|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
140-400 |
5.12e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.70 E-value: 5.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 140 AIKYKDKIKTLEKNQEILDDTAKNLRV---MLESEREQNVKNQDLLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTH 216
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKalaELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 217 KDDNINALTNCITQlnLLECESESEGQNKGGNDSDELANGEVGGDRNEkMKNQIKQM----MDVSRTQTAISVVEEDLKL 292
Cdd:TIGR02168 752 LSKELTELEAEIEE--LEERLEEAEEELAEAEAEIEELEAQIEQLKEE-LKALREALdelrAELTLLNEEAANLRERLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 293 LQLKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQKE---MALQKKLSQEEYERQEREH 369
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEealALLRSELEELSEELRELES 908
|
250 260 270
....*....|....*....|....*....|.
gi 2462508900 370 RLSAADEKAVSAAEEVKTYKRRIEEMEDELQ 400
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLEGLEVRID 939
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
91-410 |
1.37e-11 |
|
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: 68.12 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 91 EQQISEK---LKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILsdeaikyKDKIKTLEKNQEILDDTAKNLRVM 167
Cdd:TIGR04523 362 QRELEEKqneIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQK-------DEQIKKLQQEKELLEKEIERLKET 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 168 LESEREQ--NVKNQD-LLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNllECESESEGQN 244
Cdd:TIGR04523 435 IIKNNSEikDLTNQDsVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLN--EEKKELEEKV 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 245 KGGND-SDELANGEvggdrnEKMKNQIKQMmdvsrtQTAISVVEEDLKLLQLKLrasvsTKCNLEDQVKKLEDDRNSLQA 323
Cdd:TIGR04523 513 KDLTKkISSLKEKI------EKLESEKKEK------ESKISDLEDELNKDDFEL-----KKENLEKEIDEKNKEIEELKQ 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 324 AKAGLEdecKTLRQKVEILNElYQQKEMALQKKLSQEEYERQEREHRLSAADEKavsaAEEVKTYKRRIEEMEDELQKTE 403
Cdd:TIGR04523 576 TQKSLK---KKQEEKQELIDQ-KEKEKKDLIKEIEEKEKKISSLEKELEKAKKE----NEKLSSIIKNIKSKKNKLKQEV 647
|
....*..
gi 2462508900 404 RSFKNQI 410
Cdd:TIGR04523 648 KQIKETI 654
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
91-415 |
1.89e-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: 64.27 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 91 EQQISEKLKTIMKE--NTELVQK-----LSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKN 163
Cdd:TIGR04523 35 EKQLEKKLKTIKNElkNKEKELKnldknLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 164 LR----------VMLESEREQNVKNQDL-------LQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTN 226
Cdd:TIGR04523 115 DKeqknklevelNKLEKQKKENKKNIDKflteikkKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKN 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 227 CITQLN--LLECESESEGQNKGGNDSDELANgevggdRNEKMKNQIKQM-MDVSRTQTAISVVEEDLKllqlklrasvST 303
Cdd:TIGR04523 195 KLLKLEllLSNLKKKIQKNKSLESQISELKK------QNNQLKDNIEKKqQEINEKTTEISNTQTQLN----------QL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 304 KCNLEDQVKKLEDDRNSLQAAKA---GLEDECKTLRQKVEILNelyQQKEMALQKKLSqeeyerqerehrlsaadekavs 380
Cdd:TIGR04523 259 KDEQNKIKKQLSEKQKELEQNNKkikELEKQLNQLKSEISDLN---NQKEQDWNKELK---------------------- 313
|
330 340 350
....*....|....*....|....*....|....*...
gi 2462508900 381 aaEEVKTYKRRIEEMEDELQKTER---SFKNQIATHEK 415
Cdd:TIGR04523 314 --SELKNQEKKLEEIQNQISQNNKiisQLNEQISQLKK 349
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
96-423 |
3.72e-10 |
|
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: 63.45 E-value: 3.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 96 EKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKqnmilsdEAIKYKDKIKTLEKNQEILDDTAKNL--RVMLESERE 173
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELKLKEQAKK-------ALEYYQLKEKLELEEEYLLYLDYLKLneERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 174 QNVKNQ--DLLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALtncITQLNLLECESESEGQNKGGNDSD 251
Cdd:pfam02463 246 LRDEQEeiESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEEL---KSELLKLERRKVDDEEKLKESEKE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 252 ELANGEVGGDRNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRAsvstkcNLEDQVKKLEDDRNSLQAAKAGLEDE 331
Cdd:pfam02463 323 KKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQ------LEEELLAKKKLESERLSSAAKLKEEE 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 332 cKTLR----QKVEILNELYQQKEMALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTERSFK 407
Cdd:pfam02463 397 -LELKseeeKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLK 475
|
330
....*....|....*.
gi 2462508900 408 NQIATHEKKAHENWLK 423
Cdd:pfam02463 476 ETQLVKLQEQLELLLS 491
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
90-423 |
6.20e-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: 62.73 E-value: 6.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 90 TEQQISEKLKTIMKENTELVQKLSNYEQKIKEskkhvqetrkqnmilsdeaiKYKDKIKTLEKNQEILDDTAKNLrvmle 169
Cdd:TIGR04523 236 KKQQEINEKTTEISNTQTQLNQLKDEQNKIKK--------------------QLSEKQKELEQNNKKIKELEKQL----- 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 170 sereQNVKNQ--DLLQQEIEDWSKlhaELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNLLECESESEGQNKGG 247
Cdd:TIGR04523 291 ----NQLKSEisDLNNQKEQDWNK---ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 248 NDSDELANGEVGGDRNEKMKNQIKQM-MDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQVKKLEDDRNSLQAAKA 326
Cdd:TIGR04523 364 ELEEKQNEIEKLKKENQSYKQEIKNLeSQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIK 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 327 GLEDECKTLRQKVEILNELYQQkemaLQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTER-- 404
Cdd:TIGR04523 444 DLTNQDSVKELIIKNLDNTRES----LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKki 519
|
330 340
....*....|....*....|..
gi 2462508900 405 -SFKNQIA--THEKKAHENWLK 423
Cdd:TIGR04523 520 sSLKEKIEklESEKKEKESKIS 541
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
90-350 |
2.14e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.23 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 90 TEQQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRV--- 166
Cdd:TIGR02168 741 EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEeaa 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 167 MLESEREQNVKNQDLLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNLLECESESEGQNKg 246
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL- 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 247 gndSDELANGEvggDRNEKMKNQIKQMMD-VSRTQTAISVVEEDLKLLQLKLRASVSTkcNLEDQVKKLEDDRNSLQAAk 325
Cdd:TIGR02168 900 ---SEELRELE---SKRSELRRELEELREkLAQLELRLEGLEVRIDNLQERLSEEYSL--TLEEAEALENKIEDDEEEA- 970
|
250 260 270
....*....|....*....|....*....|...
gi 2462508900 326 aglEDECKTLRQKVEIL--------NELYQQKE 350
Cdd:TIGR02168 971 ---RRRLKRLENKIKELgpvnlaaiEEYEELKE 1000
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
183-458 |
5.70e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.69 E-value: 5.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 183 QQEIEdwsklhaELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNLLECESEsegqnkggndsDELANGEVGGDR 262
Cdd:TIGR02168 676 RREIE-------ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS-----------RQISALRKDLAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 263 NEKMKNQIKQMMDvsRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEIL 342
Cdd:TIGR02168 738 LEAEVEQLEERIA--QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 343 NELYQQKEMA---LQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQkterSFKNQIATHEKKAHE 419
Cdd:TIGR02168 816 NEEAANLRERlesLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE----ALLNERASLEEALAL 891
|
250 260 270
....*....|....*....|....*....|....*....
gi 2462508900 420 NWLKARAAERAIAEEKREAANLRHKLLELTQKMAMLQEE 458
Cdd:TIGR02168 892 LRSELEELSEELRELESKRSELRRELEELREKLAQLELR 930
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
87-348 |
8.20e-09 |
|
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: 58.88 E-value: 8.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 87 YQVTEQQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRv 166
Cdd:TIGR04523 403 QEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIK- 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 167 mlesereqnvKNQDLLQQEIEDWSKLHAELSEQIKSFEKSQKDLEvalthkdDNINALTNCITQLNL--LECESE-SEGQ 243
Cdd:TIGR04523 482 ----------QNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLT-------KKISSLKEKIEKLESekKEKESKiSDLE 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 244 NKGGNDSDELANGEVGGDRNEKMKNqIKQMmdvSRTQTAISVVEEDLKLL-------QLKLRASVSTKcnlEDQVKKLED 316
Cdd:TIGR04523 545 DELNKDDFELKKENLEKEIDEKNKE-IEEL---KQTQKSLKKKQEEKQELidqkekeKKDLIKEIEEK---EKKISSLEK 617
|
250 260 270
....*....|....*....|....*....|..
gi 2462508900 317 DRNSLQAAKAGLEDECKTLRQKVEILNELYQQ 348
Cdd:TIGR04523 618 ELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
86-350 |
9.75e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 9.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 86 VYQVTEQQisEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDK-------IKTLEKNQEILD 158
Cdd:TIGR02168 231 VLRLEELR--EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKElyalaneISRLEQQKQILR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 159 DTAKNLR---VMLESEREQNVKNQDLLQQEIEDWSK-------LHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCI 228
Cdd:TIGR02168 309 ERLANLErqlEELEAQLEELESKLDELAEELAELEEkleelkeELESLEAELEELEAELEELESRLEELEEQLETLRSKV 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 229 TQLNLLEcesesegqnkggndsdELANGEVGgdRNEKMKNQIKQMmdVSRTQTAISVVEEDLKLLQLK-LRASVSTK--- 304
Cdd:TIGR02168 389 AQLELQI----------------ASLNNEIE--RLEARLERLEDR--RERLQQEIEELLKKLEEAELKeLQAELEELeee 448
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2462508900 305 --------CNLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQKE 350
Cdd:TIGR02168 449 leelqeelERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
90-331 |
1.24e-08 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 58.43 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 90 TEQQISEKLKTIMKE---------------NTELVQKLSNYEQKIKESKKHV---QETRKQNMILSDEAIKYKDKIKTLE 151
Cdd:COG5185 294 TKEKIAEYTKSIDIKkatesleeqlaaaeaEQELEESKRETETGIQNLTAEIeqgQESLTENLEAIKEEIENIVGEVELS 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 152 KNQEILDDTAKNLRvmlESEREQNVKNQDLLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQL 231
Cdd:COG5185 374 KSSEELDSFKDTIE---STKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISEL 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 232 NLLECESESEGQNKGGNDSDELANgevggdRNEKMKNQIKQmmDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQV 311
Cdd:COG5185 451 NKVMREADEESQSRLEEAYDEINR------SVRSKKEDLNE--ELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQV 522
|
250 260
....*....|....*....|..
gi 2462508900 312 KKLEDDRNSLQ--AAKAGLEDE 331
Cdd:COG5185 523 AESLKDFMRARgyAHILALENL 544
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
92-410 |
2.52e-08 |
|
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: 57.34 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 92 QQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRVM---L 168
Cdd:TIGR04523 317 KNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQindL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 169 ESE-REQNVKNQDL------LQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCI----TQLNLLECE 237
Cdd:TIGR04523 397 ESKiQNQEKLNQQKdeqikkLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTResleTQLKVLSRS 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 238 SESEGQNKGGNdSDELANGEvggDRNEKMKNQIKQMmdvsrtQTAISVVEEDLKLLQLKLRASVSTKCNLEDQVKKLEDD 317
Cdd:TIGR04523 477 INKIKQNLEQK-QKELKSKE---KELKKLNEEKKEL------EEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDE 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 318 RNSLQA--AKAGLEDECKTLRQKVEILNELYQ-----QKEmaLQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYK- 389
Cdd:TIGR04523 547 LNKDDFelKKENLEKEIDEKNKEIEELKQTQKslkkkQEE--KQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKk 624
|
330 340
....*....|....*....|...
gi 2462508900 390 --RRIEEMEDELQKTERSFKNQI 410
Cdd:TIGR04523 625 enEKLSSIIKNIKSKKNKLKQEV 647
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
466-711 |
9.25e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 56.10 E-value: 9.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 466 PGKPNTQNPPRRGPLSqNGSFGPSPVSGGECSPPLTV-EPPVRPLSATLNRRDMPRSEfGSVDGPLPHPRWSAEASGKPS 544
Cdd:PHA03247 2748 PATPGGPARPARPPTT-AGPPAPAPPAAPAAGPPRRLtRPAVASLSESRESLPSPWDP-ADPPAAVLAPAAALPPAASPA 2825
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 545 PSDPGSGTATMMNSS-SRGSSPTRVLDEGKVnmAPKGP-----PPFPGVPLMSTPMGGPVPPPIRYGPPPQLC------- 611
Cdd:PHA03247 2826 GPLPPPTSAQPTAPPpPPGPPPPSLPLGGSV--APGGDvrrrpPSRSPAAKPAAPARPPVRRLARPAVSRSTEsfalppd 2903
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 612 --GPFGPRPLPPPFGPGMRPPLGLREFAPGVPPGRRDLPLHPR------GFLPGHAPFRPLGSLGPREYFIPGTRLPPPT 683
Cdd:PHA03247 2904 qpERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTtdpagaGEPSGAVPQPWLGALVPGRVAVPRFRVPQPA 2983
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2462508900 684 HG-PQEYPPPPAVRDLLPSG-----------SRDEPPPAS 711
Cdd:PHA03247 2984 PSrEAPASSTPPLTGHSLSRvsswasslalhEETDPPPVS 3023
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
90-349 |
1.37e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.03 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 90 TEQQISEK---LKTIMKENTELVQKLSNYEQKIKESKKHVQEtrkqnmiLSDEAIKYKDKIKTLEKNQEILDDTAKnlRV 166
Cdd:TIGR04523 487 KQKELKSKekeLKKLNEEKKELEEKVKDLTKKISSLKEKIEK-------LESEKKEKESKISDLEDELNKDDFELK--KE 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 167 MLESEREQNVKNQDLLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNcitQLNLLECESES-EGQNK 245
Cdd:TIGR04523 558 NLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEK---ELEKAKKENEKlSSIIK 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 246 GGNDSDELANGEVggdrnEKMKNQIKQMMD-----VSRTQTAISVVEEDLKLLQLKLR-ASVSTKCNLEDQVK-----KL 314
Cdd:TIGR04523 635 NIKSKKNKLKQEV-----KQIKETIKEIRNkwpeiIKKIKESKTKIDDIIELMKDWLKeLSLHYKKYITRMIRikdlpKL 709
|
250 260 270
....*....|....*....|....*....|....*
gi 2462508900 315 EDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQK 349
Cdd:TIGR04523 710 EEKYKEIEKELKKLDEFSKELENIIKNFNKKFDDA 744
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
456-712 |
1.61e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 55.33 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 456 QEEPVIVKPMPGKPNTQNPPrrGPLSQNGSF-------GPSPVSGGECSPPLTVEPPVRPLSATLNRRDMPRSEFGSVDG 528
Cdd:PHA03247 2704 PPPTPEPAPHALVSATPLPP--GPAAARQASpalpaapAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPR 2781
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 529 PLPHP---RWSAEASGKPSPSDPGSGTATMM--NSSSRGSSPTRVLDEGKVNMAPKGPPPFPGVPLMSTPMGGPVPPPIR 603
Cdd:PHA03247 2782 RLTRPavaSLSESRESLPSPWDPADPPAAVLapAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGD 2861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 604 ygpppqLCGPFGPRPLPPPFGPGMRPPLGlREFAPGVPPGRRDLPLHPRGFLPGHAPFRPLGSLGPREYFIPGTRLPPPT 683
Cdd:PHA03247 2862 ------VRRRPPSRSPAAKPAAPARPPVR-RLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPP 2934
|
250 260
....*....|....*....|....*....
gi 2462508900 684 HGPQEYPPPPAVRDLLPSGSRDEPPPASQ 712
Cdd:PHA03247 2935 PPPRPQPPLAPTTDPAGAGEPSGAVPQPW 2963
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
115-458 |
2.15e-07 |
|
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: 54.59 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 115 YEQKIKESKK--HVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLEseREQNVKNQDLLQQEIEDWSKL 192
Cdd:pfam02463 168 KRKKKEALKKliEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEE--YLLYLDYLKLNEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 193 HAELSEQIKSFEKSQKDLE--VALTHKDDNINALTNCITQLNLLECESESEGQNKGGNDSDELANGEVGGDRNEKMKNQI 270
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEekLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 271 KQmmdvSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQKE 350
Cdd:pfam02463 326 AE----KELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKS 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 351 MALQKKLSQEEYERQEREHRLSAADEKA--VSAAEEVKTYKRRIEEMEDELQKTERSfKNQIATHEKKAHENWLKarAAE 428
Cdd:pfam02463 402 EEEKEAQLLLELARQLEDLLKEEKKEELeiLEEEEESIELKQGKLTEEKEELEKQEL-KLLKDELELKKSEDLLK--ETQ 478
|
330 340 350
....*....|....*....|....*....|
gi 2462508900 429 RAIAEEKREAANLRHKLLELTQKMAMLQEE 458
Cdd:pfam02463 479 LVKLQEQLELLLSRQKLEERSQKESKARSG 508
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
111-423 |
2.75e-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: 53.87 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 111 KLSNYEQKIKESKKHVQETRKQ------NMILSDEAIKY-KDKIKTLEKNQEILDDTAKNLRVMLES--------EREQN 175
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKElknldkNLNKDEEKINNsNNKIKILEQQIKDLNDKLKKNKDKINKlnsdlskiNSEIK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 176 VKNQDLLQQEIEdwsklHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNLLECESESEgQNKGGNDSDELAN 255
Cdd:TIGR04523 114 NDKEQKNKLEVE-----LNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENE-LNLLEKEKLNIQK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 256 gevggdRNEKMKNQIkqmmdvSRTQTAISVVE---EDLKLLQLKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAGLEDEC 332
Cdd:TIGR04523 188 ------NIDKIKNKL------LKLELLLSNLKkkiQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 333 KTLRQK-VEILNELyQQKEmalqkklsqeeyerqerehrlsaadekavsaaEEVKTYKRRIEEMEDELQKtersFKNQIA 411
Cdd:TIGR04523 256 NQLKDEqNKIKKQL-SEKQ--------------------------------KELEQNNKKIKELEKQLNQ----LKSEIS 298
|
330
....*....|..
gi 2462508900 412 THEKKAHENWLK 423
Cdd:TIGR04523 299 DLNNQKEQDWNK 310
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
92-458 |
3.26e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 92 QQISEKLKTIMKENTELVQKLSNYEQKIkESKKHVQETRKQNMILSDEAIKY---KDKIKTLEKNQEILDDTAKNLRVML 168
Cdd:COG4717 98 EELEEELEELEAELEELREELEKLEKLL-QLLPLYQELEALEAELAELPERLeelEERLEELRELEEELEELEAELAELQ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 169 ESEREQNVKNQDLLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNLLECESESEG------ 242
Cdd:COG4717 177 EELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLllliaa 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 243 ----------------------------------------QNKGGNDSDELANGEVGGDRNEKMKNQIKQMMDVSRTQTA 282
Cdd:COG4717 257 allallglggsllsliltiagvlflvlgllallflllareKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSP 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 283 ISVVEEDLKLLQLKLRASVSTKCNLEDQVKKLEDDRNSLqAAKAGLEDEcKTLRQKVEILNElYQQKEMALQKKLSQEEY 362
Cdd:COG4717 337 EELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL-LAEAGVEDE-EELRAALEQAEE-YQELKEELEELEEQLEE 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 363 ERQEREHRLSAADEKAVsaAEEVKTYKRRIEEMEDE---LQKTERSFKNQIATHEKkahenwlkaraaeraiaeeKREAA 439
Cdd:COG4717 414 LLGELEELLEALDEEEL--EEELEELEEELEELEEEleeLREELAELEAELEQLEE-------------------DGELA 472
|
410
....*....|....*....
gi 2462508900 440 NLRHKLLELTQKMAMLQEE 458
Cdd:COG4717 473 ELLQELEELKAELRELAEE 491
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
142-458 |
4.17e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.53 E-value: 4.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 142 KYKDKIKTLEKNQEILD---DTAKNLRVMLESEREQNVKNQDLLQ--QEIEDWSKLHA---------ELSEQIKSFEKSQ 207
Cdd:TIGR02169 174 KALEELEEVEENIERLDliiDEKRQQLERLRREREKAERYQALLKekREYEGYELLKEkealerqkeAIERQLASLEEEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 208 KDLEVALTHKDDNINALTNCITQLNL-LECESESEG---QNKGGNDSDELANGEvggdRNEKMKNQikQMMDVsrtqtai 283
Cdd:TIGR02169 254 EKLTEEISELEKRLEEIEQLLEELNKkIKDLGEEEQlrvKEKIGELEAEIASLE----RSIAEKER--ELEDA------- 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 284 svvEEDLKLLQLKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQ---QKEMALQKKLSQE 360
Cdd:TIGR02169 321 ---EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAetrDELKDYREKLEKL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 361 EYER---QEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTERSFKNQIATHEKKAHENwlkaraaERAIAEEKRE 437
Cdd:TIGR02169 398 KREInelKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL-------AADLSKYEQE 470
|
330 340
....*....|....*....|.
gi 2462508900 438 AANLRHKLLELTQKMAMLQEE 458
Cdd:TIGR02169 471 LYDLKEEYDRVEKELSKLQRE 491
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
92-345 |
8.60e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.76 E-value: 8.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 92 QQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLE-------------------- 151
Cdd:TIGR02169 726 EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEarlshsripeiqaelsklee 805
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 152 ---KNQEILDDTAKNL------RVMLESEREQNVKNQDLLQ-------QEIEDWSKLHAELSEQIKSFEKSQKDLEVALT 215
Cdd:TIGR02169 806 evsRIEARLREIEQKLnrltleKEYLEKEIQELQEQRIDLKeqiksieKEIENLNGKKEELEEELEELEAALRDLESRLG 885
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 216 HKDDNINALTNCITQLNLLECESESEGQNKGGNDSDELANGEVGGDRNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQL 295
Cdd:TIGR02169 886 DLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEE 965
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2462508900 296 KLRASVSTKCNLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNEL 345
Cdd:TIGR02169 966 EIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
102-465 |
1.10e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 52.36 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 102 MKENTELVQKLSNYEQ-----KIKESKKHVQETRKQNMILSDEAIKYKDKIKtlEKNQEILDD-TAKnlRVMLESEREQN 175
Cdd:TIGR00606 165 LSEGKALKQKFDEIFSatryiKALETLRQVRQTQGQKVQEHQMELKYLKQYK--EKACEIRDQiTSK--EAQLESSREIV 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 176 VKNQDLL------QQEIED-WSKLHaELSEQIKSFEKSQKDLE---VALTHKDDNINALTNciTQLNLLECESESEGQNK 245
Cdd:TIGR00606 241 KSYENELdplknrLKEIEHnLSKIM-KLDNEIKALKSRKKQMEkdnSELELKMEKVFQGTD--EQLNDLYHNHQRTVREK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 246 GgndsDELANGEVGGDRNEKMKNQIKQ-----MMDVSRTQTAISVVEEDLKLLQLkLRASVSTKCNLEDQVKKLEDDR-- 318
Cdd:TIGR00606 318 E----RELVDCQRELEKLNKERRLLNQektelLVEQGRLQLQADRHQEHIRARDS-LIQSLATRLELDGFERGPFSERqi 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 319 -NSLQAAKAGLEDECKTLRQkveILNELyQQKEMALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKR------- 390
Cdd:TIGR00606 393 kNFHTLVIERQEDEAKTAAQ---LCADL-QSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKelqqleg 468
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462508900 391 ---RIEEMEDELQKTERSFknqiatheKKAHENWLkARAAERAIAEEKREAANLRHKLLELTQKMAMLQEEPVIVKPM 465
Cdd:TIGR00606 469 ssdRILELDQELRKAEREL--------SKAEKNSL-TETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQM 537
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
91-357 |
1.62e-06 |
|
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: 51.75 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 91 EQQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNqeilddtaknlrvmLES 170
Cdd:pfam10174 463 DRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIA--------------VEQ 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 171 EREQNVKNQDLLQ--QEIEDWSKLHAELSEQIKSFEKsqkdlEVALtHKDDNINALTNCITQLNLL-ECESESEGQNKGG 247
Cdd:pfam10174 529 KKEECSKLENQLKkaHNAEEAVRTNPEINDRIRLLEQ-----EVAR-YKEESGKAQAEVERLLGILrEVENEKNDKDKKI 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 248 NDSDELANGEVgGDRNEKMKNqiKQMMDVSRTQTAISVVEEDLKllQLKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAG 327
Cdd:pfam10174 603 AELESLTLRQM-KEQNKKVAN--IKHGQQEMKKKGAQLLEEARR--REDNLADNSQQLQLEELMGALEKTRQELDATKAR 677
|
250 260 270
....*....|....*....|....*....|
gi 2462508900 328 LEDECKTLRQKVEILNELYQQKEMALQKKL 357
Cdd:pfam10174 678 LSSTQQSLAEKDGHLTNLRAERRKQLEEIL 707
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
83-415 |
2.96e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 51.21 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 83 KDRVYQVTEQQISEKLKTIMKENTELVQK---------LSNYEQKIKESKKHVQETRK------QNM-ILS--DEAIKY- 143
Cdd:TIGR01612 847 KVDKFINFENNCKEKIDSEHEQFAELTNKikaeisddkLNDYEKKFNDSKSLINEINKsieeeyQNInTLKkvDEYIKIc 926
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 144 ---KDKIKTLEKNQEILDDTA-KNLRVMLESER-EQNVKNQ--DLLQQEIEDWSKLHAELS---------EQIKSFEKSQ 207
Cdd:TIGR01612 927 entKESIEKFHNKQNILKEILnKNIDTIKESNLiEKSYKDKfdNTLIDKINELDKAFKDASlndyeaknnELIKYFNDLK 1006
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 208 KDL----EVALTHKDDNINALTNCITQlnllecesESEGQNKG------------GNDSDELANgEVGGDRNEKMKNQIK 271
Cdd:TIGR01612 1007 ANLgknkENMLYHQFDEKEKATNDIEQ--------KIEDANKNipnieiaihtsiYNIIDEIEK-EIGKNIELLNKEILE 1077
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 272 QmmdVSRTQTAISVVEEDLKLLqlklrasvstkcNLEDQVK----KLEDDRNSLQaakagleDECKTLRQKVEI-LNELY 346
Cdd:TIGR01612 1078 E---AEINITNFNEIKEKLKHY------------NFDDFGKeeniKYADEINKIK-------DDIKNLDQKIDHhIKALE 1135
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462508900 347 QqkemaLQKKLSQEEYERQEREHRLSAADEKAVSaAEEVKTYKRRIEEMEDELQKTERSFK------NQIATHEK 415
Cdd:TIGR01612 1136 E-----IKKKSENYIDEIKAQINDLEDVADKAIS-NDDPEEIEKKIENIVTKIDKKKNIYDeikkllNEIAEIEK 1204
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
123-351 |
3.08e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.40 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 123 KKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLESEREQNVKNQDLLQQEIEdwsklhaELSEQIKS 202
Cdd:PHA02562 173 KDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIE-------ELTDELLN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 203 FEKSQKDLEVALTHKDDNINALTNCITQLNLLE-----------CESE-SEGQNKGGNDSDELANGEVGGDRNEKMKNQI 270
Cdd:PHA02562 246 LVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIkmyekggvcptCTQQiSEGPDRITKIKDKLKELQHSLEKLDTAIDEL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 271 KQMMDVSRTQTaiSVVEEdlklLQLKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQKE 350
Cdd:PHA02562 326 EEIMDEFNEQS--KKLLE----LKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELV 399
|
.
gi 2462508900 351 M 351
Cdd:PHA02562 400 K 400
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
91-404 |
3.49e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 91 EQQISEKlktimkENTELVQKLSNYEQKIKESK---KHVQETRKQ--------NMILS------------DEAI-KYKDK 146
Cdd:PRK02224 193 KAQIEEK------EEKDLHERLNGLESELAELDeeiERYEEQREQaretrdeaDEVLEeheerreeletlEAEIeDLRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 147 IKTLEKNQEILDDTAKNLRVM---LESEREQNVKNQDLLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINA 223
Cdd:PRK02224 267 IAETEREREELAEEVRDLRERleeLEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAES 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 224 LTNCITQLnllecESESEG-QNKGGNDSDELANGEVG-GDRNEKMKNQIKQMMDVSR----TQTAISVVEEDLKLLQ--- 294
Cdd:PRK02224 347 LREDADDL-----EERAEElREEAAELESELEEAREAvEDRREEIEELEEEIEELRErfgdAPVDLGNAEDFLEELReer 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 295 -------LKLRASVST---------------KC-------------------------------NLEDQVKKLEDDRNSL 321
Cdd:PRK02224 422 delrereAELEATLRTarerveeaealleagKCpecgqpvegsphvetieedrerveeleaeleDLEEEVEEVEERLERA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 322 QAAKAgLEDECKTLRQKVEILNELYQQKEMALQKKLSQEEYERQEREHRLSAADEK----------AVSAAEEVKTYKRR 391
Cdd:PRK02224 502 EDLVE-AEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKreaaaeaeeeAEEAREEVAELNSK 580
|
410
....*....|...
gi 2462508900 392 IEEMEDELQKTER 404
Cdd:PRK02224 581 LAELKERIESLER 593
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
266-419 |
3.56e-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: 48.77 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 266 MKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRAsvstkcnLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNEL 345
Cdd:COG1579 2 MPEDLRALLDLQELDSELDRLEHRLKELPAELAE-------LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 346 ---YQQ--------KEM-ALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTERSFKNQIATH 413
Cdd:COG1579 75 ikkYEEqlgnvrnnKEYeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
|
....*.
gi 2462508900 414 EKKAHE 419
Cdd:COG1579 155 EAELEE 160
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
92-404 |
3.77e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 3.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 92 QQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMI-------LSDE-----AIKYKDKIKTLEKNQEILDD 159
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgreLTEEhrkelLEEYTAELKRIEKELKEIEE 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 160 TAKNLR---VMLESEREQN---VKNQDLLQQEIEDWSKLHA----ELSEQIKSFEKsqkdLEVALTHKDDNINALTNCIT 229
Cdd:PRK03918 474 KERKLRkelRELEKVLKKEselIKLKELAEQLKELEEKLKKynleELEKKAEEYEK----LKEKLIKLKGEIKSLKKELE 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 230 QLNLLECESEsEGQNKGGNDSDELANgevggdrnekMKNQIKqmmdvSRTQTAISVVEEDLKLLQ------LKLRASVST 303
Cdd:PRK03918 550 KLEELKKKLA-ELEKKLDELEEELAE----------LLKELE-----ELGFESVEELEERLKELEpfyneyLELKDAEKE 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 304 KCNLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQKEMA----LQKKLSQEEYERQEREHRLSAADEKAV 379
Cdd:PRK03918 614 LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEelreEYLELSRELAGLRAELEELEKRREEIK 693
|
330 340
....*....|....*....|....*
gi 2462508900 380 SAAEEVKTYKRRIEEMEDELQKTER 404
Cdd:PRK03918 694 KTLEKLKEELEEREKAKKELEKLEK 718
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
449-710 |
4.25e-06 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 50.15 E-value: 4.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 449 TQKMAMLQEEPVIVKPMPGKPNTQNPPRRGPLSQNGSFGPSPvSGGECSPPLTVEPPVRPLS-----ATLNRRDMPRSEf 523
Cdd:pfam03154 169 TQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQG-SPATSQPPNQTQSTAAPHTliqqtPTLHPQRLPSPH- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 524 gSVDGPLPHPRWSAEASGKPSPSDPGSGTATMMNSSsrgssptrvLDEGKVNMAPKGPP-PFPGVPLMSTPMGGPVPPPI 602
Cdd:pfam03154 247 -PPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHS---------LQTGPSHMQHPVPPqPFPLTPQSSQSQVPPGPSPA 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 603 RYGPPPQLCGPFGPRPLPPPFGPGMRPPLglrEFAPGVPPGRRDLPLHPRGFLPG-HAPFRPLGSLGPREYFIPGTRLPP 681
Cdd:pfam03154 317 APGQSQQRIHTPPSQSQLQSQQPPREQPL---PPAPLSMPHIKPPPTTPIPQLPNpQSHKHPPHLSGPSPFQMNSNLPPP 393
|
250 260 270
....*....|....*....|....*....|....*...
gi 2462508900 682 P---------THGPQEYPPPPAvrDLLPSGSRDEPPPA 710
Cdd:pfam03154 394 PalkplsslsTHHPPSAHPPPL--QLMPQSQQLPPPPA 429
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
82-402 |
5.77e-06 |
|
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: 49.97 E-value: 5.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 82 VKDRVYQVTEQQISEKLKTIMKENTELVQKlsnyEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTA 161
Cdd:pfam02463 722 LLADRVQEAQDKINEELKLLKQKIDEEEEE----EEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLK 797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 162 KNLRVMLESEREQNVKNQdLLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNLLECESESE 241
Cdd:pfam02463 798 AQEEELRALEEELKEEAE-LLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKE 876
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 242 GQNKGGNDSDELANGEVGGDRNEKMKNQIKQ--MMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQVKKLEDDRN 319
Cdd:pfam02463 877 EELEEQKLKDELESKEEKEKEEKKELEEESQklNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKE 956
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 320 SLQAAKAGLEDECKTLRQKVEILNELYQQKEMALQKKLSQEEyerqerehRLSAADEKAVSAAEEVKTyKRRIEEMEDEL 399
Cdd:pfam02463 957 EEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKE--------RLEEEKKKLIRAIIEETC-QRLKEFLELFV 1027
|
...
gi 2462508900 400 QKT 402
Cdd:pfam02463 1028 SIN 1030
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
92-347 |
7.15e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 7.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 92 QQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEilddtaknlrvMLESE 171
Cdd:COG4372 62 EQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQ-----------DLEQQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 172 REQNVKNQDLLQQEIEDWSKLHAELSEQIKSFEKSQKDLEValthkddNINALTNCITQLNLLECESESEGQNKGGNDSD 251
Cdd:COG4372 131 RKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ-------ELQALSEAEAEQALDELLKEANRNAEKEEELA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 252 ELANGEVGGDRNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNL-EDQVKKLEDDRNSLQAAKAGLED 330
Cdd:COG4372 204 EAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEiEELELAILVEKDTEEEELEIAAL 283
|
250
....*....|....*..
gi 2462508900 331 ECKTLRQKVEILNELYQ 347
Cdd:COG4372 284 ELEALEEAALELKLLAL 300
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
136-398 |
1.16e-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: 48.91 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 136 LSDEAIKYKDKIKTLEKNQEILDD---TAKNLRVMLESEREQNVKNQDLLQQEIEDWSKLHAELSEQIKSFEKSQKDLEV 212
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSelrRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 213 ALTHKDDNINALTNCITQLnllecesesegQNKGGNDSDELANGE--VGGDRNEKMKNQI-KQMMDVSRTQTAISVVEED 289
Cdd:TIGR02169 752 EIENVKSELKELEARIEEL-----------EEDLHKLEEALNDLEarLSHSRIPEIQAELsKLEEEVSRIEARLREIEQK 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 290 LKLLQLKLRASVSTKCNLEDQVKKLEDDRNS-------LQAAKAGLEDECKTLRQKVEILNELYQ---------QKEM-A 352
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQELQEQRIDLKEQIKSiekeienLNGKKEELEEELEELEAALRDLESRLGdlkkerdelEAQLrE 900
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2462508900 353 LQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDE 398
Cdd:TIGR02169 901 LERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEI 946
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
81-410 |
1.46e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 48.42 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 81 VVKDRVYQVTEQQISEKLKTIMKENTELVQKLS-NYEQKIKESKKHVQETRKQNMILSDEAIKYKdkiKTLEKNQEILDD 159
Cdd:COG5185 192 ISELKKAEPSGTVNSIKESETGNLGSESTLLEKaKEIINIEEALKGFQDPESELEDLAQTSDKLE---KLVEQNTDLRLE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 160 TAKNLRVMLESEREQNVKNQDL---LQQEIE------DWSKLHAELSEQIKSFEKSQKdLEVALTHKDDNINALTNCITQ 230
Cdd:COG5185 269 KLGENAESSKRLNENANNLIKQfenTKEKIAeytksiDIKKATESLEEQLAAAEAEQE-LEESKRETETGIQNLTAEIEQ 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 231 LNllecESESEGQNKGGNDSDELAnGEVGGDRNEKMKNQIKQMMDVSRT--------------------QTAISVVEEDL 290
Cdd:COG5185 348 GQ----ESLTENLEAIKEEIENIV-GEVELSKSSEELDSFKDTIESTKEsldeipqnqrgyaqeilatlEDTLKAADRQI 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 291 KLLQLKLRASVStkcNLEDQVKKL--------EDDRNSLQAAKAGLEDECK----TLRQKVEILNELYQQKEMALQKKLS 358
Cdd:COG5185 423 EELQRQIEQATS---SNEEVSKLLneliselnKVMREADEESQSRLEEAYDeinrSVRSKKEDLNEELTQIESRVSTLKA 499
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2462508900 359 QEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTERSFKNQI 410
Cdd:COG5185 500 TLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELI 551
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
83-458 |
2.01e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 83 KDRVYQVTEQQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMI--LSDEAIKYKDKIKTLE---KNQEIL 157
Cdd:PTZ00121 1344 AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAkkKAEEDKKKADELKKAAaakKKADEA 1423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 158 DDTAKNLRVMLESERE-QNVKNQDLLQQEIEDWSKLH--AELSEQIKSFEKSQKDLEVALTHKDDNINALTnciTQLNLL 234
Cdd:PTZ00121 1424 KKKAEEKKKADEAKKKaEEAKKADEAKKKAEEAKKAEeaKKKAEEAKKADEAKKKAEEAKKADEAKKKAEE---AKKKAD 1500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 235 ECESESEGQNKggndSDELANGEVGGDRNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKlRASVSTKCnleDQVKKL 314
Cdd:PTZ00121 1501 EAKKAAEAKKK----ADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELK-KAEEKKKA---EEAKKA 1572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 315 EDDRNSL--------QAAKAGLEDECKTLRQKVEI-LNELYQQKEMALQKKLSQEEYERQEREHRLSAADEKAVSAAEEV 385
Cdd:PTZ00121 1573 EEDKNMAlrkaeeakKAEEARIEEVMKLYEEEKKMkAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEEL 1652
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462508900 386 KTYKRRIEEMEDELQKTERSFKNQiATHEKKAHENWLKARAAERAIAEEKREAANLRHKLLELTQKMAMLQEE 458
Cdd:PTZ00121 1653 KKAEEENKIKAAEEAKKAEEDKKK-AEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKA 1724
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
63-200 |
2.63e-05 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 44.35 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 63 TAFLGIASFAI-------FLWRTVL-VVKDRvyqvtEQQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQEtrkqnm 134
Cdd:cd06503 1 TLIWQIINFLIllfilkkFLWKPILkALDER-----EEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQE------ 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462508900 135 ILsDEAIKYKDKIKtleknQEILDDTAKNLRVMLESEREQnvknqdlLQQEIEdwsKLHAELSEQI 200
Cdd:cd06503 70 II-EEARKEAEKIK-----EEILAEAKEEAERILEQAKAE-------IEQEKE---KALAELRKEV 119
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
107-342 |
2.89e-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: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 107 ELVQKLSNYEQKIKESKKHVQETRKQNMILSdEAIKYKDKIKTLEKNQEILDDtaknLRVMLESEREQnvKNQDLLQQEI 186
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIELLE-PIRELAERYAAARERLAELEY----LRAALRLWFAQ--RRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 187 EDWSKLHAELSEQIKSFEKSQKDLEvalthkddniNALTNCITQLnllecesesegQNKGGNDSDELANgEVggDRNEKM 266
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALR----------EELDELEAQI-----------RGNGGDRLEQLER-EI--ERLERE 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 267 KNQIKQmmDVSRTQTAISVV-------EEDLKLLQLKLRASVSTkcnLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKV 339
Cdd:COG4913 354 LEERER--RRARLEALLAALglplpasAEEFAALRAEAAALLEA---LEEELEALEEALAEAEAALRDLRRELRELEAEI 428
|
...
gi 2462508900 340 EIL 342
Cdd:COG4913 429 ASL 431
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
91-419 |
3.64e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 91 EQQISEKLKTIMKE--NTELVQKLSNYEQKIKESKKHVQETRKQNMIL--SDEAIKYKDKIKTLEKNQEILDDT--AKNL 164
Cdd:PTZ00121 1442 EAKKADEAKKKAEEakKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKkkAEEAKKKADEAKKAAEAKKKADEAkkAEEA 1521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 165 RVMLESEREQNVKNQDLLQQEIEDWSKLHAELSEQIKSFEKSQKdLEVALTHKDDNINALTNCiTQLNLLEcESESEGQN 244
Cdd:PTZ00121 1522 KKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKK-AEEAKKAEEDKNMALRKA-EEAKKAE-EARIEEVM 1598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 245 KGGNDSDELANGEVGGDRNEKMK-NQIKQMMDVSRT--QTAISVVEEDLKLLQLKlRASVSTKCNLEDQVKKLEDDRNSL 321
Cdd:PTZ00121 1599 KLYEEEKKMKAEEAKKAEEAKIKaEELKKAEEEKKKveQLKKKEAEEKKKAEELK-KAEEENKIKAAEEAKKAEEDKKKA 1677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 322 QAAKAGLEDEcktlRQKVEILNELYQQKEMALQkkLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQK 401
Cdd:PTZ00121 1678 EEAKKAEEDE----KKAAEALKKEAEEAKKAEE--LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKK 1751
|
330
....*....|....*...
gi 2462508900 402 TERSfKNQIAtHEKKAHE 419
Cdd:PTZ00121 1752 DEEE-KKKIA-HLKKEEE 1767
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
96-451 |
4.27e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 96 EKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILD-DTAKNLRVMLESEREQ 174
Cdd:PTZ00121 1070 EGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEaRKAEDARKAEEARKAE 1149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 175 NVKNQDLLQQeIEDWSKLH-AELSEQIKSFEKSQKDLEVALTH---KDDNINALTNC--------ITQLNLLECESESEG 242
Cdd:PTZ00121 1150 DAKRVEIARK-AEDARKAEeARKAEDAKKAEAARKAEEVRKAEelrKAEDARKAEAArkaeeerkAEEARKAEDAKKAEA 1228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 243 QNKG---GNDSDELANGEVGGDRNEKMKNQIKQMMDVSRTQTAISVvEEDLKLLQLKlRASVSTKCnleDQVKKLEDDRN 319
Cdd:PTZ00121 1229 VKKAeeaKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKA-EEARKADELK-KAEEKKKA---DEAKKAEEKKK 1303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 320 SLQAAKAGLE----DECKTLRQKVEILNELYQQKEMALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEM 395
Cdd:PTZ00121 1304 ADEAKKKAEEakkaDEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAA 1383
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462508900 396 E---DELQKTERSFKNqiATHEKKAHENWLKARAAERAIAEEKREAANLRhKLLELTQK 451
Cdd:PTZ00121 1384 KkkaEEKKKADEAKKK--AEEDKKKADELKKAAAAKKKADEAKKKAEEKK-KADEAKKK 1439
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
93-419 |
5.89e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 5.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 93 QISEKLKTIMKENTELVQKLSNYEqKIKESKKHVQETRKQNMILSDEaiKYKDKIKTLEKNQEILDDTAKNLRVM---LE 169
Cdd:PRK03918 342 ELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGLTPE--KLEKELEELEKAKEEIEEEISKITARigeLK 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 170 SEREQNVKN-----------------------QDLLQQ---EIEDWSKLHAELSEQIKSFEKSQKDLEVALThKDDNINA 223
Cdd:PRK03918 419 KEIKELKKAieelkkakgkcpvcgrelteehrKELLEEytaELKRIEKELKEIEEKERKLRKELRELEKVLK-KESELIK 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 224 LTNCITQLNLLECESESEGQNKGGNDSDELangevggdrnEKMKNQIKQMmdvsrtQTAISVVEEDLKllqlKLRASVST 303
Cdd:PRK03918 498 LKELAEQLKELEEKLKKYNLEELEKKAEEY----------EKLKEKLIKL------KGEIKSLKKELE----KLEELKKK 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 304 KCNLEDQVKKLEDDRNSL--QAAKAGLEDEcKTLRQKVEILNELYQQkemalQKKLSQEEYERQEREHRLSAADEKAVSA 381
Cdd:PRK03918 558 LAELEKKLDELEEELAELlkELEELGFESV-EELEERLKELEPFYNE-----YLELKDAEKELEREEKELKKLEEELDKA 631
|
330 340 350
....*....|....*....|....*....|....*...
gi 2462508900 382 AEEVKTYKRRIEEMEDELQKTERSFKNQiaTHEKKAHE 419
Cdd:PRK03918 632 FEELAETEKRLEELRKELEELEKKYSEE--EYEELREE 667
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
168-384 |
6.21e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 168 LESEREQNVKNQDLLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNlleceseSEGQNKGG 247
Cdd:COG3883 28 LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA-------RALYRSGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 248 NDS--DELANGEVGGDRNEKMkNQIKQMMDvsRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQVKKLEDDRNSLQAAK 325
Cdd:COG3883 101 SVSylDVLLGSESFSDFLDRL-SALSKIAD--ADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462508900 326 AGLEDECKTLRQKVEILNELYQQKEMALQKKLSQEEYERQEREHRLSAADEKAVSAAEE 384
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
289-458 |
6.71e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 6.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 289 DLKLLQLKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELY---QQKEMALQKKLSQEEYERQ 365
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELeeaQAEEYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 366 EREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTERsfknQIATHEKKAHEnwlkaraaeraiaeEKREAANLRHKL 445
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEE----ELEEAEEELEE--------------AEAELAEAEEAL 367
|
170
....*....|...
gi 2462508900 446 LELTQKMAMLQEE 458
Cdd:COG1196 368 LEAEAELAEAEEE 380
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
96-405 |
8.09e-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: 46.32 E-value: 8.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 96 EKLKTIMKE---NTELVQKL-SNYEQKIKESKKHVQ-ETRKQNMILSDEAIKYKdkiKTLEKNQEILDDtAKNLRVMLEs 170
Cdd:pfam01576 302 EALKTELEDtldTTAAQQELrSKREQEVTELKKALEeETRSHEAQLQEMRQKHT---QALEELTEQLEQ-AKRNKANLE- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 171 ereqnvKNQDLLQQEiedwsklHAELSEQIKSFEKSQKDLEvaltHKDDNINALTNcitQLNLLECESE---SEGQNKGG 247
Cdd:pfam01576 377 ------KAKQALESE-------NAELQAELRTLQQAKQDSE----HKRKKLEGQLQ---ELQARLSESErqrAELAEKLS 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 248 NDSDELANgeVGGDRNEKMKNQIKQMMDVSRTQTAISVVEEdlkLLQLKLRAsvstKCNLEDQVKKLEDDRNSLQAAkag 327
Cdd:pfam01576 437 KLQSELES--VSSLLNEAEGKNIKLSKDVSSLESQLQDTQE---LLQEETRQ----KLNLSTRLRQLEDERNSLQEQ--- 504
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462508900 328 LEDECKTlRQKVEILNELYQQKEMALQKKLSQEEYErqerehrLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTERS 405
Cdd:pfam01576 505 LEEEEEA-KRNVERQLSTLQAQLSDMKKKLEEDAGT-------LEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKT 574
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
168-404 |
9.06e-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: 45.53 E-value: 9.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 168 LESEREQNVKNQDLLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNLLECESESEGQNKGG 247
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 248 NDSDELANgevggdrNEKMKNQIKQMMDVSrtQTAISVVEEDLKLLQLKLRAsvstkcnLEDQVKKLEDDRNSLQAAKAG 327
Cdd:COG4942 105 ELAELLRA-------LYRLGRQPPLALLLS--PEDFLDAVRRLQYLKYLAPA-------RREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462508900 328 LEDECKTLRQkveILNELYQQKEmALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTER 404
Cdd:COG4942 169 LEAERAELEA---LLAELEEERA-ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
91-447 |
9.73e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 9.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 91 EQQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRK-QNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLE 169
Cdd:PTZ00121 1089 ADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKaEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEE 1168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 170 SEREQNVKNQDLLQQEIEDWSKLHAELSEQIKSFEKSQKDLEValthkddninaltNCITQLNLLECESESEGQNK---G 246
Cdd:PTZ00121 1169 ARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEE-------------RKAEEARKAEDAKKAEAVKKaeeA 1235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 247 GNDSDELANGEVGGDRNEKMKNQIKQMMDVSRTQTAISVVE----EDLKLLQLKLRASVSTKC----NLEDQVKKLEDDR 318
Cdd:PTZ00121 1236 KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEarkaDELKKAEEKKKADEAKKAeekkKADEAKKKAEEAK 1315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 319 NSLQAAKAGLE-----DECKTLRQKVEILNELYQQKEMALQKKLSQEEYERQEREHRLSAADEKAVSA---AEEVKT--- 387
Cdd:PTZ00121 1316 KADEAKKKAEEakkkaDAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAkkkAEEKKKade 1395
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462508900 388 YKRRIEEME---DELQKTERSfKNQIATHEKKAHEnwLKARAAERAIAEEKREAANLRHKLLE 447
Cdd:PTZ00121 1396 AKKKAEEDKkkaDELKKAAAA-KKKADEAKKKAEE--KKKADEAKKKAEEAKKADEAKKKAEE 1455
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
463-715 |
9.73e-05 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 45.93 E-value: 9.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 463 KPMPGKPNTQNPPRRGPLSQNGSFGPSPVSGGEcSPPLTVEPPVRPLSATLNRRDMPRSEfGSVDGPLPHPRWSAEASGK 542
Cdd:PHA03307 83 ESRSTPTWSLSTLAPASPAREGSPTPPGPSSPD-PPPPTPPPASPPPSPAPDLSEMLRPV-GSPGPPPAASPPAAGASPA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 543 PSPSDPGSGTATMMNSSSrGSSPTRVLDEGKVNMAPKGPPPF--PGVPLMSTPMGGPVPPPIRYGPPPQlCGPFGPRPLP 620
Cdd:PHA03307 161 AVASDAASSRQAALPLSS-PEETARAPSSPPAEPPPSTPPAAasPRPPRRSSPISASASSPAPAPGRSA-ADDAGASSSD 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 621 PPFGPGMRPPLGLREFAPGVPPGRRDLPLHPRGFLPGHAPFRPLGSLGPREYFIPGTRLPPPTHGPQEYPPPPAVRDLLP 700
Cdd:PHA03307 239 SSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSS 318
|
250
....*....|....*
gi 2462508900 701 SGSRDEPPPASQSTS 715
Cdd:PHA03307 319 SSSRESSSSSTSSSS 333
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
91-458 |
9.79e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 9.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 91 EQQISEkLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKqnmilsdeaikykdKIKTLEKNQEILDDTAKNLRvmLES 170
Cdd:COG4717 77 EEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELRE--------------ELEKLEKLLQLLPLYQELEA--LEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 171 EREQNVKNQDLLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKD--------DNINALTNCITQLNLLEcESESEG 242
Cdd:COG4717 140 ELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlateeelqDLAEELEELQQRLAELE-EELEEA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 243 QNKGGNDSDELANGEVGGdRNEKMKNQIKQMMDVSRTQTAISVVEEDLKLL---------------------------QL 295
Cdd:COG4717 219 QEELEELEEELEQLENEL-EAAALEERLKEARLLLLIAAALLALLGLGGSLlsliltiagvlflvlgllallflllarEK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 296 KLRASVSTKCNLEDQVKKLEDDRNSLQAAKAGLE-----DECKTLRQKVEILNELYQQKEMALQK-KLSQEEYERQEREH 369
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEEELEELLAALGLPpdlspEELLELLDRIEELQELLREAEELEEElQLEELEQEIAALLA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 370 RLSAADE----KAVSAAEEVKTYKRRIEEMEDELQKTERSFKNQIATHEKKAHENwlkaraaeraiaeekrEAANLRHKL 445
Cdd:COG4717 378 EAGVEDEeelrAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEE----------------ELEELEEEL 441
|
410
....*....|...
gi 2462508900 446 LELTQKMAMLQEE 458
Cdd:COG4717 442 EELEEELEELREE 454
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
92-355 |
1.01e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.98 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 92 QQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQnmiLSDEAIKYKDKIKTL--EKNQEI--LDDTAKNLRVM 167
Cdd:pfam12128 247 QQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAE---LNQLLRTLDDQWKEKrdELNGELsaADAAVAKDRSE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 168 LESEREQnvknqdLLQQEIEDWSKLHAELsEQIKSFeksQKDLEV------ALTHKDDNINALTNCITQLNLLECESESE 241
Cdd:pfam12128 324 LEALEDQ------HGAFLDADIETAAADQ-EQLPSW---QSELENleerlkALTGKHQDVTAKYNRRRSKIKEQNNRDIA 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 242 GQNKGGNDSDELANGEVGGDRN--EKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLR-----ASVSTKCNLEDQVKKL 314
Cdd:pfam12128 394 GIKDKLAKIREARDRQLAVAEDdlQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRlnqatATPELLLQLENFDERI 473
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2462508900 315 EDDRNSLQAAKAG---LEDECKTLRQKVEILNELYQQKEMALQK 355
Cdd:pfam12128 474 ERAREEQEAANAEverLQSELRQARKRRDQASEALRQASRRLEE 517
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
89-404 |
1.03e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.66 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 89 VTEQQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILS-------------DEAIK-----YKDKIKTL 150
Cdd:PRK01156 402 IDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNgqsvcpvcgttlgEEKSNhiinhYNEKKSRL 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 151 EKNQEILDDTAKNlrvmLESEREQNVKNQDLLqqEIEDWSKLHAElSEQIKSFEKSQKDLEVA---LTHKDDNINALTNC 227
Cdd:PRK01156 482 EEKIREIEIEVKD----IDEKIVDLKKRKEYL--ESEEINKSINE-YNKIESARADLEDIKIKineLKDKHDKYEEIKNR 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 228 ITQLNLLECESESEGQNKgGNDSDELANGEVGGDRNEKMKNQIKQMMDvsRTQTAISVVEEDLKLLQLKLRasvstkcNL 307
Cdd:PRK01156 555 YKSLKLEDLDSKRTSWLN-ALAVISLIDIETNRSRSNEIKKQLNDLES--RLQEIEIGFPDDKSYIDKSIR-------EI 624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 308 EDQVKKLEDDRNSLQAAKAGLEdeckTLRQKVEILNELYQQKEMAL--QKKLSQEEYERQEREHRLSAADEKAVSAAEE- 384
Cdd:PRK01156 625 ENEANNLNNKYNEIQENKILIE----KLRGKIDNYKKQIAEIDSIIpdLKEITSRINDIEDNLKKSRKALDDAKANRARl 700
|
330 340
....*....|....*....|...
gi 2462508900 385 ---VKTYKRRIEEMEDELQKTER 404
Cdd:PRK01156 701 estIEILRTRINELSDRINDINE 723
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
82-357 |
1.04e-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: 45.87 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 82 VKDRVYQVTEQQISEK--LKTIMKENTELV-QKLSNYE------QKIKESKKHVQETRKQNMIL---SDEAIKYKDKIKT 149
Cdd:pfam05483 452 IHDLEIQLTAIKTSEEhyLKEVEDLKTELEkEKLKNIEltahcdKLLLENKELTQEASDMTLELkkhQEDIINCKKQEER 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 150 LEKNQEILDDTAKNLRVMLESEREQNVKNQDLLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCIT 229
Cdd:pfam05483 532 MLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIE 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 230 QLNllecESESEGQNKGGNDSDELANGEVGGDRNE----KMKNQIKQMMDVSRTQTAISVVEEDlKLLQ----------- 294
Cdd:pfam05483 612 ELH----QENKALKKKGSAENKQLNAYEIKVNKLElelaSAKQKFEEIIDNYQKEIEDKKISEE-KLLEevekakaiade 686
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462508900 295 -LKLRASVSTKCN------------LEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQKEMALQKKL 357
Cdd:pfam05483 687 aVKLQKEIDKRCQhkiaemvalmekHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQL 762
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
92-211 |
1.39e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.20 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 92 QQISEKLKTIMKENTE----LVQKLSN----YEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEildDTAKN 163
Cdd:PRK00409 501 ENIIEEAKKLIGEDKEklneLIASLEElereLEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAE---KEAQQ 577
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2462508900 164 LRVMLESEREQNVKNQDLLQQEIEDWSKLHaELSEQIKSFEKSQKDLE 211
Cdd:PRK00409 578 AIKEAKKEADEIIKELRQLQKGGYASVKAH-ELIEARKRLNKANEKKE 624
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
92-423 |
1.54e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 92 QQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAK---NLRVML 168
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEeieELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 169 ESeREQNVKNQDLLQQEIEDWSKlhaELSEQIKSFEKSQKDLEvalthkddninaltncitqlnllECESESEgqnkggn 248
Cdd:PRK03918 248 ES-LEGSKRKLEEKIRELEERIE---ELKKEIEELEEKVKELK-----------------------ELKEKAE------- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 249 dsdelangevggdRNEKMKNQIKQMMDVSRTqtaisvVEEDLKLLQLKLRasvstkcNLEDQVKKLEDDRNSLQAakagL 328
Cdd:PRK03918 294 -------------EYIKLSEFYEEYLDELRE------IEKRLSRLEEEIN-------GIEERIKELEEKEERLEE----L 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 329 EDECKTLRQKVEILNELYQQKEMALQKKLSQEEYERQEREHRLsaadEKAVSAAEEVKTYKRRIEEMEDELQKTERSFKN 408
Cdd:PRK03918 344 KKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTP----EKLEKELEELEKAKEEIEEEISKITARIGELKK 419
|
330
....*....|....*
gi 2462508900 409 QIAthEKKAHENWLK 423
Cdd:PRK03918 420 EIK--ELKKAIEELK 432
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
464-716 |
1.55e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 45.31 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 464 PMPGKPNTQNPPRRGPLSQNGSFGPSPVSGGECSPPLTVEPPVRPlsatlnRRDMPRSEFGSV--------DGPLPHPRW 535
Cdd:PHA03247 2639 DPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRP------RRRAARPTVGSLtsladpppPPPTPEPAP 2712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 536 SAEASGKPSPSDPGSGT----ATMMNSSSRGSSPTRVLDEGKvnmAPKGPPPFPGVPLMSTPMGGPVPPPIRYGPPPQLC 611
Cdd:PHA03247 2713 HALVSATPLPPGPAAARqaspALPAAPAPPAVPAGPATPGGP---ARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVA 2789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 612 GPFGPRPLPPPFGPGMRPPLGLREFAPGVPPGRRDLPLHP-----RGFLPGHAPFRPLGSLGPREYFIPG---TRLPPpt 683
Cdd:PHA03247 2790 SLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPpptsaQPTAPPPPPGPPPPSLPLGGSVAPGgdvRRRPP-- 2867
|
250 260 270
....*....|....*....|....*....|...
gi 2462508900 684 hgPQEYPPPPAVRDLLPSGSRDEPPPASQSTSQ 716
Cdd:PHA03247 2868 --SRSPAAKPAAPARPPVRRLARPAVSRSTESF 2898
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
138-458 |
1.63e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 138 DEAI---KYKDKIK-TLEKnqeiLDDTAKNL-RVM------------LESEREQ-----------NVKNQDLLQQEIEDW 189
Cdd:COG1196 162 EEAAgisKYKERKEeAERK----LEATEENLeRLEdilgelerqlepLERQAEKaeryrelkeelKELEAELLLLKLREL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 190 SKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNLlECESESEGQNKGGNDSDELANGEvggDRNEKMKNQ 269
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL-ELEEAQAEEYELLAELARLEQDI---ARLEERRRE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 270 IKQmmDVSRTQTAISVVEEDLKLLQLKLRASVSTkcnLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQK 349
Cdd:COG1196 314 LEE--RLEELEEELAELEEELEELEEELEELEEE---LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 350 EMALQKKLSQEEYERQERE----------HRLSAADEKAVSAAEEvktykrriEEMEDELQKTERSFKNQIATHEKKAHE 419
Cdd:COG1196 389 LEALRAAAELAAQLEELEEaeeallerleRLEEELEELEEALAEL--------EEEEEEEEEALEEAAEEEAELEEEEEA 460
|
330 340 350
....*....|....*....|....*....|....*....
gi 2462508900 420 NWLKARAAERAIAEEKREAANLRHKLLELTQKMAMLQEE 458
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
77-245 |
1.91e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 44.03 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 77 RTVLVVKDRVYQVTEQQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMIL----------SDEAIKYKDK 146
Cdd:pfam15905 165 RNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLleyitelscvSEQVEKYKLD 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 147 IKTLEknqEILDDTAKNLRVMlesereqnvknQDLLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTN 226
Cdd:pfam15905 245 IAQLE---ELLKEKNDEIESL-----------KQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLNAELE 310
|
170
....*....|....*....
gi 2462508900 227 CITQLNLLECESESEGQNK 245
Cdd:pfam15905 311 ELKEKLTLEEQEHQKLQQK 329
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
463-597 |
2.35e-04 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 44.67 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 463 KPMPGKPNTQNPPRRGPlsqngsfgpspvsgGECSPPLTVEPPVRPLSATLNRRDMPRSEFGSVDGPLPHPRWSAEASGK 542
Cdd:PHA03378 675 QPSPTGANTMLPIQWAP--------------GTMQPPPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAA 740
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2462508900 543 PSPSDPGSGTATMMNSSSRGSSPTRVLDEGKVNMAPKGPPPFPGVPlMSTPMGGP 597
Cdd:PHA03378 741 PGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAP-QQRPRGAP 794
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
103-375 |
2.74e-04 |
|
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: 43.98 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 103 KENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNqeiLDDTAKNLRVmLESEREQNVKNQDLL 182
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR---IRALEQELAA-LEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 183 QQEIEdwsKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNLLecesesegqnkggndsdelangevggdr 262
Cdd:COG4942 96 RAELE---AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYL---------------------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 263 NEKMKNQIKQMMdvsRTQTAISVVEEDLKLLQLKLRASVStkcNLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEIL 342
Cdd:COG4942 145 APARREQAEELR---ADLAELAALRAELEAERAELEALLA---ELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218
|
250 260 270
....*....|....*....|....*....|...
gi 2462508900 343 nelyQQKEMALQKKLSQEEYERQEREHRLSAAD 375
Cdd:COG4942 219 ----QQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
497-697 |
3.79e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 44.01 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 497 SPPLTVEPPvrpLSATLNRRDMPRSEFGSVDGPLPHPRWSAEASGKPSPSDPGSGTATmmNSSSRGSSPTRVLDEGKVNM 576
Cdd:PHA03307 759 SNPSLVPAK---LAEALALLEPAEPQRGAGSSPPVRAEAAFRRPGRLRRSGPAADAAS--RTASKRKSRSHTPDGGSESS 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 577 APKGPPP--FPGVPLMSTPMGGPVPPPIRYGPPPQLCGPFGPRPLPPPFGPGMRPPLGLREFAPGVPPGRRDLPLHPRGF 654
Cdd:PHA03307 834 GPARPPGaaARPPPARSSESSKSKPAAAGGRARGKNGRRRPRPPEPRARPGAAAPPKAAAAAPPAGAPAPRPRPAPRVKL 913
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462508900 655 LPghapfRPLGSLGPREYFipgTRLPP-PTHGPqeyPPPPAVRD 697
Cdd:PHA03307 914 GP-----MPPGGPDPRGGF---RRVPPgDLHTP---APSAAALA 946
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
86-335 |
3.88e-04 |
|
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA).
Pssm-ID: 439149 [Multi-domain] Cd Length: 224 Bit Score: 42.40 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 86 VYQVTEQQIseklktIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIK-YKDKIktleknqeilDDTAKNL 164
Cdd:cd21116 15 VTAILNQPN------INLIPLDLLPSLNTHQALARAHALEWLNEIKPKLLSLPNDIIgYNNTF----------QSYYPDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 165 RVMLESEREQNVKNQDLLQQEIEDwskLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNllecesesegqn 244
Cdd:cd21116 79 IELADNLIKGDQGAKQQLLQGLEA---LQSQVTKKQTSVTSFINELTTFKNDLDDDSRNLQTDATKAQ------------ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 245 kggndsDELANGEVggdrnekMKNQIKQMMD-VSRTQTAISVVEEDLKLLQLKLrASVSTKCNLEDQVKKLEDDRNSLQA 323
Cdd:cd21116 144 ------AQVAVLNA-------LKNQLNSLAEqIDAAIDALEKLSNDWQTLDSDI-KELITDLEDAESSIDAAFLQADLKA 209
|
250
....*....|....*
gi 2462508900 324 AKA---GLEDECKTL 335
Cdd:cd21116 210 AKAdwnQLYEQAKSL 224
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
79-400 |
5.46e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 79 VLVVKDRVYQVTEQQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEild 158
Cdd:COG1196 229 LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA--- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 159 dtaknlrvmLESEREQNVKNQdlLQQ---EIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKddninaltncitQLNLLE 235
Cdd:COG1196 306 ---------RLEERRRELEER--LEEleeELAELEEELEELEEELEELEEELEEAEEELEEA------------EAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 236 CESESEgqnkggndsdelangEVGGDRNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQVKKLE 315
Cdd:COG1196 363 AEEALL---------------EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 316 DDRNSLQAAKAGLEDEcktLRQKVEILNELyQQKEMALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEM 395
Cdd:COG1196 428 EALAELEEEEEEEEEA---LEEAAEEEAEL-EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
....*
gi 2462508900 396 EDELQ 400
Cdd:COG1196 504 EGFLE 508
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
91-458 |
5.92e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 5.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 91 EQQISEKLKtimKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRvmles 170
Cdd:PTZ00121 1313 EAKKADEAK---KKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAK----- 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 171 EREQNVKNQDLLQQEIEDWSKlhaeLSEQIKSFEKSQKDLEVALTHKDDNINAltncitqlnlLECESESEGQNKggndS 250
Cdd:PTZ00121 1385 KKAEEKKKADEAKKKAEEDKK----KADELKKAAAAKKKADEAKKKAEEKKKA----------DEAKKKAEEAKK----A 1446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 251 DELANgevGGDRNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLE-----------DQVKKLEDDRN 319
Cdd:PTZ00121 1447 DEAKK---KAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEakkaaeakkkaDEAKKAEEAKK 1523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 320 SLQAAKAGLEDECKTLRQ-----------------------KVEILNELYQQKEMALQKKLSQEEYERQEREHRLSAADE 376
Cdd:PTZ00121 1524 ADEAKKAEEAKKADEAKKaeekkkadelkkaeelkkaeekkKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE 1603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 377 KAVSAAEEVKT---YKRRIEEM--EDELQKTERSFKNQIATHEKKAHE-------NWLKARAAERAIAEEKREAANLRHK 444
Cdd:PTZ00121 1604 EKKMKAEEAKKaeeAKIKAEELkkAEEEKKKVEQLKKKEAEEKKKAEElkkaeeeNKIKAAEEAKKAEEDKKKAEEAKKA 1683
|
410
....*....|....
gi 2462508900 445 LLELTQKMAMLQEE 458
Cdd:PTZ00121 1684 EEDEKKAAEALKKE 1697
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
88-401 |
6.21e-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: 43.17 E-value: 6.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 88 QVTEQQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRkqnmilsdeaikykDKIKTLEKNQEILDDTAKnlrvm 167
Cdd:pfam05483 225 QHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESR--------------DKANQLEEKTKLQDENLK----- 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 168 lesereQNVKNQDLLQQEIEDwskLHAELSEQIKSFEKSQKDLEVAlthkddninalTNCITQLNlLECESESEGQNKGG 247
Cdd:pfam05483 286 ------ELIEKKDHLTKELED---IKMSLQRSMSTQKALEEDLQIA-----------TKTICQLT-EEKEAQMEELNKAK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 248 NDSDELANgevggdrneKMKNQIKQMMDVSRT-QTAISVVEEDLKLLQLKLRASVStkcNLEDQVKKLEDDRNSLQAAKA 326
Cdd:pfam05483 345 AAHSFVVT---------EFEATTCSLEELLRTeQQRLEKNEDQLKIITMELQKKSS---ELEEMTKFKNNKEVELEELKK 412
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462508900 327 GLEDECKTL--RQKVEILNELYQQKEMALQKKLSQEEYERQEREHRLSaadekAVSAAEEvkTYKRRIEEMEDELQK 401
Cdd:pfam05483 413 ILAEDEKLLdeKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLT-----AIKTSEE--HYLKEVEDLKTELEK 482
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
91-398 |
6.86e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.14 E-value: 6.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 91 EQQISEKLKTI----MKENTELVQKLSNYEQKIKESKKHVQETRKqnMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRv 166
Cdd:COG5022 905 ESEIIELKKSLssdlIENLEFKTELIARLKKLLNNIDLEEGPSIE--YVKLPELNKLHEVESKLKETSEEYEDLLKKST- 981
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 167 mlESEREQNVKNQdllqqEIEDWSKLHAELSEQIKSFEKSQKDLEVaLTHKDDNINALTNCITQlnllecESESEGQNKG 246
Cdd:COG5022 982 --ILVREGNKANS-----ELKNFKKELAELSKQYGALQESTKQLKE-LPVEVAELQSASKIISS------ESTELSILKP 1047
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 247 GNDS---DELANGEVGG---------DRNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTkcNLEDQVKKL 314
Cdd:COG5022 1048 LQKLkglLLLENNQLQArykalklrrENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQ--FIVAQMIKL 1125
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 315 eddrNSLQAAKAGLEDECKTLRQKVEILNEL-----YQQKEMALQKKLSQEEYERQEREHRLSAA--DEKAVSAAEEVKT 387
Cdd:COG5022 1126 ----NLLQEISKFLSQLVNTLEPVFQKLSVLqleldGLFWEANLEALPSPPPFAALSEKRLYQSAlyDEKSKLSSSEVND 1201
|
330
....*....|.
gi 2462508900 388 YKRRIEEMEDE 398
Cdd:COG5022 1202 LKNELIALFSK 1212
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
116-350 |
9.82e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 9.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 116 EQKIKESKkHV---QETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKnlrvmLESEREQNVKNQDLLQQEIEDWSKL 192
Cdd:PRK02224 458 GQPVEGSP-HVetiEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVE-----AEDRIERLEERREDLEELIAERRET 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 193 HAELSEQIKSFEKSQKDLEV-------ALTHKDDNINALTNCITQLN--LLECESESEGQNKGGNDSDELAN-GEVGGDR 262
Cdd:PRK02224 532 IEEKRERAEELRERAAELEAeaeekreAAAEAEEEAEEAREEVAELNskLAELKERIESLERIRTLLAAIADaEDEIERL 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 263 NEKMKnQIKQMMDVSR----------TQTAISVVEEDLKLLQLKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAGLE--- 329
Cdd:PRK02224 612 REKRE-ALAELNDERRerlaekrerkRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVEnel 690
|
250 260
....*....|....*....|....*...
gi 2462508900 330 -------DECKTLRQKVEILNELYQQKE 350
Cdd:PRK02224 691 eeleelrERREALENRVEALEALYDEAE 718
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
92-224 |
9.95e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 9.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 92 QQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEIL-DDTAKNLRVMLES 170
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQkEELAELLRALYRL 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462508900 171 ER-------------EQNVKNQDLL-------QQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINAL 224
Cdd:COG4942 117 GRqpplalllspedfLDAVRRLQYLkylaparREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL 190
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
107-224 |
1.01e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 107 ELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLESEREQ--NVKNQ---DL 181
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgNVRNNkeyEA 93
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2462508900 182 LQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINAL 224
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAEL 136
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
105-405 |
1.02e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.90 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 105 NTELVQKLSNYEQKIKES-KKHVQETRKQNMILSDEAIKYKDKI-KTLEKNQEILDDTAKNlrvMLESEREQNVKNQDLL 182
Cdd:PTZ00440 895 NKQLVEHLLNNKIDLKNKlEQHMKIINTDNIIQKNEKLNLLNNLnKEKEKIEKQLSDTKIN---NLKMQIEKTLEYYDKS 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 183 QQEIEDWSKLHAElseQIKSFEKSQKDLEVALTHKDDNINALTNCITQL---------NLLECESESEGQN------KGG 247
Cdd:PTZ00440 972 KENINGNDGTHLE---KLDKEKDEWEHFKSEIDKLNVNYNILNKKIDDLikkqhddiiELIDKLIKEKGKEieekvdQYI 1048
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 248 NDSDELA--------NGEVGGDRNEKMKNQIK----QMMDVSRtqtaiSVVEEDLKLLQLKLRAS---VSTKCNLEDQVK 312
Cdd:PTZ00440 1049 SLLEKMKtklssfhfNIDIKKYKNPKIKEEIKlleeKVEALLK-----KIDENKNKLIEIKNKSHehvVNADKEKNKQTE 1123
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 313 KLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQKEMALQKKLsqeeYERQEREHRLSAADEKAVSAAEEVKTYKRRI 392
Cdd:PTZ00440 1124 HYNKKKKSLEKIYKQMEKTLKELENMNLEDITLNEVNEIEIEYER----ILIDHIVEQINNEAKKSKTIMEEIESYKKDI 1199
|
330
....*....|...
gi 2462508900 393 EEMEDELQKTERS 405
Cdd:PTZ00440 1200 DQVKKNMSKERND 1212
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
82-235 |
1.04e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.97 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 82 VKDRVYQVTEQQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQE----TRKQNMILSDEAIKYKDKIKTleKNQEIL 157
Cdd:cd22656 100 IDDLADATDDEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDfenqTEKDQTALETLEKALKDLLTD--EGGAIA 177
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462508900 158 DDTAKNLRVMLESEREQNVKNqdlLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNLLE 235
Cdd:cd22656 178 RKEIKDLQKELEKLNEEYAAK---LKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPALEKLQ 252
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
92-420 |
1.18e-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: 42.15 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 92 QQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQnmiLSDEAIKYKDKIKTLEKN-QEILDD--TAKNL---- 164
Cdd:pfam06160 96 DDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKT---LLANRFSYGPAIDELEKQlAEIEEEfsQFEELtesg 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 165 -----RVMLESEREQNvknqDLLQQEIEDWSKLHAELS-------EQIKSFEKSQKDLEVALTHK--DDNINALTNCITQ 230
Cdd:pfam06160 173 dyleaREVLEKLEEET----DALEELMEDIPPLYEELKtelpdqlEELKEGYREMEEEGYALEHLnvDKEIQQLEEQLEE 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 231 LnllecesesegqnkggndSDELANGEVGG--DRNEKMKNQIKQMMDVsrtqtaisvveedlkllqlkLRASVSTKCNLE 308
Cdd:pfam06160 249 N------------------LALLENLELDEaeEALEEIEERIDQLYDL--------------------LEKEVDAKKYVE 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 309 DQVKKLEDdrnSLQAAKAGLedecKTLRQKVEILNELYQ------QKEMALQKKLSQEEYERQEREHRLsAADEKAVSA- 381
Cdd:pfam06160 291 KNLPEIED---YLEHAEEQN----KELKEELERVQQSYTlnenelERVRGLEKQLEELEKRYDEIVERL-EEKEVAYSEl 362
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2462508900 382 AEEVKTYKRRIEEMEDELQKtersFKNQIAT---HEKKAHEN 420
Cdd:pfam06160 363 QEELEEILEQLEEIEEEQEE----FKESLQSlrkDELEAREK 400
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
88-357 |
1.52e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.13 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 88 QVTEQQisEKLKTIMKENTELVQKLSNYEQKIKESKK----HVQETRK-----QNMilSDEAIKYKD-----------KI 147
Cdd:PTZ00440 725 QYTIKY--NDLKSSIEEYKEEEEKLEVYKHQIINRKNefilHLYENDKdlpdgKNT--YEEFLQYKDtilnkenkisnDI 800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 148 KTLEKNQEILDDTAKNLRVM---LESEREQNVKN-QDLLQ---QEIED--WSKLHAELSEQIKSFEKSQKDLEvalthkd 218
Cdd:PTZ00440 801 NILKENKKNNQDLLNSYNILiqkLEAHTEKNDEElKQLLQkfpTEDENlnLKELEKEFNENNQIVDNIIKDIE------- 873
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 219 dNINALTNCITQLNLLECESESEGQNkggndSDELANGEvgGDRNEKMKNQIKQM-----MDVSRTQTAISVVEEDLKLL 293
Cdd:PTZ00440 874 -NMNKNINIIKTLNIAINRSNSNKQL-----VEHLLNNK--IDLKNKLEQHMKIIntdniIQKNEKLNLLNNLNKEKEKI 945
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462508900 294 QLKLRASVSTKCNLE-----DQVKKLEDDRNSLQAAKA----GLEDECKTLRQKVEILNELYQqkemALQKKL 357
Cdd:PTZ00440 946 EKQLSDTKINNLKMQiektlEYYDKSKENINGNDGTHLekldKEKDEWEHFKSEIDKLNVNYN----ILNKKI 1014
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
91-355 |
1.58e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.80 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 91 EQQISEkLKTIMKENTELVQKLsnyEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLES 170
Cdd:pfam07888 79 ESRVAE-LKEELRQSREKHEEL---EEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 171 EREQNVKNQDLLQQEIEDWSKLHAEL---SEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNLL-----ECESESEG 242
Cdd:pfam07888 155 MKERAKKAGAQRKEEEAERKQLQAKLqqtEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKlttahRKEAENEA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 243 QNKGGNDSDELANgeVGGDRNEKMKNQIKQMMDV-SRTQTAISVVEedLKLLQLKLRasvstkcnLEDQVKKLEDDRNSL 321
Cdd:pfam07888 235 LLEELRSLQERLN--ASERKVEGLGEELSSMAAQrDRTQAELHQAR--LQAAQLTLQ--------LADASLALREGRARW 302
|
250 260 270
....*....|....*....|....*....|....
gi 2462508900 322 QAAKAGLEDECKTLRQKVEILNELYQQKEMALQK 355
Cdd:pfam07888 303 AQERETLQQSAEADKDRIEKLSAELQRLEERLQE 336
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
92-403 |
1.94e-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: 41.70 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 92 QQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLESE 171
Cdd:pfam01576 387 AELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSL 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 172 REQNVKNQDLLQQEIEdwSKLhaELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNL--------LECESES--- 240
Cdd:pfam01576 467 ESQLQDTQELLQEETR--QKL--NLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAqlsdmkkkLEEDAGTlea 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 241 --EGQNKGGNDSD----ELANGEVGGDRNEKMKNQIKQMMDvsrtqtaisvveeDLKLLQLKLRASVStkcNLEDQVKK- 313
Cdd:pfam01576 543 leEGKKRLQRELEaltqQLEEKAAAYDKLEKTKNRLQQELD-------------DLLVDLDHQRQLVS---NLEKKQKKf 606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 314 ---LEDDRN-SLQAAKA-------GLEDECKTLRQKVEILNELYQQKEMALQKK--------LSQEEYERQEREHRLSAA 374
Cdd:pfam01576 607 dqmLAEEKAiSARYAEErdraeaeAREKETRALSLARALEEALEAKEELERTNKqlraemedLVSSKDDVGKNVHELERS 686
|
330 340
....*....|....*....|....*....
gi 2462508900 375 DEKAVSAAEEVKTykrRIEEMEDELQKTE 403
Cdd:pfam01576 687 KRALEQQVEEMKT---QLEELEDELQATE 712
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
89-193 |
1.96e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 89 VTEQQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLE---------------KN 153
Cdd:COG2433 385 LIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLErelsearseerreirKD 464
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2462508900 154 QEI--LDDTAKNLRVMLESEREQNVKNQDLLQQEIEDWSKLH 193
Cdd:COG2433 465 REIsrLDREIERLERELEEERERIEELKRKLERLKELWKLEH 506
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
93-423 |
2.03e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 93 QISEKLKTIMKENTELVQKLSNYEQKikesKKHVQETRKQNMILSDEAIKYKDKIKT--------LEKNQEILDDTAKNL 164
Cdd:PRK01156 208 DDEKSHSITLKEIERLSIEYNNAMDD----YNNLKSALNELSSLEDMKNRYESEIKTaesdlsmeLEKNNYYKELEERHM 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 165 RVmlesEREQNVKNQDL------LQQEIEDWSKLHAELSEQIKSFEKSQKDLEV-----------------------ALT 215
Cdd:PRK01156 284 KI----INDPVYKNRNYindyfkYKNDIENKKQILSNIDAEINKYHAIIKKLSVlqkdyndyikkksryddlnnqilELE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 216 HKDDNINALTNCITQLNLLECESESEGQNKGGNDSDELANGEVGGDRNEKMKNQIKQMMDvsrtqtaisVVEEDLKLLQL 295
Cdd:PRK01156 360 GYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQ---------DISSKVSSLNQ 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 296 KLRASVSTKCNLEDQV------------------KKLEDDRNSLQAAKAGLEDECKTLRQKVEILNElyqqKEMALQKKL 357
Cdd:PRK01156 431 RIRALRENLDELSRNMemlngqsvcpvcgttlgeEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDE----KIVDLKKRK 506
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 358 SqeeYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTErSFKNQIATHE----KKAHENWLK 423
Cdd:PRK01156 507 E---YLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYE-EIKNRYKSLKledlDSKRTSWLN 572
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
113-419 |
2.20e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.43 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 113 SNYEQKIKESKKHVQETRKQNMILSDeaIKYKD---KIKTLEKNQEILDDTaknlRVMLESEREQNVKNQDLLQQEIEDW 189
Cdd:PLN02939 102 MQRDEAIAAIDNEQQTNSKDGEQLSD--FQLEDlvgMIQNAEKNILLLNQA----RLQALEDLEKILTEKEALQGKINIL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 190 SKLHAELSEQIKSFEKSQKDLEVALThkddninaltncitQLNLLECESESEGQNKGGNDSDELANGEVGGDRNEKMKNQ 269
Cdd:PLN02939 176 EMRLSETDARIKLAAQEKIHVEILEE--------------QLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDD 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 270 IK----QMMDVSRTQTAISVVEEDLKLLQLKLR----------ASVSTKCNLE-----DQVKKLED--DRNSLQAAKAGL 328
Cdd:PLN02939 242 IQflkaELIEVAETEERVFKLEKERSLLDASLReleskfivaqEDVSKLSPLQydcwwEKVENLQDllDRATNQVEKAAL 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 329 E-DECKTLRQKVEILNElyqQKEMALQKKLSQEEYERQEreHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTERSFK 407
Cdd:PLN02939 322 VlDQNQDLRDKVDKLEA---SLKEANVSKFSSYKVELLQ--QKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLK 396
|
330
....*....|..
gi 2462508900 408 NQiatHEKKAHE 419
Cdd:PLN02939 397 EE---SKKRSLE 405
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
96-410 |
2.30e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 96 EKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILsDEAI-----KYKDKIKTLEKNQEILDDTAKN------- 163
Cdd:PRK02224 349 EDADDLEERAEELREEAAELESELEEAREAVEDRREEIEEL-EEEIeelreRFGDAPVDLGNAEDFLEELREErdelrer 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 164 ---LRVMLESEREQNVKNQDLLQ--------QEIEDWSKLHA--ELSEQIKSFEKSQKDLEVALTHKDDNINALTNcitq 230
Cdd:PRK02224 428 eaeLEATLRTARERVEEAEALLEagkcpecgQPVEGSPHVETieEDRERVEELEAELEDLEEEVEEVEERLERAED---- 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 231 lnLLECESESEG-QNKGGNDSDELANGEVGGDRNE-------KMKNQIKQMMDVSR--TQTAISVVE---EDLKLLQLKL 297
Cdd:PRK02224 504 --LVEAEDRIERlEERREDLEELIAERRETIEEKReraeelrERAAELEAEAEEKReaAAEAEEEAEearEEVAELNSKL 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 298 RAsvstkcnLEDQVKKLEDDRNSLqAAKAGLEDECKTLRQKVEILNELY-QQKEMALQKKLSQEEYERQEREHRLSAADE 376
Cdd:PRK02224 582 AE-------LKERIESLERIRTLL-AAIADAEDEIERLREKREALAELNdERRERLAEKRERKRELEAEFDEARIEEARE 653
|
330 340 350
....*....|....*....|....*....|....*..
gi 2462508900 377 K---AVSAAEEVKTYKRRIEEMEDELQKTERSFKNQI 410
Cdd:PRK02224 654 DkerAEEYLEQVEEKLDELREERDDLQAEIGAVENEL 690
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
264-464 |
2.41e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 264 EKMKNQIKQMMD-VSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEIL 342
Cdd:COG4372 62 EQLEEELEQARSeLEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 343 NELYQQKE---MALQKKLSQEEYERQEREHRLSAADEKAVSAA-----EEVKTYKRRIEEMEDELQKTERSFKNQIATHE 414
Cdd:COG4372 142 QSEIAEREeelKELEEQLESLQEELAALEQELQALSEAEAEQAldellKEANRNAEKEEELAEAEKLIESLPRELAEELL 221
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2462508900 415 KKAHENWLKARAAERAIAEEKREAANLRHKLLELTQKMAMLQEEPVIVKP 464
Cdd:COG4372 222 EAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEK 271
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
210-350 |
2.44e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 41.20 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 210 LEVALTHKDDNINALTNCITQLNLLECESESEGQNKGGNDSDELANGEVGGDRNEKMKNQIKQMMDVSRTQTAIS---VV 286
Cdd:pfam05911 642 SENKVAQVDNGCSEIDNLSSDPEIPSDGPLVSGSNDLKTEENKRLKEEFEQLKSEKENLEVELASCTENLESTKSqlqES 721
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462508900 287 EEDLKLLQLKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEIL-NELYQQKE 350
Cdd:pfam05911 722 EQLIAELRSELASLKESNSLAETQLKCMAESYEDLETRLTELEAELNELRQKFEALeVELEEEKN 786
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
110-211 |
2.53e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 40.35 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 110 QKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEIlddTAKNLRVMLESEREQNVKNQD--LLQQEIE 187
Cdd:pfam02841 197 QALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQE---HVKQLIEKMEAEREQLLAEQErmLEHKLQE 273
|
90 100
....*....|....*....|....
gi 2462508900 188 DWSKLHAELSEQIKSFEKSQKDLE 211
Cdd:pfam02841 274 QEELLKEGFKTEAESLQKEIQDLK 297
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
261-459 |
2.61e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 261 DRNEKMKNQIKQMMD-----VSRTQTAISVVEEDLKLLQLKLRAsvstkcnLEDQVKKLEDDRNSLQAAKAGLEDECKTL 335
Cdd:COG4942 23 AEAEAELEQLQQEIAelekeLAALKKEEKALLKQLAALERRIAA-------LARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 336 RQKVEILNELYQQKEMALQKK------------------------LSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRR 391
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLgrqpplalllspedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462508900 392 IEEMEDELQKTERSFKNQIATHEKKAHENWLKARAAERAIAEEKREAANLRHKLLELTQKMAMLQEEP 459
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
95-356 |
3.04e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.04 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 95 SEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMilsDEAIKYKDKIKTLEknQEILDDTAKNLRVMLESEREQ 174
Cdd:PRK01156 475 NEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEI---NKSINEYNKIESAR--ADLEDIKIKINELKDKHDKYE 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 175 NVKNQ------DLLQQEIEDWSKLHAELSeqiksfeksQKDLEVALTHKDDNINALTNCITQLNLLECE---SESEGQNK 245
Cdd:PRK01156 550 EIKNRykslklEDLDSKRTSWLNALAVIS---------LIDIETNRSRSNEIKKQLNDLESRLQEIEIGfpdDKSYIDKS 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 246 GGNDSDELANgevggdrnekMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKL------RASVSTKCN-LEDQVKKLEDDR 318
Cdd:PRK01156 621 IREIENEANN----------LNNKYNEIQENKILIEKLRGKIDNYKKQIAEIdsiipdLKEITSRINdIEDNLKKSRKAL 690
|
250 260 270
....*....|....*....|....*....|....*...
gi 2462508900 319 NSLQAAKAGLEDECKTLRQKVEILNELYQQKEMALQKK 356
Cdd:PRK01156 691 DDAKANRARLESTIEILRTRINELSDRINDINETLESM 728
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
93-410 |
3.21e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 40.97 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 93 QISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKnqeilddtaknlrvmLESER 172
Cdd:PTZ00440 474 DLIISEKDSMDSKEKKESSDSNYQEKVDELLQIINSIKEKNNIVNNNFKNIEDYYITIEG---------------LKNEI 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 173 EQNVKNQDLLQQEIEDwsklhaelseqIKSFEKSQKDLEVALTHKDDNINALTNCITQLNLLECESESEGQNKGGNDSDE 252
Cdd:PTZ00440 539 EGLIELIKYYLQSIET-----------LIKDEKLKRSMKNDIKNKIKYIEENVDHIKDIISLNDEIDNIIQQIEELINEA 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 253 LANGEVGGDRNEKMKNQIKQMMDvsrtqtaiSVVEEDLKLLQLKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAgledEC 332
Cdd:PTZ00440 608 LFNKEKFINEKNDLQEKVKYILN--------KFYKGDLQELLDELSHFLDDHKYLYHEAKSKEDLQTLLNTSKN----EY 675
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 333 KTLRQKV-----EILNELYQQKEMALQKKLSQEEYERQEREHRLSAADEKAVsaaEEVKTYKRRIEEMEDELQKTErSFK 407
Cdd:PTZ00440 676 EKLEFMKsdnidNIIKNLKKELQNLLSLKENIIKKQLNNIEQDISNSLNQYT---IKYNDLKSSIEEYKEEEEKLE-VYK 751
|
...
gi 2462508900 408 NQI 410
Cdd:PTZ00440 752 HQI 754
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
102-472 |
3.48e-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: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 102 MKENTELVQKLSN-YEQKIKESKKHV-----QETRKQNMI-----LSDEAikyKDKIKTLEKNQEILDDTAKNL---RVM 167
Cdd:pfam05483 217 LKEDHEKIQHLEEeYKKEINDKEKQVsllliQITEKENKMkdltfLLEES---RDKANQLEEKTKLQDENLKELiekKDH 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 168 LESERE-------QNVKNQDLLQQEIEDWSKLHAELSE----QIKSFEKSQKDLEVALTHKDDNINALTNCI-------- 228
Cdd:pfam05483 294 LTKELEdikmslqRSMSTQKALEEDLQIATKTICQLTEekeaQMEELNKAKAAHSFVVTEFEATTCSLEELLrteqqrle 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 229 ---TQLNLLECE-----SESEGQNKGGNDSD-ELANGEVGGDRNEKMKNQIKQMMDVS-----RTQTAISVV---EEDLK 291
Cdd:pfam05483 374 kneDQLKIITMElqkksSELEEMTKFKNNKEvELEELKKILAEDEKLLDEKKQFEKIAeelkgKEQELIFLLqarEKEIH 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 292 LLQLKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNElyQQKEMALQ-KKLSQEEYERQEREHR 370
Cdd:pfam05483 454 DLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQ--EASDMTLElKKHQEDIINCKKQEER 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 371 LSaadeKAVSAAEEVKTYKR-RIEEMEDELQKTERSFKNQIATHEKKAHENWLKARAAERAIAEEKREAANLRHKLLELT 449
Cdd:pfam05483 532 ML----KQIENLEEKEMNLRdELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKN 607
|
410 420
....*....|....*....|...
gi 2462508900 450 QKMAMLQEEPVIVKPMPGKPNTQ 472
Cdd:pfam05483 608 KNIEELHQENKALKKKGSAENKQ 630
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
308-409 |
3.59e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 308 EDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQKEMalqkklsqeeyerqerehRLSAADEKAVSAAEEVKT 387
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQA------------------ELEALQAEIDKLQAEIAE 76
|
90 100
....*....|....*....|..
gi 2462508900 388 YKRRIEEMEDELQKTERSFKNQ 409
Cdd:COG3883 77 AEAEIEERREELGERARALYRS 98
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
85-471 |
3.65e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.72 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 85 RVYQVTEQQISEKLKTIMKENTELVQ---KLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKD----KIKTLEKNQEIL 157
Cdd:TIGR00618 145 RVVLLPQGEFAQFLKAKSKEKKELLMnlfPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLctpcMPDTYHERKQVL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 158 DDTAKNLRVMLESEREQNVK--NQDLLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNLLE 235
Cdd:TIGR00618 225 EKELKHLREALQQTQQSHAYltQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQ 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 236 CESESEGQNKggndsdELangevggdrNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLE------- 308
Cdd:TIGR00618 305 IEQQAQRIHT------EL---------QSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEvatsire 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 309 --DQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQ------KEMALQKKLSQEEYERQEREHRLSAADEKAVS 380
Cdd:TIGR00618 370 isCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATidtrtsAFRDLQGQLAHAKKQQELQQRYAELCAAAITC 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 381 AAEEVKTYKRRIEEMEDELQKTERSFKNQIATHEKKAHenwlKARAAERAIAEEKREAANLRHKLLELTQKMAMLQEEPV 460
Cdd:TIGR00618 450 TAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETR----KKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGP 525
|
410
....*....|.
gi 2462508900 461 IVKPMPGKPNT 471
Cdd:TIGR00618 526 LTRRMQRGEQT 536
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
104-442 |
3.73e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 104 ENTELVQKLSNYE--------QKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLESEREQN 175
Cdd:PTZ00121 1209 EEERKAEEARKAEdakkaeavKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE 1288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 176 VKNQDLLQQeiedwsklhaelSEQIKSFEKSQKDLEVAltHKDDNINALTNcitqlnllECESESEGQNKGGNDS---DE 252
Cdd:PTZ00121 1289 KKKADEAKK------------AEEKKKADEAKKKAEEA--KKADEAKKKAE--------EAKKKADAAKKKAEEAkkaAE 1346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 253 LANGEVGGDRNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLE-----DQVKKLEDDRNSLQAAKAG 327
Cdd:PTZ00121 1347 AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEdkkkaDELKKAAAAKKKADEAKKK 1426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 328 LEDECKT--LRQKVEILNELYQQKEMALQKKLSQEEYERQEREHRLSAADEKAVSA--AEEVKT----YKRRIEEME--- 396
Cdd:PTZ00121 1427 AEEKKKAdeAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAkkADEAKKkaeeAKKKADEAKkaa 1506
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2462508900 397 ------DELQKTERSFKnqiATHEKKAHEnwlKARAAERAIAEEKREAANLR 442
Cdd:PTZ00121 1507 eakkkaDEAKKAEEAKK---ADEAKKAEE---AKKADEAKKAEEKKKADELK 1552
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
85-407 |
4.44e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.45 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 85 RVYQVTEQQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLE-KNQEILDDTAKN 163
Cdd:COG5022 853 RSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDLiENLEFKTELIAR 932
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 164 LRVMLeseREQNVKNQDLLQQEIEDwskLHAELSEQIKSFEKSQKDLEvalthkddninaltncitqlNLLECESESEGQ 243
Cdd:COG5022 933 LKKLL---NNIDLEEGPSIEYVKLP---ELNKLHEVESKLKETSEEYE--------------------DLLKKSTILVRE 986
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 244 NKGgndsdelangevggdRNEKMKNQIKQMMDVSRTQTAISvveEDLKLLQLKLRASVStkcnLEDQVKKLeddrNSLQA 323
Cdd:COG5022 987 GNK---------------ANSELKNFKKELAELSKQYGALQ---ESTKQLKELPVEVAE----LQSASKII----SSEST 1040
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 324 AKAGLEDEcktlrQKVEILNELyqqKEMALQKKLsqeeyERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTE 403
Cdd:COG5022 1041 ELSILKPL-----QKLKGLLLL---ENNQLQARY-----KALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTNRN 1107
|
....
gi 2462508900 404 RSFK 407
Cdd:COG5022 1108 LVKP 1111
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
92-205 |
4.75e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.51 E-value: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 92 QQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEknqEILDDTAKNLRVMLESE 171
Cdd:COG1340 170 KELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELH---EEIIELQKELRELRKEL 246
|
90 100 110
....*....|....*....|....*....|....*
gi 2462508900 172 REQNVKNQDLLQQEI-EDWSKLHAELSEQIKSFEK 205
Cdd:COG1340 247 KKLRKKQRALKREKEkEELEEKAEEIFEKLKKGEK 281
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
91-241 |
5.93e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 5.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 91 EQQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEaikykdkiktLEKNQEILDDTAKN------- 163
Cdd:COG3883 32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE----------IEERREELGERARAlyrsggs 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 164 ---LRVMLESE-------REQNVK-----NQDLLQQ---EIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALT 225
Cdd:COG3883 102 vsyLDVLLGSEsfsdfldRLSALSkiadaDADLLEElkaDKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQE 181
|
170
....*....|....*.
gi 2462508900 226 NCITQLNLLECESESE 241
Cdd:COG3883 182 ALLAQLSAEEAAAEAQ 197
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
464-715 |
5.97e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 40.31 E-value: 5.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 464 PMPGKPNTQNPPRRGPLSQNGSFGPSPVSGGECSPPLTVEPPVRPLSATLNRRDMPRSEFGSVDGPLPHPRWSAEASGKP 543
Cdd:PHA03247 2554 PLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSP 2633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 544 SPSDPGSGTATMMNSSSR---GSSPTRVLDEGKVNMAPKGPPPfpgvplmSTPMGGPvPPPIRYGPPPQLCGPFGPRPLP 620
Cdd:PHA03247 2634 AANEPDPHPPPTVPPPERprdDPAPGRVSRPRRARRLGRAAQA-------SSPPQRP-RRRAARPTVGSLTSLADPPPPP 2705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 621 PPFGPGMRPPLGLREFAPGVPPGRRDLPLHPRGFLPGHAPFRPLGSLGPREyfiPGTrlPPPTHGPQEyPPPPAVRDLLP 700
Cdd:PHA03247 2706 PTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPAR---PAR--PPTTAGPPA-PAPPAAPAAGP 2779
|
250
....*....|....*
gi 2462508900 701 SGSRDEPPPASQSTS 715
Cdd:PHA03247 2780 PRRLTRPAVASLSES 2794
|
|
| PilN |
COG3166 |
Type IV pilus assembly protein PilN [Cell motility, Extracellular structures]; |
55-244 |
7.48e-03 |
|
Type IV pilus assembly protein PilN [Cell motility, Extracellular structures];
Pssm-ID: 442399 [Multi-domain] Cd Length: 185 Bit Score: 38.02 E-value: 7.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 55 LPWKP-----------VFITAFLGIASFAIFLWRTVLVvkdrvYQVTEQQiseklktimKENTELVQKLSNYEQKIKEsk 123
Cdd:COG3166 7 LPWREerrkrrkrrflALLVLALLLALAVLFLVYLYLQ-----GQIAQQQ---------ARNAALQQEIAKLDKQIAE-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 124 khVQETRKQnmilsdeaikykdkIKTLEKNQEILDDtaknlrvmlesereqnvknqdlLQQEIEDWSKLHAELSEQI--- 200
Cdd:COG3166 71 --IKELKKQ--------------KAELLARLQVIEQ----------------------LQQSRPPWVHLLDELARLLpeg 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2462508900 201 ---KSFEKSQKDLE---VALTHKD-----DNINAlTNCITQLNLLECESESEGQN 244
Cdd:COG3166 113 vwlTSLSQQGGTLTltgVAQSNARvaefmRNLEA-SPWFSDVELVEIEAKDDGKG 166
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
149-358 |
7.70e-03 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 38.92 E-value: 7.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 149 TLEKNQEILDdtakNLRVMLESEREQNVKN---------QDLLQQEiEDWS-KLHAELS--------EQIKSFEKSqkdl 210
Cdd:pfam15294 31 TIDEVTEMLD----GLQTVVRGEVESELINtshtnvlllRQLFSQA-EKWHlKLQADISelenrellEQIAEFEER---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 211 EVALTHKDDNinaltnciTQLNllecESESEGQNKGGndSDELANGEVG--GDRNEKMKNQIKQMMdvSRTQTAI---SV 285
Cdd:pfam15294 102 EFTSSNKKPN--------FELN----KPKLEPLNEGG--GSALLHMEIErlKEENEKLKERLKTLE--SQATQALdekSK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 286 VEEDLKLLQLKLRA------SVSTKCNLEDQVKKLEDD----RNSLQAAKAGLEDECKTLRQKVEILNELYQQKEMALQK 355
Cdd:pfam15294 166 LEKALKDLQKEQGAkkdvksNLKEISDLEEKMAALKSDlektLNASTALQKSLEEDLASTKHELLKVQEQLEMAEKELEK 245
|
...
gi 2462508900 356 KLS 358
Cdd:pfam15294 246 KFQ 248
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
91-211 |
8.82e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 38.37 E-value: 8.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 91 EQQISEKLKTIMKENTELVQ---KLSNYEQKIKESKKHVQETRKQnmilSDEAIKYKD------KIKTLEKNQEILDDTA 161
Cdd:COG1579 37 EDELAALEARLEAAKTELEDlekEIKRLELEIEEVEARIKKYEEQ----LGNVRNNKEyealqkEIESLKRRISDLEDEI 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2462508900 162 KNLRVMLESEREQNVKNQDLLQQEIEDWSKLHAELSEQIKSFEKSQKDLE 211
Cdd:COG1579 113 LELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
92-344 |
9.34e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.67 E-value: 9.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 92 QQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMI-LSDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLES 170
Cdd:TIGR02169 254 EKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGeLEAEIASLERSIAEKERELEDAEERLAKLEAEIDK 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 171 EREQnvknQDLLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKD--------------DNINALTNCITQLNLLEC 236
Cdd:TIGR02169 334 LLAE----IEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDkefaetrdelkdyrEKLEKLKREINELKRELD 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 237 ESESEGQNKggndSDELANGEVGGDRNEKMKNQIKQMMD-----VSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQV 311
Cdd:TIGR02169 410 RLQEELQRL----SEELADLNAAIAGIEAKINELEEEKEdkaleIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEL 485
|
250 260 270
....*....|....*....|....*....|...
gi 2462508900 312 KKLEDDRNSLQAAKAGLEDECKTLRQKVEILNE 344
Cdd:TIGR02169 486 SKLQRELAEAEAQARASEERVRGGRAVEEVLKA 518
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
84-456 |
9.51e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 39.64 E-value: 9.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 84 DRVYQVTEQQISEKLKTIMKENTELVQKLSNYEQ---KIKESKKHVQET-RKQNMILSDEAIKYKDKIKTLEKNQEILDD 159
Cdd:TIGR00606 393 KNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEqadEIRDEKKGLGRTiELKKEILEKKQEELKFVIKELQQLEGSSDR 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 160 TAKNLRVMLESEREQNVKNQDLLQQEiedwsklhaeLSEQIKSFEKSQKDLE---VALTHKDDNINALTNCITQLNLLEC 236
Cdd:TIGR00606 473 ILELDQELRKAERELSKAEKNSLTET----------LKKEVKSLQNEKADLDrklRKLDQEMEQLNHHTTTRTQMEMLTK 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 237 ESESEGQNKGGND---SDELA-------NGEVGGDRNEKMKNQIKQMmdvsrtqtaisvvEEDLKLLQLKLRASVSTKCN 306
Cdd:TIGR00606 543 DKMDKDEQIRKIKsrhSDELTsllgyfpNKKQLEDWLHSKSKEINQT-------------RDRLAKLNKELASLEQNKNH 609
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 307 LEDQVKKLEDDRNSLQAA---KAGLEDECKTLRQKVEILNELYQQKEMalqkkLSQEEYERQEREHRLSAADEKAVSAAE 383
Cdd:TIGR00606 610 INNELESKEEQLSSYEDKlfdVCGSQDEESDLERLKEEIEKSSKQRAM-----LAGATAVYSQFITQLTDENQSCCPVCQ 684
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508900 384 EVKTYKRRIEEMEDELQKTERSF-------KNQIATHEKKAHENWLKARAAERAIAEEKREAANLRHKLLELTQKMAMLQ 456
Cdd:TIGR00606 685 RVFQTEAELQEFISDLQSKLRLApdklkstESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLK 764
|
|
| |
