|
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 |
2.79e-16 |
|
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: 83.15 E-value: 2.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 90 TEQQISEKLKTIMKENTELVQKLSNYEQKIK----ESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEilDDTAKNLR 165
Cdd:TIGR04523 236 KKQQEINEKTTEISNTQTQLNQLKDEQNKIKkqlsEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKE--QDWNKELK 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 166 VMLESEREQNVKNQDLISENKKSIEKLKDVIS------MNA-SEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKK 238
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQISQNNKIISQLNEQISqlkkelTNSeSENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 239 EQLQQEIEDWSKLHAELSEQIKSF-------EKSQKDLEVALTHKDDNINALTNCITQLNLL--ECESESEGQNKG---- 305
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLqqekellEKEIERLKETIIKNNSEIKDLTNQDSVKELIikNLDNTRESLETQlkvl 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 306 ----GNDSDELANGEVGGDRNEKMKNQIKQmmDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQVKKLEDDRNSLQ 381
Cdd:TIGR04523 474 srsiNKIKQNLEQKQKELKSKEKELKKLNE--EKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDD 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 382 A--AKAGLEDECKTLRQKVEIL---NELYQQKEMALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYK---RRIEE 453
Cdd:TIGR04523 552 FelKKENLEKEIDEKNKEIEELkqtQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKkenEKLSS 631
|
410
....*....|....*.
gi 664806007 454 MEDELQKTERSFKNQI 469
Cdd:TIGR04523 632 IIKNIKSKKNKLKQEV 647
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
95-404 |
1.12e-15 |
|
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: 81.65 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 95 SEKLKTIMKENTELVQKLSNYEQKIKESKKHVQEtrkqnmiLSDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLES-ERE 173
Cdd:TIGR02169 715 SRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS-------LEQEIENVKSELKELEARIEELEEDLHKLEEALNDlEAR 787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 174 QNvknQDLISENKKSIEKLKDVISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIEDWSKLHA 253
Cdd:TIGR02169 788 LS---HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE 864
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 254 ELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNLLECESESEGQNKGGNDSDELANGEVGGDRNEKMKNQIKQMM 333
Cdd:TIGR02169 865 ELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 664806007 334 DVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNEL 404
Cdd:TIGR02169 945 EIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
98-478 |
2.28e-13 |
|
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: 74.33 E-value: 2.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 98 LKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLESEREQNVK 177
Cdd:TIGR02169 690 LSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEE 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 178 NQDLISENKKSIEKLKDVISMnasefSEVQIALNEAKLSEEKVKSECHRVQEENARLKK---KKEQLQQEIEDWSKLHAE 254
Cdd:TIGR02169 770 LEEDLHKLEEALNDLEARLSH-----SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRltlEKEYLEKEIQELQEQRID 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 255 LSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLnllecesesegqnkggndSDELanGEVGGDRnEKMKNQIKQMMD 334
Cdd:TIGR02169 845 LKEQIKSIEKEIENLNGKKEELEEELEELEAALRDL------------------ESRL--GDLKKER-DELEAQLRELER 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 335 vSRTQTAISVVEEDLKLLQLKLRASvstkcNLEDQVKKLEDdrnslqAAKAGLEDECKTLrqkveILNELYQQKEMALQk 414
Cdd:TIGR02169 904 -KIEELEAQIEKKRKRLSELKAKLE-----ALEEELSEIED------PKGEDEEIPEEEL-----SLEDVQAELQRVEE- 965
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 664806007 415 klsqeeyerqerehRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTE---RSFKNQIATHEKKAHE 478
Cdd:TIGR02169 966 --------------EIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEeerKAILERIEEYEKKKRE 1018
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
88-399 |
3.54e-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: 73.55 E-value: 3.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 88 QVTEQQisEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRVM 167
Cdd:TIGR02168 685 KIEELE--EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 168 LESEREQNVKNQDLISENKKSIEKLKDVISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIED 247
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 248 WSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNLLECESESEGQNKggndSDELANGEvggDRNEKMKN 327
Cdd:TIGR02168 843 LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL----SEELRELE---SKRSELRR 915
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 664806007 328 QIKQMMD-VSRTQTAISVVEEDLKLLQLKLRASVSTkcNLEDQVKKLEDDRNSLQAAkaglEDECKTLRQKVE 399
Cdd:TIGR02168 916 ELEELREkLAQLELRLEGLEVRIDNLQERLSEEYSL--TLEEAEALENKIEDDEEEA----RRRLKRLENKIK 982
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
184-459 |
2.16e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.86 E-value: 2.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 184 ENKKSIEKLKDVISMNASEFSEVQIALNEAKlseekvksechrvqEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFE 263
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELR--------------KELEELEEELEQLRKELEELSRQISALRKDLARLE 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 264 KSQKDLEVALTHKDDNINALTNCITQlnLLECESESEGQNKGGNDSDELANGEVGGDRNEkMKNQIKQM----MDVSRTQ 339
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTELEAEIEE--LEERLEEAEEELAEAEAEIEELEAQIEQLKEE-LKALREALdelrAELTLLN 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 340 TAISVVEEDLKLLQLKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQKE---MALQKKL 416
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEealALLRSEL 896
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 664806007 417 SQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQ 459
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
110-455 |
2.46e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.86 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 110 QKLSNYEQKIKESKKHVQETRKQnmilsdeaikykdkIKTLEKNQEILDDTAKNLRVMLESEREQnvknqdlISENKKSI 189
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKA--------------LAELRKELEELEEELEQLRKELEELSRQ-------ISALRKDL 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 190 EKLKDVISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDL 269
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 270 EVALThkdDNINALTNCITQLNLLECESE-SEGQNKGGNDSDELANGEVG--GDRNEKMKNQIKQMMDvsrtqtAISVVE 346
Cdd:TIGR02168 816 NEEAA---NLRERLESLERRIAATERRLEdLEEQIEELSEDIESLAAEIEelEELIEELESELEALLN------ERASLE 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 347 EDLKLLQLKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKV----EILNELYQQKEMALQKKLSQEEYE 422
Cdd:TIGR02168 887 EALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIdnlqERLSEEYSLTLEEAEALENKIEDD 966
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 664806007 423 RQEREHRLSAADEK-----AV--SAAEEVKTYKRRIEEME 455
Cdd:TIGR02168 967 EEEARRRLKRLENKikelgPVnlAAIEEYEELKERYDFLT 1006
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
91-407 |
3.53e-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: 70.05 E-value: 3.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 91 EQQISEK---LKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILsdeaikyKDKIKTLEKNQEILDDTAKNLRvm 167
Cdd:TIGR04523 362 QRELEEKqneIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQK-------DEQIKKLQQEKELLEKEIERLK-- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 168 leserEQNVKNQDLISENKKSIEKLKdvismnasefsevqIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIED 247
Cdd:TIGR04523 433 -----ETIIKNNSEIKDLTNQDSVKE--------------LIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKS 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 248 WSKLHAELSEQIKSFEKSQKDLEvalthkdDNINALTNCITQLNLLECESESE---GQNKGGNDSDELANGEVGGDRNEK 324
Cdd:TIGR04523 494 KEKELKKLNEEKKELEEKVKDLT-------KKISSLKEKIEKLESEKKEKESKisdLEDELNKDDFELKKENLEKEIDEK 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 325 MKNqIKQMmdvSRTQTAISVVEEDLKLL-------QLKLRASVSTKcnlEDQVKKLEDDRNSLQAAKAGLEDECKTLRQK 397
Cdd:TIGR04523 567 NKE-IEEL---KQTQKSLKKKQEEKQELidqkekeKKDLIKEIEEK---EKKISSLEKELEKAKKENEKLSSIIKNIKSK 639
|
330
....*....|
gi 664806007 398 VEILNELYQQ 407
Cdd:TIGR04523 640 KNKLKQEVKQ 649
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
96-414 |
7.83e-12 |
|
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: 69.23 E-value: 7.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 96 EKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRK---------------QNMILSDEAIKYKDKIKTLEKNQEILDDT 160
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELKLKEQAKKaleyyqlkekleleeEYLLYLDYLKLNEERIDLLQELLRDEQEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 161 AKNLRVMLESEREQNVKNQDLISENKKSIEKLKDVISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQ 240
Cdd:pfam02463 253 IESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 241 LQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKddniNALTNCITQLNLLECESESEGQnKGGNDSDELANGEVGGD 320
Cdd:pfam02463 333 EKEEIEELEKELKELEIKREAEEEEEEELEKLQEKL----EQLEEELLAKKKLESERLSSAA-KLKEEELELKSEEEKEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 321 RNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEI 400
Cdd:pfam02463 408 QLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLE 487
|
330
....*....|....
gi 664806007 401 LNELYQQKEMALQK 414
Cdd:pfam02463 488 LLLSRQKLEERSQK 501
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
140-470 |
1.78e-11 |
|
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: 68.16 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 140 AIKYKDKIKTLEKNQEILDDTAKNLRVMLESEREQNvknqdliSENKKSIEKLKDVISMNASEFSEVQIALNEAKLSEEK 219
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRKEL-------EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 220 VKSECHRVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNlleceses 299
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN-------- 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 300 egqnkggndsDELANGEVGGDRNEKMKNQIKQMMDvsRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQVKKLEDDRNS 379
Cdd:TIGR02168 817 ----------EEAANLRERLESLERRIAATERRLE--DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 380 LQAAKAGLEDECKTLRQKVEILN----ELYQQKEmALQKKLSQEEYERQEREHRL----SAADEKAVSAAEEVKTYKRRI 451
Cdd:TIGR02168 885 LEEALALLRSELEELSEELRELEskrsELRRELE-ELREKLAQLELRLEGLEVRIdnlqERLSEEYSLTLEEAEALENKI 963
|
330
....*....|....*....
gi 664806007 452 EEMEDELQKTERSFKNQIA 470
Cdd:TIGR02168 964 EDDEEEARRRLKRLENKIK 982
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
91-517 |
2.97e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 66.71 E-value: 2.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 91 EQQISEkLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILsDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLES 170
Cdd:COG4717 77 EEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKLLQLLPLYQELEALEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 171 EREqnvknqdlISENKKSIEKLKDVISMNASEFSEVQIALNEAKLSEEKvksechRVQEENARLKKKKEQLQQEIEDWSK 250
Cdd:COG4717 155 LEE--------LRELEEELEELEAELAELQEELEELLEQLSLATEEELQ------DLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 251 LHAELSEQIKSFEKSQKDLE------------------VALTHKDDNINALTNCIT-------QLNLLECESESEGQNKG 305
Cdd:COG4717 221 ELEELEEELEQLENELEAAAleerlkearlllliaaalLALLGLGGSLLSLILTIAgvlflvlGLLALLFLLLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 306 GNDSDELANGEVGGDRNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQVKKLEDDRNSLqAAKA 385
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL-LAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 386 GLEDEcKTLRQKVEILNElYQQKEMALQKKLSQEEYERQEREHRLSAADEKAVsaAEEVKTYKRRIEEMEDE---LQKTE 462
Cdd:COG4717 380 GVEDE-EELRAALEQAEE-YQELKEELEELEEQLEELLGELEELLEALDEEEL--EEELEELEEELEELEEEleeLREEL 455
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 664806007 463 RSFKNQIATHEKkahenwlkaraaeraiaeeKREAANLRHKLLELTQKMAMLQEE 517
Cdd:COG4717 456 AELEAELEQLEE-------------------DGELAELLQELEELKAELRELAEE 491
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
92-507 |
5.80e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.24 E-value: 5.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 92 QQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAK---NLRVML 168
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEeieELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 169 ESeREQNVKN--------QDLISENKKSIEKLKDvismNASEFSEVQ-IALNEAKLSE--EKVKSECHRVQEENARLKKK 237
Cdd:PRK03918 248 ES-LEGSKRKleekirelEERIEELKKEIEELEE----KVKELKELKeKAEEYIKLSEfyEEYLDELREIEKRLSRLEEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 238 KEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEV---------ALTHKDDNINALTNCITQLNLLECESESEGQNKGGND 308
Cdd:PRK03918 323 INGIEERIKELEEKEERLEELKKKLKELEKRLEEleerhelyeEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 309 SDELANgEVGGDRNEkMKNQIKQMMD-VSRTQTAISVV--------EEDLKLLQLKLRASVStkcNLEDQVKKLEDDRNS 379
Cdd:PRK03918 403 IEEEIS-KITARIGE-LKKEIKELKKaIEELKKAKGKCpvcgreltEEHRKELLEEYTAELK---RIEKELKEIEEKERK 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 380 LQAAKAGLEDECKTLRqKVEILNELYQQKEmALQKKLSQEEYErqerehRLSAADEKAVSAAEEVKTYKRRIEEMEDELQ 459
Cdd:PRK03918 478 LRKELRELEKVLKKES-ELIKLKELAEQLK-ELEEKLKKYNLE------ELEKKAEEYEKLKEKLIKLKGEIKSLKKELE 549
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 664806007 460 KTErSFKNQIATHEKKAHEnwlkaraaeraiaeEKREAANLRHKLLEL 507
Cdd:PRK03918 550 KLE-ELKKKLAELEKKLDE--------------LEEELAELLKELEEL 582
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
91-517 |
1.14e-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: 65.04 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 91 EQQISEKLKTIMKE--NTELVQK-----LSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKN 163
Cdd:TIGR04523 35 EKQLEKKLKTIKNElkNKEKELKnldknLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 164 lrvmlesEREQNVKNQDLISENKKSIEKLKDVISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQ 243
Cdd:TIGR04523 115 -------DKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 244 EIED-----------------WSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCI----TQLN----------- 291
Cdd:TIGR04523 188 NIDKiknkllklelllsnlkkKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEIsntqTQLNqlkdeqnkikk 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 292 -LLECESESEGQNKGGND-SDELA---------NGEVGGDRNEKMKNQIKQM--------MDVSRTQTAISVVEEDLKLL 352
Cdd:TIGR04523 268 qLSEKQKELEQNNKKIKElEKQLNqlkseisdlNNQKEQDWNKELKSELKNQekkleeiqNQISQNNKIISQLNEQISQL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 353 QLKLRASVSTKCNL-------EDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQKEMALqKKLSQEEYERQE 425
Cdd:TIGR04523 348 KKELTNSESENSEKqreleekQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI-KKLQQEKELLEK 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 426 REHRLSAADEKAVSAAEE-----------VKTYKRRIEEMEDELQKTERSFKNQIATHEKKAHENWLKaraaERAIAEEK 494
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDltnqdsvkeliIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSK----EKELKKLN 502
|
490 500
....*....|....*....|...
gi 664806007 495 REAANLRHKLLELTQKMAMLQEE 517
Cdd:TIGR04523 503 EEKKELEEKVKDLTKKISSLKEK 525
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
119-462 |
2.65e-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: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 119 IKESKKHVQETRKQnmilSDEAIKYKDKiktleKNQeiLDDTAKNLRVM-LESEREQNVKNQDLISENKKSIEKLKDVIS 197
Cdd:TIGR02168 195 LNELERQLKSLERQ----AEKAERYKEL-----KAE--LRELELALLVLrLEELREELEELQEELKEAEEELEELTAELQ 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 198 MNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKD 277
Cdd:TIGR02168 264 ELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 278 DNINALTNCITQLNLLECESESEGQNkggndsdelangevggdRNEKMKNQIKQMMDVSRtqtAISVVEEDLKLLQLKLR 357
Cdd:TIGR02168 344 EKLEELKEELESLEAELEELEAELEE-----------------LESRLEELEEQLETLRS---KVAQLELQIASLNNEIE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 358 asvstkcNLEDQVKKLEDDRNSLQAAKAGLEDEcKTLRQKVEILNELYQQKEMA--LQKKLSQEEYERQEREHRLSAADE 435
Cdd:TIGR02168 404 -------RLEARLERLEDRRERLQQEIEELLKK-LEEAELKELQAELEELEEELeeLQEELERLEEALEELREELEEAEQ 475
|
330 340
....*....|....*....|....*..
gi 664806007 436 KAVSAAEEVKTYKRRIEEMEDELQKTE 462
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLERLQENLE 502
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
94-478 |
1.25e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.00 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 94 ISEKLKTIMKENTELVQKLSNYEQKIKESKKhVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLEsERE 173
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELEEKVKELKE-LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-ELE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 174 QNVKNQDLISENKKSIEKLKDVISMNASEFSEVQIALNEA-KLSEEKVKSECHRVQEENARLKKKKEQLQQEIEDWSKLH 252
Cdd:PRK03918 335 EKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELeRLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARI 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 253 AELSEQIKSFEKSQKDLEVA----------LT--HKDDNINALTNCITQL--NLLECESESEGQNKGGNDSDELANGEVG 318
Cdd:PRK03918 415 GELKKEIKELKKAIEELKKAkgkcpvcgreLTeeHRKELLEEYTAELKRIekELKEIEEKERKLRKELRELEKVLKKESE 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 319 GDRNEKMKNQIKQM------MDVSRTQTAISVVEEdLKLLQLKLRASVStkcNLEDQVKKLEDDRNSLQA---AKAGLED 389
Cdd:PRK03918 495 LIKLKELAEQLKELeeklkkYNLEELEKKAEEYEK-LKEKLIKLKGEIK---SLKKELEKLEELKKKLAElekKLDELEE 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 390 ECKTLRQK--------VEILNELYQQKEMALQK--KLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQ 459
Cdd:PRK03918 571 ELAELLKEleelgfesVEELEERLKELEPFYNEylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE 650
|
410
....*....|....*....
gi 664806007 460 KTERSFKNQiaTHEKKAHE 478
Cdd:PRK03918 651 ELEKKYSEE--EYEELREE 667
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
103-478 |
1.95e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.70 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 103 KENTELVQKLSNYEQKIKESKKHVQETRKqnmilSDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLESEREQNVKNQDLI 182
Cdd:PTZ00121 1404 KKKADELKKAAAAKKKADEAKKKAEEKKK-----ADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK 1478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 183 SENKKSIEKLKDVISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEE--NARLKKKKEQLQQEIEDWSKLHAELSEQIK 260
Cdd:PTZ00121 1479 AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEakKAEEAKKADEAKKAEEKKKADELKKAEELK 1558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 261 SFEKSQKdLEVALTHKDDNINALTNCiTQLNLLEcESESEGQNKGGNDSDELANGEVGGDRNEKMK-NQIKQMMDVSRT- 338
Cdd:PTZ00121 1559 KAEEKKK-AEEAKKAEEDKNMALRKA-EEAKKAE-EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKaEELKKAEEEKKKv 1635
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 339 -QTAISVVEEDLKLLQLKlRASVSTKCNLEDQVKKLEDDRNSLQAAKAGLEDEcktlRQKVEILNELYQQKEMALQkkLS 417
Cdd:PTZ00121 1636 eQLKKKEAEEKKKAEELK-KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE----KKAAEALKKEAEEAKKAEE--LK 1708
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 664806007 418 QEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTERSfKNQIAtHEKKAHE 478
Cdd:PTZ00121 1709 KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE-KKKIA-HLKKEEE 1767
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
92-517 |
3.52e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.46 E-value: 3.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 92 QQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLESE 171
Cdd:TIGR02168 340 AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 172 REQNVKNQDLISENKK-----SIEKLKDVISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKK---EQLQQ 243
Cdd:TIGR02168 420 QQEIEELLKKLEEAELkelqaELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLdslERLQE 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 244 EIEDWSK--------------LHAELSEQIKSFEKSQKDLEVAL-------THKDDN-----INALT-NCITQLNLLECE 296
Cdd:TIGR02168 500 NLEGFSEgvkallknqsglsgILGVLSELISVDEGYEAAIEAALggrlqavVVENLNaakkaIAFLKqNELGRVTFLPLD 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 297 SESEGQNKgGNDSDELAN--GEVG-GDRNEKMKNQIKQMMD--------VSRTQTAIsvveEDLKLLQLKLR-------- 357
Cdd:TIGR02168 580 SIKGTEIQ-GNDREILKNieGFLGvAKDLVKFDPKLRKALSyllggvlvVDDLDNAL----ELAKKLRPGYRivtldgdl 654
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 358 ---------ASVSTKC----------NLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQKEM---ALQKK 415
Cdd:TIGR02168 655 vrpggvitgGSAKTNSsilerrreieELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRqisALRKD 734
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 416 LSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTER---SFKNQIATHEKKAHENWLKARAAERAIAE 492
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAeieELEAQIEQLKEELKALREALDELRAELTL 814
|
490 500
....*....|....*....|....*
gi 664806007 493 EKREAANLRHKLLELTQKMAMLQEE 517
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERR 839
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
139-459 |
4.42e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 4.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 139 EAIKYKDKIKTLEKNQEILDDTAKNLRVMLESEREQNVKNQDLISENKKSIEKLKDvismnasEFSEVQIALNEAKLSEE 218
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL-------ELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 219 KVKSECHRVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKddninaltncitQLNLLECESE 298
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA------------EAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 299 SEgqnkggndsdelangEVGGDRNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQVKKLEDDRN 378
Cdd:COG1196 367 LL---------------EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 379 SLQAAKAGLEDEcktLRQKVEILNELyQQKEMALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDEL 458
Cdd:COG1196 432 ELEEEEEEEEEA---LEEAAEEEAEL-EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFL 507
|
.
gi 664806007 459 Q 459
Cdd:COG1196 508 E 508
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
92-283 |
6.47e-09 |
|
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: 58.62 E-value: 6.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 92 QQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEIL-DDTAKNLRVMLES 170
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQkEELAELLRALYRL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 171 EREQNVK---NQDLISENKKSIEKLKDVISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIED 247
Cdd:COG4942 117 GRQPPLAlllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAE 196
|
170 180 190
....*....|....*....|....*....|....*.
gi 664806007 248 WSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINAL 283
Cdd:COG4942 197 RQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
92-517 |
8.39e-09 |
|
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: 59.36 E-value: 8.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 92 QQISEKLKTIMKENTELVQKLSNYEQKIKESKKH-------VQETRKQNMILSDEAIKYKDKIktleknQEILDDTAKNL 164
Cdd:pfam15921 317 RQLSDLESTVSQLRSELREAKRMYEDKIEELEKQlvlanseLTEARTERDQFSQESGNLDDQL------QKLLADLHKRE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 165 RvMLESEREQNVKNQDLISENKKSIEKLKDVISMNASEFSEVQIALneaklseEKVKSECH-RVQEENARLKKKKE---- 239
Cdd:pfam15921 391 K-ELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALL-------KAMKSECQgQMERQMAAIQGKNEslek 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 240 ------QLQQEIEDWSKLHAELSEQIKSFEKSQK---DLEVALTHKDDNINALTNCITQL---------NLLECESESEG 301
Cdd:pfam15921 463 vssltaQLESTKEMLRKVVEELTAKKMTLESSERtvsDLTASLQEKERAIEATNAEITKLrsrvdlklqELQHLKNEGDH 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 302 QNKGGNDSDELANGEVGGDRN-EKMKNQIKQMMDV----SRTQTAISV----VEEDLKLLQLKLRASVSTKCNLEDQVKK 372
Cdd:pfam15921 543 LRNVQTECEALKLQMAEKDKViEILRQQIENMTQLvgqhGRTAGAMQVekaqLEKEINDRRLELQEFKILKDKKDAKIRE 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 373 LEDDRNSLQAAK-----AGLE----------------DECKTLRQKVEILNELYQqkemALQKKLSQEEYERQEREHRLS 431
Cdd:pfam15921 623 LEARVSDLELEKvklvnAGSErlravkdikqerdqllNEVKTSRNELNSLSEDYE----VLKRNFRNKSEEMETTTNKLK 698
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 432 AADEKAVSAAEEVKTYKRRIEEMEDELQKTERSFKNQIATHEKKAHENWLKARAAERAIAEEKREAANLRHKLLELTQKM 511
Cdd:pfam15921 699 MQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQEL 778
|
....*.
gi 664806007 512 AMLQEE 517
Cdd:pfam15921 779 STVATE 784
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
83-517 |
8.39e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.38 E-value: 8.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 83 KDRVYQVTEQQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMI--LSDEAIKYKDKIKTLEKNQEILDDT 160
Cdd:PTZ00121 1344 AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAkkKAEEDKKKADELKKAAAAKKKADEA 1423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 161 AKNLRvmlESEREQNVKNQdliSENKKSIEKLKdvismnaSEFSEVQIALNEAKLSEEKVKSECHRVQEENAR----LKK 236
Cdd:PTZ00121 1424 KKKAE---EKKKADEAKKK---AEEAKKADEAK-------KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKkadeAKK 1490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 237 KKEQLQQEIEDWSKLHAE--LSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNLLECESESEGQNKGGNDSDELAN 314
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEAkkKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAK 1570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 315 GEVGGDRNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEdQVKKLEDDRNSLQAAKAGLEDECKTL 394
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE-ELKKAEEEKKKVEQLKKKEAEEKKKA 1649
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 395 RQkVEILNELYQQKEMALQKKlsqeEYERQEREHRLSAADEKAVSAAEEVktyKRRIEEME--DELQKTERSFKNQIATH 472
Cdd:PTZ00121 1650 EE-LKKAEEENKIKAAEEAKK----AEEDKKKAEEAKKAEEDEKKAAEAL---KKEAEEAKkaEELKKKEAEEKKKAEEL 1721
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 664806007 473 EKKAHENWLKARAAERAIAEEKREAANLRhKLLELTQKMAMLQEE 517
Cdd:PTZ00121 1722 KKAEEENKIKAEEAKKEAEEDKKKAEEAK-KDEEEKKKIAHLKKE 1765
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
87-373 |
8.72e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 58.88 E-value: 8.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 87 YQVTEQQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRV 166
Cdd:TIGR04523 403 QEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQ 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 167 MLE-SEREQNVKNQD---LISENKKSIEKLKDVISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKK---KKE 239
Cdd:TIGR04523 483 NLEqKQKELKSKEKElkkLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKenlEKE 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 240 --QLQQEIEdwsklhaELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNLLECESESEGqnkggndsdELANGEv 317
Cdd:TIGR04523 563 idEKNKEIE-------ELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKEL---------EKAKKE- 625
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 664806007 318 ggdrNEKMKNQIKQMmdvsrtQTAISVVEEDLKLLQLKLRASVSTKCNLEDQVKKL 373
Cdd:TIGR04523 626 ----NEKLSSIIKNI------KSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKES 671
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
91-463 |
1.11e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.90 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 91 EQQISEKlktimkENTELVQKLSNYEQKIKESK---KHVQETRKQ--------NMILS------------DEAI-KYKDK 146
Cdd:PRK02224 193 KAQIEEK------EEKDLHERLNGLESELAELDeeiERYEEQREQaretrdeaDEVLEeheerreeletlEAEIeDLRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 147 IKTLEKNQEILDDTAKNLRVMLESEREQnvkNQDLISE---NKKSIEKLKDVISMNASEFSEVQIALNEAKLSEEKVKSE 223
Cdd:PRK02224 267 IAETEREREELAEEVRDLRERLEELEEE---RDDLLAEaglDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 224 CHRVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALthkDDNINALTNCITQLNLLECESESEGQN 303
Cdd:PRK02224 344 AESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI---EELRERFGDAPVDLGNAEDFLEELREE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 304 KGGNDSDElanGEVGGD----RNEKMKNQikQMMDVSRTQTA---------ISVVEEDLKLLQlKLRASVSTkcnLEDQV 370
Cdd:PRK02224 421 RDELRERE---AELEATlrtaRERVEEAE--ALLEAGKCPECgqpvegsphVETIEEDRERVE-ELEAELED---LEEEV 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 371 KKLEDDRNSLQAAKAgLEDECKTLRQKVEILNELYQQKEMALQKKLSQEEYERQEREHRLSAADEK----------AVSA 440
Cdd:PRK02224 492 EEVEERLERAEDLVE-AEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKreaaaeaeeeAEEA 570
|
410 420
....*....|....*....|...
gi 664806007 441 AEEVKTYKRRIEEMEDELQKTER 463
Cdd:PRK02224 571 REEVAELNSKLAELKERIESLER 593
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
96-409 |
2.16e-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: 58.14 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 96 EKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLESEREQN 175
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 176 VKNQDLISENKKSIEKLkdvismnasefsevqialneaklseekvksechrvQEENARLKKKKEQLQQEIEDWSKLHAEL 255
Cdd:TIGR02168 319 EELEAQLEELESKLDEL-----------------------------------AEELAELEEKLEELKEELESLEAELEEL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 256 SEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLN--LLECESESEGQNkggndsdelangevggDRNEKMKNQI---- 329
Cdd:TIGR02168 364 EAELEELESRLEELEEQLETLRSKVAQLELQIASLNneIERLEARLERLE----------------DRRERLQQEIeell 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 330 --KQMMDVSRTQTAISVVEEDLKLLQLKLRAsvstkcnLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQ 407
Cdd:TIGR02168 428 kkLEEAELKELQAELEELEEELEELQEELER-------LEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN 500
|
..
gi 664806007 408 KE 409
Cdd:TIGR02168 501 LE 502
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
90-463 |
3.11e-08 |
|
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: 57.06 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 90 TEQQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILddTAKNLRVMlE 169
Cdd:pfam05557 98 QLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSL--AEAEQRIK-E 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 170 SEREQNVKNQDLIsENKKSIEKLKDVISMNAS-EFSEVQIA-LNEAKLSEEKVKSECH----------RVQEENARLKKK 237
Cdd:pfam05557 175 LEFEIQSQEQDSE-IVKNSKSELARIPELEKElERLREHNKhLNENIENKLLLKEEVEdlkrklereeKYREEAATLELE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 238 KEQLQQEIEDWSKLHAE----------LSEQIKSFEKSQkdlevaLTHKDDNiNALTNCITQLNLLECESESEGQNKGGN 307
Cdd:pfam05557 254 KEKLEQELQSWVKLAQDtglnlrspedLSRRIEQLQQRE------IVLKEEN-SSLTSSARQLEKARRELEQELAQYLKK 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 308 DSDElangevggdrNEKMKNQIKQmmdVSRTQTAISVVEEDLKLLQLKLR------ASVSTKCNLEDQVKKLEDDRNSLQ 381
Cdd:pfam05557 327 IEDL----------NKKLKRHKAL---VRRLQRRVLLLTKERDGYRAILEsydkelTMSNYSPQLLERIEEAEDMTQKMQ 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 382 AAKAGLEDECKTLRQKVEILNELYQQKEMALQKKlsqeeyerqerehRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKT 461
Cdd:pfam05557 394 AHNEEMEAQLSVAEEELGGYKQQAQTLERELQAL-------------RQQESLADPSYSKEEVDSLRRKLETLELERQRL 460
|
..
gi 664806007 462 ER 463
Cdd:pfam05557 461 RE 462
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
525-770 |
3.16e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 57.64 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 525 PGKPNTQNPPRRGPLSqNGSFGPSPVSGGECSPPLTV-EPPVRPLSATLNRRDMPRSEfGSVDGPLPHPRWSAEASGKPS 603
Cdd:PHA03247 2748 PATPGGPARPARPPTT-AGPPAPAPPAAPAAGPPRRLtRPAVASLSESRESLPSPWDP-ADPPAAVLAPAAALPPAASPA 2825
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 604 PSDPGSGTATMMNSS-SRGSSPTRVLDEGKVnmAPKGP-----PPFPGVPLMSTPMGGPVPPPIRYGPPPQLC------- 670
Cdd:PHA03247 2826 GPLPPPTSAQPTAPPpPPGPPPPSLPLGGSV--APGGDvrrrpPSRSPAAKPAAPARPPVRRLARPAVSRSTEsfalppd 2903
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 671 --GPFGPRPLPPPFGPGMRPPLGLREFAPGVPPGRRDLPLHPR------GFLPGHAPFRPLGSLGPREYFIPGTRLPPPT 742
Cdd:PHA03247 2904 qpERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTtdpagaGEPSGAVPQPWLGALVPGRVAVPRFRVPQPA 2983
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 664806007 743 HG-PQEYPPPPAVRDLLPSG-----------SRDEPPPAS 770
Cdd:PHA03247 2984 PSrEAPASSTPPLTGHSLSRvsswasslalhEETDPPPVS 3023
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
107-401 |
3.16e-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: 57.39 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 107 ELVQKLSNYEQKIKESKKHVQETRKQNmILSDEAikykDKIKTLEKNQEILDDTAK------------NLRVMLESEREQ 174
Cdd:TIGR02169 215 ALLKEKREYEGYELLKEKEALERQKEA-IERQLA----SLEEELEKLTEEISELEKrleeieqlleelNKKIKDLGEEEQ 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 175 N-VKNQdlISENKKSIEKLKDVISMNASEfsevqiaLNEAKLSEEKVKSECHRVQEEnarlkkkKEQLQQEIEDWSKLHA 253
Cdd:TIGR02169 290 LrVKEK--IGELEAEIASLERSIAEKERE-------LEDAEERLAKLEAEIDKLLAE-------IEELEREIEEERKRRD 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 254 ELSEQIKSFEKSQKDLEVALTHKDDninalTNCITQLNLLECESESEGQNKGGNDSdeLANGEVGGDRNEKMKNQIKQM- 332
Cdd:TIGR02169 354 KLTEEYAELKEELEDLRAELEEVDK-----EFAETRDELKDYREKLEKLKREINEL--KRELDRLQEELQRLSEELADLn 426
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 664806007 333 MDVSRTQTAISVVEEDLKLLQLKLRAS----VSTKCNLEDQVKKLEDDRNSLQAakagLEDECKTLRQKVEIL 401
Cdd:TIGR02169 427 AAIAGIEAKINELEEEKEDKALEIKKQewklEQLAADLSKYEQELYDLKEEYDR----VEKELSKLQRELAEA 495
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
103-512 |
3.55e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.46 E-value: 3.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 103 KENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEilddtAKNLRVMLESEREQNVKNQdli 182
Cdd:PTZ00121 1315 KKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAE-----AAEKKKEEAKKKADAAKKK--- 1386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 183 SENKKSIEKLKDVISMNASEFSEVQIALNEAKLSEE-KVKSECHRVQEE---NARLKKKKEQLQQEIEDWSKLH--AELS 256
Cdd:PTZ00121 1387 AEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEaKKKAEEKKKADEakkKAEEAKKADEAKKKAEEAKKAEeaKKKA 1466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 257 EQIKSFEKSQKDLEVALTHKDDNINALTnciTQLNLLECESESEGQNKggndSDELANGEVGGDRNEKMKNQIKQMMDVS 336
Cdd:PTZ00121 1467 EEAKKADEAKKKAEEAKKADEAKKKAEE---AKKKADEAKKAAEAKKK----ADEAKKAEEAKKADEAKKAEEAKKADEA 1539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 337 RTQTAISVVEEDLKLLQLKlRASVSTKCnleDQVKKLEDDRNSL--------QAAKAGLEDECKTLRQKVEI-LNELYQQ 407
Cdd:PTZ00121 1540 KKAEEKKKADELKKAEELK-KAEEKKKA---EEAKKAEEDKNMAlrkaeeakKAEEARIEEVMKLYEEEKKMkAEEAKKA 1615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 408 KEMALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTykrriEEMEDELQKTERSFKnqiATHEKKAHENWLKARAAE 487
Cdd:PTZ00121 1616 EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK-----AEEENKIKAAEEAKK---AEEDKKKAEEAKKAEEDE 1687
|
410 420
....*....|....*....|....*
gi 664806007 488 RAIAEEKREAANLRHKLLELTQKMA 512
Cdd:PTZ00121 1688 KKAAEALKKEAEEAKKAEELKKKEA 1712
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
515-771 |
6.83e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 56.49 E-value: 6.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 515 QEEPVIVKPMPGKPNTQNPPrrGPLSQNGSF-------GPSPVSGGECSPPLTVEPPVRPLSATLNRRDMPRSEFGSVDG 587
Cdd:PHA03247 2704 PPPTPEPAPHALVSATPLPP--GPAAARQASpalpaapAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPR 2781
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 588 PLPHP---RWSAEASGKPSPSDPG------SGTATMMNSSSRGSSPTrvldEGKVNMAPKGPPPFPGVPLMSTPMGGPVP 658
Cdd:PHA03247 2782 RLTRPavaSLSESRESLPSPWDPAdppaavLAPAAALPPAASPAGPL----PPPTSAQPTAPPPPPGPPPPSLPLGGSVA 2857
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 659 PPIRygpppqLCGPFGPRPLPPPFGPGMRPPLGlREFAPGVPPGRRDLPLHPRGFLPGHAPFRPLGSLGPREYFIPGTRL 738
Cdd:PHA03247 2858 PGGD------VRRRPPSRSPAAKPAAPARPPVR-RLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQ 2930
|
250 260 270
....*....|....*....|....*....|...
gi 664806007 739 PPPTHGPQEYPPPPAVRDLLPSGSRDEPPPASQ 771
Cdd:PHA03247 2931 PPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPW 2963
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
92-461 |
1.27e-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: 55.36 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 92 QQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLESE 171
Cdd:pfam02463 665 KASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQK 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 172 REQNVKNQDLISENKKSIEKLKDVISMNASEFSEV---QIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIEDW 248
Cdd:pfam02463 745 IDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEErekTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLI 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 249 SKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNLLECESESEGQNKGGNDSDELANGEVGGDRNEKMKNQ 328
Cdd:pfam02463 825 EQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEE 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 329 IKQ--MMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQ 406
Cdd:pfam02463 905 ESQklNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFE 984
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 664806007 407 QKEMALQKKLSQEEyerqerehRLSAADeKAVSAAEEVKTYKRRIEEMEDELQKT 461
Cdd:pfam02463 985 EKEERYNKDELEKE--------RLEEEK-KKLIRAIIEETCQRLKEFLELFVSIN 1030
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
93-463 |
1.80e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 93 QISEKLKTIMKENTELVQKLSNYEqKIKESKKHVQETRKQNMILSDEaiKYKDKIKTLEKNQEILDDTAKNLRvmlesER 172
Cdd:PRK03918 342 ELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGLTPE--KLEKELEELEKAKEEIEEEISKIT-----AR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 173 EQNVKNQdlISENKKSIEKLKD------VISMNASEFSEVQIaLNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIE 246
Cdd:PRK03918 414 IGELKKE--IKELKKAIEELKKakgkcpVCGRELTEEHRKEL-LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLK 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 247 DWSKLHA--ELSEQIKSFEKSQKDLevalthkddNINALTNCITQLNLLECES-ESEGQNKGGNDSDELANG-------- 315
Cdd:PRK03918 491 KESELIKlkELAEQLKELEEKLKKY---------NLEELEKKAEEYEKLKEKLiKLKGEIKSLKKELEKLEElkkklael 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 316 -EVGGDRNEKMKNQIKQMMdvSRTQTAISVVEEDLKLLQ------LKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAGLE 388
Cdd:PRK03918 562 eKKLDELEEELAELLKELE--ELGFESVEELEERLKELEpfyneyLELKDAEKELEREEKELKKLEEELDKAFEELAETE 639
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 664806007 389 DECKTLRQKVEILNELYQQKEMA----LQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTER 463
Cdd:PRK03918 640 KRLEELRKELEELEKKYSEEEYEelreEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEK 718
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
91-282 |
2.12e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.07 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 91 EQQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEaikykdkiktLEKNQEILDDTAKN------- 163
Cdd:COG3883 32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE----------IEERREELGERARAlyrsggs 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 164 ---LRVMLESEreqNVknQDLISenkkSIEKLKDVISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQ 240
Cdd:COG3883 102 vsyLDVLLGSE---SF--SDFLD----RLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 664806007 241 LQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINA 282
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
81-416 |
2.98e-07 |
|
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: 53.81 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 81 VVKDRVYQVTEQQISEKLKTIMKENTELVQKLS-NYEQKIKESKKHVQETRKQNMILSDEAIKYKdkiKTLEKNQEILDD 159
Cdd:COG5185 192 ISELKKAEPSGTVNSIKESETGNLGSESTLLEKaKEIINIEEALKGFQDPESELEDLAQTSDKLE---KLVEQNTDLRLE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 160 TAKNLRVMLESEREQNVKNQDLISENKKSIEKLKDVISMNAS-EFSEVQIALNEAKLSEEKVKSEchrVQEENARLKKKK 238
Cdd:COG5185 269 KLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKAtESLEEQLAAAEAEQELEESKRE---TETGIQNLTAEI 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 239 EQLQQEI-EDWSKLHAELSE--QIKSFEKSQKDLEVALTH----KDDNINALTNCITQLNLLEcesESEGQNKGGNDSD- 310
Cdd:COG5185 346 EQGQESLtENLEAIKEEIENivGEVELSKSSEELDSFKDTiestKESLDEIPQNQRGYAQEIL---ATLEDTLKAADRQi 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 311 ELANGEVGGDR--NEKMKNQIKQMMDvSRTQTAISVVEEDLKLLQLKLRASVSTkcnLEDQVKKLEDDRNSLQAAKAGLE 388
Cdd:COG5185 423 EELQRQIEQATssNEEVSKLLNELIS-ELNKVMREADEESQSRLEEAYDEINRS---VRSKKEDLNEELTQIESRVSTLK 498
|
330 340
....*....|....*....|....*...
gi 664806007 389 DECKTLRQKVEILNELYQQKEMALQKKL 416
Cdd:COG5185 499 ATLEKLRAKLERQLEGVRSKLDQVAESL 526
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
96-510 |
3.24e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.38 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 96 EKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILD-DTAKNLRVMLESEREQ 174
Cdd:PTZ00121 1070 EGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEaRKAEDARKAEEARKAE 1149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 175 NVKNQDLiseNKKSIEKLKDVISMNASEFSEVQialnEAKLSEEKVKSECHRVQEENARLKK-KKEQLQQEIEDWSKLH- 252
Cdd:PTZ00121 1150 DAKRVEI---ARKAEDARKAEEARKAEDAKKAE----AARKAEEVRKAEELRKAEDARKAEAaRKAEEERKAEEARKAEd 1222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 253 AELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNLLE-CESESEGQNKGGNDSDELANGEvggdrNEKMKNQIKQ 331
Cdd:PTZ00121 1223 AKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHfARRQAAIKAEEARKADELKKAE-----EKKKADEAKK 1297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 332 MMDVSRTQTAISVVEEDLKLLQLKLRASVSTKcNLEDQVKKLEDDRNSLQAAKAGLEDECKTL----------------- 394
Cdd:PTZ00121 1298 AEEKKKADEAKKKAEEAKKADEAKKKAEEAKK-KADAAKKKAEEAKKAAEAAKAEAEAAADEAeaaeekaeaaekkkeea 1376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 395 RQKVEILNELYQQKEMALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTERSFKNQIATHEK 474
Cdd:PTZ00121 1377 KKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA 1456
|
410 420 430
....*....|....*....|....*....|....*.
gi 664806007 475 KAHENWLKARAAERAIAEEKREAANLRhKLLELTQK 510
Cdd:PTZ00121 1457 KKAEEAKKKAEEAKKADEAKKKAEEAK-KADEAKKK 1491
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
522-785 |
5.26e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 53.79 E-value: 5.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 522 KPMPGKPNTQNPPRrgPLSQNGSFGPSPVSGGECSPPLTVE--PPVRPLSATLNRRDMPRSEFGSVDGPL---------- 589
Cdd:PHA03247 2700 DPPPPPPTPEPAPH--ALVSATPLPPGPAAARQASPALPAApaPPAVPAGPATPGGPARPARPPTTAGPPapappaapaa 2777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 590 -PHPR--------WSAEASGKPSPSDPG------SGTATMMNSSSRGSSPTrvldEGKVNMAPKGPPPFPGVPLMSTPMG 654
Cdd:PHA03247 2778 gPPRRltrpavasLSESRESLPSPWDPAdppaavLAPAAALPPAASPAGPL----PPPTSAQPTAPPPPPGPPPPSLPLG 2853
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 655 GPVPPPIRygpppqLCGPFGPRPLPPPFGPGMRPPLGlREFAPGVPPGRRDLPLHPRGflpghaPFRPlgslgpreyfiP 734
Cdd:PHA03247 2854 GSVAPGGD------VRRRPPSRSPAAKPAAPARPPVR-RLARPAVSRSTESFALPPDQ------PERP-----------P 2909
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 664806007 735 GTRLPPPTHGPQEYPPPPAVRDLLPSGSRDEPPPASQSTSQDCSQALKQSP 785
Cdd:PHA03247 2910 QPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVP 2960
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
93-476 |
7.35e-07 |
|
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: 53.13 E-value: 7.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 93 QISEKLKTIMKENTELVQKLSNYEQKIKESK------------------KHVQE-----TRKQNMILSDE---------A 140
Cdd:TIGR01612 1366 EVKEYTKEIEENNKNIKDELDKSEKLIKKIKddinleeckskiestlddKDIDEcikkiKELKNHILSEEsnidtyfknA 1445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 141 IKYKDKIKTLEKNQEILDDTAKNLrvmLESEREQNVKNQDL----ISENKKSIEKLKDVISMNASEFSEVQIALNEAKLS 216
Cdd:TIGR01612 1446 DENNENVLLLFKNIEMADNKSQHI---LKIKKDNATNDHDFnineLKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKD 1522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 217 EEKVKSECHRVQEEN--ARLKKKKEQLQQEIEDWSK---LHAELSEQ-IKSFEKSQKDLEVALTHKDDNINALTNCITQL 290
Cdd:TIGR01612 1523 VTELLNKYSALAIKNkfAKTKKDSEIIIKEIKDAHKkfiLEAEKSEQkIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSL 1602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 291 NLLEcesesegqNKGGNDSDELANGEVGGDRNEKMKNQIKQmMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQV 370
Cdd:TIGR01612 1603 ENFE--------NKFLKISDIKKKINDCLKETESIEKKISS-FSIDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKK 1673
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 371 KKLEDDRNSLQAAKAGLEDECKTLRQK-VEILNELYQQKEMALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKR 449
Cdd:TIGR01612 1674 KELDELDSEIEKIEIDVDQHKKNYEIGiIEKIKEIAIANKEEIESIKELIEPTIENLISSFNTNDLEGIDPNEKLEEYNT 1753
|
410 420
....*....|....*....|....*..
gi 664806007 450 RIEEMEDELQKTERSFKNQIATHEKKA 476
Cdd:TIGR01612 1754 EIGDIYEEFIELYNIIAGCLETVSKEP 1780
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
82-415 |
1.04e-06 |
|
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: 52.42 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 82 VKDRVYQVTEQQISEK--LKTIMKENTELV-QKLSNYE------QKIKESKKHVQETRKQNMIL---SDEAIKYKDKIKT 149
Cdd:pfam05483 452 IHDLEIQLTAIKTSEEhyLKEVEDLKTELEkEKLKNIEltahcdKLLLENKELTQEASDMTLELkkhQEDIINCKKQEER 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 150 LEKNQEILDDTAKNLRVMLESEREQNVKNQDlisENKKSIEKlkdviSMNASEFSEVQIALNEAKLSEEKVKSECHRVQE 229
Cdd:pfam05483 532 MLKQIENLEEKEMNLRDELESVREEFIQKGD---EVKCKLDK-----SEENARSIEYEVLKKEKQMKILENKCNNLKKQI 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 230 ENArlKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNC---------ITQLNLLEcESEse 300
Cdd:pfam05483 604 ENK--NKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNyqkeiedkkISEEKLLE-EVE-- 678
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 301 gqnKGGNDSDELAngEVGGDRNEKMKNQIKQM---MDVSRTQTAISVVEED--LKLLQLKLRASVSTKCNLEDQVKKLed 375
Cdd:pfam05483 679 ---KAKAIADEAV--KLQKEIDKRCQHKIAEMvalMEKHKHQYDKIIEERDseLGLYKNKEQEQSSAKAALEIELSNI-- 751
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 664806007 376 dRNSLQAAKAGLEDEcktlRQKVEILNELYQQKEMALQKK 415
Cdd:pfam05483 752 -KAELLSLKKQLEIE----KEEKEKLKMEAKENTAILKDK 786
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
88-475 |
1.12e-06 |
|
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: 52.42 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 88 QVTEQQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETR-KQNMI-----LSDEAIKY----KDKI---------- 147
Cdd:pfam05483 225 QHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRdKANQLeektkLQDENLKEliekKDHLtkeledikms 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 148 --------KTLEKNQEILDDTAKNLRVMLESEREQNVKN------------------QDLISENKKSIEKLKD---VISM 198
Cdd:pfam05483 305 lqrsmstqKALEEDLQIATKTICQLTEEKEAQMEELNKAkaahsfvvtefeattcslEELLRTEQQRLEKNEDqlkIITM 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 199 ----NASEFSEVQIALNEAKLSEEKVKsechRVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALT 274
Cdd:pfam05483 385 elqkKSSELEEMTKFKNNKEVELEELK----KILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLT 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 275 HKDDNINALTNCITQLNL-LECESESEGQNKGGNDSDELANGEV---GGDRNEKMKNQIKQMMDVSRTQTAISVVEEDLK 350
Cdd:pfam05483 461 AIKTSEEHYLKEVEDLKTeLEKEKLKNIELTAHCDKLLLENKELtqeASDMTLELKKHQEDIINCKKQEERMLKQIENLE 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 351 LLQLKLRASVST------------KCNL---EDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILN---ELYQQKEMAL 412
Cdd:pfam05483 541 EKEMNLRDELESvreefiqkgdevKCKLdksEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNkniEELHQENKAL 620
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 664806007 413 QKKlsqeeyerqerehrlSAADEKAVSAaeevktYKRRIEEMEDELQKTERSFKNQIATHEKK 475
Cdd:pfam05483 621 KKK---------------GSAENKQLNA------YEIKVNKLELELASAKQKFEEIIDNYQKE 662
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
173-410 |
1.29e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 51.94 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 173 EQNVKNQDLISENKKSIeklkDVISMNASEFSEvQIALNEAKLSEEKVKSEchrvqEENARLKKKKEQLQQEIEDWSKLH 252
Cdd:PHA02562 167 EMDKLNKDKIRELNQQI----QTLDMKIDHIQQ-QIKTYNKNIEEQRKKNG-----ENIARKQNKYDELVEEAKTIKAEI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 253 AELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNLLE-----------CESE-SEGQNKGGNDSDELANGEVGGD 320
Cdd:PHA02562 237 EELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIkmyekggvcptCTQQiSEGPDRITKIKDKLKELQHSLE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 321 RNEKMKNQIKQMMDVSRTQTaisvveEDLKLLQLKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEI 400
Cdd:PHA02562 317 KLDTAIDELEEIMDEFNEQS------KKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDK 390
|
250
....*....|
gi 664806007 401 LNELYQQKEM 410
Cdd:PHA02562 391 IVKTKSELVK 400
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
91-506 |
1.56e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 91 EQQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRK-QNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLE 169
Cdd:PTZ00121 1089 ADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKaEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEE 1168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 170 SEREQNVKNqdlISENKKSIEKLKDVISMNASEFSEVQialnEAKLSEEKVKSECHRVQEENARLK--KKKEQLQQEIED 247
Cdd:PTZ00121 1169 ARKAEDAKK---AEAARKAEEVRKAEELRKAEDARKAE----AARKAEEERKAEEARKAEDAKKAEavKKAEEAKKDAEE 1241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 248 wsklhAELSEQIKSFEKSQKDLEVALTHKDDNINALtncitqlnllecesESEGQNKggndSDELANGEvggdrNEKMKN 327
Cdd:PTZ00121 1242 -----AKKAEEERNNEEIRKFEEARMAHFARRQAAI--------------KAEEARK----ADELKKAE-----EKKKAD 1293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 328 QIKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTKcNLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKveilnelyQQ 407
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK-KADAAKKKAEEAKKAAEAAKAEAEAAADEAEAA--------EE 1364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 408 KEMALQKKLSQEEYerqerehRLSAADEKA--VSAAEEVKTYKRRIEEMEDELQKTERSfKNQIATHEKKAHEnwLKARA 485
Cdd:PTZ00121 1365 KAEAAEKKKEEAKK-------KADAAKKKAeeKKKADEAKKKAEEDKKKADELKKAAAA-KKKADEAKKKAEE--KKKAD 1434
|
410 420
....*....|....*....|.
gi 664806007 486 AERAIAEEKREAANLRHKLLE 506
Cdd:PTZ00121 1435 EAKKKAEEAKKADEAKKKAEE 1455
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
508-769 |
1.66e-06 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 51.69 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 508 TQKMAMLQEEPVIVKPMPGKPNTQNPPRRGPLSQNGSFGPSPvSGGECSPPLTVEPPVRPLS-----ATLNRRDMPRSEf 582
Cdd:pfam03154 169 TQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQG-SPATSQPPNQTQSTAAPHTliqqtPTLHPQRLPSPH- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 583 gSVDGPLPHPRWSAEASGKPSPSDPGSGTATMMNSSsrgssptrvLDEGKVNMAPKGPP-PFPGVPLMSTPMGGPVPPPI 661
Cdd:pfam03154 247 -PPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHS---------LQTGPSHMQHPVPPqPFPLTPQSSQSQVPPGPSPA 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 662 RYGPPPQLCGPFGPRPLPPPFGPGMRPPLglrEFAPGVPPGRRDLPLHPRGFLPG-HAPFRPLGSLGPREYFIPGTRLPP 740
Cdd:pfam03154 317 APGQSQQRIHTPPSQSQLQSQQPPREQPL---PPAPLSMPHIKPPPTTPIPQLPNpQSHKHPPHLSGPSPFQMNSNLPPP 393
|
250 260 270
....*....|....*....|....*....|....*...
gi 664806007 741 P---------THGPQEYPPPPAvrDLLPSGSRDEPPPA 769
Cdd:pfam03154 394 PalkplsslsTHHPPSAHPPPL--QLMPQSQQLPPPPA 429
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
195-443 |
1.77e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 195 VISMNASEFSEVQIALNEAKLSEekvksechrVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALT 274
Cdd:COG3883 5 ALAAPTPAFADPQIQAKQKELSE---------LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 275 HKDDNINALTNCITQLNlleceseSEGQNKGGNDS--DELANGEVGGDRNEKMkNQIKQMMDvsRTQTAISVVEEDLKLL 352
Cdd:COG3883 76 EAEAEIEERREELGERA-------RALYRSGGSVSylDVLLGSESFSDFLDRL-SALSKIAD--ADADLLEELKADKAEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 353 QLKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQKEMALQKKLSQEEYERQEREHRLSA 432
Cdd:COG3883 146 EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
250
....*....|.
gi 664806007 433 ADEKAVSAAEE 443
Cdd:COG3883 226 AAAAAAAAAAA 236
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
111-404 |
1.90e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 51.98 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 111 KLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEI---------------LDDTAKNLRV----MLESE 171
Cdd:TIGR01612 1356 KLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINLeeckskiestlddkdIDECIKKIKElknhILSEE 1435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 172 REQNV--KNQDlisENKKSIEKLKDVISM--NASEF----------SEVQIALNEakLSEEKVKSE-CHRVQEENAR-LK 235
Cdd:TIGR01612 1436 SNIDTyfKNAD---ENNENVLLLFKNIEMadNKSQHilkikkdnatNDHDFNINE--LKEHIDKSKgCKDEADKNAKaIE 1510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 236 KKKEQLQQEIEDWSKLHAELSE-QIKS-FEKSQKDLEVALthkdDNINALTNCITqlnlLECESESEGQNKGGND----S 309
Cdd:TIGR01612 1511 KNKELFEQYKKDVTELLNKYSAlAIKNkFAKTKKDSEIII----KEIKDAHKKFI----LEAEKSEQKIKEIKKEkfriE 1582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 310 DELANGEVGG----DRNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRA-SVSTKcnlEDQVKKLEDDRNSLQAAK 384
Cdd:TIGR01612 1583 DDAAKNDKSNkaaiDIQLSLENFENKFLKISDIKKKINDCLKETESIEKKISSfSIDSQ---DTELKENGDNLNSLQEFL 1659
|
330 340
....*....|....*....|
gi 664806007 385 AGLEDECKTLRQKVEILNEL 404
Cdd:TIGR01612 1660 ESLKDQKKNIEDKKKELDEL 1679
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
69-469 |
3.14e-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: 50.73 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 69 ASFAIFLWRTVLVVKDRVYQVTEQQISEKLKTIMKENTELVQKLSNYEQKIKESK---KHVQETRKQNMILSDEAIKYKD 145
Cdd:COG5185 148 DIEASYGEVETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGtvnSIKESETGNLGSESTLLEKAKE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 146 KIKTLEKNQEILDDtaknlrvmlESEREQNVKNQDLISENKKSIEKLKDvismnaSEFSEvqialneaklSEEKVKsech 225
Cdd:COG5185 228 IINIEEALKGFQDP---------ESELEDLAQTSDKLEKLVEQNTDLRL------EKLGE----------NAESSK---- 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 226 RVQEENARLKKKKEQLQQEIE------DWSKLHAELSEQIKSFEKSQKdLEVALTHKDDNINALTNCITQLNllecESES 299
Cdd:COG5185 279 RLNENANNLIKQFENTKEKIAeytksiDIKKATESLEEQLAAAEAEQE-LEESKRETETGIQNLTAEIEQGQ----ESLT 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 300 EGQNKGGNDSDELAnGEVGGDRNEKMKNQIKQMMDVSRT--------------------QTAISVVEEDLKLLQLKLRAS 359
Cdd:COG5185 354 ENLEAIKEEIENIV-GEVELSKSSEELDSFKDTIESTKEsldeipqnqrgyaqeilatlEDTLKAADRQIEELQRQIEQA 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 360 VSTKCNLEDQVKKLED-----DRNSLQAAKAGLEDECK----TLRQKVEILNELYQQKEMALQKKLSQEEYERQEREHRL 430
Cdd:COG5185 433 TSSNEEVSKLLNELISelnkvMREADEESQSRLEEAYDeinrSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQL 512
|
410 420 430
....*....|....*....|....*....|....*....
gi 664806007 431 SAADEKAVSAAEEVKTYKRRIEEMEDELQKTERSFKNQI 469
Cdd:COG5185 513 EGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELI 551
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
92-463 |
4.02e-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: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 92 QQISEKLKTIMKENTELVQKLSN----YEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDtaknlrvm 167
Cdd:pfam01576 74 EEILHELESRLEEEEERSQQLQNekkkMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLED-------- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 168 lesereQNVKnqdLISENKKSIEKLKDVISmNASEFSEVQIALNEAKLSEEKVKS--ECHRVQEENAR--LKKKKEQLQQ 243
Cdd:pfam01576 146 ------QNSK---LSKERKLLEERISEFTS-NLAEEEEKAKSLSKLKNKHEAMISdlEERLKKEEKGRqeLEKAKRKLEG 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 244 EIEDWSKLHAELSEQIK----SFEKSQKDLEVALTHKDDNINALTNCITQLNLLEC---------ESESEGQNKGGND-- 308
Cdd:pfam01576 216 ESTDLQEQIAELQAQIAelraQLAKKEEELQAALARLEEETAQKNNALKKIRELEAqiselqedlESERAARNKAEKQrr 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 309 --SDEL---------------ANGEVGGDRNEKMKNQIKQMMDVSRT---------QTAISVVEEDLKLLQLKLRASVS- 361
Cdd:pfam01576 296 dlGEELealkteledtldttaAQQELRSKREQEVTELKKALEEETRSheaqlqemrQKHTQALEELTEQLEQAKRNKANl 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 362 --TKCNLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQKEMA---LQKKLSQEEYERQEREHRLSAADEK 436
Cdd:pfam01576 376 ekAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQraeLAEKLSKLQSELESVSSLLNEAEGK 455
|
410 420
....*....|....*....|....*..
gi 664806007 437 AVSAAEEVKTYKRRIEEMEDELQKTER 463
Cdd:pfam01576 456 NIKLSKDVSSLESQLQDTQELLQEETR 482
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
88-384 |
4.38e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 88 QVTEQQISEKLKTIMKENTELVQKLSNYEQ-KIK-ESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLR 165
Cdd:PTZ00121 1588 KAEEARIEEVMKLYEEEKKMKAEEAKKAEEaKIKaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA 1667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 166 VMLESEREQNVKNQDLISENKKSIEKL-------KDVISMNASEFSEVQIAlNEAKLSEEKVKSECHRVQEENARLKKKK 238
Cdd:PTZ00121 1668 KKAEEDKKKAEEAKKAEEDEKKAAEALkkeaeeaKKAEELKKKEAEEKKKA-EELKKAEEENKIKAEEAKKEAEEDKKKA 1746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 239 EQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNLLECESESEGQNKGGNDSDELANgevg 318
Cdd:PTZ00121 1747 EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVIN---- 1822
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 664806007 319 gDRNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTK-CNLEDQVKKLEDDRNSLQAAK 384
Cdd:PTZ00121 1823 -DSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKeADFNKEKDLKEDDEEEIEEAD 1888
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
103-290 |
4.55e-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: 49.76 E-value: 4.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 103 KENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLESEREQNVKNQDLI 182
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 183 SENKKSIEKLKDVISM-----------NASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIEDWSKL 251
Cdd:COG4942 100 EAQKEELAELLRALYRlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190
....*....|....*....|....*....|....*....
gi 664806007 252 HAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQL 290
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
116-501 |
4.69e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 4.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 116 EQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLESEREQNVKNqdliSENKKSIEKLKDV 195
Cdd:PTZ00121 1211 ERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIK----AEEARKADELKKA 1286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 196 ismnasefSEVQIAlNEAKLSEEKVKSECHRVQEENARlkkKKEQLQQEIEDWSKLHAELSeqiKSFEKSQKDLEVAlth 275
Cdd:PTZ00121 1287 --------EEKKKA-DEAKKAEEKKKADEAKKKAEEAK---KADEAKKKAEEAKKKADAAK---KKAEEAKKAAEAA--- 1348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 276 kddninaltncitqlnllecESESEGQNKGGNDSDELANGEVGGDRNEKMKNQI--KQMMDVSRTQTAISVVEEDLKLLQ 353
Cdd:PTZ00121 1349 --------------------KAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAakKKAEEKKKADEAKKKAEEDKKKAD 1408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 354 lKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAGLE-DECKTLRQKVEILNELYQQKEMALQKKLSQEEYERQEREHRLSA 432
Cdd:PTZ00121 1409 -ELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEaKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADE 1487
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 664806007 433 ADEKAVSAAEEVKTYKRRIEEME--DELQKTERSFKnqiATHEKKAHEnwlKARAAERAIAEEKREAANLR 501
Cdd:PTZ00121 1488 AKKKAEEAKKKADEAKKAAEAKKkaDEAKKAEEAKK---ADEAKKAEE---AKKADEAKKAEEKKKADELK 1552
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
95-464 |
5.56e-06 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 50.22 E-value: 5.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 95 SEKLKTIM-KENTELVQ-KLSNYEQKIKESKKHVQETRKQ--NMILSDEAIK-YKDKIKTLEKNQEILDDTAKNLRVMLE 169
Cdd:PTZ00440 832 DEELKQLLqKFPTEDENlNLKELEKEFNENNQIVDNIIKDieNMNKNINIIKtLNIAINRSNSNKQLVEHLLNNKIDLKN 911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 170 --SEREQNVKNQDLISENKKSIekLKDVISmnaSEFSEVQIALNEAKLSEEKVKSEC------HRVQEENARLKKKKEQL 241
Cdd:PTZ00440 912 klEQHMKIINTDNIIQKNEKLN--LLNNLN---KEKEKIEKQLSDTKINNLKMQIEKtleyydKSKENINGNDGTHLEKL 986
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 242 QQEIEDWSKLHAE----------LSEQIKSFEKSQKDLEVALTHK-------------DDNINALTNCITQLNLLEcese 298
Cdd:PTZ00440 987 DKEKDEWEHFKSEidklnvnyniLNKKIDDLIKKQHDDIIELIDKlikekgkeieekvDQYISLLEKMKTKLSSFH---- 1062
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 299 segqnkggndsdelANGEVGGDRNEKMKNQIK----QMMDVSRtqtaiSVVEEDLKLLQLKLRAS---VSTKCNLEDQVK 371
Cdd:PTZ00440 1063 --------------FNIDIKKYKNPKIKEEIKlleeKVEALLK-----KIDENKNKLIEIKNKSHehvVNADKEKNKQTE 1123
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 372 KLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQKEMALQKKLsqeeYERQEREHRLSAADEKAVSAAEEVKTYKRRI 451
Cdd:PTZ00440 1124 HYNKKKKSLEKIYKQMEKTLKELENMNLEDITLNEVNEIEIEYER----ILIDHIVEQINNEAKKSKTIMEEIESYKKDI 1199
|
410
....*....|...
gi 664806007 452 EEMEDELQKTERS 464
Cdd:PTZ00440 1200 DQVKKNMSKERND 1212
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
228-463 |
6.28e-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: 49.38 E-value: 6.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 228 QEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLN--LLECESESEGQNKg 305
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEaeLAELEKEIAELRA- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 306 gndsdELAngevggDRNEKMKNQIKQMMDVSRT--------QTAISVVEEDLKLLQLKLRAsvstkcnLEDQVKKLEDDR 377
Cdd:COG4942 98 -----ELE------AQKEELAELLRALYRLGRQpplalllsPEDFLDAVRRLQYLKYLAPA-------RREQAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 378 NSLQAAKAGLEDECKTLRQkveILNELYQQKEmALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDE 457
Cdd:COG4942 160 AELAALRAELEAERAELEA---LLAELEEERA-ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
....*.
gi 664806007 458 LQKTER 463
Cdd:COG4942 236 AAAAAE 241
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
83-509 |
6.48e-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: 6.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 83 KDRVYQVTEQQISEKLKTIMKENTELVQK---------LSNYEQKIKESKKHVQETRK------QN---MILSDEAIKY- 143
Cdd:TIGR01612 847 KVDKFINFENNCKEKIDSEHEQFAELTNKikaeisddkLNDYEKKFNDSKSLINEINKsieeeyQNintLKKVDEYIKIc 926
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 144 ---KDKIKTLEKNQEILDDTA-KNLRVMLESER-EQNVKNQ--DLISENKKSIEKLKDVISMNASEF--SEVQIALNEAK 214
Cdd:TIGR01612 927 entKESIEKFHNKQNILKEILnKNIDTIKESNLiEKSYKDKfdNTLIDKINELDKAFKDASLNDYEAknNELIKYFNDLK 1006
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 215 --LSEEKVKSECHRVQEEnarlKKKKEQLQQEIEDWSK-------------------LHAELSEQIKSFEKS-QKDLEVA 272
Cdd:TIGR01612 1007 anLGKNKENMLYHQFDEK----EKATNDIEQKIEDANKnipnieiaihtsiyniideIEKEIGKNIELLNKEiLEEAEIN 1082
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 273 LTH-----------------KDDNI------NALTNCITQLNLL---ECESESEGQNKGGNDSDElangevggdrnekMK 326
Cdd:TIGR01612 1083 ITNfneikeklkhynfddfgKEENIkyadeiNKIKDDIKNLDQKidhHIKALEEIKKKSENYIDE-------------IK 1149
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 327 NQIKQMMDVsrTQTAISvvEEDLKLLQLKLRASVS---TKCNLEDQVKKLEDDRNSLQAAKAGLEdecktlrqKVEILNE 403
Cdd:TIGR01612 1150 AQINDLEDV--ADKAIS--NDDPEEIEKKIENIVTkidKKKNIYDEIKKLLNEIAEIEKDKTSLE--------EVKGINL 1217
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 404 LYQQKEMALqkklsqeeyerqerehRLSAADEKAVSAAEEVKTYKRRIEEMeDELQKTERSFKNQIATH-EKKAHENWL- 481
Cdd:TIGR01612 1218 SYGKNLGKL----------------FLEKIDEEKKKSEHMIKAMEAYIEDL-DEIKEKSPEIENEMGIEmDIKAEMETFn 1280
|
490 500 510
....*....|....*....|....*....|..
gi 664806007 482 ----KARAAERAIAEEKREAANLRHKLLELTQ 509
Cdd:TIGR01612 1281 ishdDDKDHHIISKKHDENISDIREKSLKIIE 1312
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
191-457 |
7.13e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.68 E-value: 7.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 191 KLKDVISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLE 270
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 271 VALTHKDDNINALTNCITQLnllecesesegQNKGGNDSDELANGE--VGGDRNEKMKNQI-KQMMDVSRTQTAISVVEE 347
Cdd:TIGR02169 751 QEIENVKSELKELEARIEEL-----------EEDLHKLEEALNDLEarLSHSRIPEIQAELsKLEEEVSRIEARLREIEQ 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 348 DLKLLQLKLRASVSTKCNLEDQVKKLEDDRNS-------LQAAKAGLEDECKTLRQKVEILNELYQ---------QKEM- 410
Cdd:TIGR02169 820 KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSiekeienLNGKKEELEEELEELEAALRDLESRLGdlkkerdelEAQLr 899
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 664806007 411 ALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDE 457
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEI 946
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
92-264 |
7.37e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 7.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 92 QQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQeildDTAKNLRVMLESE 171
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL----GNVRNNKEYEALQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 172 REqnvknqdlISENKKSIEKLKDVIS--MNASEFSEVQIALNEAKLSEEKVksechRVQEENARLKKKKEQLQQEIEdws 249
Cdd:COG1579 96 KE--------IESLKRRISDLEDEILelMERIEELEEELAELEAELAELEA-----ELEEKKAELDEELAELEAELE--- 159
|
170
....*....|....*
gi 664806007 250 KLHAELSEQIKSFEK 264
Cdd:COG1579 160 ELEAEREELAAKIPP 174
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
92-435 |
9.08e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 9.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 92 QQISEKLKTimKENTELVQKLSNYEQKIKESKKHVQETrkqnmilsdeaikyKDKIKTLEKNQEILDDTAKNLRVMLESE 171
Cdd:COG1196 216 RELKEELKE--LEAELLLLKLRELEAELEELEAELEEL--------------EAELEELEAELAELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 172 REQNVKNQDLISENKKSIEKLkdvismnasefsEVQIALNEAKLSEEKVKSEchRVQEENARLKKKKEQLQQEIEDWSKL 251
Cdd:COG1196 280 ELELEEAQAEEYELLAELARL------------EQDIARLEERRRELEERLE--ELEEELAELEEELEELEEELEELEEE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 252 HAELSEQIKSFEKSQKDLEVALTHKddninaltncitQLNLLECESESEGQNKggndsdelangevggDRNEKMKNQIKQ 331
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEA------------EAELAEAEEELEELAE---------------ELLEALRAAAEL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 332 MMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQKEMA 411
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
330 340
....*....|....*....|....
gi 664806007 412 LQKKLSQEEYERQEREHRLSAADE 435
Cdd:COG1196 479 LAELLEELAEAAARLLLLLEAEAD 502
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
92-270 |
9.45e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.30 E-value: 9.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 92 QQISEKLKTIMKENTELVQKLSNYEQKIKES--KKHVQETRKQNmiLSDEAIKYKDKIKTLEKNQEILDdtaKNLRVMLE 169
Cdd:TIGR02169 794 PEIQAELSKLEEEVSRIEARLREIEQKLNRLtlEKEYLEKEIQE--LQEQRIDLKEQIKSIEKEIENLN---GKKEELEE 868
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 170 SEREQNVKNQDLISEN---KKSIEKLKdvismnaSEFSEVQIALNEAKLSEEKVKsecHRVQEENARLKKKKEQLqQEIE 246
Cdd:TIGR02169 869 ELEELEAALRDLESRLgdlKKERDELE-------AQLRELERKIEELEAQIEKKR---KRLSELKAKLEALEEEL-SEIE 937
|
170 180
....*....|....*....|....
gi 664806007 247 DWSKLHAELSEQIKSFEKSQKDLE 270
Cdd:TIGR02169 938 DPKGEDEEIPEEELSLEDVQAELQ 961
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
86-268 |
1.19e-05 |
|
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: 47.41 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 86 VYQVTEQQIseklktIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIK--------YKDKIKTLEKNQEIL 157
Cdd:cd21116 15 VTAILNQPN------INLIPLDLLPSLNTHQALARAHALEWLNEIKPKLLSLPNDIIgynntfqsYYPDLIELADNLIKG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 158 DDTAKN-LRVMLESEREQNVKNQDLISENKKSIEKLKDVISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKK 236
Cdd:cd21116 89 DQGAKQqLLQGLEALQSQVTKKQTSVTSFINELTTFKNDLDDDSRNLQTDATKAQAQVAVLNALKNQLNSLAEQIDAAID 168
|
170 180 190
....*....|....*....|....*....|..
gi 664806007 237 KKEQLQQeieDWSKLHAELSEQIKSFEKSQKD 268
Cdd:cd21116 169 ALEKLSN---DWQTLDSDIKELITDLEDAESS 197
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
170-462 |
1.34e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.91 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 170 SEREQNVKNQDLISENKKSIEKLKDVISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQ-------LQ 242
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEleedlssLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 243 QEIEDW----SKLHAELS---EQIKSFEKSQKDLEVALTH-KDDNINALTNCI--------TQLNLLECESESEGQNKgg 306
Cdd:TIGR02169 751 QEIENVkselKELEARIEeleEDLHKLEEALNDLEARLSHsRIPEIQAELSKLeeevsrieARLREIEQKLNRLTLEK-- 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 307 ndsdELANGEVGG--DRNEKMKNQIKQMMD-VSRTQTAISVVEEDLKLLQLKLRasvstkcNLEDQVKKLEDDRNSLQAA 383
Cdd:TIGR02169 829 ----EYLEKEIQElqEQRIDLKEQIKSIEKeIENLNGKKEELEEELEELEAALR-------DLESRLGDLKKERDELEAQ 897
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 664806007 384 KAGLEDECKTLRQKVEILNELYQQKEMALQKKLSQEEYERqerehRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTE 462
Cdd:TIGR02169 898 LRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE-----DPKGEDEEIPEEELSLEDVQAELQRVEEEIRALE 971
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
325-478 |
1.52e-05 |
|
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: 47.23 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 325 MKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRAsvstkcnLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNEL 404
Cdd:COG1579 2 MPEDLRALLDLQELDSELDRLEHRLKELPAELAE-------LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 405 ---YQQ--------KEM-ALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTERSFKNQIATH 472
Cdd:COG1579 75 ikkYEEqlgnvrnnKEYeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
|
....*.
gi 664806007 473 EKKAHE 478
Cdd:COG1579 155 EAELEE 160
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
148-481 |
1.61e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 148 KTLEKNQEILDDTAKNLRVmLESEREQNvknQDLISENKKSIEKLKDVISMNASEFSEVQIALNEAKLSEEKVKSECHRV 227
Cdd:COG4372 31 EQLRKALFELDKLQEELEQ-LREELEQA---REELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 228 QEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNLLECESESEGQNKGGN 307
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 308 DSDELANGEVggDRNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAGL 387
Cdd:COG4372 187 ELLKEANRNA--EKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 388 EDECKTLRQKVEILNELYQQKEMALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTERSFKN 467
Cdd:COG4372 265 LAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQ 344
|
330
....*....|....
gi 664806007 468 QIATHEKKAHENWL 481
Cdd:COG4372 345 LLLVGLLDNDVLEL 358
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
85-270 |
1.89e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 48.54 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 85 RVYQVTEQQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLE-KNQEILDDTAKN 163
Cdd:COG5022 853 RSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDLiENLEFKTELIAR 932
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 164 LRVMLES---------EREQNVKNQDLISEN---KKSIEKLKDVISMNASEFSEVQIALNEAKlseeKVKSECHRVQEEN 231
Cdd:COG5022 933 LKKLLNNidleegpsiEYVKLPELNKLHEVEsklKETSEEYEDLLKKSTILVREGNKANSELK----NFKKELAELSKQY 1008
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 664806007 232 ARLKKKKEQLQQEIEDWSKLHAELS--EQIKSFEKSQKDLE 270
Cdd:COG5022 1009 GALQESTKQLKELPVEVAELQSASKiiSSESTELSILKPLQ 1049
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
142-517 |
2.95e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.76 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 142 KYKDKIKTLEKNQEILD---DTAKNLRVMLESEREQNVKNQDLISENKKSieklkdvismnasEFSEVQIALNEAKLSEE 218
Cdd:TIGR02169 174 KALEELEEVEENIERLDliiDEKRQQLERLRREREKAERYQALLKEKREY-------------EGYELLKEKEALERQKE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 219 KVKSECHRVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKsfeksqkdlevALThkDDNINALTnciTQLNLLECESE 298
Cdd:TIGR02169 241 AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIK-----------DLG--EEEQLRVK---EKIGELEAEIA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 299 SegqnkgGNDSDELANgevggDRNEKMKNQIKQM-MDVSRTQTAISVVEEDLKLLQLKLRAsvstkcnLEDQVKKLEDDR 377
Cdd:TIGR02169 305 S------LERSIAEKE-----RELEDAEERLAKLeAEIDKLLAEIEELEREIEEERKRRDK-------LTEEYAELKEEL 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 378 NSLQAAKAGLEDECKTLRQKVEilneLYQQKEMALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKtykrRIEEMEDE 457
Cdd:TIGR02169 367 EDLRAELEEVDKEFAETRDELK----DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIA----GIEAKINE 438
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 458 LQKTERSFKNQIATHEKKAHENwlkaraaERAIAEEKREAANLRHKLLELTQKMAMLQEE 517
Cdd:TIGR02169 439 LEEEKEDKALEIKKQEWKLEQL-------AADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
80-452 |
3.00e-05 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 47.90 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 80 LVVKDRVYQVTEQqiSEKLKTIMKEntelvqkLSNYEQKIKESKKHVQETRKQnmILSD-EAIKYKDKIKTLEKNQEILD 158
Cdd:PTZ00440 1169 ILIDHIVEQINNE--AKKSKTIMEE-------IESYKKDIDQVKKNMSKERND--HLTTfEYNAYYDKATASYENIEELT 1237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 159 DTAKNLRVmlESEREQNVKN------------QDLISENKKSIEKLKDVISMNA---SEFSEVQIA--LNEAKLSEEKVK 221
Cdd:PTZ00440 1238 TEAKGLKG--EANRSTNVDElkeiklqvfsylQQVIKENNKMENALHEIKNMYEfliSIDSEKILKeiLNSTKKAEEFSN 1315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 222 SECHRVQEENARLKKKKEQLQQEIEDWSKLHAELS-----EQIKSFEKSQKDlevaLTHKDDNINaltNCITQL--NLLE 294
Cdd:PTZ00440 1316 DAKKELEKTDNLIKQVEAKIEQAKEHKNKIYGSLEdkqidDEIKKIEQIKEE----ISNKRKEIN---KYLSNIksNKEK 1388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 295 CESESEGQNKGGNDSDELANGEV--GGDRNEKMKNQIKQMMDVSRTqtaisvVEEDLKLLQLKLRASVSTKCNLEDQVKK 372
Cdd:PTZ00440 1389 CDLHVRNASRGKDKIDFLNKHEAiePSNSKEVNIIKITDNINKCKQ------YSNEAMETENKADENNDSIIKYEKEITN 1462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 373 LEDDrNSLQAAKAGLE---DECKTLRQKVEILNELYQQKEMALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKR 449
Cdd:PTZ00440 1463 ILNN-SSILGKKTKLEkkkKEATNIMDDINGEHSIIKTKLTKSSEKLNQLNEQPNIKREGDVLNNDKSTIAYETIQYNLG 1541
|
...
gi 664806007 450 RIE 452
Cdd:PTZ00440 1542 RVK 1544
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
92-389 |
3.56e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 92 QQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLrvmlese 171
Cdd:COG4372 62 EQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQL------- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 172 REQNVKNQDLISENKKSIEKLKDVISMNASEFSEVQIALNEAKLSE-EKVKSECHRVQEENARLKKKKEQLQQEIEDWSK 250
Cdd:COG4372 135 EAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 251 LHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNLLEC--ESESEGQNKGGNDSDELANGEVGGDRNEKMKNQ 328
Cdd:COG4372 215 ELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEieELELAILVEKDTEEEELEIAALELEALEEAALE 294
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 664806007 329 IKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAGLED 389
Cdd:COG4372 295 LKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDV 355
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
148-284 |
3.72e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.08 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 148 KTLEKNQEILDDTAKnlRVMLESEREQNVKNQDLISENKKSIEKLKdvismnaSEF-SEVQIALNEAKLSEEKVKSECHR 226
Cdd:PRK12704 27 KIAEAKIKEAEEEAK--RILEEAKKEAEAIKKEALLEAKEEIHKLR-------NEFeKELRERRNELQKLEKRLLQKEEN 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 664806007 227 VQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALthkdDNINALT 284
Cdd:PRK12704 98 LDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL----ERISGLT 151
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
522-774 |
4.53e-05 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 47.09 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 522 KPMPGKPNTQNPPRRGPLSQNGSFGPSPVSGGEcSPPLTVEPPVRPLSATLNRRDMPRSEfGSVDGPLPHPRWSAEASGK 601
Cdd:PHA03307 83 ESRSTPTWSLSTLAPASPAREGSPTPPGPSSPD-PPPPTPPPASPPPSPAPDLSEMLRPV-GSPGPPPAASPPAAGASPA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 602 PSPSDPGSGTATMMNSSSrGSSPTRVLDEGKVNMAPKGPPPF--PGVPLMSTPMGGPVPPPIRYGPPPQlCGPFGPRPLP 679
Cdd:PHA03307 161 AVASDAASSRQAALPLSS-PEETARAPSSPPAEPPPSTPPAAasPRPPRRSSPISASASSPAPAPGRSA-ADDAGASSSD 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 680 PPFGPGMRPPLGLREFAPGVPPGRRDLPLHPRGFLPGHAPFRPLGSLGPREYFIPGTRLPPPTHGPQEYPPPPAVRDLLP 759
Cdd:PHA03307 239 SSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSS 318
|
250
....*....|....*
gi 664806007 760 SGSRDEPPPASQSTS 774
Cdd:PHA03307 319 SSSRESSSSSTSSSS 333
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
90-272 |
5.12e-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: 46.66 E-value: 5.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 90 TEQQISEKLKTIMKENTELVQKLsnyeqkikesKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLE 169
Cdd:pfam05557 370 TMSNYSPQLLERIEEAEDMTQKM----------QAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYS 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 170 SEREQNV--KNQDLISENKKsIEKLKDVISM-----------NASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKK 236
Cdd:pfam05557 440 KEEVDSLrrKLETLELERQR-LREQKNELEMelerrclqgdyDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKR 518
|
170 180 190
....*....|....*....|....*....|....*..
gi 664806007 237 KKEQLQQEIEDWSKLHAELSE-QIKSFEKSQKDLEVA 272
Cdd:pfam05557 519 LLKKLEDDLEQVLRLPETTSTmNFKEVLDLRKELESA 555
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
108-469 |
6.14e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 6.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 108 LVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLESEREQnvknqdlISENKK 187
Cdd:PRK02224 312 VEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREA-------VEDRRE 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 188 SIEKLKDVISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLK----------KKKEQLQ---------QEIEDW 248
Cdd:PRK02224 385 EIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEatlrtarervEEAEALLeagkcpecgQPVEGS 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 249 SKLHA--ELSEQIKSFEKSQKDLEVALTHKDDNINALTncitqlNLLECESESEG-QNKGGNDSDELANGEVGGDRNE-- 323
Cdd:PRK02224 465 PHVETieEDRERVEELEAELEDLEEEVEEVEERLERAE------DLVEAEDRIERlEERREDLEELIAERRETIEEKRer 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 324 -----KMKNQIKQMMDVSR--TQTAISVVE---EDLKLLQLKLRAsvstkcnLEDQVKKLEDDRNSLqAAKAGLEDECKT 393
Cdd:PRK02224 539 aeelrERAAELEAEAEEKReaAAEAEEEAEearEEVAELNSKLAE-------LKERIESLERIRTLL-AAIADAEDEIER 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 394 LRQKVEILNELY-QQKEMALQKKLSQEEYERQEREHRLSAADEK---AVSAAEEVKTYKRRIEEMEDELQKTERSFKNQI 469
Cdd:PRK02224 611 LREKREALAELNdERRERLAEKRERKRELEAEFDEARIEEAREDkerAEEYLEQVEEKLDELREERDDLQAEIGAVENEL 690
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
523-775 |
7.82e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.47 E-value: 7.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 523 PMPGKPNTQNPPRRGPLSQNGSFGPSPVSGGECSPPLTVEPPVRPlsatlnRRDMPRSEFGSV--------DGPLPHPRW 594
Cdd:PHA03247 2639 DPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRP------RRRAARPTVGSLtsladpppPPPTPEPAP 2712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 595 SAEASGKPSPSDPGSGT----ATMMNSSSRGSSPTRVLDEGKvnmAPKGPPPFPGVPLMSTPMGGPVPPPIRYGPPPQLC 670
Cdd:PHA03247 2713 HALVSATPLPPGPAAARqaspALPAAPAPPAVPAGPATPGGP---ARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVA 2789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 671 GPFGPRPLPPPFGPGMRPPLGLREFAPGVPPGRRDLPLHP-----RGFLPGHAPFRPLGSLGPREYFIPG---TRLPPpt 742
Cdd:PHA03247 2790 SLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPpptsaQPTAPPPPPGPPPPSLPLGGSVAPGgdvRRRPP-- 2867
|
250 260 270
....*....|....*....|....*....|...
gi 664806007 743 hgPQEYPPPPAVRDLLPSGSRDEPPPASQSTSQ 775
Cdd:PHA03247 2868 --SRSPAAKPAAPARPPVRRLARPAVSRSTESF 2898
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
63-197 |
8.09e-05 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 43.20 E-value: 8.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 63 TAFLGIASFAI-------FLWRTVL-VVKDRvyqvtEQQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQEtrkqnm 134
Cdd:cd06503 1 TLIWQIINFLIllfilkkFLWKPILkALDER-----EEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQE------ 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 664806007 135 ILsDEAIKYKDKIKtleknQEILDDTAKnlrvmlESEREQNVKNQDLISENKKSIEKLKDVIS 197
Cdd:cd06503 70 II-EEARKEAEKIK-----EEILAEAKE------EAERILEQAKAEIEQEKEKALAELRKEVA 120
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
119-409 |
9.37e-05 |
|
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: 46.21 E-value: 9.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 119 IKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLESEREQNVKNQDLISENKKSIEKLKDVI-- 196
Cdd:pfam05911 481 IRCALQDINDSLPEADSCLSSGHPSTDASCDYITCKENSSVVEKEGSVSGDDKSSEETSKQSIQQDLSKAISKIIDFVeg 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 197 -SMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQqEIEDWSKLH-------AELSEQIKSFEKSQKD 268
Cdd:pfam05911 561 lSKEALDDQDTSSDSSELSEVLQQFSATCNDVLSGKADLEDFVLELS-HILDWISNHcfslldvSSMEDEIKKHDCIDKV 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 269 --LEVALTHKDDNINALTNCITQLNLLECESESEGQNKGGNDSDELANGEVGGDRNEKMKNQIKQMMDVSRTQTAIS--- 343
Cdd:pfam05911 640 tlSENKVAQVDNGCSEIDNLSSDPEIPSDGPLVSGSNDLKTEENKRLKEEFEQLKSEKENLEVELASCTENLESTKSqlq 719
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 664806007 344 VVEEDLKLLQLKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEIL-NELYQQKE 409
Cdd:pfam05911 720 ESEQLIAELRSELASLKESNSLAETQLKCMAESYEDLETRLTELEAELNELRQKFEALeVELEEEKN 786
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
98-313 |
1.07e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.78 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 98 LKTIMKENTELVQ----KLSNYEQKIKESKKHVQETRKQNmilSDEAIKYKDKIKTLEKNQEilddTAKNLRVMLESERE 173
Cdd:PHA02562 172 NKDKIRELNQQIQtldmKIDHIQQQIKTYNKNIEEQRKKN---GENIARKQNKYDELVEEAK----TIKAEIEELTDELL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 174 QNVKNQDLISENKKSIEKLKDVISMNASEFSEV---------------QIALNEAKLSEekvksechrVQEENARLKKKK 238
Cdd:PHA02562 245 NLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVikmyekggvcptctqQISEGPDRITK---------IKDKLKELQHSL 315
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 664806007 239 EQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEvalTHKDDninaLTNCITQLNLLECESEsEGQNKGGNDSDELA 313
Cdd:PHA02562 316 EKLDTAIDELEEIMDEFNEQSKKLLELKNKIS---TNKQS----LITLVDKAKKVKAAIE-ELQAEFVDNAEELA 382
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
348-517 |
1.09e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 348 DLKLLQLKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELY---QQKEMALQKKLSQEEYERQ 424
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELeeaQAEEYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 425 EREHRLSAADEKAVSAAEEVKTYKRRIEEMEDEL---QKTERSFKNQIATHEKKAHENWLKARAAERAIAEEKREAANLR 501
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELeelEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
170
....*....|....*.
gi 664806007 502 HKLLELTQKMAMLQEE 517
Cdd:COG1196 386 EELLEALRAAAELAAQ 401
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
96-273 |
1.25e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 96 EKLKTIMKENTELVQKLSNYEQKIKESKKHVQEtrkqnmiLSDEAIK-YKDKIKTLEK--NQEIlddTAKNLRVMLESER 172
Cdd:PRK03918 549 EKLEELKKKLAELEKKLDELEEELAELLKELEE-------LGFESVEeLEERLKELEPfyNEYL---ELKDAEKELEREE 618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 173 EQNVKNQDLISENKKSIEKLKDVISMNASEFSEVQIALNE---AKLSEEKVK--SECHRVQEENARLKKKKEQLQQEIEd 247
Cdd:PRK03918 619 KELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEeeyEELREEYLElsRELAGLRAELEELEKRREEIKKTLE- 697
|
170 180
....*....|....*....|....*.
gi 664806007 248 wsKLHAELsEQIKSFEKSQKDLEVAL 273
Cdd:PRK03918 698 --KLKEEL-EEREKAKKELEKLEKAL 720
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
522-656 |
1.30e-04 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 45.83 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 522 KPMPGKPNTQNPPRRGPlsqngsfgpspvsgGECSPPLTVEPPVRPLSATLNRRDMPRSEFGSVDGPLPHPRWSAEASGK 601
Cdd:PHA03378 675 QPSPTGANTMLPIQWAP--------------GTMQPPPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAA 740
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 664806007 602 PSPSDPGSGTATMMNSSSRGSSPTRVLDEGKVNMAPKGPPPFPGVPlMSTPMGGP 656
Cdd:PHA03378 741 PGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAP-QQRPRGAP 794
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
556-756 |
1.57e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 45.55 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 556 SPPLTVEPPvrpLSATLNRRDMPRSEFGSVDGPLPHPRWSAEASGKPSPSDPGSGTATmmNSSSRGSSPTRVLDEGKVNM 635
Cdd:PHA03307 759 SNPSLVPAK---LAEALALLEPAEPQRGAGSSPPVRAEAAFRRPGRLRRSGPAADAAS--RTASKRKSRSHTPDGGSESS 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 636 APKGPPP--FPGVPLMSTPMGGPVPPPIRYGPPPQLCGPFGPRPLPPPFGPGMRPPLGLREFAPGVPPGRRDLPLHPRGF 713
Cdd:PHA03307 834 GPARPPGaaARPPPARSSESSKSKPAAAGGRARGKNGRRRPRPPEPRARPGAAAPPKAAAAAPPAGAPAPRPRPAPRVKL 913
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 664806007 714 LPghapfRPLGSLGPREYFipgTRLPP-PTHGPqeyPPPPAVRD 756
Cdd:PHA03307 914 GP-----MPPGGPDPRGGF---RRVPPgDLHTP---APSAAALA 946
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
84-416 |
2.32e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 44.82 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 84 DRVYQVTEQQISEKLKTIMKENTELVQKLSNYEQKIK--ESKKHVQETRKQNMILS---------------DEAIKYKDK 146
Cdd:PTZ00440 709 KKQLNNIEQDISNSLNQYTIKYNDLKSSIEEYKEEEEklEVYKHQIINRKNEFILHlyendkdlpdgkntyEEFLQYKDT 788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 147 IktLEKNQEILDDTaknlrVMLESEREqnvKNQDLISENKKSIEKLKDVISMNaseFSEVQIALNeaKLSEEKVKSECHR 226
Cdd:PTZ00440 789 I--LNKENKISNDI-----NILKENKK---NNQDLLNSYNILIQKLEAHTEKN---DEELKQLLQ--KFPTEDENLNLKE 853
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 227 VQEENARLKKKKEQLQQEIEDWSK---LHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNLLECESESEGQN 303
Cdd:PTZ00440 854 LEKEFNENNQIVDNIIKDIENMNKninIIKTLNIAINRSNSNKQLVEHLLNNKIDLKNKLEQHMKIINTDNIIQKNEKLN 933
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 304 KGGNDSDELANGEvggdrnekmknqiKQMMDVSRTQTAISVVeedlKLLQLKLRASVSTKCNLEDQVKKLEDDrnslqaa 383
Cdd:PTZ00440 934 LLNNLNKEKEKIE-------------KQLSDTKINNLKMQIE----KTLEYYDKSKENINGNDGTHLEKLDKE------- 989
|
330 340 350
....*....|....*....|....*....|...
gi 664806007 384 kaglEDECKTLRQKVEILNELYQqkemALQKKL 416
Cdd:PTZ00440 990 ----KDEWEHFKSEIDKLNVNYN----ILNKKI 1014
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
81-467 |
2.39e-04 |
|
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: 45.04 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 81 VVKDRVYQVTEQQISEKLKTIMKENTELV-QKLSNYEQKiKESKKHVQETRKQNMILSdEAIKYKDKIKTLEKNQE---- 155
Cdd:TIGR01612 444 IFKDDFDEFNKPIPKSKLKALEKRFFEIFeEEWGSYDIK-KDIDENSKQDNTVKLILM-RMKDFKDIIDFMELYKPdevp 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 156 ----ILDDTAKNLRVMLESEREQNVK----------------NQDLISENKKSIeKLKDVISMNASEFSEV---QIALNE 212
Cdd:TIGR01612 522 skniIGFDIDQNIKAKLYKEIEAGLKesyelaknwkkliheiKKELEEENEDSI-HLEKEIKDLFDKYLEIddeIIYINK 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 213 AKLS-EEKVK--SECHRVQEENARLKKKKEQLQQEIEDWSKLHA-ELSEQIKSFEKSQKDLEVALTH-KDDNINALTNci 287
Cdd:TIGR01612 601 LKLElKEKIKniSDKNEYIKKAIDLKKIIENNNAYIDELAKISPyQVPEHLKNKDKIYSTIKSELSKiYEDDIDALYN-- 678
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 288 tQLNLLECEsesegqnkggNDSDELANGEVGGDRNEKMKNQIK--QMMDVSRTQTAISVVEEDL-KLLQ--LKLRASVST 362
Cdd:TIGR01612 679 -ELSSIVKE----------NAIDNTEDKAKLDDLKSKIDKEYDkiQNMETATVELHLSNIENKKnELLDiiVEIKKHIHG 747
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 363 KCNlEDQVKKLEDDRNSLQAAKAGLEDECKtlrqkveilnelYQQKEMALQKKLSQEEYERQEREHRLSAADEKAVSAAE 442
Cdd:TIGR01612 748 EIN-KDLNKILEDFKNKEKELSNKINDYAK------------EKDELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYD 814
|
410 420
....*....|....*....|....*
gi 664806007 443 EVKTYKRRIEEMEDELQKTERSFKN 467
Cdd:TIGR01612 815 KSKEYIKTISIKEDEIFKIINEMKF 839
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
90-460 |
2.96e-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: 44.57 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 90 TEQQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNmilsdeaiKYKDKIKTLEKNQEILDDTAKNLRVMLE 169
Cdd:TIGR00618 227 ELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIE--------ELRAQEAVLEETQERINRARKAAPLAAH 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 170 SER-EQNVKNQDLISENKKSIEKLKDVISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIEDW 248
Cdd:TIGR00618 299 IKAvTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLT 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 249 SKLHAElsEQIKSFEKSQKDLEVALTHKDDNINAltnciTQLNLLECESESEGQNKGGNDSDELangevggdrnEKMKNQ 328
Cdd:TIGR00618 379 QHIHTL--QQQKTTLTQKLQSLCKELDILQREQA-----TIDTRTSAFRDLQGQLAHAKKQQEL----------QQRYAE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 329 IKQMMDVSRTQTAISVVEEDLKLLQ-----LKLRASVSTKCNLEDQVKKLEDDRNSLQAakaglEDECKTLRQKVEILNE 403
Cdd:TIGR00618 442 LCAAAITCTAQCEKLEKIHLQESAQslkerEQQLQTKEQIHLQETRKKAVVLARLLELQ-----EEPCPLCGSCIHPNPA 516
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 664806007 404 LYQQKEM-ALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQK 460
Cdd:TIGR00618 517 RQDIDNPgPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSI 574
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
198-384 |
3.10e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 198 MNASEFSEVQIALNEAKLSEEkvksECHRVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQ--KDLEVALTH 275
Cdd:COG4717 68 LNLKELKELEEELKEAEEKEE----EYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQelEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 276 KDDNINALTNCITQLNLL--ECESESEGQNKGGNDSDELANgevggDRNEKMKNQIKQMM-DVSRTQTAISVVEEDLKLL 352
Cdd:COG4717 144 LPERLEELEERLEELRELeeELEELEAELAELQEELEELLE-----QLSLATEEELQDLAeELEELQQRLAELEEELEEA 218
|
170 180 190
....*....|....*....|....*....|..
gi 664806007 353 QLKLRAsvstkcnLEDQVKKLEDDRNSLQAAK 384
Cdd:COG4717 219 QEELEE-------LEEELEQLENELEAAALEE 243
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
92-405 |
3.17e-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: 44.07 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 92 QQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQnmiLSDEAIKYKDKIKTLEKN-QEILDD--TAKNL---- 164
Cdd:pfam06160 96 DDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKT---LLANRFSYGPAIDELEKQlAEIEEEfsQFEELtesg 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 165 -----RVMLESEREQNVKNQDLISENKKSIEKLKDVIsmnASEFSEVQIALNEAK-----LSEEKVKSECHRVQEENARL 234
Cdd:pfam06160 173 dyleaREVLEKLEEETDALEELMEDIPPLYEELKTEL---PDQLEELKEGYREMEeegyaLEHLNVDKEIQQLEEQLEEN 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 235 KKKKEQLqqEIEDWSKLHAELSEQI--------------KSFEKSQKDLEVALTHKDDNINALTNCITQLnllecesese 300
Cdd:pfam06160 250 LALLENL--ELDEAEEALEEIEERIdqlydllekevdakKYVEKNLPEIEDYLEHAEEQNKELKEELERV---------- 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 301 gqnkggNDSDELANGEVGgdRNEKMKNQIKQMM-DVSRTQTAI-------SVVEEDLKllqlklrasvstkcNLEDQVKK 372
Cdd:pfam06160 318 ------QQSYTLNENELE--RVRGLEKQLEELEkRYDEIVERLeekevaySELQEELE--------------EILEQLEE 375
|
330 340 350
....*....|....*....|....*....|....*..
gi 664806007 373 LEDDRNSLQAAKAGLEDECKTLRQKVE----ILNELY 405
Cdd:pfam06160 376 IEEEQEEFKESLQSLRKDELEAREKLDefklELREIK 412
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
93-256 |
3.41e-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: 43.47 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 93 QISEKLKTIMKENTELVqklsnyeqkiKESKKHVqetRKQNMILSDEAIKYKDKIKTLEKNqeilddtaknLRVMLESER 172
Cdd:smart00787 140 KLLEGLKEGLDENLEGL----------KEDYKLL---MKELELLNSIKPKLRDRKDALEEE----------LRQLKQLED 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 173 EQNVKNQDLISENKKSIEKLKDVISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQ-EIEDWSKL 251
Cdd:smart00787 197 ELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGfTFKEIEKL 276
|
....*
gi 664806007 252 HAELS 256
Cdd:smart00787 277 KEQLK 281
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
103-264 |
3.41e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.36 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 103 KENtELVQKLSNYEQKIK------ESKKHVQETRKQNMILSDEAIKYKDKIKTLeknqeilddtaknlrvmleSEREQNV 176
Cdd:COG1340 134 EEK-ELVEKIKELEKELEkakkalEKNEKLKELRAELKELRKEAEEIHKKIKEL-------------------AEEAQEL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 177 KNQdlISENKKSIEKLKDVISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIED--WSKLHAE 254
Cdd:COG1340 194 HEE--MIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKeeLEEKAEE 271
|
170
....*....|
gi 664806007 255 LSEQIKSFEK 264
Cdd:COG1340 272 IFEKLKKGEK 281
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
107-270 |
3.71e-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: 42.99 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 107 ELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLESEREQ--NVKNQDLISE 184
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgNVRNNKEYEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 185 NKKSIEKLKDVISmnasEFSEVQIALNEaklseekvksechRVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEK 264
Cdd:COG1579 94 LQKEIESLKRRIS----DLEDEILELME-------------RIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
....*.
gi 664806007 265 SQKDLE 270
Cdd:COG1579 157 ELEELE 162
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
84-259 |
3.92e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.67 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 84 DRV---YQVTE------QQISEKLKTIMKENTELVQKLSnyEQKIKESkkhvqetrkqnmILSDEAIKYKDKIKTLEKNQ 154
Cdd:PRK04778 334 DRVkqsYTLNEselesvRQLEKQLESLEKQYDEITERIA--EQEIAYS------------ELQEELEEILKQLEEIEKEQ 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 155 EILDDTAKNLRvmlESERE--QNVKN-QDLISENKKSIEKL------KDVISM--NAS-EFSEVQIALNEAKLSEEKVKS 222
Cdd:PRK04778 400 EKLSEMLQGLR---KDELEarEKLERyRNKLHEIKRYLEKSnlpglpEDYLEMffEVSdEIEALAEELEEKPINMEAVNR 476
|
170 180 190
....*....|....*....|....*....|....*..
gi 664806007 223 ECHRVQEENARLKKKKEQLQQeiedwsklHAELSEQI 259
Cdd:PRK04778 477 LLEEATEDVETLEEETEELVE--------NATLTEQL 505
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
102-531 |
4.44e-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: 43.94 E-value: 4.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 102 MKENTELVQKLSN-YEQKIKESKKHV-----QETRKQNmilsdeaiKYKDKIKTLEKNQEILDDTAKNLRVMLESEREQN 175
Cdd:pfam05483 217 LKEDHEKIQHLEEeYKKEINDKEKQVsllliQITEKEN--------KMKDLTFLLEESRDKANQLEEKTKLQDENLKELI 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 176 VKNQDLISENKKSIEKLKDVISMNASEFSEVQIAlneaklseekVKSECHRVQEENARLkkkkEQLQQEIEDWSKLHAEL 255
Cdd:pfam05483 289 EKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIA----------TKTICQLTEEKEAQM----EELNKAKAAHSFVVTEF 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 256 SEQIKSFEKSQKDLEVALTHKDDNINALTncitqLNLLECESESEGQNKGGNDSD-ELANGEVGGDRNEKMKNQIKQMMD 334
Cdd:pfam05483 355 EATTCSLEELLRTEQQRLEKNEDQLKIIT-----MELQKKSSELEEMTKFKNNKEvELEELKKILAEDEKLLDEKKQFEK 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 335 VS-----RTQTAISVV---EEDLKLLQLKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNElyQ 406
Cdd:pfam05483 430 IAeelkgKEQELIFLLqarEKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQ--E 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 407 QKEMALQ-KKLSQEEYERQEREHRLSaadeKAVSAAEEVKTYKR-RIEEMEDELQKTERSFKNQIATHEKKAHENWLKAR 484
Cdd:pfam05483 508 ASDMTLElKKHQEDIINCKKQEERML----KQIENLEEKEMNLRdELESVREEFIQKGDEVKCKLDKSEENARSIEYEVL 583
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 664806007 485 AAERAIAEEKREAANLRHKLLELTQKMAMLQEEPVIVKPMPGKPNTQ 531
Cdd:pfam05483 584 KKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQ 630
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
77-251 |
4.51e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 43.26 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 77 RTVLVVKDRVYQVTEQQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMilsdeaikykdkiKTLEKNQEI 156
Cdd:pfam15905 165 RNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETE-------------KLLEYITEL 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 157 lddtaKNLRVMLESEREQNVKNQDLISENKKSIEKLKDVISMNASEFSEVQIALNEA-----KLSEEKVKSECHRVQEEN 231
Cdd:pfam15905 232 -----SCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKcklleSEKEELLREYEEKEQTLN 306
|
170 180
....*....|....*....|
gi 664806007 232 ARLKKKKEQLQQEIEDWSKL 251
Cdd:pfam15905 307 AELEELKEKLTLEEQEHQKL 326
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
95-268 |
4.64e-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: 43.08 E-value: 4.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 95 SEKLKTIMKENTELVQKLSNYEqkikeSKKHVQETRKQNMilsdeaikyKDKIKTLEKNQEILDDtaknlrvmlesEREQ 174
Cdd:smart00787 108 SPDVKLLMDKQFQLVKTFARLE-----AKKMWYEWRMKLL---------EGLKEGLDENLEGLKE-----------DYKL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 175 NVKNQDLISENKKSIEKLKDVISMNASEFSEVQIALNEAKLSE-----EKVKSECHRVQEEN---ARLKKKKEQLQQEIE 246
Cdd:smart00787 163 LMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTEldrakEKLKKLLQEIMIKVkklEELEEELQELESKIE 242
|
170 180
....*....|....*....|..
gi 664806007 247 DWSKLHAELSEQIKSFEKSQKD 268
Cdd:smart00787 243 DLTNKKSELNTEIAEAEKKLEQ 264
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
106-468 |
5.42e-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: 5.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 106 TELVQKLSNYEQKIKESKKHVQETRKQNMIL---SDEAIKYKDKIkTLEKNQEildDTAKNLRVMLESEREQNVKNQDLI 182
Cdd:TIGR00606 182 TRYIKALETLRQVRQTQGQKVQEHQMELKYLkqyKEKACEIRDQI-TSKEAQL---ESSREIVKSYENELDPLKNRLKEI 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 183 SENKKSIEKLKDVISMNASEFSEVQIALNEAKL--------SEEKVKSECHRVQEENARLKKKKEQLQQEIEDWSKLHAE 254
Cdd:TIGR00606 258 EHNLSKIMKLDNEIKALKSRKKQMEKDNSELELkmekvfqgTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRL 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 255 LSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNLlecESESEGQNKGGNDSDELANGEV----GGDRNEKMKNQ-I 329
Cdd:TIGR00606 338 LNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLAT---RLELDGFERGPFSERQIKNFHTlvieRQEDEAKTAAQlC 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 330 KQMMDVSRT-QTAISVVEEDLKLLQLKLRasvSTKCNLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQK 408
Cdd:TIGR00606 415 ADLQSKERLkQEQADEIRDEKKGLGRTIE---LKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAE 491
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 664806007 409 EMA----LQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTERSFKNQ 468
Cdd:TIGR00606 492 KNSltetLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIK 555
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
88-462 |
7.52e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.13 E-value: 7.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 88 QVTEQQIseKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLrvm 167
Cdd:TIGR02169 344 EIEEERK--RRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRL--- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 168 leSEREQNVKNQ--DLISENKKSIEKLKDVI-SMNASEFSEVQIALNEAKLSEE---------KVKSECHRVQEENARLK 235
Cdd:TIGR02169 419 --SEELADLNAAiaGIEAKINELEEEKEDKAlEIKKQEWKLEQLAADLSKYEQElydlkeeydRVEKELSKLQRELAEAE 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 236 KKKEQLQQEI-----------EDWSKLHAELSEQIKSFEKSQKDLEVAL------------------------------- 273
Cdd:TIGR02169 497 AQARASEERVrggraveevlkASIQGVHGTVAQLGSVGERYATAIEVAAgnrlnnvvveddavakeaiellkrrkagrat 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 274 ---------THKDDNINALTNCIT-QLNLLECESESEG------QNKGGNDSDELANGEVGGDRNEKMKNQIkqmMDVSR 337
Cdd:TIGR02169 577 flplnkmrdERRDLSILSEDGVIGfAVDLVEFDPKYEPafkyvfGDTLVVEDIEAARRLMGKYRMVTLEGEL---FEKSG 653
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 338 TQTAISVVEEDLKLLQLKLRASVStkcNLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEI----LNELYQQKEMaLQ 413
Cdd:TIGR02169 654 AMTGGSRAPRGGILFSRSEPAELQ---RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDasrkIGEIEKEIEQ-LE 729
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 664806007 414 KKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTE 462
Cdd:TIGR02169 730 QEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLE 778
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
89-415 |
7.67e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.97 E-value: 7.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 89 VTEQQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILS-------------DEAIK-----YKDKIKTL 150
Cdd:PRK01156 402 IDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNgqsvcpvcgttlgEEKSNhiinhYNEKKSRL 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 151 EKNQEILDDTAKNLrvmlESEREQNVKNQDLIseNKKSIEKLkdVISMNASEFSEVQIALNEAKLSEEKVKSEchRVQEE 230
Cdd:PRK01156 482 EEKIREIEIEVKDI----DEKIVDLKKRKEYL--ESEEINKS--INEYNKIESARADLEDIKIKINELKDKHD--KYEEI 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 231 NARLKKKK-EQLQQEIEDWSKLHAELSeqiksfeksQKDLEVALTHKDDNINALTNCITQLNLLECE---SESEGQNKGG 306
Cdd:PRK01156 552 KNRYKSLKlEDLDSKRTSWLNALAVIS---------LIDIETNRSRSNEIKKQLNDLESRLQEIEIGfpdDKSYIDKSIR 622
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 307 NDSDELANgevggdrnekMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKL------RASVSTKCN-LEDQVKKLEDDRNS 379
Cdd:PRK01156 623 EIENEANN----------LNNKYNEIQENKILIEKLRGKIDNYKKQIAEIdsiipdLKEITSRINdIEDNLKKSRKALDD 692
|
330 340 350
....*....|....*....|....*....|....*.
gi 664806007 380 LQAAKAGLEDECKTLRQKVEILNELYQQKEMALQKK 415
Cdd:PRK01156 693 AKANRARLESTIEILRTRINELSDRINDINETLESM 728
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
91-464 |
7.90e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.24 E-value: 7.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 91 EQQISEKLKTIMKENTELVQKLSNYEQKI---KESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRVM 167
Cdd:pfam01576 228 QAQIAELRAQLAKKEEELQAALARLEEETaqkNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTE 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 168 LESEREQNVKNQDLISENKKSIEKLKDVIsmnasefsEVQIALNEAKLSEEKVK--SECHRVQEENARLKKKKEQLQQEI 245
Cdd:pfam01576 308 LEDTLDTTAAQQELRSKREQEVTELKKAL--------EEETRSHEAQLQEMRQKhtQALEELTEQLEQAKRNKANLEKAK 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 246 EDWSKLHAELSEQIKSFEKSQKDLEvaltHKDDNINALTNcitQLNLLECESE---SEGQNKGGNDSDELANgeVGGDRN 322
Cdd:pfam01576 380 QALESENAELQAELRTLQQAKQDSE----HKRKKLEGQLQ---ELQARLSESErqrAELAEKLSKLQSELES--VSSLLN 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 323 EKMKNQIKQMMDVSRTQTAISVVEEdlkLLQLKLRAsvstKCNLEDQVKKLEDDRNSLQAAkagLEDECKTlRQKVEILN 402
Cdd:pfam01576 451 EAEGKNIKLSKDVSSLESQLQDTQE---LLQEETRQ----KLNLSTRLRQLEDERNSLQEQ---LEEEEEA-KRNVERQL 519
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 664806007 403 ELYQQKEMALQKKLSQEEYErqerehrLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTERS 464
Cdd:pfam01576 520 STLQAQLSDMKKKLEEDAGT-------LEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKT 574
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
92-223 |
1.05e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 92 QQISEKLKTIMKENTE----LVQKLSN----YEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEildDTAKN 163
Cdd:PRK00409 501 ENIIEEAKKLIGEDKEklneLIASLEElereLEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAE---KEAQQ 577
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 664806007 164 LRVMLESEREQNVKNQDLISENKKSIEKLKDVIsmnasefsEVQIALNEA--KLSEEKVKSE 223
Cdd:PRK00409 578 AIKEAKKEADEIIKELRQLQKGGYASVKAHELI--------EARKRLNKAneKKEKKKKKQK 631
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
93-516 |
1.29e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.20 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 93 QISEKLKTIMKENTELVQKLSNYEQKikesKKHVQETRKQNMILSDEAIKYKDKIKT--------LEKNQEILDDTAKNL 164
Cdd:PRK01156 208 DDEKSHSITLKEIERLSIEYNNAMDD----YNNLKSALNELSSLEDMKNRYESEIKTaesdlsmeLEKNNYYKELEERHM 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 165 RVmlesEREQNVKNQDLISE---NKKSIEKLKDVISMNASEFSEVQIALNEAKLSE------EKVKSECHRVQEENARLK 235
Cdd:PRK01156 284 KI----INDPVYKNRNYINDyfkYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQkdyndyIKKKSRYDDLNNQILELE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 236 ----------KKKEQLQQEIEDWSK----LHAELSEQIKSFE-------KSQKDLEVALTHKDDNINALTNCITQLNLLE 294
Cdd:PRK01156 360 gyemdynsylKSIESLKKKIEEYSKnierMSAFISEILKIQEidpdaikKELNEINVKLQDISSKVSSLNQRIRALRENL 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 295 CESESEGQNKGGNDSDELANGEVGGDRNEKMKNQIKQmmDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLE-DQVKKL 373
Cdd:PRK01156 440 DELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNE--KKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLEsEEINKS 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 374 EDDRNSLQAAKAGLED---ECKTLRQKVEILNELYQQ-KEMALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVktyKR 449
Cdd:PRK01156 518 INEYNKIESARADLEDikiKINELKDKHDKYEEIKNRyKSLKLEDLDSKRTSWLNALAVISLIDIETNRSRSNEI---KK 594
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 664806007 450 RIEEMEDELQKTERSFKNqiathEKKAHENWLKaraaeraiaEEKREAANLRHKLLELTQKMAMLQE 516
Cdd:PRK01156 595 QLNDLESRLQEIEIGFPD-----DKSYIDKSIR---------EIENEANNLNNKYNEIQENKILIEK 647
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
98-417 |
1.39e-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: 42.34 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 98 LKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQ-----------NMILSDEAI--KYKDKIKTLEKNQEI-------- 156
Cdd:TIGR00606 739 IDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLlgtimpeeesaKVCLTDVTImeRFQMELKDVERKIAQqaaklqgs 818
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 157 -LDDTAKNLRVMLESEREQNVK-------NQDLISENKKSIEKLKDVISMNASEFSEVQIALNEAKLSEEKVKSECHRVQ 228
Cdd:TIGR00606 819 dLDRTVQQVNQEKQEKQHELDTvvskielNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQ 898
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 229 EENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALthkDDNINALTNCITQLNLLECESESEGQNKGGND 308
Cdd:TIGR00606 899 SLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKV---NDIKEKVKNIHGYMKDIENKIQDGKDDYLKQK 975
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 309 SDELANGEVGGDRNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQVKKLEDDRNSLQ-----AA 383
Cdd:TIGR00606 976 ETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQvlqmkQE 1055
|
330 340 350
....*....|....*....|....*....|....*..
gi 664806007 384 KAGLEDECKTL-RQKVEILNEL--YQQKEMALQKKLS 417
Cdd:TIGR00606 1056 HQKLEENIDLIkRNHVLALGRQkgYEKEIKHFKKELR 1092
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
110-406 |
2.74e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.19 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 110 QKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKnlrvMLESEREQNvKNQDLISENKKSI 189
Cdd:PRK10929 65 ERAKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPNMSTDALEQEILQVSSQ----LLEKSRQAQ-QEQDRAREISDSL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 190 EKLkdvismnASEFSEVQIALNEAK------------LSEEKVKSechrVQEENARLKKKKEQLQ---------QEIedw 248
Cdd:PRK10929 140 SQL-------PQQQTEARRQLNEIErrlqtlgtpntpLAQAQLTA----LQAESAALKALVDELElaqlsannrQEL--- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 249 SKLHAELseqiksFEKSQKDLevalthkDDNINALTNcitQLNLL---ECESESEGQNKGGNDSDELANG---EVGGDRN 322
Cdd:PRK10929 206 ARLRSEL------AKKRSQQL-------DAYLQALRN---QLNSQrqrEAERALESTELLAEQSGDLPKSivaQFKINRE 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 323 -EKMKNQIKQMMDV-------SRTQT-----AISVVEE------DLKLLQLKLRASVST--------------------K 363
Cdd:PRK10929 270 lSQALNQQAQRMDLiasqqrqAASQTlqvrqALNTLREqsqwlgVSNALGEALRAQVARlpempkpqqldtemaqlrvqR 349
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 664806007 364 CNLEDQVKKLEDDRNSLQAAKAGLEDECK-----TLRQKVEILNELYQ 406
Cdd:PRK10929 350 LRYEDLLNKQPQLRQIRQADGQPLTAEQNrildaQLRTQRELLNSLLS 397
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
523-774 |
3.23e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.08 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 523 PMPGKPNTQNPPRRGPLSQNGSFGPSPVSGGECSPPLTVEPPVRPLSATLNRRDMPRSEFGSVDGPLPHPRWSAEASGKP 602
Cdd:PHA03247 2554 PLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSP 2633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 603 SPSDPGSGTATMMN---------SSSRGSSPTRVLDEGKVNMA---PKGPPPfPGVPlmstPMGGPVPPPIrygpppqlc 670
Cdd:PHA03247 2634 AANEPDPHPPPTVPpperprddpAPGRVSRPRRARRLGRAAQAsspPQRPRR-RAAR----PTVGSLTSLA--------- 2699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 671 gpfgprplpppfgpgmRPPLGLREFAPGVPPGRRDLPLHP-----RGFLPGH--APFRPLGSLGPREYFIPGTRLPPPTH 743
Cdd:PHA03247 2700 ----------------DPPPPPPTPEPAPHALVSATPLPPgpaaaRQASPALpaAPAPPAVPAGPATPGGPARPARPPTT 2763
|
250 260 270
....*....|....*....|....*....|.
gi 664806007 744 GPQEYPPPPAVRDLLPSGSRDEPPPASQSTS 774
Cdd:PHA03247 2764 AGPPAPAPPAAPAAGPPRRLTRPAVASLSES 2794
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
154-294 |
3.74e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 40.05 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 154 QEILDDTAKNLRVMLESEREQNVKN--------QDLISENKKSIEKLKDVISMNASEFSEVQIALNE------AKLSEEK 219
Cdd:cd22656 94 AEILELIDDLADATDDEELEEAKKTikallddlLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETlekalkDLLTDEG 173
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 664806007 220 VKSECHRVQEENARLKKKKE----QLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNLLE 294
Cdd:cd22656 174 GAIARKEIKDLQKELEKLNEeyaaKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPALEKLQ 252
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
144-258 |
3.80e-03 |
|
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: 38.00 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 144 KDKIKTLEKNQEILDDTAKNLRVMLESEREQNVKNQD-------LISENKKSIEKLKdvismnaSEFSEVQIALNEAKLS 216
Cdd:pfam07926 7 QSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQnyerelvLHAEDIKALQALR-------EELNELKAEIAELKAE 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 664806007 217 EEKVKSEchrVQEENARLKKKKEQLQQEIEDWSKLHAELSEQ 258
Cdd:pfam07926 80 AESAKAE---LEESEESWEEQKKELEKELSELEKRIEDLNEQ 118
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
320-518 |
4.07e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 320 DRNEKMKNQIKQMMD-----VSRTQTAISVVEEDLKLLQLKLRAsvstkcnLEDQVKKLEDDRNSLQAAKAGLEDECKTL 394
Cdd:COG4942 23 AEAEAELEQLQQEIAelekeLAALKKEEKALLKQLAALERRIAA-------LARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 395 RQKVEILNELYQQKEMALQKK------------------------LSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRR 450
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLgrqpplalllspedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 664806007 451 IEEMEDELQKTERSFKNQIATHEKKAHENWLKARAAERAIAEEKREAANLRHKLLELTQKMAMLQEEP 518
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
58-407 |
4.45e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 58 KPVFITAFLGIASFAIFlwrtVLVVKDRVYQVTEQ-QI-SEKLKTIMKENTELVQKLSNYEQKIKeskkhvqetrkqnMI 135
Cdd:COG3206 28 KWLILLVFLLVLALALL----YALLLPPVYEASATlLVePQSSDVLLSGLSSLSASDSPLETQIE-------------IL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 136 LSDE----AIK----YKDKIKTLEKNQEILDDTAKNLRVmlesereQNVKNQDLI-----SENKksiEKLKDVISMNASE 202
Cdd:COG3206 91 KSRPvlerVVDklnlDEDPLGEEASREAAIERLRKNLTV-------EPVKGSNVIeisytSPDP---ELAAAVANALAEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 203 FSEVQIALNEAKLSEEKVksechRVQEENARLKKKKEQLQQEIEDWSKLH--AELSEQIKSFEKSQKDLEVALTHKDDNI 280
Cdd:COG3206 161 YLEQNLELRREEARKALE-----FLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 281 NALTNCITQLnllecesESEGQNKGGNDSDELANGEVGGDRNE--KMKNQIKQMM--------DVSRTQTAISVVEEDLK 350
Cdd:COG3206 236 AEAEARLAAL-------RAQLGSGPDALPELLQSPVIQQLRAQlaELEAELAELSarytpnhpDVIALRAQIAALRAQLQ 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 664806007 351 LLQLKLRASvstkcnLEDQVKKLEDDRNSLQAAKAGLEDECKT----------LRQKVEILNELYQQ 407
Cdd:COG3206 309 QEAQRILAS------LEAELEALQAREASLQAQLAQLEARLAElpeleaelrrLEREVEVARELYES 369
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
89-202 |
4.76e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.23 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 89 VTEQQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLE---------------KN 153
Cdd:COG2433 385 LIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLErelsearseerreirKD 464
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 664806007 154 QEI--LDDTAKNLRVMLESEREQnvknqdlISENKKSIEKLKDVISMNASE 202
Cdd:COG2433 465 REIsrLDREIERLERELEEERER-------IEELKRKLERLKELWKLEHSG 508
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
137-414 |
5.03e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.59 E-value: 5.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 137 SDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLESEREQNVKNQDLiseNKKSIEK-LKDV-----ISMNASEFSEVQIAL 210
Cdd:pfam12128 174 SESPLRHIDKIAKAMHSKEGKFRDVKSMIVAILEDDGVVPPKSRL---NRQQVEHwIRDIqaiagIMKIRPEFTKLQQEF 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 211 N-----EAKLSEEKVKSECHRVQEEN------ARLKKKKEQLQQEIEDWSKLHAELS---------------------EQ 258
Cdd:pfam12128 251 NtlesaELRLSHLHFGYKSDETLIASrqeerqETSAELNQLLRTLDDQWKEKRDELNgelsaadaavakdrselealeDQ 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 259 IKSFEKS---------------QKDLEV------ALTHKDDNINALTNCITQLNLLECESESEGQNKGGNDSDELANGEV 317
Cdd:pfam12128 331 HGAFLDAdietaaadqeqlpswQSELENleerlkALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQL 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 318 GGDRN--EKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLR-----ASVSTKCNLEDQVKKLEDDRNSLQAAKAG---L 387
Cdd:pfam12128 411 AVAEDdlQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRlnqatATPELLLQLENFDERIERAREEQEAANAEverL 490
|
330 340
....*....|....*....|....*..
gi 664806007 388 EDECKTLRQKVEILNELYQQKEMALQK 414
Cdd:pfam12128 491 QSELRQARKRRDQASEALRQASRRLEE 517
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
87-486 |
5.94e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 40.20 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 87 YQVTEQQISEKLKTIMKENTELVQKLsnyeqkIKESKKHVQETRKQNMILSDEAikyKDKIKTLEKNQEIlddtaknlrv 166
Cdd:PTZ00440 1007 YNILNKKIDDLIKKQHDDIIELIDKL------IKEKGKEIEEKVDQYISLLEKM---KTKLSSFHFNIDI---------- 1067
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 167 mlesEREQNVKNQDLISENKKSIEKLKDVISMNASEFSEVQIALNEAKLSEEKVKsechrvQEENARLKKKKEQLQQEIE 246
Cdd:PTZ00440 1068 ----KKYKNPKIKEEIKLLEEKVEALLKKIDENKNKLIEIKNKSHEHVVNADKEK------NKQTEHYNKKKKSLEKIYK 1137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 247 DWSKLHAELS----EQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNLLECESESEGQ-------NKGGNDSDELANG 315
Cdd:PTZ00440 1138 QMEKTLKELEnmnlEDITLNEVNEIEIEYERILIDHIVEQINNEAKKSKTIMEEIESYKKdidqvkkNMSKERNDHLTTF 1217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 316 EVGGDRNE--KMKNQIKQMMDVSRTQTAISVVEEDLKLLQlklrasvSTKCNLEDQVKKLEDDRNSLQAAKAGLEDeCKT 393
Cdd:PTZ00440 1218 EYNAYYDKatASYENIEELTTEAKGLKGEANRSTNVDELK-------EIKLQVFSYLQQVIKENNKMENALHEIKN-MYE 1289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 394 LRQKV-------EILNELYQQKEMALQ--KKLSQEEYERQEREHRLSAADE--KAVSAAEE---VKTYKRRIEEMEDELQ 459
Cdd:PTZ00440 1290 FLISIdsekilkEILNSTKKAEEFSNDakKELEKTDNLIKQVEAKIEQAKEhkNKIYGSLEdkqIDDEIKKIEQIKEEIS 1369
|
410 420
....*....|....*....|....*..
gi 664806007 460 KTERSFKNQIATHEKKAHENWLKARAA 486
Cdd:PTZ00440 1370 NKRKEINKYLSNIKSNKEKCDLHVRNA 1396
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
171-478 |
6.44e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.27 E-value: 6.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 171 EREQNVKnqdliSENKKSIEKLKDVISMNASEFSEVqIALNEAKLseekvksechRVQEENARLKKKKEQLQQEIEDWSK 250
Cdd:PLN02939 114 EQQTNSK-----DGEQLSDFQLEDLVGMIQNAEKNI-LLLNQARL----------QALEDLEKILTEKEALQGKINILEM 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 251 LHAELSEQIKSFEKSQKDLEVALThkddninaltncitQLNLLECESESEGQNKGGNDSDELANGEVGGDRNEKMKNQIK 330
Cdd:PLN02939 178 RLSETDARIKLAAQEKIHVEILEE--------------QLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQ 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 331 ----QMMDVSRTQTAISVVEEDLKLLQLKLR----------ASVSTKCNLE-----DQVKKLED--DRNSLQAAKAGLE- 388
Cdd:PLN02939 244 flkaELIEVAETEERVFKLEKERSLLDASLReleskfivaqEDVSKLSPLQydcwwEKVENLQDllDRATNQVEKAALVl 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 389 DECKTLRQKVEILNElyqQKEMALQKKLSQEEYERQEreHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTERSFKNQ 468
Cdd:PLN02939 324 DQNQDLRDKVDKLEA---SLKEANVSKFSSYKVELLQ--QKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKEE 398
|
330
....*....|
gi 664806007 469 iatHEKKAHE 478
Cdd:PLN02939 399 ---SKKRSLE 405
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
80-267 |
7.06e-03 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 38.95 E-value: 7.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 80 LVVKDRVYQVTEQQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDD 159
Cdd:pfam17078 29 LLSKLEIAQQKESKFLENLASLKHENDNLSSMLNRKERRLKDLEDQLSELKNSYEELTESNKQLKKRLENSSASETTLEA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 160 TAKNLRV----MLESEREQNVKNQDLISENKKSIEKLKDVISMNASEFSEVQIALN---EAKLSE--EKVKSECHRVQEE 230
Cdd:pfam17078 109 ELERLQIqydaLVDSQNEYKDHYQQEINTLQESLEDLKLENEKQLENYQQRISSNDkdiDTKLDSynNKFKNLDNIYVNK 188
|
170 180 190
....*....|....*....|....*....|....*....
gi 664806007 231 NARLKKKKEQLQQE--IEDWSKLHAELseQIKSFEKSQK 267
Cdd:pfam17078 189 NNKLLTKLDSLAQLldLPSWLNLYPES--RNKILEYAEK 225
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
222-401 |
7.38e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 38.75 E-value: 7.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 222 SECHRVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINaltncitqlnllecesESEG 301
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK----------------KYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 302 QNKGGNDSDELAN--GEVGG--DRNEKMKNQIKQMMDvsrtqtAISVVEEDLKLLQLKlrasvstkcnLEDQVKKLEDDR 377
Cdd:COG1579 81 QLGNVRNNKEYEAlqKEIESlkRRISDLEDEILELME------RIEELEEELAELEAE----------LAELEAELEEKK 144
|
170 180
....*....|....*....|....
gi 664806007 378 NSLQAAKAGLEDECKTLRQKVEIL 401
Cdd:COG1579 145 AELDEELAELEAELEELEAEREEL 168
|
|
| PRK08475 |
PRK08475 |
F0F1 ATP synthase subunit B; Validated |
200-271 |
7.83e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 236272 [Multi-domain] Cd Length: 167 Bit Score: 38.07 E-value: 7.83e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 664806007 200 ASEFSEVQIALNEAKLSEEKVKSECHRVQEENARL----KKKKEQLQQEIEDWSKlhAELSEQIKSFEkSQKDLEV 271
Cdd:PRK08475 59 SKRLEEIQEKLKESKEKKEDALKKLEEAKEKAELIvetaKKEAYILTQKIEKQTK--DDIENLIKSFE-ELMEFEV 131
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
367-468 |
8.25e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 8.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 367 EDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQKEMalqkklsqeeyerqerehRLSAADEKAVSAAEEVKT 446
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQA------------------ELEALQAEIDKLQAEIAE 76
|
90 100
....*....|....*....|..
gi 664806007 447 YKRRIEEMEDELQKTERSFKNQ 468
Cdd:COG3883 77 AEAEIEERREELGERARALYRS 98
|
|
| mS26_Tt |
cd23695 |
Tetrahymena thermophila ribosomal protein mS26 and similar proteins; Ribosomal protein mS26 is ... |
87-354 |
8.31e-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: 39.42 E-value: 8.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 87 YQVTEQQISEKLKTIMKENTELVQKLS--------NYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILD 158
Cdd:cd23695 200 YQDAKAIIIEDFRESSEEGAEKLEKLEkafatllkNYKEELEEPEKQLEFMQKRLLDLYNLLRLWGQYITIVKMPDSVVR 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 159 DTAKNLRVMLE---SEREQNVKNQDLISENKKSIEKLKDVISMNASEFSEVQIALNEAKLSEEKVksechrvqeenarlK 235
Cdd:cd23695 280 DIMNKTQARPEvakLNSKQELEDAKNRKRDTEENEFDDDYESADEGETSDEEDEIEEENFQLQKE--------------K 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 236 KKKEQLQQEIEDWSKLHAELSEQ-----IKSFEK-SQKDLEVALTHKD-DNINALTNCITQlNLLECESESEGQ---NKG 305
Cdd:cd23695 346 KKEEELNAEFNIAKNSLYKFSPQndknvVDDRDFySGVDLENVFPRALlNNLNDFTGLDFQ-NVKEILNNEEKLkiiQGE 424
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 664806007 306 GNDSDELANGEVGGDRN----EKMKNQIKQMMDVSRTQTAISVVEEDLKLLQL 354
Cdd:cd23695 425 DDQNDQEDFNNPRKFQTslivQTYKQKINNLDAESLTRATQEKKNDIQKLLDL 477
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
93-274 |
8.54e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 39.81 E-value: 8.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 93 QISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLES-- 170
Cdd:PTZ00440 474 DLIISEKDSMDSKEKKESSDSNYQEKVDELLQIINSIKEKNNIVNNNFKNIEDYYITIEGLKNEIEGLIELIKYYLQSie 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 171 ------EREQNVKNQ-----DLISENkksIEKLKDVISMNAS---EFSEVQIALNEAKLSEEKVKSECHRVQEENARLKK 236
Cdd:PTZ00440 554 tlikdeKLKRSMKNDiknkiKYIEEN---VDHIKDIISLNDEidnIIQQIEELINEALFNKEKFINEKNDLQEKVKYILN 630
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 664806007 237 K--KEQLQQEIEDWSKLhaeLSEQIKSFE--KSQKDLEVALT 274
Cdd:PTZ00440 631 KfyKGDLQELLDELSHF---LDDHKYLYHeaKSKEDLQTLLN 669
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
85-515 |
8.69e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 39.64 E-value: 8.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 85 RVYQVTEQQISEKLKTIMKENTELVQKLSNYEQKIK----ESKKHVQETRKQNMILSDEAIKYKdkIKTLEKNQEI---L 157
Cdd:TIGR00606 315 REKERELVDCQRELEKLNKERRLLNQEKTELLVEQGrlqlQADRHQEHIRARDSLIQSLATRLE--LDGFERGPFSerqI 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 158 DDTAKNLRVMLESEREQNVKNQDLISENKKSIEKLKDVISMNASEFSEVqIALNEAKLSEEK-----VKSECHRVQEENA 232
Cdd:TIGR00606 393 KNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRT-IELKKEILEKKQeelkfVIKELQQLEGSSD 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 233 RLKKKKEQLQQEIEDWSKLHAE-----LSEQIKSFEKSQKDLE---VALTHKDDNINALTNCITQLNLLECESESEGQNK 304
Cdd:TIGR00606 472 RILELDQELRKAERELSKAEKNsltetLKKEVKSLQNEKADLDrklRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQI 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 305 GGND---SDELA-------NGEVGGDRNEKMKNQIKQMmdvsrtqtaisvvEEDLKLLQLKLRASVSTKCNLEDQVKKLE 374
Cdd:TIGR00606 552 RKIKsrhSDELTsllgyfpNKKQLEDWLHSKSKEINQT-------------RDRLAKLNKELASLEQNKNHINNELESKE 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806007 375 DDRNSLQAA---KAGLEDECKTLRQKVEILNELYQQKEMalqkkLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRI 451
Cdd:TIGR00606 619 EQLSSYEDKlfdVCGSQDEESDLERLKEEIEKSSKQRAM-----LAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAEL 693
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 664806007 452 EEMEDELQKTERSF-------KNQIATHEKKAHENWLKARAAERAIAEEKREAANLRHKLLELTQKMAMLQ 515
Cdd:TIGR00606 694 QEFISDLQSKLRLApdklkstESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLK 764
|
|
| |
