529 148 -----DKATVEKKTKNVEKQIAELEAATKELNDKTESLKTLKIQQEVAKNDLEA--QRSEE 201
Cdd:COG3206 316 asleaELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESllQRLEE 376
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
26-222 |
9.64e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.17 E-value: 9.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 26 QQQDQKINALTSQMSDA-------EAKVAAIENDMVETAKQIDTLTAKKNKLSSEVSKLYSEISDLNVRIQKREVQMTKQ 98
Cdd:pfam01576 352 QKHTQALEELTEQLEQAkrnkanlEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAEL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 99 ARDVQvNGQS--DSIIDAVLDADSVADAIGR-VQAVSTMMSANNELLE---QQK-----------EDKATV-------EK 154
Cdd:pfam01576 432 AEKLS-KLQSelESVSSLLNEAEGKNIKLSKdVSSLESQLQDTQELLQeetRQKlnlstrlrqleDERNSLqeqleeeEE 510
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 642976529 155 KTKNVEKQIAELEAATKELNDKTE----SLKTLKIQQEVAKNDLEAQRSEEQGKKDGFIKQKKeAEKRLAEE 222
Cdd:pfam01576 511 AKRNVERQLSTLQAQLSDMKKKLEedagTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEK-TKNRLQQE 581
|
|
| CHAP |
pfam05257 |
CHAP domain; This domain corresponds to an amidase function. Many of these proteins are ... |
375-440 |
1.51e-04 |
|
CHAP domain; This domain corresponds to an amidase function. Many of these proteins are involved in cell wall metabolism of bacteria. This domain is found at the N-terminus of Swiss:P43675, where it functions as a glutathionylspermidine amidase EC:3.5.1.78. This domain is found to be the catalytic domain of PlyCA. CHAP is the amidase domain of bifunctional Escherichia coli glutathionylspermidine synthetase/amidase, and it catalyzes the hydrolysis of Gsp (glutathionylspermidine) into glutathione and spermidine.
Pssm-ID: 461605 [Multi-domain] Cd Length: 83 Bit Score: 40.48 E-value: 1.51e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 642976529 375 GINFGYGGpNSGYVASGATQVSWSNVQPGDVVQYESAYSPDSWigGvHTVLVTGVSGGSVQIVEAN 440
Cdd:pfam05257 22 GIYLGNAG-DWADAAAGAYKVGSTTPKVGDIVVFDPGGGGASY--G-HVAIVEKVNDGSITVSEQN 83
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
24-221 |
1.61e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 44.33 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 24 KIQQQDQKINALTSQMSDAEA------KVAAIENDMVETAKQIDT----LTAKKNKLSSEVSKLYSEISDLNVR---IQK 90
Cdd:pfam05483 385 ELQKKSSELEEMTKFKNNKEVeleelkKILAEDEKLLDEKKQFEKiaeeLKGKEQELIFLLQAREKEIHDLEIQltaIKT 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 91 REVQMTKQARDVQVNGQSDSIIDAVLDADS---VADAIGRVQAVSTMMSAnnelLEQQKEDKATVEKKTKNVEKQIAELE 167
Cdd:pfam05483 465 SEEHYLKEVEDLKTELEKEKLKNIELTAHCdklLLENKELTQEASDMTLE----LKKHQEDIINCKKQEERMLKQIENLE 540
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 642976529 168 AATKELNDKTESL-KTLKIQQEVAKNDLEaqRSEEQGKKDGFIKQKKEAEKRLAE 221
Cdd:pfam05483 541 EKEMNLRDELESVrEEFIQKGDEVKCKLD--KSEENARSIEYEVLKKEKQMKILE 593
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
24-221 |
1.76e-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: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 24 KIQQQDQKINALTS--------------QMSDAEAKVAAIENDMVETAKQIDTLTAKKNKLSSEVSKLYSEISDLNVRIQ 89
Cdd:TIGR04523 90 KLKKNKDKINKLNSdlskinseikndkeQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 90 KREVQMTKqardvqVNGQSDSIIDAVLDADSVADAIG-RVQAVSTMMSANNELLEQQKEDKATVEKKTKNVEKQIAELEA 168
Cdd:TIGR04523 170 ELENELNL------LEKEKLNIQKNIDKIKNKLLKLElLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINE 243
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 642976529 169 ATKELNDKTESLKTLKIQQEVAKNDLEAQRSE-EQGKkdgfiKQKKEAEKRLAE 221
Cdd:TIGR04523 244 KTTEISNTQTQLNQLKDEQNKIKKQLSEKQKElEQNN-----KKIKELEKQLNQ 292
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
23-168 |
1.78e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 23 TKIQQQDQKINALTSQMSDAEAKVAAIENDMVETAKQIDTLTAKKNKLS-SEVSKLYSEISDLNVRIQKREVQMTKQARD 101
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEAL 367
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 642976529 102 VQVNGQSdsiidAVLDADSVADAIGRVQAVSTMMSANNELLEQQ----KEDKATVEKKTKNVEKQIAELEA 168
Cdd:COG4913 368 LAALGLP-----LPASAEEFAALRAEAAALLEALEEELEALEEAlaeaEAALRDLRRELRELEAEIASLER 433
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
22-220 |
1.93e-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: 43.86 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 22 DTKIQQQDQKINALTSQMSDAEAKVAAIENDMVETAKqidtltaKKNKLSSEVSKLYSEISDLNVRIQKREVQMTKqard 101
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEE-------KINNSNNKIKILEQQIKDLNDKLKKNKDKINK---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 102 vqvngqsdsiidavLDADSVadaigrvqavstmmSANNElLEQQKEDKATVEKKTKNVEKQIAELEAATKELNDKTESLK 181
Cdd:TIGR04523 101 --------------LNSDLS--------------KINSE-IKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKE 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 642976529 182 TLKIQQEVAKNDLEAQRSEEQGKKDGFIKQKKEAEKRLA 220
Cdd:TIGR04523 152 KELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNID 190
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
32-222 |
2.97e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 32 INALTSQMSDAEAKVAAIENDMVETAKQIDTLTAKKNKLSSEVSKLYSEISDLNVRIQKREvqmtkqardvqvngqsdsi 111
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELN------------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 112 idavldadsvadaiGRVQAVSTMMSANNELLEQQKEDKATVEKKTKNVEKQIAELEAATKELNDKTESLKTLKIQQEVAK 191
Cdd:COG4372 87 --------------EQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEEL 152
|
170 180 190
....*....|....*....|....*....|.
gi 642976529 192 NDLEAQRSEEQGKKDGFIKQKKEAEKRLAEE 222
Cdd:COG4372 153 KELEEQLESLQEELAALEQELQALSEAEAEQ 183
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
20-221 |
4.17e-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: 43.09 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 20 EYDTKIQQQDQKINALTSQMSDAEAKVAAIENDMVETAKQIDTLTAKKNKLSSEVSKLYSEISDLNVRIQKREVQMTK-Q 98
Cdd:TIGR04523 451 VKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKlE 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 99 ARDVQVNGQSDSIIDAVLDADSVADAIGrvqaVSTMMSANNELLEQQKEDKATVEKKTKNVEKQIAELEAATKELNDKTE 178
Cdd:TIGR04523 531 SEKKEKESKISDLEDELNKDDFELKKEN----LEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIE 606
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 642976529 179 SL--KTLKIQQEVAKNDLEAQRSEEQGKKdgfIKQKKEAEKRLAE 221
Cdd:TIGR04523 607 EKekKISSLEKELEKAKKENEKLSSIIKN---IKSKKNKLKQEVK 648
|
|
| YkyA |
pfam10368 |
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein ... |
38-184 |
4.92e-04 |
|
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein signal and a hydrolase domain. It is similar to cell wall binding proteins and might also be recognisable by a host immune defence system. It is thus likely to belong to pathways important for pathogenicity.
Pssm-ID: 431235 [Multi-domain] Cd Length: 185 Bit Score: 41.04 E-value: 4.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 38 QMSDAEAKVAAIENDMVETAKQIDTLTAKKNKLSSEVSKL----YSEISDL----NVRIQKREVQMTK------QARDV- 102
Cdd:pfam10368 5 KIYDHLEEAVELEKPFEEQQEPLVELEKKEQELYEEIIELgmdeFDEIKKLsdeaLENVEEREELLEKekesieEAKEEf 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 103 -QVNGQSDSIIDAVL--DADSVADAIG-RVQAVSTMMSANNELLEQQKE-------DKATVEKktknVEKQI-------A 164
Cdd:pfam10368 85 kKIKEIIEEIEDEELkkEAEELIDAMEeRYEAYDELYDAYKKALELDKElyemlkdEDLTLEE----LQEQIekinesyE 160
|
170 180
....*....|....*....|
gi 642976529 165 ELEAATKELNDKTESLKTLK 184
Cdd:pfam10368 161 EVKEANEQFNEYTKQYNELK 180
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
23-214 |
5.35e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.70 E-value: 5.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 23 TKIQQQDQKINALTSQMSDAEAKVAAIENDMVETAKQIDTLTAKKNKLSSEVSKLYSEISDLNVRIQKREvQMTKQARDV 102
Cdd:TIGR04523 145 TEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNK-SLESQISEL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 103 --QVNGQSDSIidavldaDSVADAIGRVQAV-STMMSANNELLEQQKEDKATVEKKTKnvekqiaELEAATKELNDKTES 179
Cdd:TIGR04523 224 kkQNNQLKDNI-------EKKQQEINEKTTEiSNTQTQLNQLKDEQNKIKKQLSEKQK-------ELEQNNKKIKELEKQ 289
|
170 180 190
....*....|....*....|....*....|....*.
gi 642976529 180 LKTLKIQQEvaknDLEAQRSEEQGKK-DGFIKQKKE 214
Cdd:TIGR04523 290 LNQLKSEIS----DLNNQKEQDWNKElKSELKNQEK 321
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
24-221 |
5.76e-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: 42.75 E-value: 5.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 24 KIQQQDQKINALTSQMSDAEAKVAAIEndmvetaKQIDTLTAKKNKLSSEVSKLYSEISDLNVRIQK-REVQMTKQARDV 102
Cdd:TIGR02169 302 EIASLERSIAEKERELEDAEERLAKLE-------AEIDKLLAEIEELEREIEEERKRRDKLTEEYAElKEELEDLRAELE 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 103 QVNGQSDSIIDAVLDADSVADAIGR-VQAVSTMMSANNELLEQQKEDKATVEKKTKNVEKQIAELEAATKELNDK----T 177
Cdd:TIGR02169 375 EVDKEFAETRDELKDYREKLEKLKReINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEikkqE 454
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 642976529 178 ESLKTLKIQQEVAKNDLEAQRSEEQGKKDGFIKQKKEAEKRLAE 221
Cdd:TIGR02169 455 WKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQ 498
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
18-240 |
6.69e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 6.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 18 ADEYDTKIQQQDQKINALTSQMSDAEAKVAAIENDMVETAKQIDTLTAKKNKLSSEVSKLYSEISDLNVRIQKREVQMTK 97
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 98 QARDVQVNGQSDSIIDAVLDA--DSVADAIGRVQAVSTMMSANNELLEQQKEDKATVEKKTKNVEKQIAELEAATKELND 175
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERleEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 642976529 176 KTESLKTLKIQQEVAKNDLEAQRSEEQGKKDGFIKQKKEAEKRLAEEQARQRAAAKKAEEQAAAQ 240
Cdd:COG1196 478 ALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEA 542
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
26-220 |
6.90e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.47 E-value: 6.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 26 QQQDQKINALtSQMSDAEAKVAAIENDMVETAKQIDTLTAKKNKLSSEVSKLYSEISDL--------NVRIQK-REVQMT 96
Cdd:pfam01576 254 EETAQKNNAL-KKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTldttaaqqELRSKReQEVTEL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 97 KQARDVQVNGQSDSIIDAvldadsvadAIGRVQAVSTMmsanNELLEQQKEDKATVEKKTKNVEKQIAELEAATKelndk 176
Cdd:pfam01576 333 KKALEEETRSHEAQLQEM---------RQKHTQALEEL----TEQLEQAKRNKANLEKAKQALESENAELQAELR----- 394
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 642976529 177 teSLKTLKIQQEVAKNDLEAQRSEEQGKKDGFIKQKKEAEKRLA 220
Cdd:pfam01576 395 --TLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLS 436
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
18-222 |
8.29e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 8.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 18 ADEYDTKIQQQDQKINALTSQmsdAEAKVAAIENDMVETAKQIDTLTAKKNKlsSEVSKLYSEISDLNVRIQKREVQMTK 97
Cdd:PTZ00121 1317 ADEAKKKAEEAKKKADAAKKK---AEEAKKAAEAAKAEAEAAADEAEAAEEK--AEAAEKKKEEAKKKADAAKKKAEEKK 1391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 98 QARDVQVNGQSDSiidavLDADSVADAIGRVQAVSTMMSANNELLEQQKEDKATVEKKTKNVEKQIAELEAATKELNDKT 177
Cdd:PTZ00121 1392 KADEAKKKAEEDK-----KKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKA 1466
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 642976529 178 ESLKTlkiQQEVAKNDLEAQRSEEQGKKDGFIKQKKEAEKRLAEE 222
Cdd:PTZ00121 1467 EEAKK---ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA 1508
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
38-221 |
8.78e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.81 E-value: 8.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 38 QMSDAEAKVAAIENDMVETAKQIDTLTAKKNKLSS-----------EVSKLYSEISDLNVR-IQKREVQMTKQARDVQVN 105
Cdd:PRK01156 523 KIESARADLEDIKIKINELKDKHDKYEEIKNRYKSlkledldskrtSWLNALAVISLIDIEtNRSRSNEIKKQLNDLESR 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 106 GQSdsIIDAVLDADSVAD-AIGRVQAVSTMMSANNELLEQQKEDKATVEKKTKNVEKQIAEL---EAATKELNDKTESLK 181
Cdd:PRK01156 603 LQE--IEIGFPDDKSYIDkSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIdsiIPDLKEITSRINDIE 680
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 642976529 182 TLKIQQEVAKNDLEAQRSEEQGKKDGFIKQKKEAEKRLAE 221
Cdd:PRK01156 681 DNLKKSRKALDDAKANRARLESTIEILRTRINELSDRIND 720
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
27-216 |
8.85e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.08 E-value: 8.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 27 QQDQKINALTSQMSDAEAKVAAIENDMVETAKQIDTLTAKKNKLSSEV---SKLYSEISDLNVRI--------------- 88
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLqaeTELCAEAEEMRARLaarkqeleeilhele 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 89 ------QKREVQMTKQARDVQVNGQSdsiIDAVLDADSVADAIGRVQAVST-----MMSANNELLEQQKeDKATVEKKTk 157
Cdd:pfam01576 82 srleeeEERSQQLQNEKKKMQQHIQD---LEEQLDEEEAARQKLQLEKVTTeakikKLEEDILLLEDQN-SKLSKERKL- 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 642976529 158 nVEKQIAELEAATKELNDKTESLKTLKIQQEVAKNDLEAQ-RSEEQGKKD-GFIKQKKEAE 216
Cdd:pfam01576 157 -LEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERlKKEEKGRQElEKAKRKLEGE 216
|
|
| SynN |
smart00503 |
Syntaxin N-terminal domain; Three-helix domain that (in Sso1p) slows the rate of its reaction ... |
117-203 |
2.11e-03 |
|
Syntaxin N-terminal domain; Three-helix domain that (in Sso1p) slows the rate of its reaction with the SNAP-25 homologue Sec9p
Pssm-ID: 214699 [Multi-domain] Cd Length: 117 Bit Score: 38.10 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 117 DADSVADAIGRV-QAVSTMMSANNELLEQQKEDKAT----------VEKKTKNVEKQIAELEAATKEL-NDKTESLKTLK 184
Cdd:smart00503 9 KVEEIRANIQKIsQNVAELQKLHEELLTPPDADKELreklerliddIKRLAKEIRAKLKELEKENLENrASGSASDRTRK 88
|
90
....*....|....*....
gi 642976529 185 IQQEVAKNDLEAQRSEEQG 203
Cdd:smart00503 89 AQTEKLRKKFKEVMNEFQR 107
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
137-222 |
2.26e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 37.98 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 137 ANNELLEQQkEDKATVEKKTKNVEKQIAELEAATKELNDKTESLKTLKIQQEVAKNDLEAQRSEEQGKkdgfIKQKKEAE 216
Cdd:pfam20492 25 AQEELEESE-ETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQEE----IARLEEEV 99
|
....*.
gi 642976529 217 KRLAEE 222
Cdd:pfam20492 100 ERKEEE 105
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
27-206 |
2.40e-03 |
|
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: 40.49 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 27 QQDQKINALTSQMSDAEAKVAAIENDMVETAKQIDTLTAKKNKLSSEVSKLYSEISDL---------NVRIQKREVQMTK 97
Cdd:pfam15921 615 KKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLsedyevlkrNFRNKSEEMETTT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 98 QARDVQVNGQSDSIIDAVLDADSVADAIGRVQAVSTMM----SANNELLEQQKEDKATVEKKTKNVEKQIAELEaatKEL 173
Cdd:pfam15921 695 NKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMqkqiTAKRGQIDALQSKIQFLEEAMTNANKEKHFLK---EEK 771
|
170 180 190
....*....|....*....|....*....|...
gi 642976529 174 NDKTESLKTLKIQQEVAKNDLEAQRSEEQGKKD 206
Cdd:pfam15921 772 NKLSQELSTVATEKNKMAGELEVLRSQERRLKE 804
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
22-211 |
2.57e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.19 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 22 DTKIQQQDQKINALTSQMSDAE-----------AK----------VAAIENDMVETAKQIDTLTAKKNKLSSEVSKLYSE 80
Cdd:pfam10174 302 ESELLALQTKLETLTNQNSDCKqhievlkesltAKeqraailqteVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGE 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 81 ISDL-----------NVrIQKREVQMTKQARDVqvNGQSDSIIDAV--LDADSV-ADAigrvqAVSTMMSANNE---LLE 143
Cdd:pfam10174 382 IRDLkdmldvkerkiNV-LQKKIENLQEQLRDK--DKQLAGLKERVksLQTDSSnTDT-----ALTTLEEALSEkerIIE 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 642976529 144 QQKEDKatvEKKTKNVEKQIAELEAATKELNDKTESLKTLKIQQEVAKNDLEAQRSEEQG---KKDGFIKQ 211
Cdd:pfam10174 454 RLKEQR---EREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASsglKKDSKLKS 521
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
19-221 |
3.22e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.27 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 19 DEYDTKIQQQDQKINALTSQMSDAEAKVAAIENDMV-----------ETAKQIDTLTAKKNKLSSEVSKLYSEISDLN-- 85
Cdd:PRK01156 419 QDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpvcgttlgeeKSNHIINHYNEKKSRLEEKIREIEIEVKDIDek 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 86 -VRIQKREVQMTKQ------ARDVQVNGQSDSIIDAVLDADSVADAIGRV-QAVSTMMSANNELLEQQKE---------- 147
Cdd:PRK01156 499 iVDLKKRKEYLESEeinksiNEYNKIESARADLEDIKIKINELKDKHDKYeEIKNRYKSLKLEDLDSKRTswlnalavis 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 148 --DKATVEKKTKNVEKQIAELEAATKEL-----NDKTESLKTLKIQQEVAKN---------DLEAQRSEEQGKKDGFIKQ 211
Cdd:PRK01156 579 liDIETNRSRSNEIKKQLNDLESRLQEIeigfpDDKSYIDKSIREIENEANNlnnkyneiqENKILIEKLRGKIDNYKKQ 658
|
250
....*....|...
gi 642976529 212 ---KKEAEKRLAE 221
Cdd:PRK01156 659 iaeIDSIIPDLKE 671
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
146-221 |
3.39e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.81 E-value: 3.39e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 642976529 146 KEDKATVEKKTKNVEKQIAELEAATKELNDKTESLKTLKIQQEVAKNDLEAQRSEEQGKKDGFI-KQKKEAEKRLAE 221
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLeEAEKEAQQAIKE 581
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
18-222 |
3.46e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 18 ADEYDTKIQQQDQKINALTSQmsdAEAKVAAIENDMVETAKQIDTLTAKKNKLSSEVSKLYSEISDLNVRIQKREVQMTK 97
Cdd:PTZ00121 1485 ADEAKKKAEEAKKKADEAKKA---AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE 1561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 98 QARDVQVNGQSDSIIDAVLDADSVADAIGRVQAVSTMmsannELLEQQKEDKATVEKKTKNVEKQIAELEAATKELNdkt 177
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVM-----KLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKK--- 1633
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 642976529 178 eslktlKIQQEVAKNDLEAQRSEEQGKKDGFIKQKKEAEKRLAEE 222
Cdd:PTZ00121 1634 ------KVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEE 1672
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
50-222 |
3.55e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 50 ENDMVETAKQIDTLTAKKNKLSSEVSKLYSEISDLNVRIQKREVQMTKQARDV----QVNGQSDSIIDAVLDADSVADAI 125
Cdd:PTZ00121 1573 EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELkkaeEEKKKVEQLKKKEAEEKKKAEEL 1652
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 126 GRVQAVSTMMSAnnELLEQQKEDKATVEKKTKNVEKQIAELEAATKELNDKTESLKTLKIQQEVAKNDLEAQRSEEQGK- 204
Cdd:PTZ00121 1653 KKAEEENKIKAA--EEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKi 1730
|
170
....*....|....*...
gi 642976529 205 KDGFIKQKKEAEKRLAEE 222
Cdd:PTZ00121 1731 KAEEAKKEAEEDKKKAEE 1748
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
20-222 |
3.63e-03 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153280 [Multi-domain] Cd Length: 218 Bit Score: 38.88 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 20 EYDTKIQQQDQKINALTSQMSDAEAKVAAIENDMVETAKQIDTLTAKKNKLSSEVSKLYSEISDLNVRIQKREVQMTKQA 99
Cdd:cd07596 1 EEDQEFEEAKDYILKLEEQLKKLSKQAQRLVKRRRELGSALGEFGKALIKLAKCEEEVGGELGEALSKLGKAAEELSSLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 100 RDvqvngQSDSIIDAVLDadSVADAIGRVQAVSTMMSANNELLEQQKEDKATVEKKTKNVEKqiaeLEAATKELNDKTES 179
Cdd:cd07596 81 EA-----QANQELVKLLE--PLKEYLRYCQAVKETLDDRADALLTLQSLKKDLASKKAQLEK----LKAAPGIKPAKVEE 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 642976529 180 LktlkiqqevaKNDLEAQRSEEQGKKDGF--IKQKKEAE-KRLAEE 222
Cdd:cd07596 150 L----------EEELEEAESALEEARKRYeeISERLKEElKRFHEE 185
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
25-221 |
3.78e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 39.68 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 25 IQQQDQKINALTSQMSDAEAKVAAIENDMVETakqidtltakKNKLssevSKLYSEISDLNVRIQKREVQMTKQARdvqv 104
Cdd:PRK11637 63 VRQQQQQRASLLAQLKKQEEAISQASRKLRET----------QNTL----NQLNKQIDELNASIAKLEQQQAAQER---- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 105 ngqsdsIIDAVLDAdsvADAIGRVQAVSTMMS-----------ANNELLEQQKEDKATVEKKTKnvekqiAELEAATKEL 173
Cdd:PRK11637 125 ------LLAAQLDA---AFRQGEHTGLQLILSgeesqrgerilAYFGYLNQARQETIAELKQTR------EELAAQKAEL 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 642976529 174 NDKTESLKTLKIQQEVAKNDLEAQRSEEQGKKDGFIKQKKEAEKRLAE 221
Cdd:PRK11637 190 EEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSE 237
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
41-218 |
3.93e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 41 DAEAKVAAIENDMVETAKqiDTLTAKKNKLSSEVSKLYSEISDLNVRIQKREVQMTKQARDVQvngqsdsiidavldads 120
Cdd:PRK12704 46 EAKKEAEAIKKEALLEAK--EEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLE----------------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 121 vadaigrvqavstmmSANNELLEQQKEdkatVEKKTKNVEKQIAELEAATKELNDKTESLKTLkiQQEVAKNDLeAQRSE 200
Cdd:PRK12704 107 ---------------KREEELEKKEKE----LEQKQQELEKKEEELEELIEEQLQELERISGL--TAEEAKEIL-LEKVE 164
|
170 180
....*....|....*....|....*
gi 642976529 201 EQGKKDG--FIKQ-----KKEAEKR 218
Cdd:PRK12704 165 EEARHEAavLIKEieeeaKEEADKK 189
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
25-221 |
3.99e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.88 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 25 IQQQDQKINALTSQMSDAEAKVAAIENDMVETAKQIDTLTAKK-NKLSSEVSKLYS---EISDLNVRIQKREVQMTK-QA 99
Cdd:PRK01156 471 INHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEiNKSINEYNKIESaraDLEDIKIKINELKDKHDKyEE 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 100 RDVQVNGQSDSIIDA----VLDADSVADAIGrvqaVSTMMSANNELLEQQKEdkatVEKKTKNVE-----------KQIA 164
Cdd:PRK01156 551 IKNRYKSLKLEDLDSkrtsWLNALAVISLID----IETNRSRSNEIKKQLND----LESRLQEIEigfpddksyidKSIR 622
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 642976529 165 ELEAATKELNDKTESLKTLKIQQEVAKNDLEAQRsEEQGKKDGFIKQKKEAEKRLAE 221
Cdd:PRK01156 623 EIENEANNLNNKYNEIQENKILIEKLRGKIDNYK-KQIAEIDSIIPDLKEITSRIND 678
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
19-219 |
4.20e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.12 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 19 DEYDTKIQQQDQKINALTSQMSDAEAKVAAIENDMVETAKQIDTLTAKKNKLSSEVS----------------------- 75
Cdd:COG1340 46 DELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAelnkaggsidklrkeierlewrq 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 76 -----------KLYSEISDLNVRIQKREVQMTKQARDVQVNGQSDSIIDAVLDA-DSVADAIGRVQAVSTMMSANNELLE 143
Cdd:COG1340 126 qtevlspeeekELVEKIKELEKELEKAKKALEKNEKLKELRAELKELRKEAEEIhKKIKELAEEAQELHEEMIELYKEAD 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 144 QQKED----KATVEKKTKNVEKQIAELEAATKELNDKTESLKTLKIQQEVAKndleaqRSEEQGKKDgfiKQKKEAEKRL 219
Cdd:COG1340 206 ELRKEadelHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALK------REKEKEELE---EKAEEIFEKL 276
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
22-221 |
4.37e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.77 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 22 DTKIQQQDQKINALTSQMSDAEAKVAAIENDMVETAKQIDTLTAKKNKLSSEVSKLYSEISDLNVRIQKRE---VQMTKQ 98
Cdd:pfam01576 130 EAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEkgrQELEKA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 99 ARdvQVNGQSDSIIDAVLDADS-VADAIGRVQAVSTMMSANNELLEQQKEDKATVEKKTKNVEKQIAELE---------- 167
Cdd:pfam01576 210 KR--KLEGESTDLQEQIAELQAqIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQedleseraar 287
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 642976529 168 -AATKELNDKTESLKTLKIQQE------VAKNDLEAQRSEEQGKkdgfIKQKKEAEKRLAE 221
Cdd:pfam01576 288 nKAEKQRRDLGEELEALKTELEdtldttAAQQELRSKREQEVTE----LKKALEEETRSHE 344
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
41-202 |
4.42e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 39.45 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 41 DAEAKVAAIENDMVETAKQIDTLtakknklssEVSKLYSEISDLNVRIQKREVQMTK--QARDVqVNGQSDSIIDAVLDA 118
Cdd:pfam06160 234 NVDKEIQQLEEQLEENLALLENL---------ELDEAEEALEEIEERIDQLYDLLEKevDAKKY-VEKNLPEIEDYLEHA 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 119 DSVADA----IGRVQAVSTMmsANNELLEQQKEDK--ATVEKKTKNVEKQIAELEAA----TKELNDKTESLKTLKIQQE 188
Cdd:pfam06160 304 EEQNKElkeeLERVQQSYTL--NENELERVRGLEKqlEELEKRYDEIVERLEEKEVAyselQEELEEILEQLEEIEEEQE 381
|
170
....*....|....
gi 642976529 189 VAKNDLEAQRSEEQ 202
Cdd:pfam06160 382 EFKESLQSLRKDEL 395
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
24-195 |
4.45e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 24 KIQQQDQKINALTSQMSDAEAKVAAIEN------DMVETAKQIDTLTAKKNKLSSEVSKLYSEISDLNVRIQKREvqmTK 97
Cdd:PRK03918 260 KIRELEERIEELKKEIEELEEKVKELKElkekaeEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELE---EK 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 98 QARDVQVNGQSDSIidavldADSVADAIGRVQAVSTMMSANNELLEQQKEDKA----TVEKKTKNVEKQIAELEAATKEL 173
Cdd:PRK03918 337 EERLEELKKKLKEL------EKRLEELEERHELYEEAKAKKEELERLKKRLTGltpeKLEKELEELEKAKEEIEEEISKI 410
|
170 180
....*....|....*....|..
gi 642976529 174 NDKTESLKTLKIQQEVAKNDLE 195
Cdd:PRK03918 411 TARIGELKKEIKELKKAIEELK 432
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
19-222 |
5.28e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.39 E-value: 5.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 19 DEYDTKIQQQDQKINALTSQMSDAEAK-------VAAIENDMVETAKQIDTLT-------AKKNKLSSEVSKLYSEISDL 84
Cdd:pfam01576 506 EEEEEAKRNVERQLSTLQAQLSDMKKKleedagtLEALEEGKKRLQRELEALTqqleekaAAYDKLEKTKNRLQQELDDL 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 85 NVRI-QKREVQMT---KQARDVQVNGQSDSIIDAVLDADSVADAIGR---------VQAVSTMMSANNELLEQQKEDKAT 151
Cdd:pfam01576 586 LVDLdHQRQLVSNlekKQKKFDQMLAEEKAISARYAEERDRAEAEAReketralslARALEEALEAKEELERTNKQLRAE 665
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 152 -----------------VEKKTKNVEKQIAELEAATKELNDKTESLKTLKIQQEV------AKNDLEAQRSEEQG--KKD 206
Cdd:pfam01576 666 medlvsskddvgknvheLERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVnmqalkAQFERDLQARDEQGeeKRR 745
|
250
....*....|....*.
gi 642976529 207 GFIKQKKEAEKRLAEE 222
Cdd:pfam01576 746 QLVKQVRELEAELEDE 761
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
26-219 |
5.34e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 39.68 E-value: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 26 QQQDQKINALTSQMSDAEAKVaaiendmVETAKQIDTLTAKKNKLSSEvsklysEISDLNVRIQKREV------QMTKQA 99
Cdd:COG5022 888 KIDVKSISSLKLVNLELESEI-------IELKKSLSSDLIENLEFKTE------LIARLKKLLNNIDLeegpsiEYVKLP 954
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 100 RDVQVNGQSDSIIDAVLDADSVADA--IGRVQ---AVSTMMSANNELLEQQKEDKATVE--KKTKNVEKQIAELEAATKE 172
Cdd:COG5022 955 ELNKLHEVESKLKETSEEYEDLLKKstILVREgnkANSELKNFKKELAELSKQYGALQEstKQLKELPVEVAELQSASKI 1034
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 642976529 173 LNDKTESLKTLKIQQEVAKN-DLEAQRSEEQGKKdgfIKQKKEAEKRL 219
Cdd:COG5022 1035 ISSESTELSILKPLQKLKGLlLLENNQLQARYKA---LKLRRENSLLD 1079
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
140-222 |
5.35e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 39.07 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 140 ELLEQQKEDKATVEKKTKNVEKQIAELEAATKELNDKTESLktlkiQQ--EVAKNDLEAQRS-EEQGKKdgFIKQKKEAE 216
Cdd:pfam06160 277 DLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELERV-----QQsyTLNENELERVRGlEKQLEE--LEKRYDEIV 349
|
....*.
gi 642976529 217 KRLAEE 222
Cdd:pfam06160 350 ERLEEK 355
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
18-176 |
5.71e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 39.27 E-value: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 18 ADEYDTKIQQQDQKINALT---SQMSDAEAKVAAIENDMVETAKQIDT----LTAKKNKLSSEVS---------KLYSEI 81
Cdd:pfam13166 292 IEKVESAISSLLAQLPAVSdlaSLLSAFELDVEDIESEAEVLNSQLDGlrraLEAKRKDPFKSIEldsvdakieSINDLV 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 82 SDLNVRIQKRevqmtkqardvqvNGQSDSIIDAV------LDADSVADAIGRVQAVSTMMSANNELLEQQKEDKATVEKK 155
Cdd:pfam13166 372 ASINELIAKH-------------NEITDNFEEEKnkakkkLRLHLVEEFKSEIDEYKDKYAGLEKAINSLEKEIKNLEAE 438
|
170 180
....*....|....*....|....*...
gi 642976529 156 TKNVEKQIAELEAATK-------ELNDK 176
Cdd:pfam13166 439 IKKLREEIKELEAQLRdhkpgadEINKL 466
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
13-223 |
6.32e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.25 E-value: 6.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 13 PSAAFADEYDTKIQQQDQKINALTSQMSDAEAKVAAIEnDMVETAKQIDTLTAKKnklssevsklyseiSDLNVRIQKRE 92
Cdd:PRK02224 465 PHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERR--------------EDLEELIAERR 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 93 vqmtkqardvqvngqsdsiidAVLDADSVADAIGRVQAVSTMMSAnnellEQQKEDKATVEKKTKNVEKQIAELEAATKE 172
Cdd:PRK02224 530 ---------------------ETIEEKRERAEELRERAAELEAEA-----EEKREAAAEAEEEAEEAREEVAELNSKLAE 583
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 642976529 173 LNDKTESLKTLKIQQEvAKNDLEAQRSEEQGKKDGFIKQKKEAEKRLAEEQ 223
Cdd:PRK02224 584 LKERIESLERIRTLLA-AIADAEDEIERLREKREALAELNDERRERLAEKR 633
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
64-221 |
6.38e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 6.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 64 TAKKNKLSSEVSKLYSEISDLNVRIQKREVQMTKQARdvqvngqsdsiidaVLDADSVADAIGRVQavSTMMSANNELLE 143
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELRELEKVLKKESE--------------LIKLKELAEQLKELE--EKLKKYNLEELE 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 144 QQKEDKATVEKKTKNVEKQIAELEAATKELNDKTESLKTLkiqqEVAKNDLEAQRSE--EQGKKDGFiKQKKEAEKRLAE 221
Cdd:PRK03918 522 KKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAEL----EKKLDELEEELAEllKELEELGF-ESVEELEERLKE 596
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
132-222 |
6.52e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.98 E-value: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 132 STMMSANNELLEQQ-KEDKATVEKKT-----------KNVEKQIAELEAATKELNDKTESLKTLKIQQEVAKNDLEAQRS 199
Cdd:COG4717 37 STLLAFIRAMLLERlEKEADELFKPQgrkpelnlkelKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELRE 116
|
90 100
....*....|....*....|....*...
gi 642976529 200 EEQGKKD-----GFIKQKKEAEKRLAEE 222
Cdd:COG4717 117 ELEKLEKllqllPLYQELEALEAELAEL 144
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
109-221 |
7.52e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.89 E-value: 7.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 109 DSIIDAVLDADSVADAIGRVQAVSTMMSANNELLEQQKEDKATVEKKTKNVEKQIAELEAATKELNDKTESL--KTLKIQ 186
Cdd:PRK03918 148 EKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELreELEKLE 227
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 642976529 187 QEVAK--------NDLEAQRSEEQGKKDGFIKQKKEAEKRLAE 221
Cdd:PRK03918 228 KEVKEleelkeeiEELEKELESLEGSKRKLEEKIRELEERIEE 270
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
140-223 |
7.74e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.97 E-value: 7.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 140 ELLEQQKEDKATVEKKTKNVEKQIAELEAATKELNDKTESLKTLKIQQEVAKNDLEA-QRSEEQGKKDGFIKQKKEAEKR 218
Cdd:PTZ00121 1326 EAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAaKKKAEEKKKADEAKKKAEEDKK 1405
|
....*
gi 642976529 219 LAEEQ 223
Cdd:PTZ00121 1406 KADEL 1410
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
19-176 |
8.59e-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: 38.85 E-value: 8.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 19 DEYDTKIQQQDQKINALTSQMSDAEAKVAAIENDMVETAK-------QIDTLTAKKNKLSSEVSKLYSEIsdLNVRIQKR 91
Cdd:TIGR04523 585 EEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKeneklssIIKNIKSKKNKLKQEVKQIKETI--KEIRNKWP 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 92 EvqMTKQARDVQVngQSDSIIDAVLDADSVADAigRVQAVSTMMSANNELlEQQKEDKATVEKKTKNVEKQIAELEAATK 171
Cdd:TIGR04523 663 E--IIKKIKESKT--KIDDIIELMKDWLKELSL--HYKKYITRMIRIKDL-PKLEEKYKEIEKELKKLDEFSKELENIIK 735
|
....*
gi 642976529 172 ELNDK 176
Cdd:TIGR04523 736 NFNKK 740
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
106-222 |
9.25e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 38.29 E-value: 9.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 106 GQSDSIIDAVL-DADSVADAIGRVQAVstmmsANNELLEQQKEDKATVEKKTKNVEKQIAElEAATKELNDKTESLKTLK 184
Cdd:TIGR02794 32 GGGAEIIQAVLvDPGAVAQQANRIQQQ-----KKPAAKKEQERQKKLEQQAEEAEKQRAAE-QARQKELEQRAAAEKAAK 105
|
90 100 110
....*....|....*....|....*....|....*...
gi 642976529 185 IQQEVAKNDLEAQRSEEQGKkdgfikQKKEAEKRLAEE 222
Cdd:TIGR02794 106 QAEQAAKQAEEKQKQAEEAK------AKQAAEAKAKAE 137
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
31-221 |
9.32e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.51 E-value: 9.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 31 KINALTSQMSDAEAKVAAIENDMVETAKQIDTLTAKKNKLSSEV----------------SKLYSEISDLNVRIQKREVQ 94
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVkelkelkekaeeyiklSEFYEEYLDELREIEKRLSR 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642976529 95 MTKQARDVQVNGQSDSIIDAVLDA---------DSVADAIGRVQAVSTMMSANNEL------------------LEQQKE 147
Cdd:PRK03918 319 LEEEINGIEERIKELEEKEERLEElkkklkeleKRLEELEERHELYEEAKAKKEELerlkkrltgltpeklekeLEELEK 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 642976529 148 DKATVEKKTKNVEKQIAELEAATKELNDKTESLKTLKIQQEVAKNDLEAQRSEEQGKKdgFIKQKKEAEKRLAE 221
Cdd:PRK03918 399 AKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEE--YTAELKRIEKELKE 470
|
|
| |
