|
Name |
Accession |
Description |
Interval |
E-value |
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
90-469 |
1.37e-15 |
|
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: 80.83 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 90 TEQQISEKLKNIMKENAELVQK------LSSYEQKIKESKKHVQETKKQNMILSDEAIKFKDKIkslEETNEILGDTAKS 163
Cdd:TIGR04523 178 LEKEKLNIQKNIDKIKNKLLKLelllsnLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEI---NEKTTEISNTQTQ 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 164 LRAMLESerEQNAKNQdlISENKKSIEKLKDVISVNASEFSEVQIALNEakLSEEKVKSECHRVQEENARLKKKKEQLQQ 243
Cdd:TIGR04523 255 LNQLKDE--QNKIKKQ--LSEKQKELEQNNKKIKELEKQLNQLKSEISD--LNNQKEQDWNKELKSELKNQEKKLEEIQN 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 244 EIKDWSKSHAELSEQIRSFEKSQKDLEVALTHKDDNINALTNCITQLNRldcESESEDQNKGGSESdelangevggdRSE 323
Cdd:TIGR04523 329 QISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKK---ENQSYKQEIKNLES-----------QIN 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 324 KVKNQIKQMMDVSRT-QTAISVVEEDLKLLQCKLRASMSTKCNLEDQIKKLEEDRSSLQSAKTVLEDECKTLRQKVEILN 402
Cdd:TIGR04523 395 DLESKIQNQEKLNQQkDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLS 474
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387212246 403 ELYQQKEMALQKKlsqeEYERQEREQRLSAADEKAVLAAEEVKTYKRRIEEMEDELQKTErSFKNQI 469
Cdd:TIGR04523 475 RSINKIKQNLEQK----QKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLE-SEKKEK 536
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
90-474 |
2.00e-15 |
|
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: 80.45 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 90 TEQQISEKLKNIMKENAELVQKLSSYEQKIK----ESKKHVQETKKQNMILSDEAIKFKDKIKSLEetNEILGDTAKSLR 165
Cdd:TIGR04523 236 KKQQEINEKTTEISNTQTQLNQLKDEQNKIKkqlsEKQKELEQNNKKIKELEKQLNQLKSEISDLN--NQKEQDWNKELK 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 166 AMLESEREQ--NAKNQdlISENKKSIEKLKDVISV-------NASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKK 236
Cdd:TIGR04523 314 SELKNQEKKleEIQNQ--ISQNNKIISQLNEQISQlkkeltnSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLES 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 237 KKEQLQQEIKDWSKSHAELSEQIRSF-------EKSQKDLEVALTHKDDNINALTNCITQLNRL--DCESESEDQNKggs 307
Cdd:TIGR04523 392 QINDLESKIQNQEKLNQQKDEQIKKLqqekellEKEIERLKETIIKNNSEIKDLTNQDSVKELIikNLDNTRESLET--- 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 308 ESDELangevggdrsEKVKNQIKQMMDvsRTQTAISVVEEDLKLLQCKLRASMSTKCNLEDQIKKLEEDRSSLQSAKTVL 387
Cdd:TIGR04523 469 QLKVL----------SRSINKIKQNLE--QKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEK 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 388 EDECKTLRQKVEILN-----ELYQQKEMALQKKLSQEEYERQEREQRLSAADEKAVLAAEEVKTYKRRIEEMEDELQKTE 462
Cdd:TIGR04523 537 ESKISDLEDELNKDDfelkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLE 616
|
410
....*....|..
gi 1387212246 463 RSFKNQIATHEK 474
Cdd:TIGR04523 617 KELEKAKKENEK 628
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
84-478 |
1.91e-14 |
|
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: 77.45 E-value: 1.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 84 SRVYQVTEQQiSEKLKNI-MKENAELVQKlssyEQKIKESKKHVQETKK--QNMILSDEAIKFKDKiKSLEETNEILGDT 160
Cdd:pfam05483 77 SRLYSKLYKE-AEKIKKWkVSIEAELKQK----ENKLQENRKIIEAQRKaiQELQFENEKVSLKLE-EEIQENKDLIKEN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 161 aKSLRAMLESEREQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNEAKLSEEKVKSECH-RVQEENARLKKKKE 239
Cdd:pfam05483 151 -NATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHfKLKEDHEKIQHLEE 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 240 QLQQEIKDWSKSHAELSEQIRSFEKSQKDLEVALTHKDDNINALTncitQLNRLDCESESEDQNKGGSESDELangevgg 319
Cdd:pfam05483 230 EYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLE----EKTKLQDENLKELIEKKDHLTKEL------- 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 320 drsEKVKNQIKQMMDVSRTqtaisvVEEDLKLlqcklraSMSTKCNL----EDQIKKLEEDRSS-------LQSAKTVLE 388
Cdd:pfam05483 299 ---EDIKMSLQRSMSTQKA------LEEDLQI-------ATKTICQLteekEAQMEELNKAKAAhsfvvteFEATTCSLE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 389 DECKTLRQKVEILNELYQQKEMALQKKLSQEEYERQEREQRLSAADE-KAVLAAEEVKTY-KRRIEEMEDELQKTERSFK 466
Cdd:pfam05483 363 ELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEElKKILAEDEKLLDeKKQFEKIAEELKGKEQELI 442
|
410
....*....|..
gi 1387212246 467 NQIATHEKKAHD 478
Cdd:pfam05483 443 FLLQAREKEIHD 454
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
96-414 |
6.44e-14 |
|
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: 75.78 E-value: 6.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 96 EKLKNIMKENAELVQKLSSYEQKIKESKKHVQETKK---------------QNMILSDEAIKFKDKIKSLEETNEILGDT 160
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELKLKEQAKKaleyyqlkekleleeEYLLYLDYLKLNEERIDLLQELLRDEQEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 161 AKSLRAMLESEREQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQ 240
Cdd:pfam02463 253 IESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 241 LQQEIKDWSKSHAELSEQIRSFEKSQKDLEVALTHKddninaltncITQLNRLDCESESEDQNKGGSESD-----ELANG 315
Cdd:pfam02463 333 EKEEIEELEKELKELEIKREAEEEEEEELEKLQEKL----------EQLEEELLAKKKLESERLSSAAKLkeeelELKSE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 316 EVGGDRSEKVKNQIKQMMDVSRTQTAISVVEEDLKLLQCKLRASMSTKCNLEDQIKKLEEDRSSLQSAKTVLEDECKTLR 395
Cdd:pfam02463 403 EEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKL 482
|
330
....*....|....*....
gi 1387212246 396 QKVEILNELYQQKEMALQK 414
Cdd:pfam02463 483 QEQLELLLSRQKLEERSQK 501
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
79-399 |
1.11e-13 |
|
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: 75.09 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 79 VLAVKSRVYQVTEQ--QISEKLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIKFKDKIKSLEETNEI 156
Cdd:TIGR02168 672 ILERRREIEELEEKieELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 157 LGDTAKSLRAMLESEREQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKK 236
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 237 KKEQLQQEIKDWSKSHAELSEQIRSFEKSQKDLEVALTHKDDNINALTNCITQLNRLDCESESEDQNKggseSDELANGE 316
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL----SEELRELE 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 317 vgGDRSEKVKNQIKQMMDVSRTQTAISVVEEDLKLLQCKLRASMSTkcNLEDQIKKLEEDRSSLQSAktvlEDECKTLRQ 396
Cdd:TIGR02168 908 --SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSL--TLEEAEALENKIEDDEEEA----RRRLKRLEN 979
|
...
gi 1387212246 397 KVE 399
Cdd:TIGR02168 980 KIK 982
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
81-475 |
4.11e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.17 E-value: 4.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 81 AVKSRVYQVTEQQISEKLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKqnmilSDEAIKFKDKIKSLEETNEILGDT 160
Cdd:PTZ00121 1382 AAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKK-----ADEAKKKAEEAKKADEAKKKAEEA 1456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 161 AKSLRAMLESEREQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNEAKLSEEKVKSECHRVQEE--NARLKKKK 238
Cdd:PTZ00121 1457 KKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEakKAEEAKKA 1536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 239 EQLQQEIKDWSKSHAELSEQIRSFEKSQKdLEVALTHKDDNINALTNciTQLNRLDCESESEDQNKGGSESDELANGEVG 318
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKAEELKKAEEKKK-AEEAKKAEEDKNMALRK--AEEAKKAEEARIEEVMKLYEEEKKMKAEEAK 1613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 319 GDRSEKVK-NQIKQMMDVSRTQTAISVVEEDLKLLQCKLR-ASMSTKCNLEDQIKKLEEDRSSLQSAKTVLEDEcktlRQ 396
Cdd:PTZ00121 1614 KAEEAKIKaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKkAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE----KK 1689
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387212246 397 KVEILNELYQQKEMALQkkLSQEEYERQEREQRLSAADEKAVLAAEEVKTYKRRIEEMEDELQKTERSfKNQIATHEKK 475
Cdd:PTZ00121 1690 AAEALKKEAEEAKKAEE--LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE-KKKIAHLKKE 1765
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
90-403 |
5.82e-12 |
|
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: 69.28 E-value: 5.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 90 TEQQISE---KLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIKFKDKIKSLEETNEILGDTAKSLRA 166
Cdd:TIGR04523 333 NNKIISQlneQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDE 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 167 MLESEREQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIK 246
Cdd:TIGR04523 413 QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELK 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 247 DWSKSHAELSEQIRSFEKSQKDLEvalthkdDNINALTNCITQLNRLDCESESEDQNKggseSDELANGEVGGDRS--EK 324
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKVKDLT-------KKISSLKEKIEKLESEKKEKESKISDL----EDELNKDDFELKKEnlEK 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 325 VKNQIKQMMD-VSRTQTAISVVEEDLKLLQCKLRAS-----------MSTKCNLEDQIKKLEEDRSSLQSAKTVLEDECK 392
Cdd:TIGR04523 562 EIDEKNKEIEeLKQTQKSLKKKQEEKQELIDQKEKEkkdlikeieekEKKISSLEKELEKAKKENEKLSSIIKNIKSKKN 641
|
330
....*....|.
gi 1387212246 393 TLRQKVEILNE 403
Cdd:TIGR04523 642 KLKQEVKQIKE 652
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
91-462 |
1.48e-10 |
|
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: 65.09 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 91 EQQISEKLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKqnmilsdeaikfkdKIKSLEETNEILGDTAKSLRAMLES 170
Cdd:TIGR02169 676 LQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASR--------------KIGEIEKEIEQLEQEEEKLKERLEE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 171 EREQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALN--EAKLSEEKVksechrvqeenarlkkkkEQLQQEIKDW 248
Cdd:TIGR02169 742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNdlEARLSHSRI------------------PEIQAELSKL 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 249 SKSHAELSEQIRSFEKSqkdlevalthkddninaltncitqLNRLDCESESEDqnkggsesDELANGEVGGDRSEKVKNQ 328
Cdd:TIGR02169 804 EEEVSRIEARLREIEQK------------------------LNRLTLEKEYLE--------KEIQELQEQRIDLKEQIKS 851
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 329 IKQMMDVSRTQtaISVVEEDLKLLQCKLRasmstkcNLEDQIKKLEEDRSSLQSAKTVLEDECKTLRQKVEILNELYQQK 408
Cdd:TIGR02169 852 IEKEIENLNGK--KEELEEELEELEAALR-------DLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL 922
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1387212246 409 EMALQKKLSQEEYERQEREQRLSAADEKAVLaaeevKTYKRRIEEMEDELQKTE 462
Cdd:TIGR02169 923 KAKLEALEEELSEIEDPKGEDEEIPEEELSL-----EDVQAELQRVEEEIRALE 971
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
119-462 |
2.27e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.31 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 119 IKESKKHVQETKKQnmilSDEAIKFKDKIKSLEETN-EILGDTAKSLRAMLESEREQNAKNQDLISENKKSIEKLKDVIS 197
Cdd:TIGR02168 195 LNELERQLKSLERQ----AEKAERYKELKAELRELElALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 198 VNASEFSEVQIALNEAKlseekvkSECHRVQEENARLKKKKEQLQQEIKDWSKSHAELSEQIRSFEKSQKDLEVALTHKD 277
Cdd:TIGR02168 271 ELRLEVSELEEEIEELQ-------KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 278 DNINALTNCItqlnrldcESESEDQNKGGSESDELANgevggdRSEKVKNQIKQMmdvsrtQTAISVVEEDLKLLQCKLR 357
Cdd:TIGR02168 344 EKLEELKEEL--------ESLEAELEELEAELEELES------RLEELEEQLETL------RSKVAQLELQIASLNNEIE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 358 ASMSTKCNLEDQIKKLEEDRSSLQSAKTvlEDECKTLRQKVEILNELYQQkemaLQKKLSQEEYERQEREQRLSAADEKA 437
Cdd:TIGR02168 404 RLEARLERLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEEELEE----LQEELERLEEALEELREELEEAEQAL 477
|
330 340
....*....|....*....|....*
gi 1387212246 438 VLAAEEVKTYKRRIEEMEDELQKTE 462
Cdd:TIGR02168 478 DAAERELAQLQARLDSLERLQENLE 502
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
80-530 |
2.86e-10 |
|
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: 63.97 E-value: 2.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 80 LAVKSrVYQVTEQQiSEKLKNIMKENA-------ELVQKLSSYEQKIKESKKHVQETKKQNMILS----------DEAIK 142
Cdd:pfam05483 321 IATKT-ICQLTEEK-EAQMEELNKAKAahsfvvtEFEATTCSLEELLRTEQQRLEKNEDQLKIITmelqkksselEEMTK 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 143 FKD-KIKSLEETNEILGDTAKSLRAMLESER---EQNAKNQDLI---SENKKSIEKLKDVISVNAS-------EFSEVQI 208
Cdd:pfam05483 399 FKNnKEVELEELKKILAEDEKLLDEKKQFEKiaeELKGKEQELIfllQAREKEIHDLEIQLTAIKTseehylkEVEDLKT 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 209 ALNEAKLSEEKVKSECHRVQEENARLKKKKEQL-------QQEIKDWSKSHAELSEQIRSFEKSQKDLEVALTHKDDNIn 281
Cdd:pfam05483 479 ELEKEKLKNIELTAHCDKLLLENKELTQEASDMtlelkkhQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEF- 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 282 altncITQLNRLDCESESEDQNKGGSESDELANGEVGGDRSEKVKNQIKQMMDVSRTqtaISVVEEDLKLLQCKLRASMS 361
Cdd:pfam05483 558 -----IQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKN---IEELHQENKALKKKGSAENK 629
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 362 TKCNLEDQIKKLEEDrssLQSAKTVLEDECKTLRQKVEIlnelyqqkemalqKKLSQEEYERQEREQRLSAaDEKAVLAA 441
Cdd:pfam05483 630 QLNAYEIKVNKLELE---LASAKQKFEEIIDNYQKEIED-------------KKISEEKLLEEVEKAKAIA-DEAVKLQK 692
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 442 EEVKTYKRRIEEMEDELQKTERSFKNQIATHEKKAHDNWLKARAAERAIAEEKREAANLRHKLLELTQKMAMMQEEPVIV 521
Cdd:pfam05483 693 EIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKL 772
|
....*....
gi 1387212246 522 KpMPGRPNT 530
Cdd:pfam05483 773 K-MEAKENT 780
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
91-414 |
3.17e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 63.89 E-value: 3.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 91 EQQISEKLKNIMKE--NAELVQK-----LSSYEQKIKESKKHVQETKKQNMILSDEAIKFKDKIKSLEETneilgdtAKS 163
Cdd:TIGR04523 35 EKQLEKKLKTIKNElkNKEKELKnldknLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSD-------LSK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 164 LRAMLESEREQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQ 243
Cdd:TIGR04523 108 INSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 244 EIKD-----------------WSKSHAELSEQIRSFEKSQKDLEVALTHKDDNINALTNCI----TQLNRL--------- 293
Cdd:TIGR04523 188 NIDKiknkllklelllsnlkkKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEIsntqTQLNQLkdeqnkikk 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 294 ---DCESESEDQNKGGSE-SDELANGEVggdRSEKVKNQIKQMMDvSRTQTAISVVEEDLKLLQCKLRASMSTKCNLEDQ 369
Cdd:TIGR04523 268 qlsEKQKELEQNNKKIKElEKQLNQLKS---EISDLNNQKEQDWN-KELKSELKNQEKKLEEIQNQISQNNKIISQLNEQ 343
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1387212246 370 IKKLEEDRSSLQSAKTVLEDECKTLRQKVEILNELYQQKEMALQK 414
Cdd:TIGR04523 344 ISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKN 388
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
77-463 |
3.81e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.52 E-value: 3.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 77 RTVLAVKSRVYQVTEQQISEKlknimkENAELVQKLSSYEQKIKESK---KHVQETKKQ--------NMILS-------- 137
Cdd:PRK02224 179 ERVLSDQRGSLDQLKAQIEEK------EEKDLHERLNGLESELAELDeeiERYEEQREQaretrdeaDEVLEeheerree 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 138 ----DEAI-KFKDKIKSLEETNEILGDTAKSLRAMLESEREQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNE 212
Cdd:PRK02224 253 letlEAEIeDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 213 AKLSEEKVKSECHRVQEENARLKKKKEQLQQEIKDWSKSHAELSEQIRSFEKSQKDLEVALthkDDNINALTNCITQLNR 292
Cdd:PRK02224 333 CRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI---EELRERFGDAPVDLGN 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 293 LDCESESEDQNKGGSESDElanGEVGGDRS--EKVKNQIKQMMDVSRTQTA---------ISVVEEDLKLLQcKLRASMS 361
Cdd:PRK02224 410 AEDFLEELREERDELRERE---AELEATLRtaRERVEEAEALLEAGKCPECgqpvegsphVETIEEDRERVE-ELEAELE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 362 TkcnLEDQIKKLEEDRSSLQSAKTvLEDECKTLRQKVEILNELYQQKEMALQKKLSQEEYERQEREQRLSAADEK----- 436
Cdd:PRK02224 486 D---LEEEVEEVEERLERAEDLVE-AEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKreaaa 561
|
410 420 430
....*....|....*....|....*....|..
gi 1387212246 437 -----AVLAAEEVKTYKRRIEEMEDELQKTER 463
Cdd:PRK02224 562 eaeeeAEEAREEVAELNSKLAELKERIESLER 593
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
94-517 |
7.96e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.39 E-value: 7.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 94 ISEKLKNIMKENAELVQKLSSYEQKIKESKKhVQETKKQNMILSDEAIKFKDKIKSLEETNEILGDTAKSLRAMLEsERE 173
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELEEKVKELKE-LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-ELE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 174 QNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNEA-KLSEEKVKSECHRVQEENARLKKKKEQLQQEIKdwsksh 252
Cdd:PRK03918 335 EKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELeRLKKRLTGLTPEKLEKELEELEKAKEEIEEEIS------ 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 253 aELSEQIRSFEKSQKDLEvalthkdDNINALTN----CITQLNRLDCESESEDQNKGGSESDELANG-EVGGDRSEKVKN 327
Cdd:PRK03918 409 -KITARIGELKKEIKELK-------KAIEELKKakgkCPVCGRELTEEHRKELLEEYTAELKRIEKElKEIEEKERKLRK 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 328 QIKQMMDVSRTQTAISVVEEDLKLLQcKLRASMStKCNLEDqIKKLEEDRSSLQSAKTVLEDECKTLRQKVEILNELYQQ 407
Cdd:PRK03918 481 ELRELEKVLKKESELIKLKELAEQLK-ELEEKLK-KYNLEE-LEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKK 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 408 KEmALQKKLSqeeyerqereqrlSAADEKAVLAAEEVKTYKRRIEEMEDELQKTErsfknqiathekKAHDNWLKARAAE 487
Cdd:PRK03918 558 LA-ELEKKLD-------------ELEEELAELLKELEELGFESVEELEERLKELE------------PFYNEYLELKDAE 611
|
410 420 430
....*....|....*....|....*....|
gi 1387212246 488 RAIAEEKREAANLRhklLELTQKMAMMQEE 517
Cdd:PRK03918 612 KELEREEKELKKLE---EELDKAFEELAET 638
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
95-501 |
2.09e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.31 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 95 SEKLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNMIL--SDEAIKFKDKIKSLEETNEILGDTAKSLRAMLESER 172
Cdd:PTZ00121 1376 AKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKkkADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEE 1455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 173 EQNAKNQDLISENKKSIEKLKDvisvNASEFSEVQIAlnEAKLSEEKVKSECHRVQEENarlKKKKEQLQQEIKDWSKSH 252
Cdd:PTZ00121 1456 AKKAEEAKKKAEEAKKADEAKK----KAEEAKKADEA--KKKAEEAKKKADEAKKAAEA---KKKADEAKKAEEAKKADE 1526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 253 AELSEQIRSFEKSQKDLEValtHKDDninaltncitQLNRLDCESESEDQNKGGSESDELANGEVGGDRSEKVKnQIKQm 332
Cdd:PTZ00121 1527 AKKAEEAKKADEAKKAEEK---KKAD----------ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAK-KAEE- 1591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 333 mdvSRTQTAISVVEEDLKLLQCKLRASMSTKCNLEdQIKKLEEDRSSLQSAKTVLEDECKTLRQkVEILNELYQQKEMAL 412
Cdd:PTZ00121 1592 ---ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE-ELKKAEEEKKKVEQLKKKEAEEKKKAEE-LKKAEEENKIKAAEE 1666
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 413 QKKlsqeEYERQEREQRLSAADEKAVLAAEEVKtykRRIEEME--DELQKTERSFKNQIATHEKKAHDNWLKARAAERAI 490
Cdd:PTZ00121 1667 AKK----AEEDKKKAEEAKKAEEDEKKAAEALK---KEAEEAKkaEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEA 1739
|
410
....*....|.
gi 1387212246 491 AEEKREAANLR 501
Cdd:PTZ00121 1740 EEDKKKAEEAK 1750
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
523-781 |
3.47e-09 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 60.72 E-value: 3.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 523 PMPGRPNTQNPPrrgPLSQNGSFGPSPVSGGECSPPLTAD--PPA----------------RPLSATLNRREMPRSEFGS 584
Cdd:PHA03247 2702 PPPPPTPEPAPH---ALVSATPLPPGPAAARQASPALPAApaPPAvpagpatpggparparPPTTAGPPAPAPPAAPAAG 2778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 585 VDGPLPRPRWASEASGKPSASDPESGAAPTV-----NSSSRSSSPSKVMDEGKVSMAAKGPPPFPGTPLMSSPVGGPLLP 659
Cdd:PHA03247 2779 PPRRLTRPAVASLSESRESLPSPWDPADPPAavlapAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAP 2858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 660 --PIRYGPPPQlcgpfgprPLPPPFGPGMRPPLGlREYAPGVPPGKRDLPL--DPREFLPPGHAPFRPLGslgpreyffP 735
Cdd:PHA03247 2859 ggDVRRRPPSR--------SPAAKPAAPARPPVR-RLARPAVSRSTESFALppDQPERPPQPQAPPPPQP---------Q 2920
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1387212246 736 GTRLPPPNHGPQDYPPSSAARDLPPsgsrdEPPPASQGASQDCSPA 781
Cdd:PHA03247 2921 PQPPPPPQPQPPPPPPPRPQPPLAP-----TTDPAGAGEPSGAVPQ 2961
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
95-415 |
4.62e-09 |
|
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: 60.12 E-value: 4.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 95 SEKLKNI---------MKENAELVQKLSSYEQKIKESKKHVQETKKQNMilsdeaiKFKDKIKSLEETNEILGDTAKSLR 165
Cdd:pfam05483 482 KEKLKNIeltahcdklLLENKELTQEASDMTLELKKHQEDIINCKKQEE-------RMLKQIENLEEKEMNLRDELESVR 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 166 AMLESEREQNAKNQDLISENKKSIEklkdvisvnasefSEVQIALNEAKLSEEKvkseCHRVQEENARLKKKKEQLQQEI 245
Cdd:pfam05483 555 EEFIQKGDEVKCKLDKSEENARSIE-------------YEVLKKEKQMKILENK----CNNLKKQIENKNKNIEELHQEN 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 246 KDWSKSHAELSEQIRSFEKSQKDLEVALTHKDDNINALTNCIT---QLNRLDCESESEDQNKGGSESDELANGEVGGDRs 322
Cdd:pfam05483 618 KALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQkeiEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDK- 696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 323 eKVKNQIKQM---MDVSRTQTAISVVEED--LKLLQCKLRASMSTKCNLEDQIKKLeedRSSLQSAKTVLEDEcktlRQK 397
Cdd:pfam05483 697 -RCQHKIAEMvalMEKHKHQYDKIIEERDseLGLYKNKEQEQSSAKAALEIELSNI---KAELLSLKKQLEIE----KEE 768
|
330
....*....|....*...
gi 1387212246 398 VEILNELYQQKEMALQKK 415
Cdd:pfam05483 769 KEKLKMEAKENTAILKDK 786
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
94-403 |
7.97e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.31 E-value: 7.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 94 ISEKLKN-----IMKENAELVQKLSS----YEQKIKESKKHVQETKKQNMI-----LSDEAIKFKDKI----KSLEETNE 155
Cdd:TIGR02169 193 IDEKRQQlerlrREREKAERYQALLKekreYEGYELLKEKEALERQKEAIErqlasLEEELEKLTEEIseleKRLEEIEQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 156 ILGDTAKSLRAMleSEREQNAKNQDlISENKKSIEKLKDVISVNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLK 235
Cdd:TIGR02169 273 LLEELNKKIKDL--GEEEQLRVKEK-IGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEER 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 236 KKKEQLQQEIKDWSKSHAELSEQIRSFEKSQKDLEVALTHKDDNINALTNCITQLNRLDCESESEDQNKggseSDELANG 315
Cdd:TIGR02169 350 KRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRL----SEELADL 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 316 EVGGDRSEKVKNQIKQMMD-----VSRTQTAISVVEEDLKLLQCKLRASMSTKCNLEDQIKKLEEDRSSLQSAKTVLEDE 390
Cdd:TIGR02169 426 NAAIAGIEAKINELEEEKEdkaleIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
330
....*....|...
gi 1387212246 391 CKTLRQKVEILNE 403
Cdd:TIGR02169 506 VRGGRAVEEVLKA 518
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
95-476 |
8.33e-09 |
|
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: 59.68 E-value: 8.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 95 SEKLKNIMKENAELVQKLSSYE------------QKIKESKKHV--QETK-----------KQNMILSDEAIKFKD---- 145
Cdd:TIGR01612 1388 SEKLIKKIKDDINLEECKSKIEstlddkdideciKKIKELKNHIlsEESNidtyfknadenNENVLLLFKNIEMADnksq 1467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 146 ---KIKSLEET-------NEILGDTAKSLRAMLESEreqnaKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNEAKl 215
Cdd:TIGR01612 1468 hilKIKKDNATndhdfniNELKEHIDKSKGCKDEAD-----KNAKAIEKNKELFEQYKKDVTELLNKYSALAIKNKFAK- 1541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 216 seekVKSECHRVQEENARLKKK----KEQLQQEIKDWSKSHAELSEQIRSFEKSQK---DLEVALTHKDDNINALTNCIT 288
Cdd:TIGR01612 1542 ----TKKDSEIIIKEIKDAHKKfileAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKaaiDIQLSLENFENKFLKISDIKK 1617
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 289 QLNrlDCESESEdqnkggsesdelangevggdrseKVKNQIKQMmDVSRTQTAISVVEEDLKLLQCKLRASMSTKCNLED 368
Cdd:TIGR01612 1618 KIN--DCLKETE-----------------------SIEKKISSF-SIDSQDTELKENGDNLNSLQEFLESLKDQKKNIED 1671
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 369 QIKKLEEDRSSLQSAKTVLEDECKTLRQK-VEILNELYQQKEMALQKKLSQEEYERQEREQRLSAADEKAVLAAEEVKTY 447
Cdd:TIGR01612 1672 KKKELDELDSEIEKIEIDVDQHKKNYEIGiIEKIKEIAIANKEEIESIKELIEPTIENLISSFNTNDLEGIDPNEKLEEY 1751
|
410 420
....*....|....*....|....*....
gi 1387212246 448 KRRIEEMEDELQKTERSFKNQIATHEKKA 476
Cdd:TIGR01612 1752 NTEIGDIYEEFIELYNIIAGCLETVSKEP 1780
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
91-517 |
8.53e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.01 E-value: 8.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 91 EQQISEkLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNMILsDEAIKFKDKIKSLEETNEILGDTAKSLRAMLES 170
Cdd:COG4717 77 EEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKLLQLLPLYQELEALEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 171 EREqnaknqdlISENKKSIEKLKDvisvnasEFSEVQIALNEA-KLSEEKVKSECHRVQEENARLKKKKEQLQQEIKDWS 249
Cdd:COG4717 155 LEE--------LRELEEELEELEA-------ELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 250 KSHAELSEQIRSFEKSQKDLE------------------VALTHKDDNINALTNCIT-------QLNRLDCESESEDQNK 304
Cdd:COG4717 220 EELEELEEELEQLENELEAAAleerlkearlllliaaalLALLGLGGSLLSLILTIAgvlflvlGLLALLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 305 GGSESDELANGEVGGDRSEKVKNQIKQMMDVSRTQTAISVVEEDLKLLQCKLRASMSTKCNLEDQIKKLEEDRSSLQSAK 384
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 385 TVLEDEckTLRQKVEILNElYQQKEMALQKKLSQEEYERQEREQRLSAADEKAVLAA-EEVKTYKRRIEEMEDELQKTER 463
Cdd:COG4717 380 GVEDEE--ELRAALEQAEE-YQELKEELEELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELA 456
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1387212246 464 SFKNQIATHEKkahdnwlkaraaeraiaeeKREAANLRHKLLELTQKMAMMQEE 517
Cdd:COG4717 457 ELEAELEQLEE-------------------DGELAELLQELEELKAELRELAEE 491
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
523-786 |
1.65e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 58.41 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 523 PMPGRPNTQNPPRRGPLSQNGSFGPSPV-SGGECSPPLTADPPARPLSATLN----RREMPRSEFGSVDG---------- 587
Cdd:PHA03247 2628 PPSPSPAANEPDPHPPPTVPPPERPRDDpAPGRVSRPRRARRLGRAAQASSPpqrpRRRAARPTVGSLTSladppppppt 2707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 588 PLPRPRWASEASGKPSASDPESGAAP--TVNSSSRSSSPSKVMDegkVSMAAKGPPPFPGTPLMSSPVGGPLLPPIRYGP 665
Cdd:PHA03247 2708 PEPAPHALVSATPLPPGPAAARQASPalPAAPAPPAVPAGPATP---GGPARPARPPTTAGPPAPAPPAAPAAGPPRRLT 2784
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 666 PPQLCGPFGPRPLPPPFGPGMRPPLGLREYAPGVPPGKRDLPLDPREFLPPGHAPFRPLGSLGPRE----YFFPG---TR 738
Cdd:PHA03247 2785 RPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLplggSVAPGgdvRR 2864
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1387212246 739 LPPPnhgpQDYPPSSAARDLPPSGSRDEPPPASQGASQDCSPALKQSP 786
Cdd:PHA03247 2865 RPPS----RSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERP 2908
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
146-459 |
2.20e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 146 KIKSLEETNEILGDTAKSLRAMLESEREQNAKNQDLISENKKSIEKLKDvisvnasEFSEVQIALNEAKLSEEKVKSECH 225
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL-------ELEEAQAEEYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 226 RVQEENARLKKKKEQLQQEIKDWSKSHAELSEQIRSFEKSQKDLEVALTHKDdninaltncitqlnrldcesESEDQNKG 305
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE--------------------AELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 306 GSESDELANGEVGGDRSEKVKNQIKQMMDVSRTQTAISVVEEDLKllqcklrasmstkcNLEDQIKKLEEDRSSLQSAKT 385
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE--------------ALLERLERLEEELEELEEALA 431
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387212246 386 VLEDECKTLRQKVEILNELYQQKEmALQKKLSQEEYERQEREQRLSAADEKAVLAAEEVKTYKRRIEEMEDELQ 459
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEAELE-EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
515-771 |
3.42e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 57.64 E-value: 3.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 515 QEEPVIVKPMPGRPNTQNPPrrGPLSQNGSF-------GPSPVSGGECSPPLTADPPARPLSATLNRREMPRSEFGSVDG 587
Cdd:PHA03247 2704 PPPTPEPAPHALVSATPLPP--GPAAARQASpalpaapAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPR 2781
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 588 PLPRPRWASEASGKPSASDPESGAAPTV-----NSSSRSSSPSKVMDEGKVSMAAKGPPPFPGTPLMSSPVGG------- 655
Cdd:PHA03247 2782 RLTRPAVASLSESRESLPSPWDPADPPAavlapAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGsvapggd 2861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 656 ----------------PLLPPIRYGPPPQLCGPFGPRPLPPPFGPGMRPP-------------LGLREYAPGVPPGKRDL 706
Cdd:PHA03247 2862 vrrrppsrspaakpaaPARPPVRRLARPAVSRSTESFALPPDQPERPPQPqappppqpqpqppPPPQPQPPPPPPPRPQP 2941
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 707 PLDPR-----EFLPPGHAPFRPLGSLGPREYFFPGTRLPPPNHG-PQDYPPSSAARDLPPSG-----------SRDEPPP 769
Cdd:PHA03247 2942 PLAPTtdpagAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSrEAPASSTPPLTGHSLSRvsswasslalhEETDPPP 3021
|
..
gi 1387212246 770 AS 771
Cdd:PHA03247 3022 VS 3023
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
226-517 |
6.16e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 6.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 226 RVQEENARLKKKkeqlqQEIKDWSKSHAELSEQIRSFEKSQKDLEVALThkddninALTNCITQLNRLDCESEsedqnkg 305
Cdd:TIGR02168 665 SAKTNSSILERR-----REIEELEEKIEELEEKIAELEKALAELRKELE-------ELEEELEQLRKELEELS------- 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 306 gsesDELANGEVGGDRSEKVKNQIKQMMDvsRTQTAISVVEEDLKLLQCKLRASMSTKCNLEDQIKKLEEDRSSLQSAKT 385
Cdd:TIGR02168 726 ----RQISALRKDLARLEAEVEQLEERIA--QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 386 VLEDECKTLRQKVEILNELYQQKEMA---LQKKLSQEEYERQEREQRLSAADEKAVLAAEEVKTYKRRIEEMEDELQkte 462
Cdd:TIGR02168 800 ALREALDELRAELTLLNEEAANLRERlesLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE--- 876
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1387212246 463 rSFKNQIATHEKKAHDNWLKARAAERAIAEEKREAANLRHKLLELTQKMAMMQEE 517
Cdd:TIGR02168 877 -ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELR 930
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
111-463 |
8.01e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.23 E-value: 8.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 111 KLSSYEQKIKESKKHVQETKKQNMILSDE---AIKFKDKIKSLEETNeilgdtAKSLRAMLESEREQNAKNQDLISENKK 187
Cdd:TIGR02169 178 ELEEVEENIERLDLIIDEKRQQLERLRRErekAERYQALLKEKREYE------GYELLKEKEALERQKEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 188 SIEKLKDVISVNASEFSEVQIALNEA-----KLSEEK---VKSECHRVQEENARLKKKKEQLQQEIKDWSKSHAELSEQI 259
Cdd:TIGR02169 252 ELEKLTEEISELEKRLEEIEQLLEELnkkikDLGEEEqlrVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEI 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 260 RSFEKSQKDLEVALTHKDDNINALTNCI----TQLNRLDCESESEDQnKGGSESDELANGEVggdRSEKVKNQIKQMmdv 335
Cdd:TIGR02169 332 DKLLAEIEELEREIEEERKRRDKLTEEYaelkEELEDLRAELEEVDK-EFAETRDELKDYRE---KLEKLKREINEL--- 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 336 srtQTAISVVEEDLKLLQCKLRasmstkcNLEDQIKKLEEDRSSLQSAKTVLEDECKTLRQKVEILnelyqqkemalqkk 415
Cdd:TIGR02169 405 ---KRELDRLQEELQRLSEELA-------DLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL-------------- 460
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1387212246 416 lsqeeyerqereqrlsaadeKAVLAAEEVKTYKRR--IEEMEDELQKTER 463
Cdd:TIGR02169 461 --------------------AADLSKYEQELYDLKeeYDRVEKELSKLQR 490
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
92-482 |
9.68e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 55.89 E-value: 9.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 92 QQISEKLKNIMKENAELVQKLSSYEQKIKESKKHV-------QETKKQNMILSDEAIKFKDKIKSLeetneiLGDTAKSL 164
Cdd:pfam15921 317 RQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLvlanselTEARTERDQFSQESGNLDDQLQKL------LADLHKRE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 165 RAmLESEREQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALneaklseEKVKSECH-RVQEENARLKKKKE---- 239
Cdd:pfam15921 391 KE-LSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALL-------KAMKSECQgQMERQMAAIQGKNEslek 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 240 ------QLQQEIKDWSKSHAELSEQIRSFEKSQK---DLEVALTHKDDNINALTNCITQL-NRLDCE--------SESED 301
Cdd:pfam15921 463 vssltaQLESTKEMLRKVVEELTAKKMTLESSERtvsDLTASLQEKERAIEATNAEITKLrSRVDLKlqelqhlkNEGDH 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 302 QNKGGSESDELANGEVGGDRS-EKVKNQIKQMMDV----SRTQTAISV----VEEDLKLLQCKLRASMSTKCNLEDQIKK 372
Cdd:pfam15921 543 LRNVQTECEALKLQMAEKDKViEILRQQIENMTQLvgqhGRTAGAMQVekaqLEKEINDRRLELQEFKILKDKKDAKIRE 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 373 LEEDRSSLQSAKTVLEDECKtlrQKVEILNELYQQKEMALQkklsqeeyerqereqrlsaadekavlaaeEVKTYKRRIE 452
Cdd:pfam15921 623 LEARVSDLELEKVKLVNAGS---ERLRAVKDIKQERDQLLN-----------------------------EVKTSRNELN 670
|
410 420 430
....*....|....*....|....*....|
gi 1387212246 453 EMEDELQKTERSFKNQiaTHEKKAHDNWLK 482
Cdd:pfam15921 671 SLSEDYEVLKRNFRNK--SEEMETTTNKLK 698
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
91-517 |
1.13e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 91 EQQISEKLKnimKENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIKFKDKIKSLEETNEILGDTAKSLRAMLES 170
Cdd:PTZ00121 1313 EAKKADEAK---KKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE 1389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 171 ERE-QNAKNQdlISENKKSIEKLKDVISVNASEFSEVQIALNEAKLSEEKVKSECHRVQEE---NARLKKKKEQLQQEIK 246
Cdd:PTZ00121 1390 KKKaDEAKKK--AEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEakkKAEEAKKAEEAKKKAE 1467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 247 DWSKSH--AELSEQIRSFEKSQKDLEVALTHKDdninaltncitQLNRLDCESESEDQNKGGSE---SDELANGEVGGDR 321
Cdd:PTZ00121 1468 EAKKADeaKKKAEEAKKADEAKKKAEEAKKKAD-----------EAKKAAEAKKKADEAKKAEEakkADEAKKAEEAKKA 1536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 322 SEKVKNQIKQMMDVSRTQTAISVVEEDLKLLQCKlRASMSTKCNLE--DQIKKLEEDRssLQSAKTVLEDECKtlrQKVE 399
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKAEELKKAEEKKKAEEAK-KAEEDKNMALRkaEEAKKAEEAR--IEEVMKLYEEEKK---MKAE 1610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 400 ILNELYQQKEMALQKKlsqEEYERQEREQRLSAADEKAVLAAEEVKTYKRRIEEMEDELQKTERSFKNQiATHEKKAHDN 479
Cdd:PTZ00121 1611 EAKKAEEAKIKAEELK---KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKK-AEEAKKAEED 1686
|
410 420 430
....*....|....*....|....*....|....*...
gi 1387212246 480 WLKARAAERAIAEEKREAANLRHKLLELTQKMAMMQEE 517
Cdd:PTZ00121 1687 EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKA 1724
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
92-283 |
1.69e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 92 QQISEKLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIKFKDKIKSLEET-NEILGDTAKSLRAMLES 170
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAElEAQKEELAELLRALYRL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 171 EREQNAK---NQDLISENKKSIEKLKDVISVNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIKD 247
Cdd:COG4942 117 GRQPPLAlllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAE 196
|
170 180 190
....*....|....*....|....*....|....*.
gi 1387212246 248 WSKSHAELSEQIRSFEKSQKDLEVALTHKDDNINAL 283
Cdd:COG4942 197 RQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
82-409 |
1.92e-07 |
|
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: 54.68 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 82 VKSRVYQVTEQQISEKLKNIMKENAE-LVQKLSSYE--QKIKESKKHVQETKKQNMILSDEAIKFKDKIKSLEETNEILG 158
Cdd:pfam05911 441 VPVSSKDISLGKSLSWLQSRISVILEsHVTQKSIGKilEDIRCALQDINDSLPEADSCLSSGHPSTDASCDYITCKENSS 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 159 DTAKSLRAMLESEREQNAKNQDLISENKKSIEKLKDVI---SVNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLK 235
Cdd:pfam05911 521 VVEKEGSVSGDDKSSEETSKQSIQQDLSKAISKIIDFVeglSKEALDDQDTSSDSSELSEVLQQFSATCNDVLSGKADLE 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 236 KKKEQLQqEIKDWSKSH-------AELSEQIRSFEKSQKD--LEVALTHKDDNINALTNCITQLNRLDCESESEDQNKGG 306
Cdd:pfam05911 601 DFVLELS-HILDWISNHcfslldvSSMEDEIKKHDCIDKVtlSENKVAQVDNGCSEIDNLSSDPEIPSDGPLVSGSNDLK 679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 307 SESDELANGEVGGDRSEKVKNQIKQMMDVSRTQTAIS---VVEEDLKLLQCKLRASMSTKCNLEDQIKKLEEDRSSLQSA 383
Cdd:pfam05911 680 TEENKRLKEEFEQLKSEKENLEVELASCTENLESTKSqlqESEQLIAELRSELASLKESNSLAETQLKCMAESYEDLETR 759
|
330 340
....*....|....*....|....*..
gi 1387212246 384 KTVLEDECKTLRQKVEIL-NELYQQKE 409
Cdd:pfam05911 760 LTELEAELNELRQKFEALeVELEEEKN 786
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
147-467 |
2.14e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 147 IKSLEETNEILGDTAKSLRAM---LESEREQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNEA---KLSEEKV 220
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKRRierLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLekeVKELEEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 221 KSECHRVQEENARLKKKKEQLQQEIKDWSKSHAELSEQIRSFEKSQKDLEvalthkddNINALTNCITQLNRLDCESESE 300
Cdd:PRK03918 237 KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK--------ELKEKAEEYIKLSEFYEEYLDE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 301 DQN--KGGSESDELANG--EVGGDRSEKVKNQIKQMMDVSRTQTAISVVEEDLKLLQcKLRASMSTKCNLEDQIK----- 371
Cdd:PRK03918 309 LREieKRLSRLEEEINGieERIKELEEKEERLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTgltpe 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 372 KLEEDRSSLQSAKTVLEDECKTLRQKVEILNELYQQKEMALQkKLSQEEYERQEREQRLSAADEKAVLA--AEEVKTYKR 449
Cdd:PRK03918 388 KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE-ELKKAKGKCPVCGRELTEEHRKELLEeyTAELKRIEK 466
|
330
....*....|....*...
gi 1387212246 450 RIEEMEDELQKTERSFKN 467
Cdd:PRK03918 467 ELKEIEEKERKLRKELRE 484
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
84-457 |
2.58e-07 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 54.70 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 84 SRVYQVTEQQISEKLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIKFKDKIKSleetneilgdtakS 163
Cdd:COG5022 852 GRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSS-------------D 918
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 164 LRAMLESEREQNAKNQDLISENKKSIEKLKDVISVnasefsEVQIALNEaklseekVKSECHRVQEENARLKKKKEQLQ- 242
Cdd:COG5022 919 LIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKL------PELNKLHE-------VESKLKETSEEYEDLLKKSTILVr 985
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 243 ------QEIKDWSKSHAELSEQIRSFEKSQKDLEVaLTHKDDNINALTNCITQlnrldcESESEDQNKGGSES---DELA 313
Cdd:COG5022 986 egnkanSELKNFKKELAELSKQYGALQESTKQLKE-LPVEVAELQSASKIISS------ESTELSILKPLQKLkglLLLE 1058
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 314 NGEVGG---------DRSEKVKNQIKQMMDVSRTQTAISVVEEDLKLLQC--------KLRASMStKCNLEDQIKKleed 376
Cdd:COG5022 1059 NNQLQArykalklrrENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLvkpanvlqFIVAQMI-KLNLLQEISK---- 1133
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 377 rsSLQSAKTVLEDECKTLRQKVEILNELYQQKemALQKKLSQEEYERQEREQRLSAA--DEKAVLAAEEVKTYKRRIEEM 454
Cdd:COG5022 1134 --FLSQLVNTLEPVFQKLSVLQLELDGLFWEA--NLEALPSPPPFAALSEKRLYQSAlyDEKSKLSSSEVNDLKNELIAL 1209
|
...
gi 1387212246 455 EDE 457
Cdd:COG5022 1210 FSK 1212
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
83-414 |
3.82e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 3.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 83 KSRVYQVTEQQISEKLKN-------IMKENAELVQKLSSYEQKIKESKKHVQETKKQNMI-------LSDE-----AIKF 143
Cdd:PRK03918 378 KKRLTGLTPEKLEKELEElekakeeIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgreLTEEhrkelLEEY 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 144 KDKIKSLEETNEILGDTAKSLRAMLEsEREQNAKNQDLISENKKSIEKLKDV-----------ISVNASEFSEVQIALNE 212
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELR-ELEKVLKKESELIKLKELAEQLKELeeklkkynleeLEKKAEEYEKLKEKLIK 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 213 AKLSEEKVKSECHRVQEenarLKKKKEQLQQEIKDWSKSHAELSEQIRSFE-KSQKDLEVALTHKD---DNINALTNCIT 288
Cdd:PRK03918 537 LKGEIKSLKKELEKLEE----LKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEpfyNEYLELKDAEK 612
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 289 QLNRLDCESESEdQNKGGSESDELANGEvggDRSEKVKNQIKQ----------------MMDVSRtqtAISVVEEDLKLL 352
Cdd:PRK03918 613 ELEREEKELKKL-EEELDKAFEELAETE---KRLEELRKELEElekkyseeeyeelreeYLELSR---ELAGLRAELEEL 685
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387212246 353 QCKLRASMSTKCNLEDQIKKLEEDRSSLQSAKTVLEDeCKTLRQKVEILNELyqQKEMALQK 414
Cdd:PRK03918 686 EKRREEIKKTLEKLKEELEEREKAKKELEKLEKALER-VEELREKVKKYKAL--LKERALSK 744
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
92-461 |
4.33e-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: 53.82 E-value: 4.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 92 QQISEKLKNIMKENAELVQKLSSYEQKIKESKKhvqetkKQNMILSDEAIKFKDKIKSLEETNeilGDTAKSLRAMLESE 171
Cdd:pfam02463 665 KASLSELTKELLEIQELQEKAESELAKEEILRR------QLEIKKKEQREKEELKKLKLEAEE---LLADRVQEAQDKIN 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 172 REQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQialNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIKDWSKS 251
Cdd:pfam02463 736 EELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSL---KEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKE 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 252 HAELSEQirsFEKSQKDLEVALTHKDDNINALTNCITQLNRLDCESESEDQnkggsesdELANGEVGGDRSEKVKNQIKQ 331
Cdd:pfam02463 813 EAELLEE---EQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLE--------EEITKEELLQELLLKEEELEE 881
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 332 MMDVSRTQTAISVVEEDLKLLQCKLRASmstkCNLEDQIKKLEEDRSSLQSAKTVLEDECKTLRQKVEILNELYQQ-KEM 410
Cdd:pfam02463 882 QKLKDELESKEEKEKEEKKELEEESQKL----NLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENnKEE 957
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387212246 411 ALQKKLSQEEYERQEREQRLSAADE----------------------KAVLAAEEVKTYKRRIEEMEDELQKT 461
Cdd:pfam02463 958 EEERNKRLLLAKEELGKVNLMAIEEfeekeerynkdelekerleeekKKLIRAIIEETCQRLKEFLELFVSIN 1030
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
115-415 |
5.06e-07 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 53.15 E-value: 5.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 115 YEQKIKESKKHVQETKKQN---MILSDEAIKFKDKIKSLEETNeilgDTAKSLRAMLESERE--------------QNAK 177
Cdd:pfam05622 85 YRIKCEELEKEVLELQHRNeelTSLAEEAQALKDEMDILRESS----DKVKKLEATVETYKKkledlgdlrrqvklLEER 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 178 NQDLISENKKSIEKLKDVISVNAS-EFSEVQIALNEAKLSEEKVKS-----ECHRVQEENARLKKKKEQLQQEiKDWSKs 251
Cdd:pfam05622 161 NAEYMQRTLQLEEELKKANALRGQlETYKRQVQELHGKLSEESKKAdklefEYKKLEEKLEALQKEKERLIIE-RDTLR- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 252 haELSEQIRSFEKSQKDLEVALTHKDDNINALTNCITQ---------LNRLDCESESEDQNKGGSESDELANGEVGGDRS 322
Cdd:pfam05622 239 --ETNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEimpaeirekLIRLQHENKMLRLGQEGSYRERLTELQQLLEDA 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 323 EKVKNQIKQMMDVSRTQtaISVVEEDLKLLQCKLRA-------SMSTKCNLEDQIKKLEEDRSSLQSAKTVLED-ECKTL 394
Cdd:pfam05622 317 NRRKNELETQNRLANQR--ILELQQQVEELQKALQEqgskaedSSLLKQKLEEHLEKLHEAQSELQKKKEQIEElEPKQD 394
|
330 340
....*....|....*....|.
gi 1387212246 395 RQKVEILNELyqqkEMALQKK 415
Cdd:pfam05622 395 SNLAQKIDEL----QEALRKK 411
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
91-282 |
5.23e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 5.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 91 EQQISEKLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEaikfkdkiksLEETNEILGDTAkslRAMLES 170
Cdd:COG3883 32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE----------IEERREELGERA---RALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 171 EREQ-------NAKN-QDLISenkkSIEKLKDVISVNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQ 242
Cdd:COG3883 99 GGSVsyldvllGSESfSDFLD----RLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1387212246 243 QEIKDWSKSHAELSEQIRSFEKSQKDLEVALTHKDDNINA 282
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
183-463 |
5.48e-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: 5.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 183 SENKKSIEKLKDVisvnasefsEVQIALNEAKLSEekVKSECHRVQEENAR------LKKKKEQLQQ-----EIKDWSKS 251
Cdd:TIGR02169 170 RKKEKALEELEEV---------EENIERLDLIIDE--KRQQLERLRREREKaeryqaLLKEKREYEGyellkEKEALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 252 HAELSEQIRSFEKSQKDLEVALTHKDDNINALTNCITQLNRldcesesedqnkggsESDELangevGGDRSEKVKNQIKQ 331
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNK---------------KIKDL-----GEEEQLRVKEKIGE 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 332 M-MDVSRTQTAISVVEEDLKllqcklrasmstkcNLEDQIKKLEEDRSSLQSAKTVLEDECKTLRQKVEILNELYQQKEM 410
Cdd:TIGR02169 299 LeAEIASLERSIAEKERELE--------------DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKE 364
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1387212246 411 ALQKKLSQeeyerqereqrLSAADEKAVLAAEEVKTYKRRIEEMEDELQKTER 463
Cdd:TIGR02169 365 ELEDLRAE-----------LEEVDKEFAETRDELKDYREKLEKLKREINELKR 406
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
173-410 |
1.00e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 52.32 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 173 EQNAKNQDLISENK---KSIEKLKDVIsvnasefsEVQIALNEAKLSEEKVKSEchrvqEENARLKKKKEQLQQEIKDWS 249
Cdd:PHA02562 167 EMDKLNKDKIRELNqqiQTLDMKIDHI--------QQQIKTYNKNIEEQRKKNG-----ENIARKQNKYDELVEEAKTIK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 250 KSHAELSEQIRSFEKSQKDLEVALTHKDDNINALTNCITQLNRL-----------DCESE-SEDQNKGGSESDELANGEV 317
Cdd:PHA02562 234 AEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVikmyekggvcpTCTQQiSEGPDRITKIKDKLKELQH 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 318 GGDRSEKVKNQIKQMMDVSRTQTaisvveEDLKLLQCKLRASMSTKCNLEDQIKKLEEDRSSLQSAKTVLEDECKTLRQK 397
Cdd:PHA02562 314 SLEKLDTAIDELEEIMDEFNEQS------KKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDE 387
|
250
....*....|...
gi 1387212246 398 VEILNELYQQKEM 410
Cdd:PHA02562 388 LDKIVKTKSELVK 400
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
93-463 |
1.27e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 93 QISEKLKNIMKENAELVQKLSSYEqKIKESKKHVQETKKQNMILSDEaiKFKDKIKSLEETNEILGDTAKSLRAMLESER 172
Cdd:PRK03918 342 ELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGLTPE--KLEKELEELEKAKEEIEEEISKITARIGELK 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 173 EQnaknqdlISENKKSIEKL---KDVISVNASEFSEVQIA--LNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIKD 247
Cdd:PRK03918 419 KE-------IKELKKAIEELkkaKGKCPVCGRELTEEHRKelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKK 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 248 WSK--SHAELSEQIRSFEKSQKDLEVALTHKDD---------------NINALTNCITQLNRLDCESEsEDQNKGGSESD 310
Cdd:PRK03918 492 ESEliKLKELAEQLKELEEKLKKYNLEELEKKAeeyeklkekliklkgEIKSLKKELEKLEELKKKLA-ELEKKLDELEE 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 311 ELAN-----GEVGGDRSEKVKNQIKQMMDVSRTQTAISVVEEDLKLLQCKLRasmSTKCNLEDQIKKLEEDRSSLQSAKT 385
Cdd:PRK03918 571 ELAEllkelEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELK---KLEEELDKAFEELAETEKRLEELRK 647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 386 VLED-ECKTLRQKVEILNELYQQKEMALQKKLSQEEYERQEREQRLSAADE-KAVLaaEEVKTYKRRIEEMEDELQKTER 463
Cdd:PRK03918 648 ELEElEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKlKEEL--EEREKAKKELEKLEKALERVEE 725
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
103-293 |
1.45e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 103 KENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIKFKDKIKSLEETNEILGDTAKSLRAMLESEREQNAKNQDLI 182
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 183 SENKKSIEKLKDVIS-----------VNASEFSEVQI------ALNEAKLSE-EKVKSECHRVQEENARLKKKKEQLQQE 244
Cdd:COG4942 100 EAQKEELAELLRALYrlgrqpplallLSPEDFLDAVRrlqylkYLAPARREQaEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1387212246 245 IKDWSKSHAELSEQIRSFEKSQKDLEVALTHKDDNINALTNCITQLNRL 293
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
81-414 |
2.04e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 51.66 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 81 AVKSRVYQVTEQQISE-KLKNimkENAELVQKLSSYEQKIKES-KKHVQETKKQNMIL-------SDEAIKFKDKIKSLE 151
Cdd:pfam15921 437 AMKSECQGQMERQMAAiQGKN---ESLEKVSSLTAQLESTKEMlRKVVEELTAKKMTLessertvSDLTASLQEKERAIE 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 152 ETN-EIlgdTAKSLRAMLESEREQNAKNQDlisENKKSIEKLKDVISVNASEFSEVQIALNEAKLSEEKVKSECHR---- 226
Cdd:pfam15921 514 ATNaEI---TKLRSRVDLKLQELQHLKNEG---DHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRtaga 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 227 VQEENARLKKKKEQLQQEIKDWSKSHAELSEQIRSFEKSQKDLE---VALTH---------------KDDNINALTNCIT 288
Cdd:pfam15921 588 MQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLElekVKLVNagserlravkdikqeRDQLLNEVKTSRN 667
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 289 QLNRLDCESESEDQN-KGGSESDELANGEV------GGDRSEKVKNQIKQM-----------MDVSRTQTA----ISVVE 346
Cdd:pfam15921 668 ELNSLSEDYEVLKRNfRNKSEEMETTTNKLkmqlksAQSELEQTRNTLKSMegsdghamkvaMGMQKQITAkrgqIDALQ 747
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387212246 347 EDLKLLQCKLRASMSTKCNLEDQIKKLEEDRSSLQSAKTVLEDECKTLRQKVEILNELYQQKEMALQK 414
Cdd:pfam15921 748 SKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDK 815
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
85-517 |
2.16e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.60 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 85 RVYQVTEQQISEKLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIKFKDKIKSLEETNEILGDTAKSL 164
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 165 RAMLESEREQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNEAKLSE------------EKVKSECHRVQEENA 232
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqaeleeleeelEELQEELERLEEALE 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 233 RLKKKKEQLQQEIKDWSKSHAELSEQIRSFEKSQKDLE------VALTHKDDNINALTNCITQLNRLDCESE-------- 298
Cdd:TIGR02168 465 ELREELEEAEQALDAAERELAQLQARLDSLERLQENLEgfsegvKALLKNQSGLSGILGVLSELISVDEGYEaaieaalg 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 299 -------SEDQNKGGSESDELANGEVG-----------GDRSEKVKNQIKQMMDVSRtQTAISVVEEDLKL--------- 351
Cdd:TIGR02168 545 grlqavvVENLNAAKKAIAFLKQNELGrvtflpldsikGTEIQGNDREILKNIEGFL-GVAKDLVKFDPKLrkalsyllg 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 352 -------------LQCKLRASMS---------TKC---------------NLEDQIKKLEEDRSSLQSAKTVLEDECKTL 394
Cdd:TIGR02168 624 gvlvvddldnaleLAKKLRPGYRivtldgdlvRPGgvitggsaktnssilERRREIEELEEKIEELEEKIAELEKALAEL 703
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 395 RQKVEILN-------------------------------ELYQQKEMALQKKLSQEEYERQEREQRLSAADEKAVLAAEE 443
Cdd:TIGR02168 704 RKELEELEeeleqlrkeleelsrqisalrkdlarleaevEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE 783
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387212246 444 VKTYKRRIEEMEDELQKTER---SFKNQIATHEKKAHDNWLKARAAERAIAEEKREAANLRHKLLELTQKMAMMQEE 517
Cdd:TIGR02168 784 IEELEAQIEQLKEELKALREaldELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
522-786 |
2.43e-06 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 51.33 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 522 KPMPGRPNTQNPPRRGPLSQNGSFGPSPVSGGEcSPPLTADPPARPLSATLNRREMPRSEfGSVDGPLPRPRWASEASGK 601
Cdd:PHA03307 83 ESRSTPTWSLSTLAPASPAREGSPTPPGPSSPD-PPPPTPPPASPPPSPAPDLSEMLRPV-GSPGPPPAASPPAAGASPA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 602 PSASDPESGAAPTVNSSsrssspskvMDEgkvSMAAKGPPPFPGTPLMSSPVGGPLLPPIR------YGPPPQLCGPFGP 675
Cdd:PHA03307 161 AVASDAASSRQAALPLS---------SPE---ETARAPSSPPAEPPPSTPPAAASPRPPRRsspisaSASSPAPAPGRSA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 676 RPLPPPFGPGMRPPL------GLREYAPGVPPGKRDLPLDPREFLPPGHAPFRPL---------GSLGPREYFFPGTRLP 740
Cdd:PHA03307 229 ADDAGASSSDSSSSEssgcgwGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGpasssssprERSPSPSPSSPGSGPA 308
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1387212246 741 PPNHGPQDYPPSSAARDLP---PSGSRDEPPPASQGASQDCSPALKQSP 786
Cdd:PHA03307 309 PSSPRASSSSSSSRESSSSstsSSSESSRGAAVSPGPSPSRSPSPSRPP 357
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
153-481 |
2.58e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.29 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 153 TNEILGDTAKSLRAMLESEREQNAKNQDL---ISENKKSIEKLKDVISVNASEFSEVQIALNEAKLSEEKVKSECHRVQE 229
Cdd:COG4372 22 TGILIAALSEQLRKALFELDKLQEELEQLreeLEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 230 ENARLKKKKEQLQQEIKDWSKSHAELSEQIRSFEKSQKDLEVALTHKDDNINALTNCITQLNRLDCESESEDQNKGGSES 309
Cdd:COG4372 102 ELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 310 DELANGEVGGDRSEKVKNQIKQMMDVSRTQTAISVVEEDLKLLQ------CKLRASMSTKCNLEdQIKKLEEDRSSLQSA 383
Cdd:COG4372 182 EQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDsleaklGLALSALLDALELE-EDKEELLEEVILKEI 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 384 KTVLEDECKTLRQKVEILNELYQQKEMALQKKLSQEEYERQEREQRLSAADEKAVLAAEEVKTYKRRIEEMEDELQKTER 463
Cdd:COG4372 261 EELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELA 340
|
330
....*....|....*...
gi 1387212246 464 SFKNQIATHEKKAHDNWL 481
Cdd:COG4372 341 DLLQLLLVGLLDNDVLEL 358
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
154-517 |
3.22e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 154 NEILGDTAKSLRAMLES--------EREQNAKNQ-DLISENkksIEKLKDVISvnasefsEVQIALNeaKLSEEKVKSEc 224
Cdd:TIGR02168 147 SEIIEAKPEERRAIFEEaagiskykERRKETERKlERTREN---LDRLEDILN-------ELERQLK--SLERQAEKAE- 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 225 hrvqeenaRLKKKKEQLQQ-EIKDWSKSHAELSEQIRSFEKSQKDLEVALTHKDDNINALTnciTQLNRLdcesesedqn 303
Cdd:TIGR02168 214 --------RYKELKAELRElELALLVLRLEELREELEELQEELKEAEEELEELTAELQELE---EKLEEL---------- 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 304 kggsesdELANGEVggdrsEKVKNQIKQmmDVSRTQTAISVVEEDLKLLQCKLRasmstkcNLEDQIKKLEEDRSSLQSA 383
Cdd:TIGR02168 273 -------RLEVSEL-----EEEIEELQK--ELYALANEISRLEQQKQILRERLA-------NLERQLEELEAQLEELESK 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 384 KTVLEDECKTLRQKVEILNELYQqkemALQKKLSQEEYERQEREQRLSAADE-------KAVLAAEEVKTYKRRIEEMED 456
Cdd:TIGR02168 332 LDELAEELAELEEKLEELKEELE----SLEAELEELEAELEELESRLEELEEqletlrsKVAQLELQIASLNNEIERLEA 407
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387212246 457 ELQKTERS---FKNQIATHEKKAHDNWLKarAAERAIAEEKREAANLRHKLLELTQKMAMMQEE 517
Cdd:TIGR02168 408 RLERLEDRrerLQQEIEELLKKLEEAELK--ELQAELEELEEELEELQEELERLEEALEELREE 469
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
106-463 |
3.66e-06 |
|
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: 50.56 E-value: 3.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 106 AELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIKFKDKIKSLEETNE--------------ILGDTAKSLRAMLESE 171
Cdd:pfam01576 64 ARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDeeeaarqklqlekvTTEAKIKKLEEDILLL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 172 REQNAKnqdLISENKKSIEKLKDVISvNASEFSEVQIALNEAKLSEEKVKS--ECHRVQEENAR--LKKKKEQLQQEIKD 247
Cdd:pfam01576 144 EDQNSK---LSKERKLLEERISEFTS-NLAEEEEKAKSLSKLKNKHEAMISdlEERLKKEEKGRqeLEKAKRKLEGESTD 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 248 WSKSHAELSEQIR----SFEKSQKDLEVALTHKDDNINALTNCITQLNRL---------DCESESEDQNKG-------GS 307
Cdd:pfam01576 220 LQEQIAELQAQIAelraQLAKKEEELQAALARLEEETAQKNNALKKIRELeaqiselqeDLESERAARNKAekqrrdlGE 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 308 ESDEL------------ANGEVGGDRSEKVKNQIKQMMDVSRT---------QTAISVVEEDLKLLQCKLRASMS---TK 363
Cdd:pfam01576 300 ELEALkteledtldttaAQQELRSKREQEVTELKKALEEETRSheaqlqemrQKHTQALEELTEQLEQAKRNKANlekAK 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 364 CNLEDQIKKLEEDRSSLQSAKTVLEDECKTLRQKVEILNELYQQKEMA---LQKKLSQEEYERQEREQRLSAADEKAVLA 440
Cdd:pfam01576 380 QALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQraeLAEKLSKLQSELESVSSLLNEAEGKNIKL 459
|
410 420
....*....|....*....|...
gi 1387212246 441 AEEVKTYKRRIEEMEDELQKTER 463
Cdd:pfam01576 460 SKDVSSLESQLQDTQELLQEETR 482
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
76-407 |
4.63e-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: 50.44 E-value: 4.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 76 WRTVLAVKSRVYQVTEQQISEKLKNIMKENAelvqkLSSYEQKIK----ESKKHVQETKKQNMilsdEAIKFKDKIKSLE 151
Cdd:TIGR01612 658 YSTIKSELSKIYEDDIDALYNELSSIVKENA-----IDNTEDKAKlddlKSKIDKEYDKIQNM----ETATVELHLSNIE 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 152 ETNEILGDTAKSLRAMLESE--REQNAKNQDLISENKKSIEKL------KDVISVNASEFSEVQIALNEaklseekvKSE 223
Cdd:TIGR01612 729 NKKNELLDIIVEIKKHIHGEinKDLNKILEDFKNKEKELSNKIndyakeKDELNKYKSKISEIKNHYND--------QIN 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 224 CHRVQEENArlKKKKEQLQQEIKDWSKSHAELSEQIRSFEKSQKDLevaLTHKDDNINALTNCitqlnrldceseSEDQN 303
Cdd:TIGR01612 801 IDNIKDEDA--KQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDF---LNKVDKFINFENNC------------KEKID 863
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 304 KGGSESDELANgevggdrseKVKNQIKqmmdvsrtqtaisvvEEDLKLLQCKLRASMSTkcnLEDQIKKLEEDRSSLQSA 383
Cdd:TIGR01612 864 SEHEQFAELTN---------KIKAEIS---------------DDKLNDYEKKFNDSKSL---INEINKSIEEEYQNINTL 916
|
330 340 350
....*....|....*....|....*....|...
gi 1387212246 384 KTVLE---------DECKTLRQKVEILNELYQQ 407
Cdd:TIGR01612 917 KKVDEyikicentkESIEKFHNKQNILKEILNK 949
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
135-388 |
5.70e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 5.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 135 ILSDEAIKFKDKIKSLEETNEIlGDT--AKSLRAMLESEREQNAknQDLISENKKSIEklkdvisVNASEFSEVQIALNE 212
Cdd:COG4717 13 KFRDRTIEFSPGLNVIYGPNEA-GKStlLAFIRAMLLERLEKEA--DELFKPQGRKPE-------LNLKELKELEEELKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 213 AKLSEEkvksECHRVQEENARLKKKKEQLQQEIKDWSKSHAELSEQIRSFEKSQ--KDLEVALTHKDDNINALTNCITQL 290
Cdd:COG4717 83 AEEKEE----EYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQelEALEAELAELPERLEELEERLEEL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 291 NRL--DCESESEDQNKGGSESDELANgevggDRSEKVKNQIKQMM-DVSRTQTAISVVEEDLKLLQCKLRAsmstkcnLE 367
Cdd:COG4717 159 RELeeELEELEAELAELQEELEELLE-----QLSLATEEELQDLAeELEELQQRLAELEEELEEAQEELEE-------LE 226
|
250 260
....*....|....*....|.
gi 1387212246 368 DQIKKLEEDRSSLQSAKTVLE 388
Cdd:COG4717 227 EELEQLENELEAAALEERLKE 247
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
522-775 |
6.11e-06 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 50.07 E-value: 6.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 522 KPMPGRPNTQNPPRRGPlsqngsfgpspvsgGECSPPLTADPPARPLSATLNRREMPRSEFGSVDGPLPRPRWASEASGK 601
Cdd:PHA03378 675 QPSPTGANTMLPIQWAP--------------GTMQPPPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAA 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 602 PSASDPESGaAPTVNSSSRSSSPSKVMDEGKVSMAAKGPPPFPGTPLMSSPVGGPL-LPPIRYGP------PPQLCGPFG 674
Cdd:PHA03378 741 PGRARPPAA-APGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPRGAPTpQPPPQAGPtsmqlmPRAAPGQQG 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 675 PRPLPPPFGPG---------MRPPLGLREYAPGVP-----PGKRDLPLDPREFLPPGHAPFRPLGSLG------------ 728
Cdd:PHA03378 820 PTKQILRQLLTggvkrgrpsLKKPAALERQAAAGPtpspgSGTSDKIVQAPVFYPPVLQPIQVMRQLGsvraaaastvtq 899
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1387212246 729 -PREYffPGTRLPPPNHGPQDYPPSSAARdlppSGSRDEPPPASQGAS 775
Cdd:PHA03378 900 aPTEY--TGERRGVGPMHPTDIPPSKRAK----TDAYVESQPPHGGQS 941
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
69-469 |
6.86e-06 |
|
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: 49.57 E-value: 6.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 69 VSFAVFFWRTVLAVKSRVYQVTEQQISEKLKNIMKENaELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIKFKDKIK 148
Cdd:COG5185 148 DIEASYGEVETGIIKDIFGKLTQELNQNLKKLEIFGL-TLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAK 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 149 SLEETNEILgdtakSLRAMLESEREQNAKNQDLISENKKSIEKLKDvisvnaSEFSEvqialneaklSEEKVKsechRVQ 228
Cdd:COG5185 227 EIINIEEAL-----KGFQDPESELEDLAQTSDKLEKLVEQNTDLRL------EKLGE----------NAESSK----RLN 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 229 EENARLKKKKEQLQQEI------KDWSKSHAELSEQIRSFEKSQKdLEVALTHKDDNINALTNCITQLNrldcESESEDQ 302
Cdd:COG5185 282 ENANNLIKQFENTKEKIaeytksIDIKKATESLEEQLAAAEAEQE-LEESKRETETGIQNLTAEIEQGQ----ESLTENL 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 303 NKGGSESDELAnGEVGGDRSEKVKNQIKQMMDVSRT--------------------QTAISVVEEDLKLLQCKLRASMSt 362
Cdd:COG5185 357 EAIKEEIENIV-GEVELSKSSEELDSFKDTIESTKEsldeipqnqrgyaqeilatlEDTLKAADRQIEELQRQIEQATS- 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 363 kcNLEDQIKKLEEDRSSLQSAKTVLEDECK------------TLRQKVEILNELYQQKEMALQKKLSQEEYERQEREQRL 430
Cdd:COG5185 435 --SNEEVSKLLNELISELNKVMREADEESQsrleeaydeinrSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQL 512
|
410 420 430
....*....|....*....|....*....|....*....
gi 1387212246 431 SAADEKAVLAAEEVKTYKRRIEEMEDELQKTERSFKNQI 469
Cdd:COG5185 513 EGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELI 551
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
88-467 |
7.49e-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: 50.05 E-value: 7.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 88 QVTEQQISEKLKNIMKENAELV---------QKLSSYEQKiKESKKHVQETKKQNMILSdEAIKFKDKIKSLE------- 151
Cdd:TIGR01612 443 NIFKDDFDEFNKPIPKSKLKALekrffeifeEEWGSYDIK-KDIDENSKQDNTVKLILM-RMKDFKDIIDFMElykpdev 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 152 -ETNEILGDTAKSLRAMLESEREQNAK----------------NQDLISENKKSIeKLKDVISVNASEFSEV---QIALN 211
Cdd:TIGR01612 521 pSKNIIGFDIDQNIKAKLYKEIEAGLKesyelaknwkkliheiKKELEEENEDSI-HLEKEIKDLFDKYLEIddeIIYIN 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 212 EAKLS-EEKVK--SECHRVQEENARLKKKKEQLQQEIKDWSK-SHAELSEQIRSFEKSQKDLEVALTH-KDDNINALTN- 285
Cdd:TIGR01612 600 KLKLElKEKIKniSDKNEYIKKAIDLKKIIENNNAYIDELAKiSPYQVPEHLKNKDKIYSTIKSELSKiYEDDIDALYNe 679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 286 --CITQLNRLDcesESEDQNKggseSDELANgevggdRSEKVKNQIkQMMDVSRTQTAISVVEEDL-KLLQCKLRASMST 362
Cdd:TIGR01612 680 lsSIVKENAID---NTEDKAK----LDDLKS------KIDKEYDKI-QNMETATVELHLSNIENKKnELLDIIVEIKKHI 745
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 363 KCNLEDQIKKLEEDRSSLQsaktvledecKTLRQKVeilNELYQQKEM--ALQKKLSQEEYERQEREQRLSAADEKAVLA 440
Cdd:TIGR01612 746 HGEINKDLNKILEDFKNKE----------KELSNKI---NDYAKEKDElnKYKSKISEIKNHYNDQINIDNIKDEDAKQN 812
|
410 420
....*....|....*....|....*..
gi 1387212246 441 AEEVKTYKRRIEEMEDELQKTERSFKN 467
Cdd:TIGR01612 813 YDKSKEYIKTISIKEDEIFKIINEMKF 839
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
93-469 |
1.16e-05 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 49.06 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 93 QISEKLKNIMKENAELvqkLSSYEQKIKESKkhvQETKKQNMILSDEAIKFKDKI--KSLEETNEI-----LGDTAKSLR 165
Cdd:PTZ00440 400 YFISKYTNIISLSEHT---LKAAEDVLKENS---QKIADYALYSNLEIIEIKKKYdeKINELKKSInqlktLISIMKSFY 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 166 AMLESEREQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNEAKlseeKVKSECHRVQEenarLKKKKEQLQQEI 245
Cdd:PTZ00440 474 DLIISEKDSMDSKEKKESSDSNYQEKVDELLQIINSIKEKNNIVNNNFK----NIEDYYITIEG----LKNEIEGLIELI 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 246 KDWSKSHAELSEQirsfEKSQKDLEVALTHKDDNINALTNCITQLNRLDCESESEDQNKGGSESDELANGEVGGDRSEKV 325
Cdd:PTZ00440 546 KYYLQSIETLIKD----EKLKRSMKNDIKNKIKYIEENVDHIKDIISLNDEIDNIIQQIEELINEALFNKEKFINEKNDL 621
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 326 KNQIKQMMDvsrtqtaiSVVEEDLKLLQcklrASMSTkcNLEDQiKKLEEDRSSLQSAKTVL---EDECKTLRQKV---- 398
Cdd:PTZ00440 622 QEKVKYILN--------KFYKGDLQELL----DELSH--FLDDH-KYLYHEAKSKEDLQTLLntsKNEYEKLEFMKsdni 686
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387212246 399 -EILNELYQQKEMALQKKLSQEEYERQEREQRLSAADEKAVlaaEEVKTYKRRIEEMEDELQKTErSFKNQI 469
Cdd:PTZ00440 687 dNIIKNLKKELQNLLSLKENIIKKQLNNIEQDISNSLNQYT---IKYNDLKSSIEEYKEEEEKLE-VYKHQI 754
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
82-271 |
1.34e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 82 VKSRVYQVTEQQISekLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIK-FKDKIKSLEET-NEILgd 159
Cdd:PRK03918 530 LKEKLIKLKGEIKS--LKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEeLEERLKELEPFyNEYL-- 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 160 TAKSLRAMLESEREQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNEAKLseEKVKSECHRVQEENARLKKKKE 239
Cdd:PRK03918 606 ELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEY--EELREEYLELSRELAGLRAELE 683
|
170 180 190
....*....|....*....|....*....|..
gi 1387212246 240 QLQQEIKDWSKSHAELSEQIRSFEKSQKDLEV 271
Cdd:PRK03918 684 ELEKRREEIKKTLEKLKEELEEREKAKKELEK 715
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
107-469 |
1.49e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 107 ELVQKLSSYEQKIKESKKHVQETKKQnmilsdeAIKFKDKIKSLEETNEILGDTAKSLRAMLESEREQnaknqdlISENK 186
Cdd:PRK02224 318 ELEDRDEELRDRLEECRVAAQAHNEE-------AESLREDADDLEERAEELREEAAELESELEEAREA-------VEDRR 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 187 KSIEKLKDVISVNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLK----------KKKEQLQ---------QEIKD 247
Cdd:PRK02224 384 EEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEatlrtarervEEAEALLeagkcpecgQPVEG 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 248 wsKSHA----ELSEQIRSFEKSQKDLEVALTHKDDNINALTNCI-------TQLNRLDCESESEDQNKGGSESDELA--- 313
Cdd:PRK02224 464 --SPHVetieEDRERVEELEAELEDLEEEVEEVEERLERAEDLVeaedrieRLEERREDLEELIAERRETIEEKRERaee 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 314 ----NGEVGGDRSEKVKNQIKQMMDVSRTQTAISVVEEDLKLLQC------KLRASMSTKCNLEDQIKKLEEDRSSLQSA 383
Cdd:PRK02224 542 lrerAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKEriesleRIRTLLAAIADAEDEIERLREKREALAEL 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 384 KTVLEDECKTLRQKVEILNELYQQK--EMALQKKlsqeeyerqereqrlsaadEKAVLAAEEVKTYKRRIEEMEDELQKT 461
Cdd:PRK02224 622 NDERRERLAEKRERKRELEAEFDEAriEEAREDK-------------------ERAEEYLEQVEEKLDELREERDDLQAE 682
|
....*...
gi 1387212246 462 ERSFKNQI 469
Cdd:PRK02224 683 IGAVENEL 690
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
116-477 |
1.88e-05 |
|
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: 48.28 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 116 EQKIKESKKHVQETKKQNMILSDEA--------IKFKD-KIKSLEETNEILGDTAKSLR--AMLESEREQnaknqdlisE 184
Cdd:pfam10174 202 DQKEKENIHLREELHRRNQLQPDPAktkalqtvIEMKDtKISSLERNIRDLEDEVQMLKtnGLLHTEDRE---------E 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 185 NKKSIEKLKdvisvNASEFSEVQIalneaklseEKVKSECHRVQEENARLKKKKEQLQQEIKDwSKSHAELseqirsfek 264
Cdd:pfam10174 273 EIKQMEVYK-----SHSKFMKNKI---------DQLKQELSKKESELLALQTKLETLTNQNSD-CKQHIEV--------- 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 265 sqkdLEVALTHKDDNINALTNCITQLnRLDCESESEDQNKGGSESDELANgEVGGDRSEKvkNQIKQMMDVSRTQtaISV 344
Cdd:pfam10174 329 ----LKESLTAKEQRAAILQTEVDAL-RLRLEEKESFLNKKTKQLQDLTE-EKSTLAGEI--RDLKDMLDVKERK--INV 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 345 VEEDLKLLQCKLRASMSTKCNLEDQIKKLEEDRSSLQSAKTVLEDeckTLRQKVEILNELYQQKEMA------------- 411
Cdd:pfam10174 399 LQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEE---ALSEKERIIERLKEQREREdrerleeleslkk 475
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 412 ----LQKKLSQEEYERQEREQRLSAADEKAVLAAEEVKTYKRRIEEMEDELQKTERSFkNQIATHEKKAH 477
Cdd:pfam10174 476 enkdLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEEC-SKLENQLKKAH 544
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
96-510 |
1.98e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 96 EKLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIKFKDKIKSLEETNEIL-GDTAKSLRAMLESEREQ 174
Cdd:PTZ00121 1070 EGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEeARKAEDARKAEEARKAE 1149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 175 NAKNQDLI--------------SENKKSIEKLKDVISVNASEfsEVQIAlNEAKLSEEKVKSECHRVQEENARLK--KKK 238
Cdd:PTZ00121 1150 DAKRVEIArkaedarkaeearkAEDAKKAEAARKAEEVRKAE--ELRKA-EDARKAEAARKAEEERKAEEARKAEdaKKA 1226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 239 EQLQ--QEIKDwSKSHAELSEQIRSFEKSQKDLEVALTHkddninaltncitqLNRLDCESESEDQNKggseSDELANGE 316
Cdd:PTZ00121 1227 EAVKkaEEAKK-DAEEAKKAEEERNNEEIRKFEEARMAH--------------FARRQAAIKAEEARK----ADELKKAE 1287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 317 vggdrSEKVKNQIKQMMDVSRTQTAISVVEEDLKLLQCKLRASMSTKcNLEDQIKKLEEDRSSLQSAKTVLEDECKTLRQ 396
Cdd:PTZ00121 1288 -----EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK-KADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 397 KveilnelyQQKEMALQKKLSQEEYERqereqrlSAADEKA--VLAAEEVKTYKRRIEEMEDELQKTERSfknqiathEK 474
Cdd:PTZ00121 1362 A--------EEKAEAAEKKKEEAKKKA-------DAAKKKAeeKKKADEAKKKAEEDKKKADELKKAAAA--------KK 1418
|
410 420 430
....*....|....*....|....*....|....*.
gi 1387212246 475 KAHDnwLKARAAERAIAEEKREAANLRHKLLELTQK 510
Cdd:PTZ00121 1419 KADE--AKKKAEEKKKADEAKKKAEEAKKADEAKKK 1452
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
91-257 |
2.27e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.70 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 91 EQQISEKLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIKFkdkIKSLEETNEILGDTaKSLRAMLES 170
Cdd:PHA02562 194 QQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNL---VMDIEDPSAALNKL-NTAAAKIKS 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 171 EREQNAK--------------NQDLISENKKsIEKLKDVISVNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKK 236
Cdd:PHA02562 270 KIEQFQKvikmyekggvcptcTQQISEGPDR-ITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKIST 348
|
170 180
....*....|....*....|.
gi 1387212246 237 KKEQLQQEIKDWSKSHAELSE 257
Cdd:PHA02562 349 NKQSLITLVDKAKKVKAAIEE 369
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
228-463 |
2.31e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 228 QEENARLKKKKEQLQQEIKDWSKSHAELSEQIRSFEKSQKDLEVALTHKDDNINALTNCITQLNRldceseseDQNKGGS 307
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA--------ELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 308 ESDELANgevggdRSEKVKNQIKQMMDVSRTQTAISVVE-----EDLKLLQCKLRASMSTKCNLEDQIKKLEEDRSSLQS 382
Cdd:COG4942 91 EIAELRA------ELEAQKEELAELLRALYRLGRQPPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 383 AKTVLEDECKTLRQkveILNELYQQKEmALQKKLSQEEYERQEREQRLSAADEKAVLAAEEVKTYKRRIEEMEDELQKTE 462
Cdd:COG4942 165 LRAELEAERAELEA---LLAELEEERA-ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
.
gi 1387212246 463 R 463
Cdd:COG4942 241 E 241
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
88-463 |
2.82e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 47.81 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 88 QVTEQQISEKLKnimkENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIKFKD---KIKSLEETNEILGDTAKSL 164
Cdd:pfam05557 121 QRAELELQSTNS----ELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKElefEIQSQEQDSEIVKNSKSEL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 165 RAMLESEREQnaknQDLISENKKSIEKLKDVisvnasEFSEVQIALNEAKLSEEKvksechRVQEENARLKKKKEQLQQE 244
Cdd:pfam05557 197 ARIPELEKEL----ERLREHNKHLNENIENK------LLLKEEVEDLKRKLEREE------KYREEAATLELEKEKLEQE 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 245 IKDWSKSHAELSEQIRSFEksqkdlevalthkddninALTNCITQLNRLDCESESEdqnKGGSESDELANGEVGGDRSEK 324
Cdd:pfam05557 261 LQSWVKLAQDTGLNLRSPE------------------DLSRRIEQLQQREIVLKEE---NSSLTSSARQLEKARRELEQE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 325 VKNQIKQMMDVSRTQTAISVVEEDL---KLLQCKLRASMstKCNLEDQIKKLEEDRSSLQSAKTVLEDEckTLRQKVEIL 401
Cdd:pfam05557 320 LAQYLKKIEDLNKKLKRHKALVRRLqrrVLLLTKERDGY--RAILESYDKELTMSNYSPQLLERIEEAE--DMTQKMQAH 395
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387212246 402 NELYQQKEMALQKKLSQEEYERQEREQRLSAADEKAVLA-----AEEVKTYKRRIEEMEDELQKTER 463
Cdd:pfam05557 396 NEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLAdpsysKEEVDSLRRKLETLELERQRLRE 462
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
92-322 |
3.02e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 92 QQISEKLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIKFKDKI----KSLEETNEILGDTAkslRAM 167
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIaeaeAEIEERREELGERA---RAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 168 LESEREQNAKNQDLISENkksiekLKDVIS-VNASEfsevQIALNEAKLSEEkvksechrVQEENARLKKKKEQLQQEIK 246
Cdd:COG3883 96 YRSGGSVSYLDVLLGSES------FSDFLDrLSALS----KIADADADLLEE--------LKADKAELEAKKAELEAKLA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387212246 247 DWSKSHAELSEQIRSFEKSQKDLEVALTHKDDNINALTNcitQLNRLDCESESEDQNKGGSESDELANGEVGGDRS 322
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEA---QLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
83-415 |
3.10e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.59 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 83 KSRVYQVTEQQISE------KLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIKFKDKIK-SLEETNE 155
Cdd:PRK01156 344 KKSRYDDLNNQILElegyemDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINvKLQDISS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 156 ILGDTAKSLRAMLESEREQNAKNQDLISENKKSI-------EKLKDVISVNASEFSEVQIALNEaklseekVKSECHRVQ 228
Cdd:PRK01156 424 KVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVcgttlgeEKSNHIINHYNEKKSRLEEKIRE-------IEIEVKDID 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 229 EENARLKKKKEQLQQEIKDWSKSHAELSEQIRSFEKSQKDLEVALTHKDDNINALTNCITQLNRLDCESESEDQNKGGSE 308
Cdd:PRK01156 497 EKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAV 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 309 SDeLANGEVGGDRSEKVKNQIKQMMD------------VSRTQTAISVVEEDLKLLQCKL-------------------- 356
Cdd:PRK01156 577 IS-LIDIETNRSRSNEIKKQLNDLESrlqeieigfpddKSYIDKSIREIENEANNLNNKYneiqenkilieklrgkidny 655
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387212246 357 -------------RASMSTKCN-LEDQIKKLEEDRSSLQSAKTVLEDECKTLRQKVEILNELYQQKEMALQKK 415
Cdd:PRK01156 656 kkqiaeidsiipdLKEITSRINdIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESM 728
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
143-258 |
3.92e-05 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 43.78 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 143 FKDKIKSLEETNEILGDTAKSLRAMLESEREQNAKNQD-------LISENKKSIEKLKdvisvnaSEFSEVQIALNEAKL 215
Cdd:pfam07926 6 LQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQnyerelvLHAEDIKALQALR-------EELNELKAEIAELKA 78
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1387212246 216 SEEKVKSEchrVQEENARLKKKKEQLQQEIKDWSKSHAELSEQ 258
Cdd:pfam07926 79 EAESAKAE---LEESEESWEEQKKELEKELSELEKRIEDLNEQ 118
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
91-414 |
4.28e-05 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 47.52 E-value: 4.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 91 EQQISEKLkNIMKENAELVQ-KLSSYEQKIKESKKHVQE-TKKQNMILS-----DEAIKFKDKIKSLEETNEILGDTAKS 163
Cdd:PTZ00440 793 ENKISNDI-NILKENKKNNQdLLNSYNILIQKLEAHTEKnDEELKQLLQkfpteDENLNLKELEKEFNENNQIVDNIIKD 871
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 164 LRAMLES----EREQNAKNQDliSENKKSIEKLK----DVISVNASEFSEVQ----IALNEAKLSEEKVKSECHRVQEE- 230
Cdd:PTZ00440 872 IENMNKNiniiKTLNIAINRS--NSNKQLVEHLLnnkiDLKNKLEQHMKIINtdniIQKNEKLNLLNNLNKEKEKIEKQl 949
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 231 -NARLKKKKEQLQQEIKDWSKSHAELS-------EQIRSFEKSQKDLEVALTHKDDNINALTNCITQLNRldcesesEDQ 302
Cdd:PTZ00440 950 sDTKINNLKMQIEKTLEYYDKSKENINgndgthlEKLDKEKDEWEHFKSEIDKLNVNYNILNKKIDDLIK-------KQH 1022
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 303 NKGGSESDELANgEVGGDRSEKVKNQIKQM-------------MDVSRTQTAISvvEEDLKLLQCKlrasmstkcnLEDQ 369
Cdd:PTZ00440 1023 DDIIELIDKLIK-EKGKEIEEKVDQYISLLekmktklssfhfnIDIKKYKNPKI--KEEIKLLEEK----------VEAL 1089
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1387212246 370 IKKLEEDRSSLQSAKTVLEDECKTLRQKVEILNELYQQKEMALQK 414
Cdd:PTZ00440 1090 LKKIDENKNKLIEIKNKSHEHVVNADKEKNKQTEHYNKKKKSLEK 1134
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
544-781 |
5.47e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 46.79 E-value: 5.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 544 SFGPSPvSGGECSPPLTAdppARPLSATLNRREMPRSefgsVDGPLPRPRWASEASGKPSASDPESGAAPTVNSSSRSSS 623
Cdd:PRK12323 362 AFRPGQ-SGGGAGPATAA---AAPVAQPAPAAAAPAA----AAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEAL 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 624 PSKVMDEGKVSMAAKGPPPFPgtplMSSPVGGPLLPPIRYGPPPqlcgpfgprpLPPPFGPGMRPPLGLREYAPGVPPGK 703
Cdd:PRK12323 434 AAARQASARGPGGAPAPAPAP----AAAPAAAARPAAAGPRPVA----------AAAAAAPARAAPAAAPAPADDDPPPW 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 704 RDLPLDPREFLP--PGHAPFRPLGSLGPReyffPGTRLPPPNHGPQDYPPSSAARDLPPSGSRDEPPPASQGASQDCSPA 781
Cdd:PRK12323 500 EELPPEFASPAPaqPDAAPAGWVAESIPD----PATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPD 575
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
334-468 |
7.09e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 7.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 334 DVSRTQTAISVVEEDLKllqcKLRASMSTKCNLEDQIKKLEEDRSSLQSAKTVLEDECKTLRQKVEILNELYQQKEMALQ 413
Cdd:COG4913 662 DVASAEREIAELEAELE----RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387212246 414 KKLSQEEYERQER-EQRLSAADEKAVLA------AEEVKTYKRRIEEMEDELQKTERSFKNQ 468
Cdd:COG4913 738 AAEDLARLELRALlEERFAAALGDAVERelrenlEERIDALRARLNRAEEELERAMRAFNRE 799
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
156-403 |
7.79e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 7.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 156 ILGDTAKSLRAMLESEREQNAKN----QDLISENKKSIEKLKDVISV--NASEFSEVQIALNEAKLSEEKVKSECHRVQE 229
Cdd:COG4913 603 VLGFDNRAKLAALEAELAELEEElaeaEERLEALEAELDALQERREAlqRLAEYSWDEIDVASAEREIAELEAELERLDA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 230 EN---ARLKKKKEQLQQEIKDWSKSHAELSEQIRSFEKSQKDLEVALTHKDDNINALTNCITQLNRLDCESESEDQNKGG 306
Cdd:COG4913 683 SSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDA 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 307 SESDELAN--GEVGGDRSEKVKNQ---IKQM--------MDVSRTQTAISVVEEDLKLLQcKLRASmstkcNL---EDQI 370
Cdd:COG4913 763 VERELRENleERIDALRARLNRAEeelERAMrafnrewpAETADLDADLESLPEYLALLD-RLEED-----GLpeyEERF 836
|
250 260 270
....*....|....*....|....*....|....*...
gi 1387212246 371 KKL-----EEDRSSLQSAktvLEDECKTLRQKVEILNE 403
Cdd:COG4913 837 KELlnensIEFVADLLSK---LRRAIREIKERIDPLND 871
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
525-786 |
8.75e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.47 E-value: 8.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 525 PGRPNTQNPPR-RGPLSQNGsfGPSPVSGGecsPPltaDPPARPLSATLNRREMPRSEFGSvdgPLPRPRW--------- 594
Cdd:PHA03247 2475 PGAPVYRRPAEaRFPFAAGA--APDPGGGG---PP---DPDAPPAPSRLAPAILPDEPVGE---PVHPRMLtwirgleel 2543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 595 ASEASGKPSASDPESGAAPTVNSSSRSSSPSKVMDEGKVSMAAKGP--PPFPGTPlmSSPVGGPLLPPIRYGPPPQLCGP 672
Cdd:PHA03247 2544 ASDDAGDPPPPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPdaPPQSARP--RAPVDDRGDPRGPAPPSPLPPDT 2621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 673 FGPRPLPPPFGPGMRPPLGLREYAPGVPPGKRDLPLDPREFLP-----PGHAPFRPLGSLGPREYFFPGT--------RL 739
Cdd:PHA03247 2622 HAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPrrarrLGRAAQASSPPQRPRRRAARPTvgsltslaDP 2701
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1387212246 740 PPPNHGPQDYP------------PSSAARDLPPSGSRDEPPPASQGASQDCSPALKQSP 786
Cdd:PHA03247 2702 PPPPPTPEPAPhalvsatplppgPAAARQASPALPAAPAPPAVPAGPATPGGPARPARP 2760
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
159-434 |
1.04e-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: 45.53 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 159 DTAKSLRAMLESEREQNAKNQDLISENKKSIEKLKDVIsvnasEFSEVQIALNEAKLSEekVKSECHRVQEENARLKKKK 238
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQL-----AALERRIAALARRIRA--LEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 239 EQLQQEIKdwsKSHAELSEQIRSFEKSQKDLEVALTHKDDNINALTNCITQLNRLdcesesedqnkggsesdelangevg 318
Cdd:COG4942 93 AELRAELE---AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYL------------------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 319 gdrsekVKNQIKQMMDVSRTQTAISVVEEDLKLLQCKLRASMStkcNLEDQIKKLEEDRSSLQSAKTVLEDECKTLRQKV 398
Cdd:COG4942 145 ------APARREQAEELRADLAELAALRAELEAERAELEALLA---ELEEERAALEALKAERQKLLARLEKELAELAAEL 215
|
250 260 270
....*....|....*....|....*....|....*.
gi 1387212246 399 EILnelyQQKEMALQKKLSQEEYERQEREQRLSAAD 434
Cdd:COG4942 216 AEL----QQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
68-197 |
1.11e-04 |
|
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: 42.81 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 68 IVSFAV-------FFWRTVLAV-KSRvyqvtEQQISEKLKNIMKENAELVQKLSSYEQKIKESKKHVQEtkkqnmILsDE 139
Cdd:cd06503 6 IINFLIllfilkkFLWKPILKAlDER-----EEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQE------II-EE 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1387212246 140 AIKFKDKIKsleetNEILGDtakslrAMLESEREQNAKNQDLISENKKSIEKLKDVIS 197
Cdd:cd06503 74 ARKEAEKIK-----EEILAE------AKEEAERILEQAKAEIEQEKEKALAELRKEVA 120
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
146-284 |
1.12e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 146 KIKSLEETneilgdtAKSLRAmlESEREQNAKNQDLISENKKSIEKLKdvisvnaSEF-SEVQIALNEAKLSEEKVKSEC 224
Cdd:PRK12704 32 KIKEAEEE-------AKRILE--EAKKEAEAIKKEALLEAKEEIHKLR-------NEFeKELRERRNELQKLEKRLLQKE 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 225 HRVQEENARLKKKKEQLQQEIKDWSKSHAELSEQIRSFEKSQKDLEVALthkdDNINALT 284
Cdd:PRK12704 96 ENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL----ERISGLT 151
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
201-443 |
1.13e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 201 SEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIKdwskshaELSEQIRSFEKSQKDLEVALTHKDDNI 280
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE-------ALQAEIDKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 281 NAltncitQLNRLdcesesedQNKGGSES--DELANGEVGGDRSEKVkNQIKQMMDvsRTQTAISVVEEDLKLLQCKLRA 358
Cdd:COG3883 89 GE------RARAL--------YRSGGSVSylDVLLGSESFSDFLDRL-SALSKIAD--ADADLLEELKADKAELEAKKAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 359 SMSTKCNLEDQIKKLEEDRSSLQSAKTVLEDECKTLRQKVEILNELYQQKEMALQKKLSQEEYERQEREQRLSAADEKAV 438
Cdd:COG3883 152 LEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
....*
gi 1387212246 439 LAAEE 443
Cdd:COG3883 232 AAAAA 236
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
92-259 |
1.24e-04 |
|
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: 44.15 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 92 QQISEKLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIKFKDKIKSLEETneiLGD--TAKSLRAM-- 167
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ---LGNvrNNKEYEALqk 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 168 -LESEREQNAKNQDLISENKKSIEKLKDVISVNASEFSEVqialnEAKLSEEKvksechrvqeenARLKKKKEQLQQEIK 246
Cdd:COG1579 97 eIESLKRRISDLEDEILELMERIEELEEELAELEAELAEL-----EAELEEKK------------AELDEELAELEAELE 159
|
170
....*....|...
gi 1387212246 247 DWSKSHAELSEQI 259
Cdd:COG1579 160 ELEAEREELAAKI 172
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
93-264 |
1.31e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 44.62 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 93 QISEKLKNIMKENAELVqklssyeqkiKESKKHVqeTKKQNmILSDEAIKFKDKIKSLEETNEILgdtakslramLESER 172
Cdd:smart00787 140 KLLEGLKEGLDENLEGL----------KEDYKLL--MKELE-LLNSIKPKLRDRKDALEEELRQL----------KQLED 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 173 EQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQlqqeIKDWSKSH 252
Cdd:smart00787 197 ELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQ----CRGFTFKE 272
|
170
....*....|...
gi 1387212246 253 AE-LSEQIRSFEK 264
Cdd:smart00787 273 IEkLKEQLKLLQS 285
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
103-414 |
1.43e-04 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 44.56 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 103 KENAELVQ---KLSSYEQKIKESKKHVQETKKQNMILSDEAIKFKDKIKSLEETNEILG---DTAKSLRAMLES-EREQN 175
Cdd:pfam09728 1 KAARELMQllnKLDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQselSKAILAKSKLEKlCRELQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 176 AKNQDLISENKKSIEKLKDvisvNASEFSE-VQIALNEAKLSEEKVKSECHRVQEENARLKKK-KEQLQQeikdwskshA 253
Cdd:pfam09728 81 KQNKKLKEESKKLAKEEEE----KRKELSEkFQSTLKDIQDKMEEKSEKNNKLREENEELREKlKSLIEQ---------Y 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 254 ELSEQIrsFEK--SQKDLEVALthkddninaltnCITQLNRLDCESESEDQNKGGSESDELAngevggDRSEKVKNQIKQ 331
Cdd:pfam09728 148 ELRELH--FEKllKTKELEVQL------------AEAKLQQATEEEEKKAQEKEVAKARELK------AQVQTLSETEKE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 332 MmdvsRTQtaISVVEEDLKLLQCKLRAS-------------MSTKCnledqiKKLEEDRSSLQS--------------AK 384
Cdd:pfam09728 208 L----REQ--LNLYVEKFEEFQDTLNKSnevfttfkkemekMSKKI------KKLEKENLTWKRkweksnkallemaeER 275
|
330 340 350
....*....|....*....|....*....|
gi 1387212246 385 TVLEDECKTLRQKVEILNELYQqkemALQK 414
Cdd:pfam09728 276 QKLKEELEKLQKKLEKLENLCR----ALQA 301
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
103-402 |
1.91e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.11 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 103 KENAELVqkLSSYEQKIKESKKHVQET----KKQNMILSDEAIKFKDKIKSLEETNEILGDTAKSlramlESEREQNAKN 178
Cdd:pfam15921 73 KEHIERV--LEEYSHQVKDLQRRLNESnelhEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRR-----ESQSQEDLRN 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 179 Q----------------DLISENKKSIEKLKDVISVNASEFSEVQIAL---NEA---KLSEEKVKSECHrVQEENARLKK 236
Cdd:pfam15921 146 QlqntvheleaakclkeDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILvdfEEAsgkKIYEHDSMSTMH-FRSLGSAISK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 237 KKEQLQQEIKDWSKSHAELSEQIRSFE-KSQKDLEVALTHKDDNINALTncitqlnrldceSESEDQNKGGSESDELANG 315
Cdd:pfam15921 225 ILRELDTEISYLKGRIFPVEDQLEALKsESQNKIELLLQQHQDRIEQLI------------SEHEVEITGLTEKASSARS 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 316 EvggdrSEKVKNQIKQMMDVSRTQTAISVveedlkllqcklrasmstkCNLEDQIKKLEEDRSSLQSAKTVLEDECKTLR 395
Cdd:pfam15921 293 Q-----ANSIQSQLEIIQEQARNQNSMYM-------------------RQLSDLESTVSQLRSELREAKRMYEDKIEELE 348
|
....*..
gi 1387212246 396 QKVEILN 402
Cdd:pfam15921 349 KQLVLAN 355
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
80-261 |
2.08e-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: 44.37 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 80 LAVKSRVYQVTEQQISE---KLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQN---MILSDEAikFKDKIKSLEet 153
Cdd:COG4942 64 IAALARRIRALEQELAAleaELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPplaLLLSPED--FLDAVRRLQ-- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 154 neILGDTAKSLRAMLESEREQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNEAKLSEEKVKSECHRVQEENAR 233
Cdd:COG4942 140 --YLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
170 180
....*....|....*....|....*...
gi 1387212246 234 LKKKKEQLQQEIKDWSKSHAELSEQIRS 261
Cdd:COG4942 218 LQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
523-786 |
2.18e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.93 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 523 PMPGRPNTQNPPRRGPLSQNGSFGPSPVSGGECSPPLTADPPARPLSATLNRREMPRSEFGSV---DGPLPRPRWASEAS 599
Cdd:PHA03247 2554 PLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPlppDTHAPDPPPPSPSP 2633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 600 GKPSASDPESGAAPTVNSSSRSSSPSKVMDEGKVSMAAKGPPPfpgtplmSSPVGGPLLPPIrygPPPqlcgpfgprplP 679
Cdd:PHA03247 2634 AANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQA-------SSPPQRPRRRAA---RPT-----------V 2692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 680 PPFGPGMRPPlglreyAPGVPPGKRDLPLDPREFLPPGHA---------PFRPLGSLGPREYFFPGTRLPPPNHGPQDYP 750
Cdd:PHA03247 2693 GSLTSLADPP------PPPPTPEPAPHALVSATPLPPGPAaarqaspalPAAPAPPAVPAGPATPGGPARPARPPTTAGP 2766
|
250 260 270
....*....|....*....|....*....|....*.
gi 1387212246 751 PSSAARDLPPSGSrdePPPASQGASQDCSPALKQSP 786
Cdd:PHA03247 2767 PAPAPPAAPAAGP---PRRLTRPAVASLSESRESLP 2799
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
100-399 |
3.25e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.06 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 100 NIMKENAELV---QKLSSYEQKIKESKKHVQETK---KQNMILSDEAI-KFKDKIKSLEETNEILGDTAKSLRAML---E 169
Cdd:PRK04778 99 RFRKAKHEINeieSLLDLIEEDIEQILEELQELLeseEKNREEVEQLKdLYRELRKSLLANRFSFGPALDELEKQLenlE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 170 SEREQ--NAKNQ-------DLISENKKSIEKLKDVISVNASEFSEVQI----ALNE-----AKLSEE-------KVKSEC 224
Cdd:PRK04778 179 EEFSQfvELTESgdyvearEILDQLEEELAALEQIMEEIPELLKELQTelpdQLQElkagyRELVEEgyhldhlDIEKEI 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 225 HRVQEENARLKKKKEQLqqEIKDWSKSHAELSEQIRSF--------------EKSQKDLEVALTHKDDNINALTnciTQL 290
Cdd:PRK04778 259 QDLKEQIDENLALLEEL--DLDEAEEKNEEIQERIDQLydilerevkarkyvEKNSDTLPDFLEHAKEQNKELK---EEI 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 291 NRLdcesesedqnkggSESDELANGEVggDRSEKVKNQIKQMM--------DVSRTQTAISVVEEDLKLLQCKLRAsmst 362
Cdd:PRK04778 334 DRV-------------KQSYTLNESEL--ESVRQLEKQLESLEkqydeiteRIAEQEIAYSELQEELEEILKQLEE---- 394
|
330 340 350
....*....|....*....|....*....|....*..
gi 1387212246 363 kcnLEDQIKKLEEDRSSLQSAKTVLEDECKTLRQKVE 399
Cdd:PRK04778 395 ---IEKEQEKLSEMLQGLRKDELEAREKLERYRNKLH 428
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
159-524 |
3.61e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.19 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 159 DTAKSLRAMLESEREQNAKNQDLISENKKSiekLKDVISVNASEFSEVQIALNEAKLSEEKVKSEcHRVQEENARLKKKK 238
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLCTPCMPDT---YHERKQVLEKELKHLREALQQTQQSHAYLTQK-REAQEEQLKKQQLL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 239 EQLQQEIKDWSKSHAELSEQIRSFEKSQKDLEVALTHKddninaltnCITQLNRLDCESESEDQNKGGSESDELAngevg 318
Cdd:TIGR00618 263 KQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIK---------AVTQIEQQAQRIHTELQSKMRSRAKLLM----- 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 319 gdrseKVKNQIKQMMDVSRTQTAISVVEEDLKLLQCKLRASMSTKCNLEDQiKKLEEDRSSLQSAKTVLEDECKTLRQKV 398
Cdd:TIGR00618 329 -----KRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQ-HTLTQHIHTLQQQKTTLTQKLQSLCKEL 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 399 EILNELYQQ------KEMALQKKLSQEEYERQEREQRLSAADEKAVLAAEEVKTYKRRIEEMEDELQKTERSFKNQIATH 472
Cdd:TIGR00618 403 DILQREQATidtrtsAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIH 482
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1387212246 473 EKKAHdnwlKARAAERAIAEEKREAANLRHKLLELTQKMAMMQEEPVIVKPM 524
Cdd:TIGR00618 483 LQETR----KKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRM 530
|
|
| DivIC |
pfam04977 |
Septum formation initiator; DivIC from B. subtilis is necessary for both vegetative and ... |
219-261 |
3.81e-04 |
|
Septum formation initiator; DivIC from B. subtilis is necessary for both vegetative and sporulation septum formation. These proteins are mainly composed of an amino terminal coiled-coil.
Pssm-ID: 428231 [Multi-domain] Cd Length: 69 Bit Score: 39.51 E-value: 3.81e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1387212246 219 KVKSECHRVQEENARLKKKKEQLQQEIKDWSKSHAELSEQIRS 261
Cdd:pfam04977 10 QLKQEIAQLQAEIAKLKQENEELEAEIKDLKSDPDYIEERARS 52
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
92-405 |
3.83e-04 |
|
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: 43.69 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 92 QQISEKLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQnmILSD-----EAI-KFKDKIKSLEE--------TNEil 157
Cdd:pfam06160 96 DDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKT--LLANrfsygPAIdELEKQLAEIEEefsqfeelTES-- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 158 GDTAKSlRAMLESEREQNAKNQDLISENKKSIEKLKDVIsvnASEFSEVQIALNEAK-----LSEEKVKSECHRVQEENA 232
Cdd:pfam06160 172 GDYLEA-REVLEKLEEETDALEELMEDIPPLYEELKTEL---PDQLEELKEGYREMEeegyaLEHLNVDKEIQQLEEQLE 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 233 RLKKKKEQLqqEIKDWSKSHAELSEQI--------------RSFEKSQKDLEVALTHKDDNINALTNCITQLN---RLDc 295
Cdd:pfam06160 248 ENLALLENL--ELDEAEEALEEIEERIdqlydllekevdakKYVEKNLPEIEDYLEHAEEQNKELKEELERVQqsyTLN- 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 296 ESESEDQNKGGSESDELangevggdrsEKVKNQIKQMMDvsRTQTAISVVEEDLKllqcklrasmstkcNLEDQIKKLEE 375
Cdd:pfam06160 325 ENELERVRGLEKQLEEL----------EKRYDEIVERLE--EKEVAYSELQEELE--------------EILEQLEEIEE 378
|
330 340 350
....*....|....*....|....*....|....
gi 1387212246 376 DRSSLQSAKTVLEDECKTLRQKVE----ILNELY 405
Cdd:pfam06160 379 EQEEFKESLQSLRKDELEAREKLDefklELREIK 412
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
92-326 |
4.32e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 4.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 92 QQISEKLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIKFKDKIKSLEETNEILGDTAKSLRAmlese 171
Cdd:COG4372 62 EQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEA----- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 172 reQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNEAKLSE-EKVKSECHRVQEENARLKKKKEQLQQEIKDWSK 250
Cdd:COG4372 137 --QIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387212246 251 SHAELSEQIRSFEKSQKDLEVALTHKDDNINALTNCITQLNRLDCESESEDQNKGGSESDELANGEVGGDRSEKVK 326
Cdd:COG4372 215 ELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEE 290
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
88-464 |
4.71e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.01 E-value: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 88 QVTEQQisEKLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIKFKDKIKSL----EETNEILGDTAKS 163
Cdd:pfam01576 167 NLAEEE--EKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELqaqiAELRAQLAKKEEE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 164 LRAML-ESEREQNAKNQDLisenkKSIEKLKDVISVNASEFSEVQIALNEAK-----LSEE--KVKSECHRVQEENA--- 232
Cdd:pfam01576 245 LQAALaRLEEETAQKNNAL-----KKIRELEAQISELQEDLESERAARNKAEkqrrdLGEEleALKTELEDTLDTTAaqq 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 233 RLKKKKEQ----LQQEIKDWSKSH---------------AELSEQIRSFEKSQKDLEVALTHKDDNINALTNCITQLNRL 293
Cdd:pfam01576 320 ELRSKREQevteLKKALEEETRSHeaqlqemrqkhtqalEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 294 DCESES---------EDQNKGGSESdELANGEVgGDRSEKVKNQIKQMMDV--------SRTQTAISVVEEDLKLLQCKL 356
Cdd:pfam01576 400 KQDSEHkrkklegqlQELQARLSES-ERQRAEL-AEKLSKLQSELESVSSLlneaegknIKLSKDVSSLESQLQDTQELL 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 357 RASMSTKCNLEDQIKKLEEDRSSLQSAktvLEDECKTlRQKVEILNELYQQKEMALQKKLsqeeyerQEREQRLSAADEK 436
Cdd:pfam01576 478 QEETRQKLNLSTRLRQLEDERNSLQEQ---LEEEEEA-KRNVERQLSTLQAQLSDMKKKL-------EEDAGTLEALEEG 546
|
410 420
....*....|....*....|....*...
gi 1387212246 437 AVLAAEEVKTYKRRIEEMEDELQKTERS 464
Cdd:pfam01576 547 KKRLQRELEALTQQLEEKAAAYDKLEKT 574
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
96-397 |
5.02e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 96 EKLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIK-FKDKIKSLEETNEILGDTAKSLRAMLESEREQ 174
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQdLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 175 --NAKNQDLISENKKSIEKLKDVI---------------------------------------------SVNASEFSEVQ 207
Cdd:COG4717 229 leQLENELEAAALEERLKEARLLLliaaallallglggsllsliltiagvlflvlgllallflllarekASLGKEAEELQ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 208 IALNEAKLSEEKVKSECHRVQ-------EENARLKKKKEQLQQEIKDWSKSHAELseQIRSFEKSQKDLevaLTHKD-DN 279
Cdd:COG4717 309 ALPALEELEEEELEELLAALGlppdlspEELLELLDRIEELQELLREAEELEEEL--QLEELEQEIAAL---LAEAGvED 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 280 INALTNCITQLNRL--------DCESESEDQNKGGSESDELANGEVGGDRSEKVKNQIKQ--------MMDVSRTQTAIS 343
Cdd:COG4717 384 EEELRAALEQAEEYqelkeeleELEEQLEELLGELEELLEALDEEELEEELEELEEELEEleeeleelREELAELEAELE 463
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1387212246 344 VVEEDLKLLQCKLRASMstkcnLEDQIKKLEEDRSSLQSAKTVLEDECKTLRQK 397
Cdd:COG4717 464 QLEEDGELAELLQELEE-----LKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
96-482 |
6.32e-04 |
|
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: 43.50 E-value: 6.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 96 EKLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIKF----KDKIKSLEETNEILGDTAKSLRAMLESE 171
Cdd:TIGR00606 248 DPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVfqgtDEQLNDLYHNHQRTVREKERELVDCQRE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 172 REQNAKNQDLISENKKSIEKLKDVISVNASEFSEvQIALNEAKLSEEKVKSECH--------RVQEENArLKKKKEQLQQ 243
Cdd:TIGR00606 328 LEKLNKERRLLNQEKTELLVEQGRLQLQADRHQE-HIRARDSLIQSLATRLELDgfergpfsERQIKNF-HTLVIERQED 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 244 EIKDWSKSHAELSEQIRSFEKSQKDLEVALTHKDDNInaltncitqlnRLDCESESEDQNKGGSESDELANGEVGGDRSE 323
Cdd:TIGR00606 406 EAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTI-----------ELKKEILEKKQEELKFVIKELQQLEGSSDRIL 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 324 KVKNQIKqmmdvsRTQTAISVVEEDlKLLQCKLRASMS---TKCNLEDQIKKLEEDRSSLQSAKTVLEDECKTLRQKVEI 400
Cdd:TIGR00606 475 ELDQELR------KAERELSKAEKN-SLTETLKKEVKSlqnEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDK 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 401 LNELYQQKEMALQKKLSqeEYERQEREQRLSAADEKavlAAEEVKTYKRRIEEMEDELQKTERSfKNQIATHEKKAHDNW 480
Cdd:TIGR00606 548 DEQIRKIKSRHSDELTS--LLGYFPNKKQLEDWLHS---KSKEINQTRDRLAKLNKELASLEQN-KNHINNELESKEEQL 621
|
..
gi 1387212246 481 LK 482
Cdd:TIGR00606 622 SS 623
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
102-479 |
6.47e-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: 6.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 102 MKENAELVQKLSS-YEQKIKESKKHV-----QETKKQNmilsdeaiKFKDKIKSLEETNEILGDTAKSLRAMLESEREQN 175
Cdd:pfam05483 217 LKEDHEKIQHLEEeYKKEINDKEKQVsllliQITEKEN--------KMKDLTFLLEESRDKANQLEEKTKLQDENLKELI 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 176 AKNQDLISENKKSIEKLKDVISVNASEFSEVQIA-----------------LNEAKLSEEKVKSECHR--------VQEE 230
Cdd:pfam05483 289 EKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIAtkticqlteekeaqmeeLNKAKAAHSFVVTEFEAttcsleelLRTE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 231 NARLKKKKEQLQQEIKDWSKSHAELSEQIRSFEKSQKDLEvalthkddninaltncitQLNRLDCESESE-DQNKggsES 309
Cdd:pfam05483 369 QQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELE------------------ELKKILAEDEKLlDEKK---QF 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 310 DELANgEVGGDRSEKV---KNQIKQMMDVSRTQTAISVVEE-------DLK--LLQCKLR-ASMSTKCN-LEDQIKKLEE 375
Cdd:pfam05483 428 EKIAE-ELKGKEQELIfllQAREKEIHDLEIQLTAIKTSEEhylkeveDLKteLEKEKLKnIELTAHCDkLLLENKELTQ 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 376 DRSSLQ-SAKTVLEDECKTLRQKVEILNEL--YQQKEMALQKKLSQEEYERQEREQ----RLSAADEKAVLAAEEVKTYK 448
Cdd:pfam05483 507 EASDMTlELKKHQEDIINCKKQEERMLKQIenLEEKEMNLRDELESVREEFIQKGDevkcKLDKSEENARSIEYEVLKKE 586
|
410 420 430
....*....|....*....|....*....|.
gi 1387212246 449 RRIEEMEDELQKTERSFKNQIATHEKKAHDN 479
Cdd:pfam05483 587 KQMKILENKCNNLKKQIENKNKNIEELHQEN 617
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
91-390 |
8.60e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 8.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 91 EQQISEKLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIKFKDKIKSLEETNEILGDTAKSLRAmLES 170
Cdd:PTZ00121 1618 AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEA-LKK 1696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 171 EREQNAKNQDL---ISENKKSIEKLKDVISVNASEFSEVQialneAKLSEEKVKSECHRVQEENarlKKKKEQLQQEIKD 247
Cdd:PTZ00121 1697 EAEEAKKAEELkkkEAEEKKKAEELKKAEEENKIKAEEAK-----KEAEEDKKKAEEAKKDEEE---KKKIAHLKKEEEK 1768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 248 WSKSHAELSEQIRSFEKSQKDlEVALTHKDDNINaltncitqlnrlDCESESEDQNKGGSESDELANgevggDRSEKVKN 327
Cdd:PTZ00121 1769 KAEEIRKEKEAVIEEELDEED-EKRRMEVDKKIK------------DIFDNFANIIEGGKEGNLVIN-----DSKEMEDS 1830
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387212246 328 QIKQMMDVSRTQTAISVVEEDLKLLQCKLRA--------SMSTKCNLEDQIKKLEEDRSSLQSAKTVLEDE 390
Cdd:PTZ00121 1831 AIKEVADSKNMQLEEADAFEKHKFNKNNENGedgnkeadFNKEKDLKEDDEEEIEEADEIEKIDKDDIERE 1901
|
|
| PTZ00419 |
PTZ00419 |
valyl-tRNA synthetase-like protein; Provisional |
107-293 |
8.92e-04 |
|
valyl-tRNA synthetase-like protein; Provisional
Pssm-ID: 240411 [Multi-domain] Cd Length: 995 Bit Score: 43.07 E-value: 8.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 107 ELVQKLSSYEQKIkES---KKHVQETKKQNMILSDEAIK-FKDKIKSLEETNEILGDTAK-SLRAMLESereQNAKNQDL 181
Cdd:PTZ00419 798 ELYQRLPNYLRKS-ESisiAKYPQPNPGWNNEALDEEMKiIMSIVKSIRSLIATLGIPNKtKPDCYVTA---KDAELIEL 873
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 182 ISENKKSIEKLKDVISVNASEFSEVQIALNE--------AKLSEEKVKSECHRVQEENARLKKKKEQLQQEIKDWSKS-- 251
Cdd:PTZ00419 874 IESAENLISTLAKIGSVSVIPPIEEEAEVPKgcgfdvvdNKVIIYLNLDEFIDLKKELAKLEKKLAKLQKSLESYLKKis 953
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1387212246 252 ----HAELSEQIRSFEKSQKDlevALTHkddNINALTNCITQLNRL 293
Cdd:PTZ00419 954 ipnyEDKVPEDVRKLNDEKID---ELNE---EIKQLEQAIEELKSL 993
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
90-417 |
9.17e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.90 E-value: 9.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 90 TEQQISEKLKNIMKENAELVQKLSS-YEQKIKESKKHVQETKKqnmiLSDEAIKfkdkikslEETNEILGDTAKSLRAML 168
Cdd:PTZ00440 660 SKEDLQTLLNTSKNEYEKLEFMKSDnIDNIIKNLKKELQNLLS----LKENIIK--------KQLNNIEQDISNSLNQYT 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 169 ESEREQNaKNQDLISENKKSIEKLKDVISVNASEFSeVQIALNEAKLSEEKVKSEchRVQEENARLKKKKEQLQQEIKDW 248
Cdd:PTZ00440 728 IKYNDLK-SSIEEYKEEEEKLEVYKHQIINRKNEFI-LHLYENDKDLPDGKNTYE--EFLQYKDTILNKENKISNDINIL 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 249 SKSHAELSEQIRSFEKSQKDLEVALTHKDDNINALTNCITqlNRLDCESESEDQNKGGSESDELANgevggdRSEKVKNQ 328
Cdd:PTZ00440 804 KENKKNNQDLLNSYNILIQKLEAHTEKNDEELKQLLQKFP--TEDENLNLKELEKEFNENNQIVDN------IIKDIENM 875
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 329 IKQMMDVSRTQTAISVVEEDLKLLQCKLRASMSTKCNLEDQIKKLEEDRSSLQSAKTVLEDECKTLRQKVE--ILNELYQ 406
Cdd:PTZ00440 876 NKNINIIKTLNIAINRSNSNKQLVEHLLNNKIDLKNKLEQHMKIINTDNIIQKNEKLNLLNNLNKEKEKIEkqLSDTKIN 955
|
330
....*....|.
gi 1387212246 407 QKEMALQKKLS 417
Cdd:PTZ00440 956 NLKMQIEKTLE 966
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
87-280 |
9.24e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 9.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 87 YQVTEQQISEKLKNIMKENAELVQKLSSYEQKIKESK-KHVQETKKQNMIlsdeaikfKDKIKSLEETNEILGDTAKSLR 165
Cdd:TIGR02169 348 ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRdELKDYREKLEKL--------KREINELKRELDRLQEELQRLS 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 166 AMLEserEQNAKNQDLISENKKSIEKLKDVI-SVNASEFSEVQIALNEAKLSEE---------KVKSECHRVQEENARLK 235
Cdd:TIGR02169 420 EELA---DLNAAIAGIEAKINELEEEKEDKAlEIKKQEWKLEQLAADLSKYEQElydlkeeydRVEKELSKLQRELAEAE 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1387212246 236 KKKEQLQQEIKDWSKS-----------HAELSEQIRSFEKSQKDLEVALTHKDDNI 280
Cdd:TIGR02169 497 AQARASEERVRGGRAVeevlkasiqgvHGTVAQLGSVGERYATAIEVAAGNRLNNV 552
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
533-780 |
1.09e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.85 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 533 PPRRGPLSQNGSFGPSPVSGgecSPPLTADPPARPLSATLNRREMPRSEFGSVDGPLPRPRwaseasgkPSASDPESGAA 612
Cdd:PHA03307 19 EFFPRPPATPGDAADDLLSG---SQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPG--------TEAPANESRST 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 613 PTVNSSSRSSSPSKVMDEGKvsmaAKGPPPFPGTPLMSSPVGGPllPPirygPPPQLCGPFGPRPLPPPFGPGMRPPLGL 692
Cdd:PHA03307 88 PTWSLSTLAPASPAREGSPT----PPGPSSPDPPPPTPPPASPP--PS----PAPDLSEMLRPVGSPGPPPAASPPAAGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 693 ---REYAPGVPPGKRDLPLDPREflPPGHAPFRPLGSLGPREyffPGTRLPPPNHGPqDYPPSSAARDLPPSGSRDEPPP 769
Cdd:PHA03307 158 spaAVASDAASSRQAALPLSSPE--ETARAPSSPPAEPPPST---PPAAASPRPPRR-SSPISASASSPAPAPGRSAADD 231
|
250
....*....|.
gi 1387212246 770 ASQGASQDCSP 780
Cdd:PHA03307 232 AGASSSDSSSS 242
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
130-407 |
1.12e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.83 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 130 KKQNMILSDEAIKFKDKIKSLEETNeilgdtaKSLRAMLESEREQN-AKNQDLISENKKSIEKLKDVISVNASEFSEVQI 208
Cdd:pfam00038 3 KEQLQELNDRLASYIDKVRFLEQQN-------KLLETKISELRQKKgAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 209 ALNEAKLSEEKVKSEC-----HRVQEEN----------------ARLKKKKEQLQQEIKDWSKSH-AELSEQIRSFEKSQ 266
Cdd:pfam00038 76 ELDNLRLAAEDFRQKYedelnLRTSAENdlvglrkdldeatlarVDLEAKIESLKEELAFLKKNHeEEVRELQAQVSDTQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 267 KDLEVALTHKDD------NINALTNCITQLNRLDCESESEdqnkggSESDELaNGEVGGDrSEKVKNQIKQMMDVSRTqt 340
Cdd:pfam00038 156 VNVEMDAARKLDltsalaEIRAQYEEIAAKNREEAEEWYQ------SKLEEL-QQAAARN-GDALRSAKEEITELRRT-- 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387212246 341 aisvveedLKLLQCKLRASMSTKCNLEDQIKKLEE----DRSSLQSAKTVLEDECKTLRQKVEILNELYQQ 407
Cdd:pfam00038 226 --------IQSLEIELQSLKKQKASLERQLAETEEryelQLADYQELISELEAELQETRQEMARQLREYQE 288
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
60-262 |
1.30e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.00 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 60 VLITASLGIVSFAVFFWRtvlavKSRVYQVTEQQISEKLKNIMKENAELVQKLSSYEQKIKESKKhvQETKKQNMILSDE 139
Cdd:PRK12705 10 LLLLIGLLLGVLVVLLKK-----RQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQR--QEARREREELQRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 140 AIKFKDKIKSLEETNEILGDTAKSLramLESEREQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNEAKLSEEK 219
Cdd:PRK12705 83 EERLVQKEEQLDARAEKLDNLENQL---EEREKALSARELELEELEKQLDNELYRVAGLTPEQARKLLLKLLDAELEEEK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1387212246 220 VKSecHRVQEENARLKKKKEQLQQEIKDWSKSHAELSEQIRSF 262
Cdd:PRK12705 160 AQR--VKKIEEEADLEAERKAQNILAQAMQRIASETASDLSVS 200
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
92-191 |
1.40e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.12 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 92 QQISEKLKNIMKENAE----LVQKLSS----YEQKIKESKKHVQETKKQNMILSDEAIKFKDKIKSL-----EETNEILg 158
Cdd:PRK00409 501 ENIIEEAKKLIGEDKEklneLIASLEElereLEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLleeaeKEAQQAI- 579
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1387212246 159 DTAKS-----LRAMLESEREQNA--KNQDLIsENKKSIEK 191
Cdd:PRK00409 580 KEAKKeadeiIKELRQLQKGGYAsvKAHELI-EARKRLNK 618
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
93-415 |
1.47e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.51 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 93 QISEKLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIKFKD---KIKSL----EETNEILGDTAKSLR 165
Cdd:PTZ00440 474 DLIISEKDSMDSKEKKESSDSNYQEKVDELLQIINSIKEKNNIVNNNFKNIEDyyiTIEGLkneiEGLIELIKYYLQSIE 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 166 AMLESEREQNA------KNQDLISENkksIEKLKDVISVNAS---EFSEVQIALNEAKLSEEKVKSECHRVQEENARLKK 236
Cdd:PTZ00440 554 TLIKDEKLKRSmkndikNKIKYIEEN---VDHIKDIISLNDEidnIIQQIEELINEALFNKEKFINEKNDLQEKVKYILN 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 237 K--KEQLQQEIKDWSKshaelseqirsFEKSQKDLEVALTHKDDNINALTNCITQ---LNRLDCESESEDQNKGGSESDE 311
Cdd:PTZ00440 631 KfyKGDLQELLDELSH-----------FLDDHKYLYHEAKSKEDLQTLLNTSKNEyekLEFMKSDNIDNIIKNLKKELQN 699
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 312 LANGEvgGDRSEKVKNQIKQMMDVSRTQTAISVVEedlkllqckLRASMStkcNLEDQIKKLEEDRSSLQSAK----TVL 387
Cdd:PTZ00440 700 LLSLK--ENIIKKQLNNIEQDISNSLNQYTIKYND---------LKSSIE---EYKEEEEKLEVYKHQIINRKnefiLHL 765
|
330 340
....*....|....*....|....*...
gi 1387212246 388 EDECKTLRQKVEILNELYQQKEMALQKK 415
Cdd:PTZ00440 766 YENDKDLPDGKNTYEEFLQYKDTILNKE 793
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
107-275 |
1.63e-03 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153280 [Multi-domain] Cd Length: 218 Bit Score: 40.80 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 107 ELVQKLSSYEQKIKE-SK------KHVQETKKQNMILSDEAIKF----KDKIKSLEETNEILGDTAKSLRAMLESE-REQ 174
Cdd:cd07596 8 EAKDYILKLEEQLKKlSKqaqrlvKRRRELGSALGEFGKALIKLakceEEVGGELGEALSKLGKAAEELSSLSEAQaNQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 175 NAKNQDLISENKKSIEKLKDVISVNASEFSEVQIA---LNEAKLSEEKVK----SECHRVQEENARLKKKKEQLQQEIKD 247
Cdd:cd07596 88 LVKLLEPLKEYLRYCQAVKETLDDRADALLTLQSLkkdLASKKAQLEKLKaapgIKPAKVEELEEELEEAESALEEARKR 167
|
170 180
....*....|....*....|....*....
gi 1387212246 248 WSKSHAELSEQIRSFEKS-QKDLEVALTH 275
Cdd:cd07596 168 YEEISERLKEELKRFHEErARDLKAALKE 196
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
86-275 |
1.68e-03 |
|
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: 40.86 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 86 VYQVTEQQiseklkNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIK-FKDKIKSLEET------NEILG 158
Cdd:cd21116 15 VTAILNQP------NINLIPLDLLPSLNTHQALARAHALEWLNEIKPKLLSLPNDIIgYNNTFQSYYPDlieladNLIKG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 159 DTA--KSLRAMLESEREQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNEAKLSEEKVKSECHRVQEENAR--- 233
Cdd:cd21116 89 DQGakQQLLQGLEALQSQVTKKQTSVTSFINELTTFKNDLDDDSRNLQTDATKAQAQVAVLNALKNQLNSLAEQIDAaid 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1387212246 234 ----LKKKKEQLQQEIKDWSKShAELSEQIRSFEKSQKDLEVALTH 275
Cdd:cd21116 169 alekLSNDWQTLDSDIKELITD-LEDAESSIDAAFLQADLKAAKAD 213
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
96-417 |
1.86e-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: 41.96 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 96 EKLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIKFKDKIKSLEETNeiLGDTAKSLRAMLESEREQN 175
Cdd:TIGR00606 761 QRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSD--LDRTVQQVNQEKQEKQHEL 838
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 176 AK-------NQDLISENKKSIEKLKDVISVNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIKDW 248
Cdd:TIGR00606 839 DTvvskielNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFL 918
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 249 SKSHAELSEQIRSFEKSQKDLEVALT---HKDDNINALTNCITQLNRLDCESESEDQnkggseSDELANGEVGGDRSEKV 325
Cdd:TIGR00606 919 EKDQQEKEELISSKETSNKKAQDKVNdikEKVKNIHGYMKDIENKIQDGKDDYLKQK------ETELNTVNAQLEECEKH 992
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 326 KNQIKQMMDVSRTQTAISVVEEdlKLLQCKLrasmsTKCNLEDQIKKLEEDRSS------------LQSAKTVLEDECKT 393
Cdd:TIGR00606 993 QEKINEDMRLMRQDIDTQKIQE--RWLQDNL-----TLRKRENELKEVEEELKQhlkemgqmqvlqMKQEHQKLEENIDL 1065
|
330 340
....*....|....*....|....*..
gi 1387212246 394 L-RQKVEILNEL--YQQKEMALQKKLS 417
Cdd:TIGR00606 1066 IkRNHVLALGRQkgYEKEIKHFKKELR 1092
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
90-478 |
1.91e-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: 41.88 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 90 TEQQISEKLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNmilsdeaiKFKDKIKSLEETNEILGDTAKSLRAMLE 169
Cdd:TIGR00618 227 ELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIE--------ELRAQEAVLEETQERINRARKAAPLAAH 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 170 SER-EQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQE---- 244
Cdd:TIGR00618 299 IKAvTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQhtlt 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 245 --IKDWS--KSHAELSEQIRSFEKSQKDLEVALTH---------KDDNINALTNCITQLNRLD-CESESEDQNKGGSESD 310
Cdd:TIGR00618 379 qhIHTLQqqKTTLTQKLQSLCKELDILQREQATIDtrtsafrdlQGQLAHAKKQQELQQRYAElCAAAITCTAQCEKLEK 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 311 ELANGEVGGDRSEKVKNQIKQMM--DVSRTQTAISVVEEDLKLLQCKLRASMS--------------TKCNLEdqikKLE 374
Cdd:TIGR00618 459 IHLQESAQSLKEREQQLQTKEQIhlQETRKKAVVLARLLELQEEPCPLCGSCIhpnparqdidnpgpLTRRMQ----RGE 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 375 EDRSSLQSAKTVLEDECKTLRQKVEILNELYQQKEMALQKKLSQEEYERQEREQRLSAADEKAVLAAEEVKTYKRRIEEM 454
Cdd:TIGR00618 535 QTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQ 614
|
410 420
....*....|....*....|....
gi 1387212246 455 EDELQKTErsfkNQIATHEKKAHD 478
Cdd:TIGR00618 615 HALLRKLQ----PEQDLQDVRLHL 634
|
|
| KASH_CCD |
pfam14662 |
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of ... |
133-263 |
2.18e-03 |
|
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of KASH or Klarsicht/ANC-1/Syne/homology proteins. KASH are a meiosis-specific proteins that localize at telomeres and interact with SUN1, thus being implicated in meiotic chromosome dynamics and homolog pairing.
Pssm-ID: 405365 [Multi-domain] Cd Length: 191 Bit Score: 40.16 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 133 NMILSDEAIKFKDKIKSLEETNEILGDTAKSLRAMLESEREQNAKNqdliSENKKSIEKLKdvISVNASEFSEVQIALNE 212
Cdd:pfam14662 17 NQKLLQENSKLKATVETREETNAKLLEENLNLRKQAKSQQQAVQKE----KLLEEELEDLK--LIVNSLEEARRSLLAQN 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1387212246 213 AKLSEEKVK--SECHRVQEENARLKKKKEQLQQEIKDWSKSHAELSEQIRSFE 263
Cdd:pfam14662 91 KQLEKENQSllQEIESLQEENKKNQAERDKLQKKKKELLKSKACLKEQLHSCE 143
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
546-765 |
2.18e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 41.51 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 546 GPSPVSGGECSPPltadPPARPLSATLNRRemPRSEFGSVDGPLPRPRWASEASGKPSASDPESGAAPTVNSSSRSSSPS 625
Cdd:PRK07764 589 GPAPGAAGGEGPP----APASSGPPEEAAR--PAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDA 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 626 kvmdEGKVSMAAKGPPPFPGTPLMSSPVGGPLLPPIRYGPPPQLCGPFGPRPLPPPFGPGMRPPLGLREYAPGVPPGKRD 705
Cdd:PRK07764 663 ----SDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDP 738
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387212246 706 LPL--DPREFLPPGHAPFRPLGSLGPREYFFPGTRLPPPNHGPQDYPPSSAARDLPPSGSRD 765
Cdd:PRK07764 739 VPLppEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRD 800
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
93-270 |
2.53e-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: 41.03 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 93 QISEKLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIKFKDKIKSLEETNEILGDTAKSLRAMLESER 172
Cdd:pfam07888 77 ELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMK 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 173 EQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIKDWSKSH 252
Cdd:pfam07888 157 ERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALL 236
|
170
....*....|....*...
gi 1387212246 253 AELSEQIRSFEKSQKDLE 270
Cdd:pfam07888 237 EELRSLQERLNASERKVE 254
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
77-475 |
2.60e-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: 41.31 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 77 RTVLAVKSRVYQVTEQQISEKLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDeaikfkdKIKSLEetnei 156
Cdd:pfam01576 428 RAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLST-------RLRQLE----- 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 157 lgDTAKSLRAMLESEreqnaknqdliSENKKSIEKlkdvisvnasEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKK 236
Cdd:pfam01576 496 --DERNSLQEQLEEE-----------EEAKRNVER----------QLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQR 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 237 KKEQLQQEIKDWSKSHAELSEQIRSFEKSQKDLEVALTHKDDNINALTNCITQLNRLDCEsESEDQNKGGSESDElANGE 316
Cdd:pfam01576 553 ELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAE-EKAISARYAEERDR-AEAE 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 317 VggdrSEKVKNQIKQMMDVSRTQTAISVVEEDLKLLQCKLRASMSTKcnlEDQIKKLEEdrssLQSAKTVLEDECKTLRQ 396
Cdd:pfam01576 631 A----REKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSK---DDVGKNVHE----LERSKRALEQQVEEMKT 699
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387212246 397 KVEILNELYQQKEMALQKKLSQEEYERQEREQRLSAADEKavlAAEEVKTYKRRIEEMEDELQKtERSFKNQIATHEKK 475
Cdd:pfam01576 700 QLEELEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQ---GEEKRRQLVKQVRELEAELED-ERKQRAQAVAAKKK 774
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
217-482 |
2.70e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 41.24 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 217 EEKVKSECHRVQEENARLKKKKEQLQQEikdWSKSHAELSEQIRSFEKSQKDLEVALTHKDDNINALTNCITQlNRLDCE 296
Cdd:pfam03528 3 DEDLQQRVAELEKENAEFYRLKQQLEAE---FNQKRAKFKELYLAKEEDLKRQNAVLQEAQVELDALQNQLAL-ARAEME 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 297 S-------------ESEDQNKGGSESDELANGEVGGDRSEKVKNQIKQMMDVSRTQTAISVVEEDLKLLQCKLRASMSTK 363
Cdd:pfam03528 79 NikavatvsentkqEAIDEVKSQWQEEVASLQAIMKETVREYEVQFHRRLEQERAQWNQYRESAEREIADLRRRLSEGQE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 364 -CNLEDQIKKLEEDRSSLQSAKTVLEDECKTLRQKV----EILNELYQQKEMALQKKLSQEEYERQEREQRLSAADEKAV 438
Cdd:pfam03528 159 eENLEDEMKKAQEDAEKLRSVVMPMEKEIAALKAKLteaeDKIKELEASKMKELNHYLEAEKSCRTDLEMYVAVLNTQKS 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1387212246 439 LAAEEVKTYKRRIEEMEDELQKtERSFKNQIATHEKKAHDNWLK 482
Cdd:pfam03528 239 VLQEDAEKLRKELHEVCHLLEQ-ERQQHNQLKHTWQKANDQFLE 281
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
253-517 |
3.17e-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: 41.21 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 253 AELSEQIRSFEKSQKDLEVALTHKDDNINALTNCITQLNRLDCESESEdqnkggsesdelanGEVGGDRSEKVKNQIKQM 332
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKE--------------IEQLEQEEEKLKERLEEL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 333 M-DVSRTQTAISVVEEDLKLLQCKLRASMSTKCNLEDQIKKLE--EDRSSLQSAKTVLEDECKTLRQKVEILNELyQQKE 409
Cdd:TIGR02169 743 EeDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEarLSHSRIPEIQAELSKLEEEVSRIEARLREI-EQKL 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 410 MALQKKLSQEEYERQEREQRLSAADEKAVLAAEEVKTYKRRIEEMEDELQKTERSFKNQIATH-----EKKAHDNWLKAR 484
Cdd:TIGR02169 822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLgdlkkERDELEAQLREL 901
|
250 260 270
....*....|....*....|....*....|...
gi 1387212246 485 AAERAIAEEKREaaNLRHKLLELTQKMAMMQEE 517
Cdd:TIGR02169 902 ERKIEELEAQIE--KKRKRLSELKAKLEALEEE 932
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
77-244 |
3.94e-03 |
|
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: 40.18 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 77 RTVLAVKSRVYQVTEQQISEKLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNMilsdeaikfkdkiKSLEETNEI 156
Cdd:pfam15905 165 RNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETE-------------KLLEYITEL 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 157 lgdtaKSLRAMLESEREQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNEA-----KLSEEKVKSECHRVQEEN 231
Cdd:pfam15905 232 -----SCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKcklleSEKEELLREYEEKEQTLN 306
|
170
....*....|...
gi 1387212246 232 ARLKKKKEQLQQE 244
Cdd:pfam15905 307 AELEELKEKLTLE 319
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
93-255 |
3.97e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 40.68 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 93 QISEKLKNIMKENaELVQKLSSYEQKIK-----ESKKHVQETKKQNMILSDEAIKFKDKIKSLEETNEILGDTAKSLRAM 167
Cdd:PRK05771 44 RLRKLRSLLTKLS-EALDKLRSYLPKLNplreeKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 168 LE----------------------------SEREQNAKNQDLISENKKSIEKLKD---VISVNASEFSEVQIAL------ 210
Cdd:PRK05771 123 IErlepwgnfdldlslllgfkyvsvfvgtvPEDKLEELKLESDVENVEYISTDKGyvyVVVVVLKELSDEVEEElkklgf 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1387212246 211 NEAKLSEEKVKSE-CHRVQEENARLKKKKEQLQQEIKDWSKSHAEL 255
Cdd:PRK05771 203 ERLELEEEGTPSElIREIKEELEEIEKERESLLEELKELAKKYLEE 248
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
99-480 |
4.22e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.66 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 99 KNIMKENAELVqkLSSYEQKIKESKKHVQETKKQNMILSDEAIKfkdkIKSLEETNEILGDTAKSLRAM---LESEREQN 175
Cdd:PRK01156 119 KNILGISKDVF--LNSIFVGQGEMDSLISGDPAQRKKILDEILE----INSLERNYDKLKDVIDMLRAEisnIDYLEEKL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 176 AKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNEAKLSEEKVKSECHRV--QEE-----NARLKKKKEQLQQE---- 244
Cdd:PRK01156 193 KSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELssLEDmknryESEIKTAESDLSMElekn 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 245 --IKDWSKSHAELS--------EQIRSFEKSQKDLE---VALTHKDDNINALTNCITQLNRLdcESESEDQNKGGSESDE 311
Cdd:PRK01156 273 nyYKELEERHMKIIndpvyknrNYINDYFKYKNDIEnkkQILSNIDAEINKYHAIIKKLSVL--QKDYNDYIKKKSRYDD 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 312 LAN--GEVGGDRSE------KVKNQIKQMMDVSRTQTAISV-VEEDLKLLQCKLRASMSTKCNLEDQIKKLEEDRSSLQS 382
Cdd:PRK01156 351 LNNqiLELEGYEMDynsylkSIESLKKKIEEYSKNIERMSAfISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQ 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 383 AKTVLEDECKTLRQKVEILN----------ELYQQKEMALQK----KLSQEEYERQEREQRLSAADEKAV--------LA 440
Cdd:PRK01156 431 RIRALRENLDELSRNMEMLNgqsvcpvcgtTLGEEKSNHIINhyneKKSRLEEKIREIEIEVKDIDEKIVdlkkrkeyLE 510
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1387212246 441 AEEVK---TYKRRIEEMEDELQKtersFKNQIATHeKKAHDNW 480
Cdd:PRK01156 511 SEEINksiNEYNKIESARADLED----IKIKINEL-KDKHDKY 548
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
85-512 |
4.73e-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: 40.80 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 85 RVYQVTEQQISEKLKNIMKENAELVQKLSSYEQKI-----KESKKHVQETKKQNMILSDEAIKFKDKIKSLEETNEILGD 159
Cdd:TIGR00606 315 REKERELVDCQRELEKLNKERRLLNQEKTELLVEQgrlqlQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKN 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 160 TAKSLRAMLESEREQNAKNQDLISENKKSIEKLKDVISVNASEFSEVqIALNEAKLSEEK-----VKSECHRVQEENARL 234
Cdd:TIGR00606 395 FHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRT-IELKKEILEKKQeelkfVIKELQQLEGSSDRI 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 235 KKKKEQLQQEIKDWSKSHAE-----LSEQIRSFEKSQKDLE---VALTHKDDNINALTNCITQLNRLDCESESEDQ---N 303
Cdd:TIGR00606 474 LELDQELRKAERELSKAEKNsltetLKKEVKSLQNEKADLDrklRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEqirK 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 304 KGGSESDELA-------NGEVGGDRSEKVKNQIKQMmdvsrtqtaisvvEEDLKLLQCKLRASMSTKCNLEDQIKKLEED 376
Cdd:TIGR00606 554 IKSRHSDELTsllgyfpNKKQLEDWLHSKSKEINQT-------------RDRLAKLNKELASLEQNKNHINNELESKEEQ 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 377 RSSLqSAKTVLEDECKTLRQKVEILNELYQQ--KEMALqkkLSQEEYERQEREQRLSAADEKAVLAAEEVKTYKRRIEEM 454
Cdd:TIGR00606 621 LSSY-EDKLFDVCGSQDEESDLERLKEEIEKssKQRAM---LAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEF 696
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387212246 455 EDELQKTERSF-------KNQIATHEKKAHDNWLKARAAERAIAEEKREAANLRHKLLELTQKMA 512
Cdd:TIGR00606 697 ISDLQSKLRLApdklkstESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQ 761
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
523-786 |
4.95e-03 |
|
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: 40.52 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 523 PMPGRPNTQNPPRRGPLSQNGSFGPSPVSGGECSP---PLTADPPARPLSATLNRREMPRSEFGSVDGPLPRPRWASEAS 599
Cdd:pfam03154 243 PSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPmphSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQ 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 600 GKPSASDPESGAAPtvnsssRSSSPSKVMDEGKVSMAAKGPPPFPGTPLMSSPVG----------GPLLPPIRYGPPPQL 669
Cdd:pfam03154 323 QRIHTPPSQSQLQS------QQPPREQPLPPAPLSMPHIKPPPTTPIPQLPNPQShkhpphlsgpSPFQMNSNLPPPPAL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 670 cgPFGPRPLPPPFGPGMRPPLGLREYAPGVPPGKRDLP-LDPREFLPPGHAPFRPLGSL--GPREYFFPgTRLPPPNHGP 746
Cdd:pfam03154 397 --KPLSSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQPPvLTQSQSLPPPAASHPPTSGLhqVPSQSPFP-QHPFVPGGPP 473
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1387212246 747 QDYPPSSAARDLPPSGSRDEPPPASQGASQDCSPALKQSP 786
Cdd:pfam03154 474 PITPPSGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVSCP 513
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
149-239 |
4.96e-03 |
|
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.
Pssm-ID: 439196 [Multi-domain] Cd Length: 91 Bit Score: 36.77 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 149 SLEETNEILGDTAKSLRAMLESEREQNAKNQDLISENKKSIEKLKDvisvnasEFSEVQIALNeakLSEEKVKsechRVQ 228
Cdd:cd22887 1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILND-------ELIALQIENN---LLEEKLR----KLQ 66
|
90
....*....|....*..
gi 1387212246 229 EENARL------KKKKE 239
Cdd:cd22887 67 EENDELverwmaKKQQE 83
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
87-273 |
4.98e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.20 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 87 YQVTE------QQISEKLKNIMKENAELVQKL-------SSYEQKIKESKKHVQETKKQNMilsdeaiKFKDKIKSLEET 153
Cdd:PRK04778 340 YTLNEselesvRQLEKQLESLEKQYDEITERIaeqeiaySELQEELEEILKQLEEIEKEQE-------KLSEMLQGLRKD 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 154 neilgdtakslramlESEREQNAKN-QDLISENKKSIEKL---------KDVISVNASEFSEVQIALNEAKLSEEKVKSE 223
Cdd:PRK04778 413 ---------------ELEAREKLERyRNKLHEIKRYLEKSnlpglpedyLEMFFEVSDEIEALAEELEEKPINMEAVNRL 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1387212246 224 CHRVQEENARLKKKKEQLQQeikdwsksHAELSEQI-------RSFEKS-QKDLEVAL 273
Cdd:PRK04778 478 LEEATEDVETLEEETEELVE--------NATLTEQLiqyanryRSDNEEvAEALNEAE 527
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
93-270 |
6.40e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.51 E-value: 6.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 93 QISEKLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIKFKDKIK------------------------ 148
Cdd:COG1340 47 ELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAelnkaggsidklrkeierlewrqq 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 149 ----SLEETNEILgDTAKSLRAMLESEREQNAKNQDlISENKKSIEKLKDVISVNASEFSEVQIALNEAKLSEEKVKSEC 224
Cdd:COG1340 127 tevlSPEEEKELV-EKIKELEKELEKAKKALEKNEK-LKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEA 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1387212246 225 HRVQEENARLKKKKEQLQQEIKDWSKSHAELSEQIRSFEKSQKDLE 270
Cdd:COG1340 205 DELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLR 250
|
|
| FtsB |
COG2919 |
Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning]; |
226-261 |
6.57e-03 |
|
Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442163 [Multi-domain] Cd Length: 96 Bit Score: 36.78 E-value: 6.57e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1387212246 226 RVQEENARLKKKKEQLQQEIKDWSKSHAELSEQIRS 261
Cdd:COG2919 40 ELEAENAKLKARNAELEAEVADLKDGPDYIEERARE 75
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
106-270 |
6.75e-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: 39.14 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 106 AELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIKFKDKIKSLEEtnEIlgdtaKSLRAMLESEREQNAKNQDLISEN 185
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEK--EI-----KRLELEIEEVEARIKKYEEQLGNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 186 KKSIEkLKDVISvnasefsEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIKDWSKSHAELSEQIRSFEKS 265
Cdd:COG1579 86 RNNKE-YEALQK-------EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
....*
gi 1387212246 266 QKDLE 270
Cdd:COG1579 158 LEELE 162
|
|
| mS26_Tt |
cd23695 |
Tetrahymena thermophila ribosomal protein mS26 and similar proteins; Ribosomal protein mS26 is ... |
87-352 |
6.95e-03 |
|
Tetrahymena thermophila ribosomal protein mS26 and similar proteins; Ribosomal protein mS26 is a component of small subunit (SSU) in Tetrahymena thermophila mitochondrial ribosome (mitoribosome). The structure of the mitoribosome reveals an assembly of 94-ribosomal proteins and four-rRNAs with an additional protein mass of ~700 kDa on the small subunit; the large mitoribosomal subunit (LSU) lacks 5S rRNA.
Pssm-ID: 467909 [Multi-domain] Cd Length: 496 Bit Score: 39.81 E-value: 6.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 87 YQVTEQQISEKLKNIMKENAELVQKLS--------SYEQKIKESKKHVQETKKQNMILSDEAIKFKDKIKSLEETNEILG 158
Cdd:cd23695 200 YQDAKAIIIEDFRESSEEGAEKLEKLEkafatllkNYKEELEEPEKQLEFMQKRLLDLYNLLRLWGQYITIVKMPDSVVR 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 159 DTAKSLRAMLE---SEREQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNEAKLSEEKVksechrvqeenarlK 235
Cdd:cd23695 280 DIMNKTQARPEvakLNSKQELEDAKNRKRDTEENEFDDDYESADEGETSDEEDEIEEENFQLQKE--------------K 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 236 KKKEQLQQEIKDWSKSHAELSEQIRSFEKSQKDLEVALTHKDDNINALTNCITQLNRLDCESESEDQNKGG---SESDEL 312
Cdd:cd23695 346 KKEEELNAEFNIAKNSLYKFSPQNDKNVVDDRDFYSGVDLENVFPRALLNNLNDFTGLDFQNVKEILNNEEklkIIQGED 425
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1387212246 313 ANGEVGGDRSEK----------VKNQIKQMMDVSRTQTAISVVEEDLKLL 352
Cdd:cd23695 426 DQNDQEDFNNPRkfqtslivqtYKQKINNLDAESLTRATQEKKNDIQKLL 475
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
159-395 |
7.29e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 7.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 159 DTAKSLRAMLESEREQ-------NAKNQDLIsENKKSIEKLKDVISVNASEFSEVQIALNEAKLSEEkvksechrvQEEN 231
Cdd:COG4913 235 DDLERAHEALEDAREQiellepiRELAERYA-AARERLAELEYLRAALRLWFAQRRLELLEAELEEL---------RAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 232 ARLKKKKEQLQQEIKDWSKSHAELSEQIRSfeksqkdlevaltHKDDNINALTNCITQLNRldcesESEDQNKGGSESDE 311
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQIRG-------------NGGDRLEQLEREIERLER-----ELEERERRRARLEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 312 LANG---EVGGDRSEKVKNQikqmmdvSRTQTAISVVEEDLKLLQCKLRASMSTKCNLEDQIKKLEEDRSSLQSAKTVLE 388
Cdd:COG4913 367 LLAAlglPLPASAEEFAALR-------AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIP 439
|
....*..
gi 1387212246 389 DECKTLR 395
Cdd:COG4913 440 ARLLALR 446
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
109-524 |
7.35e-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: 40.03 E-value: 7.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 109 VQKLSSYEQKIKESKKHVQETKKQNMIL---SDEAIKFKDKIKSLEETNEILGDTAKSLramlESEREQNAKNQDLISEN 185
Cdd:TIGR00606 185 IKALETLRQVRQTQGQKVQEHQMELKYLkqyKEKACEIRDQITSKEAQLESSREIVKSY----ENELDPLKNRLKEIEHN 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 186 KKSIEKLKDVISvnasefsevqiALNEAKLSEEKVKSECHRVQEE-----NARLKKKKEQLQQEIKDWSKSHAELSEQIr 260
Cdd:TIGR00606 261 LSKIMKLDNEIK-----------ALKSRKKQMEKDNSELELKMEKvfqgtDEQLNDLYHNHQRTVREKERELVDCQREL- 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 261 sfEKSQKDLEVALTHKDDNINALTNCITQLNRLDCESESED----QNKGGSESDELangEVGGDRSEKVKNqikqmmdvs 336
Cdd:TIGR00606 329 --EKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDsliqSLATRLELDGF---ERGPFSERQIKN--------- 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 337 rtqtAISVVEEdlkllqcklrasmstkcNLEDQIKKLEEDRSSLQSAKTVLEDECKTLRQKVEILNELYQQKEMALQKKL 416
Cdd:TIGR00606 395 ----FHTLVIE-----------------RQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQ 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 417 SQEEYERQEREQRLSAADekavlaaeevktykrRIEEMEDELQKTERsfknQIATHEKKAHDNWLKaraaeRAIAEEKRE 496
Cdd:TIGR00606 454 EELKFVIKELQQLEGSSD---------------RILELDQELRKAER----ELSKAEKNSLTETLK-----KEVKSLQNE 509
|
410 420
....*....|....*....|....*...
gi 1387212246 497 AANLRHKLLELTQKMAMMQEEPVIVKPM 524
Cdd:TIGR00606 510 KADLDRKLRKLDQEMEQLNHHTTTRTQM 537
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
103-264 |
7.37e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.12 E-value: 7.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 103 KENaELVQKLSSYEQKIKESKKhvqetkkqnmilsdeAIKFKDKIKSLEETNEILGDTAKSLRAMLESEREQNAKNQDLI 182
Cdd:COG1340 134 EEK-ELVEKIKELEKELEKAKK---------------ALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEM 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 183 SENKKSIEKLKDVISVNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEI--KDWSKSHAELSEQIR 260
Cdd:COG1340 198 IELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKekEELEEKAEEIFEKLK 277
|
....
gi 1387212246 261 SFEK 264
Cdd:COG1340 278 KGEK 281
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
87-486 |
7.86e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 39.81 E-value: 7.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 87 YQVTEQQISEKLKNIMKENAELVQKLssyeqkIKESKKHVQETKKQNMILSDEAikfKDKIKSLEETNEIlgdtakslra 166
Cdd:PTZ00440 1007 YNILNKKIDDLIKKQHDDIIELIDKL------IKEKGKEIEEKVDQYISLLEKM---KTKLSSFHFNIDI---------- 1067
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 167 mlesEREQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNEAKLSEEKVKsechrvQEENARLKKKKEQLQQEIK 246
Cdd:PTZ00440 1068 ----KKYKNPKIKEEIKLLEEKVEALLKKIDENKNKLIEIKNKSHEHVVNADKEK------NKQTEHYNKKKKSLEKIYK 1137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 247 DWSKSHAELS----EQIRSFEKSQKDLEVALTHKDDNINALTNCITQLNRLDCESES-------EDQNKGGSESDELANG 315
Cdd:PTZ00440 1138 QMEKTLKELEnmnlEDITLNEVNEIEIEYERILIDHIVEQINNEAKKSKTIMEEIESykkdidqVKKNMSKERNDHLTTF 1217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 316 EVGG--DRSEKVKNQIKQMMDVSRTQTAISVVEEDLKLLQCKLRASMSTKCNLEDQIKKLEEDRSSLQSAKTVLEDEcKT 393
Cdd:PTZ00440 1218 EYNAyyDKATASYENIEELTTEAKGLKGEANRSTNVDELKEIKLQVFSYLQQVIKENNKMENALHEIKNMYEFLISI-DS 1296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 394 LRQKVEILNELYQQKEMALQ--KKLSQEEYERQEREQRLSAADE--KAVLAAEE---VKTYKRRIEEMEDELQKTERSFK 466
Cdd:PTZ00440 1297 EKILKEILNSTKKAEEFSNDakKELEKTDNLIKQVEAKIEQAKEhkNKIYGSLEdkqIDDEIKKIEQIKEEISNKRKEIN 1376
|
410 420
....*....|....*....|
gi 1387212246 467 NQIATHEKKAHDNWLKARAA 486
Cdd:PTZ00440 1377 KYLSNIKSNKEKCDLHVRNA 1396
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
103-275 |
8.15e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 39.66 E-value: 8.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 103 KENAELVQKLSSYEQKIkESKKHVQETKKQNMILSD-EAIKFKDKIKSLEETNEILGDTAKSLRAMLESEREQNAKN--- 178
Cdd:pfam13166 279 DEFTEFQNRLQKLIEKV-ESAISSLLAQLPAVSDLAsLLSAFELDVEDIESEAEVLNSQLDGLRRALEAKRKDPFKSiel 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212246 179 ---QDLISENKKSIEKLKDVISVN---ASEF-SEVQIALNEAKLSE-EKVKSECHRVQEENARLKKKKEQLQQEIKDWS- 249
Cdd:pfam13166 358 dsvDAKIESINDLVASINELIAKHneiTDNFeEEKNKAKKKLRLHLvEEFKSEIDEYKDKYAGLEKAINSLEKEIKNLEa 437
|
170 180 190
....*....|....*....|....*....|..
gi 1387212246 250 ------KSHAELSEQIRSFEKSQKDLEVALTH 275
Cdd:pfam13166 438 eikklrEEIKELEAQLRDHKPGADEINKLLKA 469
|
|
| |
