|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
92-457 |
3.85e-14 |
|
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: 76.63 E-value: 3.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 92 KQISEKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKQNMILSDEAVKYKDKIKILEETNVSLGDKAKSLRLQLESE 171
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 172 REQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALNEAKLSEENVKSECHRVQEENARLKKKKEQLQQQVEEWSKS 251
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 252 HAELTEQIKSFEKSQEDLEialthkddnisaltnciTQLNRLECELESEdpdkggnesddlangetggdrsEKIRNRIkq 331
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELE-----------------ELIEELESELEAL----------------------LNERASL-- 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 332 mmdvsrtqtavsivEEDLKLLQLKLRASMSTKCNLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQKV----EILNELYQQ 407
Cdd:TIGR02168 886 --------------EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIdnlqERLSEEYSL 951
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907069530 408 KEMALQKKLSQEEYERQDREQRLTAADEK------VVLAA-EEVKTYKRRIEEMEEE 457
Cdd:TIGR02168 952 TLEEAEALENKIEDDEEEARRRLKRLENKikelgpVNLAAiEEYEELKERYDFLTAQ 1008
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
90-476 |
3.44e-13 |
|
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: 73.52 E-value: 3.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 90 TEKQISEKLENIKKENAELMQK------LSSYEQKIKESKKYVQETKKQNMILSDEAVK--------------------- 142
Cdd:TIGR04523 178 LEKEKLNIQKNIDKIKNKLLKLelllsnLKKKIQKNKSLESQISELKKQNNQLKDNIEKkqqeinektteisntqtqlnq 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 143 -----------YKDKIKILEETNVSLGDKAKSLRlQLESERE--QNVKNQDLILENKKSIEKLKDVISMNASELSEVQVA 209
Cdd:TIGR04523 258 lkdeqnkikkqLSEKQKELEQNNKKIKELEKQLN-QLKSEISdlNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKI 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 210 LNEAKLSEENVKSECHRVQEENARLKKKKEQLQQQVEEWSKSHAELTEQIKSFEKSQEDLEIALTH-------KDDNISA 282
Cdd:TIGR04523 337 ISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNqeklnqqKDEQIKK 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 283 LTnciTQLNRLECELE--SEDPDKGGNESDDLANGETggdRSEKIRNRIKQMMDVSRTQtaVSIVEEDLKLLQLKLRASM 360
Cdd:TIGR04523 417 LQ---QEKELLEKEIErlKETIIKNNSEIKDLTNQDS---VKELIIKNLDNTRESLETQ--LKVLSRSINKIKQNLEQKQ 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 361 STKCNLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEILNELYQQKEmalqKKLSQEEYERQDREQRLTAA------- 433
Cdd:TIGR04523 489 KELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKE----SKISDLEDELNKDDFELKKEnlekeid 564
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1907069530 434 --DEKVVLAAEEVKTYKRRIEEMEEELQKTERSFKN---QIAAHEKKA 476
Cdd:TIGR04523 565 ekNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDlikEIEEKEKKI 612
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
182-459 |
1.60e-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: 71.63 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 182 ILENKKSIEKLKDVISMNASELSEVQVALNEAKLSEENVKSECHRVQEEnarlkkkkeqlqqqVEEWSKSHAELTEQIKS 261
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKE--------------LEELSRQISALRKDLAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 262 FEKSQEDLEIALTHKDDNISALTNCITQLNRLECELES---EDPDKGGNESDDLANGEtggDRSEKIRNRIKQM-MDVSR 337
Cdd:TIGR02168 738 LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEelaEAEAEIEELEAQIEQLK---EELKALREALDELrAELTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 338 TQTAVSIVEEDLKLLQLKLRASMSTKCNLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEILNELYQQKE---MALQK 414
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEealALLRS 894
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1907069530 415 KLSQEEYERQDREQRLTAADEKVVLAAEEVKTYKRRIEEMEEELQ 459
Cdd:TIGR02168 895 ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
102-454 |
3.04e-11 |
|
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: 67.40 E-value: 3.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 102 KKENAelMQKLSSYEQKIKESKKYVQETKKQNMILSDE---AVKYKDKIKILEETNVSLgdkaksLRLQLESEREQNVKN 178
Cdd:TIGR02169 171 KKEKA--LEELEEVEENIERLDLIIDEKRQQLERLRRErekAERYQALLKEKREYEGYE------LLKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 179 QDLILENKKSIEKLKDVISMNASELSEVQVALNEA-----KLSEEN---VKSECHRVQEENARLKKKKEQLQQQVEEWSK 250
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkkikDLGEEEqlrVKEKIGELEAEIASLERSIAEKERELEDAEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 251 SHAELTEQIKSFEKSQEDLEIALTHKDDNISALTNCI----TQLNRLECELESEDPDkggnesddlaNGETgGDRSEKIR 326
Cdd:TIGR02169 323 RLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYaelkEELEDLRAELEEVDKE----------FAET-RDELKDYR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 327 NRIKQMmdvsrTQTAVSIVEEDLKLLQLKLRASMSTKcNLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEILNEL-- 404
Cdd:TIGR02169 392 EKLEKL-----KREINELKRELDRLQEELQRLSEELA-DLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADls 465
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1907069530 405 -YQQKEMALQKKLSQEEYERQDREQRLTAAdEKVVLAAEEVKTYKRRIEEM 454
Cdd:TIGR02169 466 kYEQELYDLKEEYDRVEKELSKLQRELAEA-EAQARASEERVRGGRAVEEV 515
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
140-471 |
3.56e-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: 67.00 E-value: 3.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 140 AVKYKDKIKILEETNVSLGDKAKSLRLQLESEREQnvknQDLILENKKSIEKLKDVISmnaSELSEVQVALNEAKLSEEN 219
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRKE----LEELEEELEQLRKELEELS---RQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 220 VKSECHRVQEENARLKKKKEQLQQQVEEWSKSHAELTEQIKSFEKSQEDLEIALTHKDDNISALTNCITQLNRleceles 299
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE------- 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 300 edpdkggnesdDLANGETGGDRSEKIRNRIKQMMDVSRTQTAVsiVEEDLKLLQLKLRASMSTKCNLEDQIKKLEDDRSS 379
Cdd:TIGR02168 818 -----------EAANLRERLESLERRIAATERRLEDLEEQIEE--LSEDIESLAAEIEELEELIEELESELEALLNERAS 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 380 LQTAKAGLEDECKTLRQKVEILN----ELYQQKEmALQKKLSQEEYE----RQDREQRLTAADEKVVLAAEEVKTYKRRI 451
Cdd:TIGR02168 885 LEEALALLRSELEELSEELRELEskrsELRRELE-ELREKLAQLELRleglEVRIDNLQERLSEEYSLTLEEAEALENKI 963
|
330 340
....*....|....*....|
gi 1907069530 452 EEMEEELQKTERSFKNQIAA 471
Cdd:TIGR02168 964 EDDEEEARRRLKRLENKIKE 983
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
92-465 |
7.22e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.86 E-value: 7.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 92 KQISEKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKqnmiLSDEAVKYKDKIKILEEtNVSLGDKAKSLRLQLESE 171
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE----LKKKLKELEKRLEELEE-RHELYEEAKAKKEELERL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 172 RE-------QNVKNQDLILENKKS-----IEKLKDVISMNASELSEVQVALNEAKlSEENVKSECHRVQEENARLKKKKE 239
Cdd:PRK03918 378 KKrltgltpEKLEKELEELEKAKEeieeeISKITARIGELKKEIKELKKAIEELK-KAKGKCPVCGRELTEEHRKELLEE 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 240 QLQQqVEEWSKSHAELTEQIKSFEKSQEDLEIALThKDDNISALTNCITQLNRLECELESEDPDKGGNESDDLangETGG 319
Cdd:PRK03918 457 YTAE-LKRIEKELKEIEEKERKLRKELRELEKVLK-KESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEY---EKLK 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 320 DRSEKIRNRIKqmmdvsrtqtavsIVEEDLKllqlKLRASMSTKCNLEDQIKKLEDDRSSL--QTAKAGLEDEcKTLRQK 397
Cdd:PRK03918 532 EKLIKLKGEIK-------------SLKKELE----KLEELKKKLAELEKKLDELEEELAELlkELEELGFESV-EELEER 593
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907069530 398 VEILNELYQQkemalQKKLSQEEYERQDREQRLTAADEKVVLAAEEVKTYKRRIEEMEEELQKTERSF 465
Cdd:PRK03918 594 LKELEPFYNE-----YLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY 656
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
82-404 |
1.15e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 65.47 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 82 VKSRVYQVTEK--QISEKLENIKKENAELMQKLSSYEQKIKESKKYVQEtkkqnmiLSDEAVKYKDKIKILEETNVSLGD 159
Cdd:TIGR02169 700 IENRLDELSQElsDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS-------LEQEIENVKSELKELEARIEELEE 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 160 KAKSLRLQLES-EREQNvknQDLILENKKSIEKLKDVISMNASELSEVQVALNEAKLSEENVKSECHRVQEENARLKKKK 238
Cdd:TIGR02169 773 DLHKLEEALNDlEARLS---HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 239 EQLQQQVEEWSKSHAELTEQIKSFEKSQEDLEIALTHKDDNISALTNCITQLNRLECELESEDPDKGGNESDDLANGETG 318
Cdd:TIGR02169 850 KSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEAL 929
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 319 GDRSEKIRNRIKQMMDVSRTQTAVSIVEEDLKLLQLKLRASMSTKCNLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQKV 398
Cdd:TIGR02169 930 EEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERI 1009
|
....*.
gi 1907069530 399 EILNEL 404
Cdd:TIGR02169 1010 EEYEKK 1015
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
93-475 |
2.12e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.78 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 93 QISEKLENIKKEnAELMQKLSSYEQKIKESKKYVQETKKqnmilSDEAVKYKDKIKILEETNVSLGDKAKSLRLQLESER 172
Cdd:PTZ00121 1395 EAKKKAEEDKKK-ADELKKAAAAKKKADEAKKKAEEKKK-----ADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEE 1468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 173 EQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALNEAKLSEENVKSECHRVQEENARLKKKKEQLQQQVEEWSKSH 252
Cdd:PTZ00121 1469 AKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKA 1548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 253 AEL--TEQIKSFEKSQEdLEIALTHKDDNISALTNCiTQLNRLEcELESEDPDKGGNESDDLANGETGGDRSEKIR-NRI 329
Cdd:PTZ00121 1549 DELkkAEELKKAEEKKK-AEEAKKAEEDKNMALRKA-EEAKKAE-EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKaEEL 1625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 330 KQMMDVSRT--QTAVSIVEEDLKLLQLKlRASMSTKCNLEDQIKKLEDDRSSLQTAKAGLEDEcktlRQKVEILNELYQQ 407
Cdd:PTZ00121 1626 KKAEEEKKKveQLKKKEAEEKKKAEELK-KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE----KKAAEALKKEAEE 1700
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907069530 408 KEMALQKKLSQEEYERQDREQRltAADEKVVLAAEEVKTYKRRIEEMEEELQKTERSfKNQIAAHEKK 475
Cdd:PTZ00121 1701 AKKAEELKKKEAEEKKKAEELK--KAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE-KKKIAHLKKE 1765
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
92-403 |
1.43e-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: 61.57 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 92 KQISEKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKQNMILSDEAVKYKDKIKILEETNVSLGDKAKSLRLQLeSE 171
Cdd:TIGR04523 317 KNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI-ND 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 172 REQNVKNQDLILENK---------------KSIEKLKDVISMNASELSEV---------------------QVALNEAKL 215
Cdd:TIGR04523 396 LESKIQNQEKLNQQKdeqikklqqekelleKEIERLKETIIKNNSEIKDLtnqdsvkeliiknldntreslETQLKVLSR 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 216 SEENVKSECHRVQEENARLKKKKEQLQQQVEEWSKSHAELTEQIKSFEKSQEDLEIALTHKDDNISALTNcitQLNRLEC 295
Cdd:TIGR04523 476 SINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLED---ELNKDDF 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 296 ELESEDPDKGGNESDdlangetggDRSEKIRNRIKQMMDV-SRTQTAVSIVEEDLKLLQLKLRASMSTKCNLEDQIKKLE 374
Cdd:TIGR04523 553 ELKKENLEKEIDEKN---------KEIEELKQTQKSLKKKqEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
|
330 340
....*....|....*....|....*....
gi 1907069530 375 DDRSSLQTAKAGLEDECKTLRQKVEILNE 403
Cdd:TIGR04523 624 KENEKLSSIIKNIKSKKNKLKQEVKQIKE 652
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
91-475 |
1.85e-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: 61.19 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 91 EKQISEKLENIKKE--NAELMQK-----LSSYEQKIKESKKYVQETKKQNMILSDEAVKYKDKIKILEETNVSLGDKAKS 163
Cdd:TIGR04523 35 EKQLEKKLKTIKNElkNKEKELKnldknLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 164 LRLQ----------LESEREQNVKNQDLILENKKSIEKLKDVISMNASElsevqvaLNEAKLSEENVK----SECHRVQE 229
Cdd:TIGR04523 115 DKEQknklevelnkLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYND-------LKKQKEELENELnlleKEKLNIQK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 230 ENARLKKKKEQLQ---QQVEEWSKSHAELTEQIKSFEKSQEDLEIALTHKDDNISALTNCI----TQLNRLECELEsEDP 302
Cdd:TIGR04523 188 NIDKIKNKLLKLElllSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEIsntqTQLNQLKDEQN-KIK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 303 DKGGNESDDLANGETGGDRSEKIRNRIKQMMDVSRTQTAVSI----------VEEDLKLLQLKLRASMSTKCNLEDQIKK 372
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWnkelkselknQEKKLEEIQNQISQNNKIISQLNEQISQ 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 373 LEDDRSSLQTAKAGLEDECKTLRQKVEILNELYQQKEMALQKKLSQeeyeRQDREQRLTAADEKVVLAAEEVKTYKRRIE 452
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQ----INDLESKIQNQEKLNQQKDEQIKKLQQEKE 422
|
410 420 430
....*....|....*....|....*....|...
gi 1907069530 453 EMEEELQ----------KTERSFKNQIAAHEKK 475
Cdd:TIGR04523 423 LLEKEIErlketiiknnSEIKDLTNQDSVKELI 455
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
88-476 |
3.81e-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: 3.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 88 QVTEKQISEKLENikkenaelMQKLssyEQKIKESKKYVQETKKQnmilSDEAVKYKDKIKILEETNVSLgdkaksLRLQ 167
Cdd:TIGR02168 175 KETERKLERTREN--------LDRL---EDILNELERQLKSLERQ----AEKAERYKELKAELRELELAL------LVLR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 168 LESEREQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALNEAKLSEENVKSECHRVQEENARLKKKKEQLQQQVEE 247
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 248 WSKSHAELTEQIKSFEKSQEDLEIALTHKDDNISALTNCITQLNRLECELESEDPD-KGGNESDDlangetggDRSEKIR 326
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEElESRLEELE--------EQLETLR 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 327 NRIKQMmdvsrtqtavsivEEDLKLLQLKLRasmstkcNLEDQIKKLEDDRSSLQTAKAGLEDEcKTLRQKVEILNELYQ 406
Cdd:TIGR02168 386 SKVAQL-------------ELQIASLNNEIE-------RLEARLERLEDRRERLQQEIEELLKK-LEEAELKELQAELEE 444
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907069530 407 QKEMALQKKLSQEEYERQDR--EQRLTAADEKVVLAAEEVKTYKRRI---EEMEEELQKTERSFKNQIAAHEKKA 476
Cdd:TIGR02168 445 LEEELEELQEELERLEEALEelREELEEAEQALDAAERELAQLQARLdslERLQENLEGFSEGVKALLKNQSGLS 519
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
92-482 |
5.35e-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: 60.13 E-value: 5.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 92 KQISEKLENIKKENAELMQKLSSYEQKIKESKKYV-------QETKKQNMILSDEAVKYKDKIKILeetnvsLGDKAKSL 164
Cdd:pfam15921 317 RQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLvlanselTEARTERDQFSQESGNLDDQLQKL------LADLHKRE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 165 RlQLESEREQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALneaklseENVKSECHRVQEENARLKKKKEQLQQQ 244
Cdd:pfam15921 391 K-ELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALL-------KAMKSECQGQMERQMAAIQGKNESLEK 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 245 V-----------EEWSKSHAELTEQ---IKSFEKSQEDLEIALTHKDDNISALTNCITQLnRLECELESEDPDKGGNESD 310
Cdd:pfam15921 463 VssltaqlestkEMLRKVVEELTAKkmtLESSERTVSDLTASLQEKERAIEATNAEITKL-RSRVDLKLQELQHLKNEGD 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 311 DLANGET----------GGDRS-EKIRNRIKQMMDV----SRTQTAVSI----VEEDLKLLQLKLRASMSTKCNLEDQIK 371
Cdd:pfam15921 542 HLRNVQTecealklqmaEKDKViEILRQQIENMTQLvgqhGRTAGAMQVekaqLEKEINDRRLELQEFKILKDKKDAKIR 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 372 KLEDDRSSLQTakagledecktlrQKVEILNelyqqkemALQKKLSQEEYERQDREQRLTaadekvvlaaeEVKTYKRRI 451
Cdd:pfam15921 622 ELEARVSDLEL-------------EKVKLVN--------AGSERLRAVKDIKQERDQLLN-----------EVKTSRNEL 669
|
410 420 430
....*....|....*....|....*....|.
gi 1907069530 452 EEMEEELQKTERSFKNQiaAHEKKAHDNWLK 482
Cdd:pfam15921 670 NSLSEDYEVLKRNFRNK--SEEMETTTNKLK 698
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
83-501 |
9.96e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.38 E-value: 9.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 83 KSRVYQVTEKQISEKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKqnmilSDEAVKYKDKIKI-LEETNVSLGDKA 161
Cdd:PTZ00121 1344 AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK-----ADEAKKKAEEDKKkADELKKAAAAKK 1418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 162 KSLRLQLESEREQNVKNQDLILENKKSIEKLKdvismnaSELSEVQVALNEAKLSEENVKSECHRVQEENARLKKKKEQL 241
Cdd:PTZ00121 1419 KADEAKKKAEEKKKADEAKKKAEEAKKADEAK-------KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK 1491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 242 qqqVEEWSKSHAELTEQIKSFEKSQEDLEIALTHKDDNISAltnciTQLNRLECELESEDPDKGGNE---SDDLANGETG 318
Cdd:PTZ00121 1492 ---AEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK-----AEEAKKADEAKKAEEKKKADElkkAEELKKAEEK 1563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 319 GDRSEKIRNRIKQMMDVSRTQTAVSI----VEEDLKLLQ--LKLRASMSTKCNLE----DQIKKLEDDRSSLQTAKAGLE 388
Cdd:PTZ00121 1564 KKAEEAKKAEEDKNMALRKAEEAKKAeearIEEVMKLYEeeKKMKAEEAKKAEEAkikaEELKKAEEEKKKVEQLKKKEA 1643
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 389 DEcktLRQKVEILNELYQQKEMALQKKLSQEEYERQDREQRLTAADEKvvlAAEEVKTYKRRIEEMEEELQKTERSFKNQ 468
Cdd:PTZ00121 1644 EE---KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK---KAAEALKKEAEEAKKAEELKKKEAEEKKK 1717
|
410 420 430
....*....|....*....|....*....|...
gi 1907069530 469 IAAHEKKAHDNWLKARAAERAMAEEKREAANLR 501
Cdd:PTZ00121 1718 AEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK 1750
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
82-463 |
1.66e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.13 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 82 VKSRVYQVTEKQISEKLENIKKENAELMQKLSSYEqkikESKKYVQETKKQ-NMILSD-------------EAVKYKDKI 147
Cdd:PRK02224 192 LKAQIEEKEEKDLHERLNGLESELAELDEEIERYE----EQREQARETRDEaDEVLEEheerreeletleaEIEDLRETI 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 148 KILEETNVSLGDKAKSLR---LQLESEREQNVKNQDLileNKKSIEKLKDVISMNASELSEVQVALNEAKLSEENVKSEC 224
Cdd:PRK02224 268 AETEREREELAEEVRDLRerlEELEEERDDLLAEAGL---DDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEA 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 225 HRVQEENARLKKKKEQLQQQVEEWSKSHAELTEQIKSFEKSQEDLEIALthkDDNISALTNCITQLNRLECELESEDPDK 304
Cdd:PRK02224 345 ESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI---EELRERFGDAPVDLGNAEDFLEELREER 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 305 GGNESDDlanGETGGDRSEkIRNRI---KQMMDVSRTQTA---------VSIVEEDLKLLQlKLRASMSTkcnLEDQIKK 372
Cdd:PRK02224 422 DELRERE---AELEATLRT-ARERVeeaEALLEAGKCPECgqpvegsphVETIEEDRERVE-ELEAELED---LEEEVEE 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 373 LEDDRSSLQTAKAgLEDECKTLRQKVEILNELYQQKEMALQKKLSQ--------EEYERQDREQRLTAAD--EKVVLAAE 442
Cdd:PRK02224 494 VEERLERAEDLVE-AEDRIERLEERREDLEELIAERRETIEEKRERaeelreraAELEAEAEEKREAAAEaeEEAEEARE 572
|
410 420
....*....|....*....|.
gi 1907069530 443 EVKTYKRRIEEMEEELQKTER 463
Cdd:PRK02224 573 EVAELNSKLAELKERIESLER 593
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
78-460 |
2.01e-08 |
|
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: 57.81 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 78 TILVVKSR--VYQVTEKQISEKlENIKKENaELMQKLSSYEQKIKESKKYVQETKKQnmILSDEAVKYKDKIKILEE--T 153
Cdd:pfam05483 260 TFLLEESRdkANQLEEKTKLQD-ENLKELI-EKKDHLTKELEDIKMSLQRSMSTQKA--LEEDLQIATKTICQLTEEkeA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 154 NVSLGDKAKSLRLQLESEREQNVKN-QDLILENKKSIEKLKD---VISM----NASELSEVQVALNEAKLSEENVKsech 225
Cdd:pfam05483 336 QMEELNKAKAAHSFVVTEFEATTCSlEELLRTEQQRLEKNEDqlkIITMelqkKSSELEEMTKFKNNKEVELEELK---- 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 226 RVQEENARLKKKKEQLQQQVEEWSKSHAELTEQIKSFEKSQEDLEIALTHKDdniSALTNCITQLNRLECELESE----- 300
Cdd:pfam05483 412 KILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIK---TSEEHYLKEVEDLKTELEKEklkni 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 301 ----DPDKGGNESDDLAngETGGDRSEKIRNRIKQMMDVSRTQTAVSIVEEDLKLLQLKLRASMST------------KC 364
Cdd:pfam05483 489 eltaHCDKLLLENKELT--QEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESvreefiqkgdevKC 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 365 NL---EDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEILN---ELYQQKEMALQKKLSQEeyerqdrEQRLTAADEKVV 438
Cdd:pfam05483 567 KLdksEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNkniEELHQENKALKKKGSAE-------NKQLNAYEIKVN 639
|
410 420
....*....|....*....|..
gi 1907069530 439 LAAEEVKTYKRRIEEMEEELQK 460
Cdd:pfam05483 640 KLELELASAKQKFEEIIDNYQK 661
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
80-461 |
6.17e-08 |
|
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: 56.52 E-value: 6.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 80 LVVKSRVYQVTEKQISEKLENIKKENAELMQKLSSYEQKIKES--KKYVQETKKQNMILSDEAVKYKDKIKILEETNVSL 157
Cdd:pfam02463 669 SELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEElkKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEE 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 158 gdKAKSLRLQLESEREQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALNEAKlsEENVKSECHRVQEENARLKKK 237
Cdd:pfam02463 749 --EEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEEL--RALEEELKEEAELLEEEQLLI 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 238 KEQLQQQVEEWSKSHAELTEQIKSFEKSQEDLEIALthKDDNISALTNCITQLNRLECELESEDpdkggnesddlangET 317
Cdd:pfam02463 825 EQEEKIKEEELEELALELKEEQKLEKLAEEELERLE--EEITKEELLQELLLKEEELEEQKLKD--------------EL 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 318 GGDRSEKirNRIKQMMDVSRTQTAVSIVEEDLKLLQLKLRASMSTKCNLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQK 397
Cdd:pfam02463 889 ESKEEKE--KEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLL 966
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907069530 398 VEILNELYQQKEMALQKKLSQEEYERQDRE-QRLTAADEKVVLAAEEVKTyKRRIEEMEEELQKT 461
Cdd:pfam02463 967 LAKEELGKVNLMAIEEFEEKEERYNKDELEkERLEEEKKKLIRAIIEETC-QRLKEFLELFVSIN 1030
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
92-456 |
7.67e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.23 E-value: 7.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 92 KQISEKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKqnmilsdEAVKYKDKIKILEEtnvsLGDKAKSLRlQLESE 171
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKK-------EIEELEEKVKELKE----LKEKAEEYI-KLSEF 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 172 REQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALNEAKLSEENVKSECHRVqEENARLKKKKEQLQQQVEEWSKS 251
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEL-EERHELYEEAKAKKEELERLKKR 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 252 HAELT-----EQIKSFEKSQEDLEIALTHKDDNISALTNCITQL----NRLE--------CELESEDPDKGG---NESDD 311
Cdd:PRK03918 381 LTGLTpekleKELEELEKAKEEIEEEISKITARIGELKKEIKELkkaiEELKkakgkcpvCGRELTEEHRKElleEYTAE 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 312 LANGE----TGGDRSEKIRNRIKQMMDVSRTQTAVSIVEEDLKllQLKLRASMSTKCNLEDQIKKLEDDRsSLQTAKAGL 387
Cdd:PRK03918 461 LKRIEkelkEIEEKERKLRKELRELEKVLKKESELIKLKELAE--QLKELEEKLKKYNLEELEKKAEEYE-KLKEKLIKL 537
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907069530 388 EDECKTLRQKVEILNELYQQKEmALQKKLSQEEYERQDREQRLTAadekvvLAAEEVKTYKRRIEEMEE 456
Cdd:PRK03918 538 KGEIKSLKKELEKLEELKKKLA-ELEKKLDELEEELAELLKELEE------LGFESVEELEERLKELEP 599
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
102-517 |
2.48e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.76 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 102 KKENAELMQKLSSYEQKIKESKKYVQETKKQNMILSDEAVKYKDKIKILEETNvslgdKAKSLRLQLESEREQNVKNQdl 181
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA-----EAAEKKKEEAKKKADAAKKK-- 1386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 182 iLENKKSIEKLKDVISMNASELSEVQVALNEAKLSEENVKSECHRVQEENARLKKKKEQLQqqveEWSKSHAELTEQIKS 261
Cdd:PTZ00121 1387 -AEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKA----DEAKKKAEEAKKAEE 1461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 262 FEKSQEDLEIALTHKDDNISALTNCITQLNRLECELESEDPDKGGNE---SDDLANGETGGDRSEKIRNRIKQMMDVSRT 338
Cdd:PTZ00121 1462 AKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAkkkADEAKKAEEAKKADEAKKAEEAKKADEAKK 1541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 339 QTAVSIVEEDLKLLQLKlRASMSTKCnleDQIKKLEDDRSslqTAKAGLEDECKTLRQKVEILNELYQQKEMALQKKLSQ 418
Cdd:PTZ00121 1542 AEEKKKADELKKAEELK-KAEEKKKA---EEAKKAEEDKN---MALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK 1614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 419 EEYERQDREQRLTAADEKvvlaaEEVKTYKRRIEE---MEEELQKTERSFKNQIAAHEKKAHDNWLKARAAERAMAEEKR 495
Cdd:PTZ00121 1615 AEEAKIKAEELKKAEEEK-----KKVEQLKKKEAEekkKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKK 1689
|
410 420
....*....|....*....|..
gi 1907069530 496 EAANLRHKLLEMTQKMAMRQDE 517
Cdd:PTZ00121 1690 AAEALKKEAEEAKKAEELKKKE 1711
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
139-481 |
3.42e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 139 EAVKYKDKIKILEETNVSLGDKAKSLRLQLESEREQNVKNQDLILENKKSIEKLKDvismnasELSEVQVALNEAKLSEE 218
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL-------ELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 219 NVKSECHRVQEENARLKKKKEQLQQQVEEWSKSHAELTEQIKSFEKSQEDLEIALTHKDDNISaltncitQLNRLECELE 298
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA-------EAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 299 SEdpdkggnesddlangetggdRSEKIRNRIKQMMDVSRTQTAVSIVEEDLKLLQLKLRASMSTKCNLEDQIKKLEDDRS 378
Cdd:COG1196 372 AE--------------------LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 379 SLQTAKAGLEDEcktLRQKVEILNELyQQKEMALQKKLSQEEYERQDREQRLTAADEKVVLAAEEVKTYKRRIEEMEEEL 458
Cdd:COG1196 432 ELEEEEEEEEEA---LEEAAEEEAEL-EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFL 507
|
330 340
....*....|....*....|...
gi 1907069530 459 QKTERSFKNQIAAHEKKAHDNWL 481
Cdd:COG1196 508 EGVKAALLLAGLRGLAGAVAVLI 530
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
92-512 |
3.62e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 3.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 92 KQISEKLENIKKENAELMQKLSSYEQKIKESKKyVQETKKQNMILSDEAVKYKDKIKILEETNVSLGDKAKSLRLQLEsE 171
Cdd:PRK03918 255 RKLEEKIRELEERIEELKKEIEELEEKVKELKE-LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-E 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 172 REQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALNEA-KLSEENVKSECHRVQEEnarlkkkkeqlqqqVEEWSK 250
Cdd:PRK03918 333 LEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELeRLKKRLTGLTPEKLEKE--------------LEELEK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 251 SHAELTEQIKSFEKSQEDLEIALTHKDDNISALTN----CITQLNRLECELESEDPDKGGNESDDLANG-ETGGDRSEKI 325
Cdd:PRK03918 399 AKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkCPVCGRELTEEHRKELLEEYTAELKRIEKElKEIEEKERKL 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 326 RNRIKQMMDVSRTQTAVSIVEEDLKllQLKLRASMSTKCNLEDQIKKLEDDRSsLQTAKAGLEDECKTLRQKVEILNELY 405
Cdd:PRK03918 479 RKELRELEKVLKKESELIKLKELAE--QLKELEEKLKKYNLEELEKKAEEYEK-LKEKLIKLKGEIKSLKKELEKLEELK 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 406 QQKEmALQKKLSQEEYERQDREQRLTAadekvvLAAEEVKTYKRRIEEMEeelqktersfknqiaahekKAHDNWLKARA 485
Cdd:PRK03918 556 KKLA-ELEKKLDELEEELAELLKELEE------LGFESVEELEERLKELE-------------------PFYNEYLELKD 609
|
410 420
....*....|....*....|....*..
gi 1907069530 486 AERAMAEEKREAANLRHKLLEMTQKMA 512
Cdd:PRK03918 610 AEKELEREEKELKKLEEELDKAFEELA 636
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
329-475 |
4.32e-07 |
|
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: 51.85 E-value: 4.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 329 IKQMMDVSRTQTAVSIVEEDLKLLQLKLRASMSTKCNLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEILNELYQQ- 407
Cdd:COG1579 6 LRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNv 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907069530 408 ---KEM-ALQKKLSQEEYERQDREQRLTAADEKVVLAAEEVKTYKRRIEEMEEELQKTERSFKNQIAAHEKK 475
Cdd:COG1579 86 rnnKEYeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
189-457 |
1.50e-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: 51.99 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 189 IEKLKDVISMNASELSEVQVALNEAKLSeenvKSECHRvqeenarlkkkkeqlqqQVEEWSKSHAELTEQIKSFEKSQED 268
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRIENRLDELSQE----LSDASR-----------------KIGEIEKEIEQLEQEEEKLKERLEE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 269 LEIALTHKDDnisALTNCITQLNRLECELESEDPDKgGNESDDLANGET--GGDRSEKIRNRI-KQMMDVSRTQTAVSIV 345
Cdd:TIGR02169 742 LEEDLSSLEQ---EIENVKSELKELEARIEELEEDL-HKLEEALNDLEArlSHSRIPEIQAELsKLEEEVSRIEARLREI 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 346 EEDLKLLQLKLRASMSTKCNLEDQIKKLEDDRSS-------LQTAKAGLEDECKTLRQKVEILNELYQ---------QKE 409
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSiekeienLNGKKEELEEELEELEAALRDLESRLGdlkkerdelEAQ 897
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1907069530 410 M-ALQKKLSQEEYERQDREQRLTAADEKVVLAAEEVKTYKRRIEEMEEE 457
Cdd:TIGR02169 898 LrELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEI 946
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
91-474 |
1.73e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 91 EKQISEkLENIKKENAELMQKLSSYEQKIKESKKYVQETKKQNMILSD--EAVKYKDKIKILEETNVSLGDKAKSLRLQL 168
Cdd:COG4717 77 EEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEERL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 169 ESEREQnvknQDLILENKKSIEKLKDVISMNASELS-EVQVALNEAKLSEENVKSECHRVQEEnarlkkkkeqlqqqVEE 247
Cdd:COG4717 156 EELREL----EEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEE--------------LEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 248 WSKSHAELTEQIKSFEKSQEDLEI------------------ALTHKDDNISALTNCITQLNRLECEL-------ESEDP 302
Cdd:COG4717 218 AQEELEELEEELEQLENELEAAALeerlkearlllliaaallALLGLGGSLLSLILTIAGVLFLVLGLlallfllLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 303 DKGGNESDDLANGETGGDRSEKIRNRIKQMMDVSRTQTAVSIVEEDLKLLQLKLRASMSTKCNLEDQIKKLEDDRSSLQt 382
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALL- 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 383 AKAGLEDEcKTLRQKVEILNElYQQKEMALQKKLSQEEYERQDREQRLTAADEKVVlaAEEVKTYKRRIEEMEEE---LQ 459
Cdd:COG4717 377 AEAGVEDE-EELRAALEQAEE-YQELKEELEELEEQLEELLGELEELLEALDEEEL--EEELEELEEELEELEEEleeLR 452
|
410
....*....|....*
gi 1907069530 460 KTERSFKNQIAAHEK 474
Cdd:COG4717 453 EELAELEAELEQLEE 467
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
253-517 |
1.74e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 253 AELTEQIKSFEKSQEDLEIAL-----THKDDNISALTNCITQLNRLECELESEdpdkggnesddLANGETGGDRSEKIRN 327
Cdd:TIGR02168 209 AEKAERYKELKAELRELELALlvlrlEELREELEELQEELKEAEEELEELTAE-----------LQELEEKLEELRLEVS 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 328 RIKQMMDVSRT-----QTAVSIVEEDLKLLQLKLRASMSTKCNLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEiln 402
Cdd:TIGR02168 278 ELEEEIEELQKelyalANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE--- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 403 elyqqkemALQKKLSQEEYERQDREQRLTAADE-------KVVLAAEEVKTYKRRIEEMEEELQKTERS---FKNQIAAH 472
Cdd:TIGR02168 355 --------SLEAELEELEAELEELESRLEELEEqletlrsKVAQLELQIASLNNEIERLEARLERLEDRrerLQQEIEEL 426
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1907069530 473 EKKAHDNWLKarAAERAMAEEKREAANLRHKLLEMTQKMAMRQDE 517
Cdd:TIGR02168 427 LKKLEEAELK--ELQAELEELEEELEELQEELERLEEALEELREE 469
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
514-805 |
2.04e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 51.86 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 514 RQDEPVIVKPMPGRPNTQNPPRRGLLSQNGSFGPSP--VSGGECSPPLPAEPPGRPLSATLSRRDTPRSEFGSLDRHLPR 591
Cdd:PHA03247 2706 PTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPpaVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTR 2785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 592 PRWPSEASGKHSA---SDPGPAPVVNSSSRSSSPAKAVDEG--------KQTVPQEPEGPSASSMAP----LAGHPVAVN 656
Cdd:PHA03247 2786 PAVASLSESRESLpspWDPADPPAAVLAPAAALPPAASPAGplppptsaQPTAPPPPPGPPPPSLPLggsvAPGGDVRRR 2865
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 657 MAPKGPPPFPGVPlmggpvpppirygpppqlcggpfgprplpppfvpgMHPPLGvREYAPGVLPGKRDLPLDPREFLPGH 736
Cdd:PHA03247 2866 PPSRSPAAKPAAP-----------------------------------ARPPVR-RLARPAVSRSTESFALPPDQPERPP 2909
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907069530 737 TPFRPPGSLGPREFFIPGTRLPPPTHGPQEYPP-----PPPAVRDSLPSGPREEAKPASPSSVQ-DRSQASKPTP 805
Cdd:PHA03247 2910 QPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPlapttDPAGAGEPSGAVPQPWLGALVPGRVAvPRFRVPQPAP 2984
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
93-516 |
2.35e-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: 51.59 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 93 QISEKLENIKKENAElmQKLSSYEQKIKESKKYVQETKK------QNMilsDEAVKYKDKIKILEETNVSLgDKAKSLRL 166
Cdd:TIGR01612 868 QFAELTNKIKAEISD--DKLNDYEKKFNDSKSLINEINKsieeeyQNI---NTLKKVDEYIKICENTKESI-EKFHNKQN 941
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 167 QLESEREQNVKnqdlILENKKSIEK-----LKDVISMNASELSEV--QVALN--EAKLSE-----ENVKSECHRVQEEna 232
Cdd:TIGR01612 942 ILKEILNKNID----TIKESNLIEKsykdkFDNTLIDKINELDKAfkDASLNdyEAKNNElikyfNDLKANLGKNKEN-- 1015
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 233 rlkkkkeQLQQQVEEWSKSHAELTEQIKSFEKSQEDLEIALTHKDDNIS---------------------ALTNcITQLN 291
Cdd:TIGR01612 1016 -------MLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNIIdeiekeigkniellnkeileeAEIN-ITNFN 1087
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 292 RLECELESEDPDKGGNE------------SDDLANGETGGDRS----EKIRNRIKQMMDVSRTQ-------TAVSIVEED 348
Cdd:TIGR01612 1088 EIKEKLKHYNFDDFGKEenikyadeinkiKDDIKNLDQKIDHHikalEEIKKKSENYIDEIKAQindledvADKAISNDD 1167
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 349 LKLLQLKLR---ASMSTKCNLEDQIKKLEDDRSSLQTAKAGLEdecktlrqKVEILNELYQQkemALQKKLSQEEYERQD 425
Cdd:TIGR01612 1168 PEEIEKKIEnivTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLE--------EVKGINLSYGK---NLGKLFLEKIDEEKK 1236
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 426 REQRLTAADEKVVLAAEEVKTYKRRIE-EMEEELQ-KTERSFKNQIAAHEKKAHdnwlkaraaeRAMAEEKREAANLRHK 503
Cdd:TIGR01612 1237 KSEHMIKAMEAYIEDLDEIKEKSPEIEnEMGIEMDiKAEMETFNISHDDDKDHH----------IISKKHDENISDIREK 1306
|
490
....*....|...
gi 1907069530 504 LLEMTQKMAMRQD 516
Cdd:TIGR01612 1307 SLKIIEDFSEESD 1319
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
99-462 |
2.92e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 99 ENIKKENAELMQKLSSYEQKIKESKKYVQETKKQnmilsdeAVKYKDKIKILEETNVSLGDKAKSLRLQLESEREQnvkn 178
Cdd:PRK02224 310 EAVEARREELEDRDEELRDRLEECRVAAQAHNEE-------AESLREDADDLEERAEELREEAAELESELEEAREA---- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 179 qdlILENKKSIEKLKDVISMNASELSEVQVALNEAKLSEENVKSECHRVQEENARLKKKKEQLQQQVEEwsksHAELTEQ 258
Cdd:PRK02224 379 ---VEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEE----AEALLEA 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 259 IKSFEKSQ--EDLEIA--LTHKDDNISALTncitqLNRLECELESEDPDKGGNESDDLANGETGGDRSEKIRNRIKQMMD 334
Cdd:PRK02224 452 GKCPECGQpvEGSPHVetIEEDRERVEELE-----AELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIA 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 335 VSRTqtavSIVEEDLKLLQL-----KLRASMSTK--------------------CN-----LEDQIKKLEDDRSSLQTAk 384
Cdd:PRK02224 527 ERRE----TIEEKRERAEELreraaELEAEAEEKreaaaeaeeeaeeareevaeLNsklaeLKERIESLERIRTLLAAI- 601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 385 AGLEDECKTLRQKVEILNELYQQKEMALQkklsqeeyERQDREQRLTAA--DEKVVLAAEEVKTYKRRIEEMEEELQKTE 462
Cdd:PRK02224 602 ADAEDEIERLREKREALAELNDERRERLA--------EKRERKRELEAEfdEARIEEAREDKERAEEYLEQVEEKLDELR 673
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
525-805 |
5.39e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 50.32 E-value: 5.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 525 PGRPNTQNPPR-RGLLSQNGsfGPSPVSGGECSPPLPAePPGRPLSATLSRRDT-----PR--------SEFGSLDRHLP 590
Cdd:PHA03247 2475 PGAPVYRRPAEaRFPFAAGA--APDPGGGGPPDPDAPP-APSRLAPAILPDEPVgepvhPRmltwirglEELASDDAGDP 2551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 591 RPRWPSE---ASGKHSASDPGPAPVVNSSSRSSSPAKAVDEGKQTVPQEPEGPSASSMAPLAGHPVAVNMAPKGPPPFPG 667
Cdd:PHA03247 2552 PPPLPPAappAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSP 2631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 668 VP---LMGGPVPPPIRYGPPPQLCGGPFGPRPLPPPFVPGMHPplgvREYAPGVLPGKRDLP---------LDPREflPG 735
Cdd:PHA03247 2632 SPaanEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAA----QASSPPQRPRRRAARptvgsltslADPPP--PP 2705
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907069530 736 HTPFRPPGSLgpreffIPGTRLPPPTHGPQEYPPPPPA--VRDSLPSGPREEAKPASPSSVQDRSQASKPTP 805
Cdd:PHA03247 2706 PTPEPAPHAL------VSATPLPPGPAAARQASPALPAapAPPAVPAGPATPGGPARPARPPTTAGPPAPAP 2771
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
98-478 |
9.95e-06 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 48.92 E-value: 9.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 98 LENIKKENAELMQKLSSYEQKIKESKKYVQETKKQN---MILSDEAVKYKDKIKILEETNvslgDKAKSLRLQLESEREQ 174
Cdd:pfam05622 68 LEQLQEENFRLETARDDYRIKCEELEKEVLELQHRNeelTSLAEEAQALKDEMDILRESS----DKVKKLEATVETYKKK 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 175 -----NVKNQDLILENKKSI---------EKLKDVISMNAS-ELSEVQVALNEAKLSEENVKSEchRVQEENARLKKKKE 239
Cdd:pfam05622 144 ledlgDLRRQVKLLEERNAEymqrtlqleEELKKANALRGQlETYKRQVQELHGKLSEESKKAD--KLEFEYKKLEEKLE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 240 QLQQQVEEWSK---SHAELTEQIKSFEKSQEDLEIALTHKDDNISALTNCITQLNRLE-CE----LESEDP----DKGGN 307
Cdd:pfam05622 222 ALQKEKERLIIerdTLRETNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEiREklirLQHENKmlrlGQEGS 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 308 ESDDLANGETGGDRSEKIRNRIKQMMDVSRTQTAV--SIVEEDLKLLQL---KLRASMSTKCNLEDQIKKLEDDRSSLQT 382
Cdd:pfam05622 302 YRERLTELQQLLEDANRRKNELETQNRLANQRILElqQQVEELQKALQEqgsKAEDSSLLKQKLEEHLEKLHEAQSELQK 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 383 AKAGLED-ECKTLRQKveilnelyQQKEMALQKKLSQEEYERQDREQRLTAADEKvvlAAEEVKTYKRRIEEMEE-ELQk 460
Cdd:pfam05622 382 KKEQIEElEPKQDSNL--------AQKIDELQEALRKKDEDMKAMEERYKKYVEK---AKSVIKTLDPKQNPASPpEIQ- 449
|
410
....*....|....*...
gi 1907069530 461 terSFKNQIAAHEKKAHD 478
Cdd:pfam05622 450 ---ALKNQLLEKDKKIEH 464
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
96-501 |
1.07e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 96 EKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKQNMILSDEAVKYKDKIKILEET-NVSLGDKAKSLRLQLESEREQ 174
Cdd:PTZ00121 1070 EGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDArKAEEARKAEDARKAEEARKAE 1149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 175 NVKNQDLileNKKSIEKLKDVISMNASELSEVQVALN--EAKLSEENVKSECHRVQEENARLKKKKEqlqqqVEEWSKSH 252
Cdd:PTZ00121 1150 DAKRVEI---ARKAEDARKAEEARKAEDAKKAEAARKaeEVRKAEELRKAEDARKAEAARKAEEERK-----AEEARKAE 1221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 253 -AELTEQIKSFEKSQEDLEIA-----LTHKDDNISALTNCITQLNRLECELESEDPDKggneSDDLANGEtggdrSEKIR 326
Cdd:PTZ00121 1222 dAKKAEAVKKAEEAKKDAEEAkkaeeERNNEEIRKFEEARMAHFARRQAAIKAEEARK----ADELKKAE-----EKKKA 1292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 327 NRIKQMMDVSRTQTAVSIVEEDLKLLQLKLRASMSTKcNLEDQIKKLEDDRSSLQTAKAGLEDECKTL------------ 394
Cdd:PTZ00121 1293 DEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK-KADAAKKKAEEAKKAAEAAKAEAEAAADEAeaaeekaeaaek 1371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 395 -----RQKVEILNELYQQKEMALQKKLSQEEYERQDREQRLTAADEKVVLAAEEVKTYKRRIEEMEEELQKTERSFKNQI 469
Cdd:PTZ00121 1372 kkeeaKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKK 1451
|
410 420 430
....*....|....*....|....*....|..
gi 1907069530 470 AAHEKKAHDNWLKARAAERAMAEEKREAANLR 501
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKAEEAKKADEAKKKAEEAK 1483
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
89-475 |
1.22e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.95 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 89 VTEKQISEKLENIKKEN-AELMQKLSSYEQKIKESKKYVQETKK--QNMILSDEAVKYKDKIKILEETNVSLGDKAKSLR 165
Cdd:pfam05483 147 IKENNATRHLCNLLKETcARSAEKTKKYEYEREETRQVYMDLNNniEKMILAFEELRVQAENARLEMHFKLKEDHEKIQH 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 166 LQLESEREQNVKNQD---LILENKKSIEKLKDVISMNASELSEVQVALNEAKLSEENVKSECHRvqeenarlkkkkeqLQ 242
Cdd:pfam05483 227 LEEEYKKEINDKEKQvslLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEK--------------KD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 243 QQVEEWSKSHAELTEQIKSFEKSQEDLEIAlthkddnisalTNCITQLNRlECELESEDPDKGGNESDDLANgetggdrs 322
Cdd:pfam05483 293 HLTKELEDIKMSLQRSMSTQKALEEDLQIA-----------TKTICQLTE-EKEAQMEELNKAKAAHSFVVT-------- 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 323 eKIRNRIKQMMDVSRT-QTAVSIVEEDLKLLQLKLRASMStkcNLEDQIKKLEDDRSSLQTAKAGLEDECKTL--RQKVE 399
Cdd:pfam05483 353 -EFEATTCSLEELLRTeQQRLEKNEDQLKIITMELQKKSS---ELEEMTKFKNNKEVELEELKKILAEDEKLLdeKKQFE 428
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069530 400 ILNELYQQKEMALQKKLSQEEYERQDREQRLTAadekvVLAAEEvkTYKRRIEEMEEELQKtERSFKNQIAAHEKK 475
Cdd:pfam05483 429 KIAEELKGKEQELIFLLQAREKEIHDLEIQLTA-----IKTSEE--HYLKEVEDLKTELEK-EKLKNIELTAHCDK 496
|
|
| RND_1 |
NF037998 |
protein translocase SecDF, variant type; Members of this family are identified by TCDB as ... |
60-223 |
1.41e-05 |
|
protein translocase SecDF, variant type; Members of this family are identified by TCDB as belonging to 2.A.6.4.4, a variant 12-TM type SecDF, as found in Spiroplasma, Mesoplasma, and Acholeplasma.
Pssm-ID: 468306 Cd Length: 1237 Bit Score: 49.01 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 60 VIITAVLGIVSFAIFSWrtiLVVKSRVYQVTEKQISEKLENIKKENAELMQKLSSYEQKI-------KESKKYVQETKKQ 132
Cdd:NF037998 580 VIISLVLVIIVARLMIW---LTIKLQWFKKYPWLLPLDTDFANQGVAILNYKISRLENKIekltnkeKLSSKLLLKIKKI 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 133 NmilsDEAVKYKDKIKILEET-NVSLGDKAKSLRLQLESEREQNVKNQDLILENKKSIEKLKDVISMNaselsEVQVALN 211
Cdd:NF037998 657 N----DKIDLLKKKEENKEAKkNAKLIEKVKAKIKKLEQKITKLKLNKKKSNKIIKIRWKKKDWIFFL-----KDNTDVI 727
|
170
....*....|..
gi 1907069530 212 EAKLSEENVKSE 223
Cdd:NF037998 728 LAIESEIEIQVI 739
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
323-518 |
1.53e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 323 EKIRNRIKQMMD-VSRTQTAVSIVEEDLKLLQLKLRAsmstkcnLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEIL 401
Cdd:COG4942 30 EQLQQEIAELEKeLAALKKEEKALLKQLAALERRIAA-------LARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 402 NELYQQKEMALQKK---------LSQEEY---------------ERQDREQRLTAADEKVVLAAEEVKTYKRRIEEMEEE 457
Cdd:COG4942 103 KEELAELLRALYRLgrqpplallLSPEDFldavrrlqylkylapARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907069530 458 LQKTERSFKNQIAAHEKKAHDNWLKARAAERAMAEEKREAANLRHKLLEMTQKMAMRQDEP 518
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
173-424 |
1.55e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.47 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 173 EQNVKNQDLILENKKSIeklkDVISMNASELSEvQVALNEAKLSEENVKSEchrvqEENARLKKKKEQLQQQVEEWSKSH 252
Cdd:PHA02562 167 EMDKLNKDKIRELNQQI----QTLDMKIDHIQQ-QIKTYNKNIEEQRKKNG-----ENIARKQNKYDELVEEAKTIKAEI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 253 AELTEQIKSFEKSQEDLEIALTHKDDNISALTNCITQLNRLECELE------------SEDPDKGGNESDDLANGETGGD 320
Cdd:PHA02562 237 EELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEkggvcptctqqiSEGPDRITKIKDKLKELQHSLE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 321 RSEKIRNRIKQMMDVSRTQTAVsiveedLKLLQLKLRASMSTKCNLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQ-KVE 399
Cdd:PHA02562 317 KLDTAIDELEEIMDEFNEQSKK------LLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDeLDK 390
|
250 260
....*....|....*....|....*
gi 1907069530 400 ILNELyqqkemalqKKLSQEEYERQ 424
Cdd:PHA02562 391 IVKTK---------SELVKEKYHRG 406
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
366-478 |
1.65e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 366 LEDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEILNELYQQ----KEMALQKKLSQEEYERQDREQR-------LTAAD 434
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERERRrarlealLAALG 372
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1907069530 435 EKVVLAAEEVKTYKRRIEEMEEELQKTERSFKNQIAAHEKKAHD 478
Cdd:COG4913 373 LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRD 416
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
202-463 |
2.85e-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: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 202 ELSEVQVALNEAKLSEENVKSECHRVQEE--NARLKKKKEQLQQQVEEWSKSHA--ELTEQIKSFEKSQEDLEIALTHKD 277
Cdd:TIGR02169 178 ELEEVEENIERLDLIIDEKRQQLERLRREreKAERYQALLKEKREYEGYELLKEkeALERQKEAIERQLASLEEELEKLT 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 278 DNISALTNCITQLNRLECELESEDPDKGGNESddlangetggdrsekirnrikqmmdvSRTQTAVSIVEEDLKLLQLKLR 357
Cdd:TIGR02169 258 EEISELEKRLEEIEQLLEELNKKIKDLGEEEQ--------------------------LRVKEKIGELEAEIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 358 ASMSTKCNLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEILNELYQQKEmalqkklsqEEYErqDREQRLTAADEKV 437
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELK---------EELE--DLRAELEEVDKEF 380
|
250 260
....*....|....*....|....*.
gi 1907069530 438 VLAAEEVKTYKRRIEEMEEELQKTER 463
Cdd:TIGR02169 381 AETRDELKDYREKLEKLKREINELKR 406
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
78-482 |
3.32e-05 |
|
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: 47.74 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 78 TILVVKSRVYQVTEKQISEKLENIKKENAELMQK----------LSSYEQKIKESKKYV----------QETKKQNMils 137
Cdd:TIGR01612 737 IIVEIKKHIHGEINKDLNKILEDFKNKEKELSNKindyakekdeLNKYKSKISEIKNHYndqinidnikDEDAKQNY--- 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 138 DEAVKYKDKIKILEETNVSLGDKAKSLRLQLESEREQNVKNQDLILENKKS--------IEKLKDVISmnASELSEVQVA 209
Cdd:TIGR01612 814 DKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDKFINFENNCKEKIDSeheqfaelTNKIKAEIS--DDKLNDYEKK 891
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 210 LNEAK-LSEENVKSECHRVQEENArlkkkkeqlQQQVEEWSKSHAELTEQIKSFEKSQEDLE---------------IAL 273
Cdd:TIGR01612 892 FNDSKsLINEINKSIEEEYQNINT---------LKKVDEYIKICENTKESIEKFHNKQNILKeilnknidtikesnlIEK 962
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 274 THKDDNISALTNCITQLNRLECELESEDPDKGGNE-----SDDLAN-GETGG-------DRSEKIRNRIKQMM-----DV 335
Cdd:TIGR01612 963 SYKDKFDNTLIDKINELDKAFKDASLNDYEAKNNElikyfNDLKANlGKNKEnmlyhqfDEKEKATNDIEQKIedankNI 1042
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 336 SRTQTAV-----SIVEE-------DLKLLQLKLRASMSTKCNLEDQIK-KLE----DDRSSLQTAKAG-----LEDECKT 393
Cdd:TIGR01612 1043 PNIEIAIhtsiyNIIDEiekeigkNIELLNKEILEEAEINITNFNEIKeKLKhynfDDFGKEENIKYAdeinkIKDDIKN 1122
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 394 LRQKVEI-LNELYQQK--------EMALQ---------KKLSQEEYERQDREQR--LTAADEKVVLaAEEVKTYKRRIEE 453
Cdd:TIGR01612 1123 LDQKIDHhIKALEEIKkksenyidEIKAQindledvadKAISNDDPEEIEKKIEniVTKIDKKKNI-YDEIKKLLNEIAE 1201
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1907069530 454 ME------EELQKTERSFKNQIAA-------HEKKAHDNWLK 482
Cdd:TIGR01612 1202 IEkdktslEEVKGINLSYGKNLGKlflekidEEKKKSEHMIK 1243
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
89-507 |
6.35e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 6.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 89 VTEKQISEKLENIKKENAELMQKLSSYEqkIKESKKYVQETKKQNMILSDEAvkyKDKI--KIL-----EETNVSLGDKA 161
Cdd:PRK03918 97 LKYLDGSEVLEEGDSSVREWVERLIPYH--VFLNAIYIRQGEIDAILESDES---REKVvrQILglddyENAYKNLGEVI 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 162 KSLRLQLES-----EREQNVKNqdLILENKKSIEKLKDVISMNASELSEVQVALNEA---KLSEENVKSECHRVQEENAR 233
Cdd:PRK03918 172 KEIKRRIERlekfiKRTENIEE--LIKEKEKELEEVLREINEISSELPELREELEKLekeVKELEELKEEIEELEKELES 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 234 LKKKKEQLQQQVEEWSKSHAELTEQIKSFEKSQEDLEiALTHKDDNISAL----TNCITQLNRLECELESEDPDKGGNEs 309
Cdd:PRK03918 250 LEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLsefyEEYLDELREIEKRLSRLEEEINGIE- 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 310 DDLANGETGGDRSEKIRNRIKQmmdvsrTQTAVSIVEEDLKLLQlKLRASMSTKCNLEDQIK-----KLEDDRSSLQTAK 384
Cdd:PRK03918 328 ERIKELEEKEERLEELKKKLKE------LEKRLEELEERHELYE-EAKAKKEELERLKKRLTgltpeKLEKELEELEKAK 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 385 AGLEDECKTLRQKVEILNELYQQKEMALQK-------------KLSQEEYERQDREQRLTAAD--EKVVLAAEEVKTYKR 449
Cdd:PRK03918 401 EEIEEEISKITARIGELKKEIKELKKAIEElkkakgkcpvcgrELTEEHRKELLEEYTAELKRieKELKEIEEKERKLRK 480
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907069530 450 RIEEMEEELQKTERSFKNQIAAHEKKAHDNWLKaRAAERAMAEEKREAANLRHKLLEM 507
Cdd:PRK03918 481 ELRELEKVLKKESELIKLKELAEQLKELEEKLK-KYNLEELEKKAEEYEKLKEKLIKL 537
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
194-434 |
6.62e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 6.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 194 DVISMNASELSEVQVALNEAKLSEENVKSECHRVQEENARLKKKKEQLQQQVEEWSKSHAELTEQIKSFEKSQEDLEIAL 273
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 274 THKDDNISALTNCITQLNR---LECELESEDPDKGGNESDDLangetggdrSEKIRNRIKQMMDVSRTQTAVSIVEEDLK 350
Cdd:COG4942 100 EAQKEELAELLRALYRLGRqppLALLLSPEDFLDAVRRLQYL---------KYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 351 LLQLKLRASMStkcNLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEILnelyQQKEMALQKKLSQEEYERQDREQRL 430
Cdd:COG4942 171 AERAELEALLA---ELEEERAALEALKAERQKLLARLEKELAELAAELAEL----QQEAEELEALIARLEAEAAAAAERT 243
|
....
gi 1907069530 431 TAAD 434
Cdd:COG4942 244 PAAG 247
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
91-474 |
8.34e-05 |
|
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: 46.58 E-value: 8.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 91 EKQISEKLENIKKENAELMQ------------KLSSYEQKIKESKKYVQETKKQNMILSDEAVKYKDKIKILEEtNVSLg 158
Cdd:TIGR01612 1324 KKELQKNLLDAQKHNSDINLylneianiynilKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKD-DINL- 1401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 159 dkaKSLRLQLESERE--------QNVK-NQDLILENKKSIeklkDVISMNASELSEvQVALNEAKLSEENVKSE-CHRVQ 228
Cdd:TIGR01612 1402 ---EECKSKIESTLDdkdideciKKIKeLKNHILSEESNI----DTYFKNADENNE-NVLLLFKNIEMADNKSQhILKIK 1473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 229 EENARLKKKKEQLQQQvEEWSKSHAELTEQIKSFEKSQEDLEIALTHKDDnisaltncITQLNRLECELESEDP-DKGGN 307
Cdd:TIGR01612 1474 KDNATNDHDFNINELK-EHIDKSKGCKDEADKNAKAIEKNKELFEQYKKD--------VTELLNKYSALAIKNKfAKTKK 1544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 308 EsddlangetggdrSEKIRNRIKQMMDVSRTQTAVSiveedlkllQLKLRASMSTKCNLEDQIKKleDDRSS-----LQT 382
Cdd:TIGR01612 1545 D-------------SEIIIKEIKDAHKKFILEAEKS---------EQKIKEIKKEKFRIEDDAAK--NDKSNkaaidIQL 1600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 383 AKAGLEDECKTLRQKVEILNELYQQKEmALQKKLSQEEYERQDREQRLTAADEKVVLA-AEEVKTYKRRIEEMEEELQKT 461
Cdd:TIGR01612 1601 SLENFENKFLKISDIKKKINDCLKETE-SIEKKISSFSIDSQDTELKENGDNLNSLQEfLESLKDQKKNIEDKKKELDEL 1679
|
410
....*....|....*.
gi 1907069530 462 E---RSFKNQIAAHEK 474
Cdd:TIGR01612 1680 DseiEKIEIDVDQHKK 1695
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
90-437 |
8.75e-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: 46.21 E-value: 8.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 90 TEKQISEK---LENIKKENAELMQKLSSYEQKIKEskkyvqETKKQNMILSDEAVKYKDKIKILEETNVSLGDKAKSLRL 166
Cdd:TIGR02169 242 IERQLASLeeeLEKLTEEISELEKRLEEIEQLLEE------LNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKER 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 167 QLESEREQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALNEAKLSEENVKSEchrvqeenarlkkkkeqlqqqVE 246
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE---------------------LE 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 247 EWSKSHAELTEQIKSFEKSqedleialthkddnISALTNCITQLNRLECELesedpdkggnesddlangetgGDRSEKIR 326
Cdd:TIGR02169 375 EVDKEFAETRDELKDYREK--------------LEKLKREINELKRELDRL---------------------QEELQRLS 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 327 NRIKQMmdvsrtqtavsivEEDLKLLQLKLRASMSTKcnlEDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEILNELyQ 406
Cdd:TIGR02169 420 EELADL-------------NAAIAGIEAKINELEEEK---EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV-E 482
|
330 340 350
....*....|....*....|....*....|...
gi 1907069530 407 QKEMALQKKLSQEEYERQ--DREQRLTAADEKV 437
Cdd:TIGR02169 483 KELSKLQRELAEAEAQARasEERVRGGRAVEEV 515
|
|
| RND_1 |
NF037998 |
protein translocase SecDF, variant type; Members of this family are identified by TCDB as ... |
55-208 |
1.46e-04 |
|
protein translocase SecDF, variant type; Members of this family are identified by TCDB as belonging to 2.A.6.4.4, a variant 12-TM type SecDF, as found in Spiroplasma, Mesoplasma, and Acholeplasma.
Pssm-ID: 468306 Cd Length: 1237 Bit Score: 45.54 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 55 LPWQPVIITAVLGIVSFAIFSwRTILVVKSRvyqvteKQISEKlenIKKENAELMQKLSSYEQKIKESKkyvqetKKQNM 134
Cdd:NF037998 1006 VPITFEILIAFVSIIGFAIAS-AIIILGKAK------SLISSK---NKKELENYFKKEIEHRAQIKRLR------RELNN 1069
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907069530 135 ILSDEAVKYKDKIKILEETNVSLgdKAKSLRLQLESEREQNVKN-QDLILENKKSIEKLKDVISMNASE---LSEVQV 208
Cdd:NF037998 1070 ELFALKVEYKEEIKKLKIKNPKP--EKKELKKEFKEFKKQKKLDfKDLKKKIKKEKKANKKEINRVSKEnnfLKEVFN 1145
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
320-563 |
1.61e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.44 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 320 DRSEKIRNRIKQMMD-VSRTQTAVSIVEEDLKLLQLKLRASMSTKCNLEDQIK----KLEDDRSSLQTAKAGLEDECKTL 394
Cdd:TIGR02169 695 SELRRIENRLDELSQeLSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSsleqEIENVKSELKELEARIEELEEDL 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 395 RQKVEILNELYQQKEMA----LQKKLSQEEYERQDREQRLTAADEKV-------VLAAEEVKTYKRRIEEMEE---ELQK 460
Cdd:TIGR02169 775 HKLEEALNDLEARLSHSripeIQAELSKLEEEVSRIEARLREIEQKLnrltlekEYLEKEIQELQEQRIDLKEqikSIEK 854
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 461 TERSFKNQIAAHEKKAHDNWLKARAAERAMAEEKREAANLRHKLLEMTQKmamRQDEPVIVKPMPGRPNTQNPPRRGLLS 540
Cdd:TIGR02169 855 EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERK---IEELEAQIEKKRKRLSELKAKLEALEE 931
|
250 260
....*....|....*....|...
gi 1907069530 541 QNGSFGPSPVSGGECSPPLPAEP 563
Cdd:TIGR02169 932 ELSEIEDPKGEDEEIPEEELSLE 954
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
547-805 |
1.70e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 45.55 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 547 PSPVSGGECSPPLPAEPPGRPlSATLSRRDTPRSEFGSLDRHLPRPRWPSEASGKHSASDPG--PAPVVNSSSRSSSPAK 624
Cdd:PHA03307 64 RFEPPTGPPPGPGTEAPANES-RSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPAspPPSPAPDLSEMLRPVG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 625 AVDEGKQTVPQEPEGPSASSMAPLAGHPVAVNMAPKGPPPFPGVPLMGGPVPPPIRYGPPPQLCGGPFGPRPLPPPFVPG 704
Cdd:PHA03307 143 SPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAP 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 705 MHPP----------------------LGVREYAPGVLPGKRDLPLDPREFLPGHTPFRPPGSLGPREFFIPGTRLPPPTH 762
Cdd:PHA03307 223 APGRsaaddagasssdssssessgcgWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSS 302
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1907069530 763 GPQEYPPPPPAVRDSLPSGPREEAKPASPSSVQDRSQASKPTP 805
Cdd:PHA03307 303 PGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGP 345
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
288-522 |
1.80e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 288 TQLNRLECELESEDPDKGGNESDDLANGETGGDRSEKIRNRIKQMM-DVSRTQTAVSIVEEDLKLLQLKLRAsmstkcnL 366
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLReELEQAREELEQLEEELEQARSELEQ-------L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 367 EDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEILNELYQQkemaLQKKLSQEEYERQDREQRLTAADEKVVLAAEEVKT 446
Cdd:COG4372 79 EEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE----LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069530 447 YKRRIEEMEEELQKTERSFKNQIAAHEKKAHDNWLKARAAERAMAEEKREAANLRHKLLEMTQKMAMRQDEPVIVK 522
Cdd:COG4372 155 LEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAK 230
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
98-464 |
2.40e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 44.82 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 98 LENIKKENAELmqKLSSYEQKIKESKKYVQETKKQ--NMILSDEAVKYKDKIKILEETNVSLGDKAKSLRLQLESEREQN 175
Cdd:PTZ00440 839 LQKFPTEDENL--NLKELEKEFNENNQIVDNIIKDieNMNKNINIIKTLNIAINRSNSNKQLVEHLLNNKIDLKNKLEQH 916
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 176 VK----------NQDLILEN-----KKSIEKLKDVISMNASELsEVQVALNEAKLSEENVKSECHRVQEENARLKKKKEQ 240
Cdd:PTZ00440 917 MKiintdniiqkNEKLNLLNnlnkeKEKIEKQLSDTKINNLKM-QIEKTLEYYDKSKENINGNDGTHLEKLDKEKDEWEH 995
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 241 LQQQVEEWSKSHAELTEQIKSFEKSQEDLEIAL-----THKDDNISALT-NCITQLNRLECELESEDpdkggnESDDLAN 314
Cdd:PTZ00440 996 FKSEIDKLNVNYNILNKKIDDLIKKQHDDIIELidkliKEKGKEIEEKVdQYISLLEKMKTKLSSFH------FNIDIKK 1069
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 315 getggDRSEKIRNRIK----QMMDVSRtqtavSIVEEDLKLLQLKLRAS---MSTKCNLEDQIKKLEDDRSSLQTAKAGL 387
Cdd:PTZ00440 1070 -----YKNPKIKEEIKlleeKVEALLK-----KIDENKNKLIEIKNKSHehvVNADKEKNKQTEHYNKKKKSLEKIYKQM 1139
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 388 EDECKTLRQKVEILNELYQQKEMALQkklsqeeYER---QDREQRLTAADEKVVLAAEEVKTYKRRIEEMEEELQKTERS 464
Cdd:PTZ00440 1140 EKTLKELENMNLEDITLNEVNEIEIE-------YERiliDHIVEQINNEAKKSKTIMEEIESYKKDIDQVKKNMSKERND 1212
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
319-510 |
3.07e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 319 GDRSEKIRNRIKQMM----DVSRTQTAVSIVEEDLKLLQLKLRASMSTKCNLEDQIKKLEDDRSSLQTAKAGLEDECKTL 394
Cdd:PRK03918 199 EKELEEVLREINEISselpELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 395 RQKVEILNEL----------------YQQKEMALQKKLSQEEYERQDREQRLTAADEKVvlaaEEVKTYKRRIEEMEEEL 458
Cdd:PRK03918 279 EEKVKELKELkekaeeyiklsefyeeYLDELREIEKRLSRLEEEINGIEERIKELEEKE----ERLEELKKKLKELEKRL 354
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1907069530 459 QKTERSFKNQIAAHEKKAHDNWLKARAAERAMAEEKREAANLRHKLLEMTQK 510
Cdd:PRK03918 355 EELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEE 406
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
90-511 |
3.59e-04 |
|
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: 43.96 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 90 TEKQISEKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKQNMILSDEAVKYKDKIKILEETNVSLgdKAKSLRLQlE 169
Cdd:pfam05557 98 QLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSL--AEAEQRIK-E 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 170 SEREQNVKNQD-LILENKKS-------IEKLKDVI-SMNA--------SELSEVQVALNEAKLS-EENVKSECHRVQEEN 231
Cdd:pfam05557 175 LEFEIQSQEQDsEIVKNSKSelaripeLEKELERLrEHNKhlnenienKLLLKEEVEDLKRKLErEEKYREEAATLELEK 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 232 ARLKKkkeqlqqQVEEWSK----------SHAELTEQIKSFEksQEDleiaLTHKDDNiSALTNCITQLNRLECELESE- 300
Cdd:pfam05557 255 EKLEQ-------ELQSWVKlaqdtglnlrSPEDLSRRIEQLQ--QRE----IVLKEEN-SSLTSSARQLEKARRELEQEl 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 301 --------DPDKG-----------------------------GNESDDLANGETGGDRSEKIRNrIKQMMDvsRTQTAVS 343
Cdd:pfam05557 321 aqylkkieDLNKKlkrhkalvrrlqrrvllltkerdgyrailESYDKELTMSNYSPQLLERIEE-AEDMTQ--KMQAHNE 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 344 IVEEDLKLLQ-----LKLRASMstkcnLEDQIKKLeddRSSLQTAKAGL-EDECKTLRQKVEILneLYQQKEMALQKKLS 417
Cdd:pfam05557 398 EMEAQLSVAEeelggYKQQAQT-----LERELQAL---RQQESLADPSYsKEEVDSLRRKLETL--ELERQRLREQKNEL 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 418 QEEYERQDREQRLTAADEKVV-------LAAEEVKtyKRRIEEMEEELQKTERSFKNQIAAHEKKAHDNwlkaraaERAM 490
Cdd:pfam05557 468 EMELERRCLQGDYDPKKTKVLhlsmnpaAEAYQQR--KNQLEKLQAEIERLKRLLKKLEDDLEQVLRLP-------ETTS 538
|
490 500
....*....|....*....|.
gi 1907069530 491 AEEKREAANLRHKLLEMTQKM 511
Cdd:pfam05557 539 TMNFKEVLDLRKELESAELKN 559
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
365-473 |
3.99e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.05 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 365 NLEDQIKKLEDDRSSLQTAKAgledECKTLRQKVEILNELYQQKEMALQKKLsQEEYERQDREqrltaadekvvlAAEEV 444
Cdd:PRK00409 517 KLNELIASLEELERELEQKAE----EAEALLKEAEKLKEELEEKKEKLQEEE-DKLLEEAEKE------------AQQAI 579
|
90 100
....*....|....*....|....*....
gi 1907069530 445 KTYKRRIEEMEEELQKTERSFKNQIAAHE 473
Cdd:PRK00409 580 KEAKKEADEIIKELRQLQKGGYASVKAHE 608
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
508-672 |
6.70e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.39 E-value: 6.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 508 TQKMAMRQDEPVIVKPMPGRPNTQNPPRRGLLSQNGSFGPSPVSGGECSPPLPAEPPGRPLSATLSRRDTPRSEFGSLdR 587
Cdd:PHA03247 2919 PQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPL-T 2997
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 588 HLPRPRWPSEAS--GKHSASDPGPAPVVNSSSRSSSPAKAVDEgkQTVPQEPEGPSASSMAPLAGHPvavnMAPKGPPPF 665
Cdd:PHA03247 2998 GHSLSRVSSWASslALHEETDPPPVSLKQTLWPPDDTEDSDAD--SLFDSDSERSDLEALDPLPPEP----HDPFAHEPD 3071
|
....*..
gi 1907069530 666 PGVPLMG 672
Cdd:PHA03247 3072 PATPEAG 3078
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
93-214 |
7.96e-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: 41.83 E-value: 7.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 93 QISEKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKQNMILSDEAVKYKDKIKILEE--TNVSLGDKAKSLRLQLES 170
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlGNVRNNKEYEALQKEIES 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1907069530 171 EREQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALNEAK 214
Cdd:COG1579 101 LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK 144
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
101-462 |
9.42e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.85 E-value: 9.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 101 IKKENAELMQKLSSYEQKIKESKkyvQETKKQNMILSDEAVKYKDKikilEETNVSLGDKAKSLRLQLESereqnvKNQD 180
Cdd:pfam01576 382 LESENAELQAELRTLQQAKQDSE---HKRKKLEGQLQELQARLSES----ERQRAELAEKLSKLQSELES------VSSL 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 181 LILENKKSIEKLKDVISMNaSELSEVQVALNEAKLSEENVKSECHRVQEENArlkkkkeQLQQQVEEWSKSHAELTEQIK 260
Cdd:pfam01576 449 LNEAEGKNIKLSKDVSSLE-SQLQDTQELLQEETRQKLNLSTRLRQLEDERN-------SLQEQLEEEEEAKRNVERQLS 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 261 SFEKSQEDLEIALTHKDDNISALTNCITQLNRlecELESEdpdkggneSDDLANGETGGDRSEKIRNRIKQMMDvsrtqt 340
Cdd:pfam01576 521 TLQAQLSDMKKKLEEDAGTLEALEEGKKRLQR---ELEAL--------TQQLEEKAAAYDKLEKTKNRLQQELD------ 583
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 341 avsiveeDLKLLQLKLRASMStkcNLEDQIKKLEDDRSSLQTAKAGLEDEcktlRQKVEILNELYQQKEMALQKKLSQ-- 418
Cdd:pfam01576 584 -------DLLVDLDHQRQLVS---NLEKKQKKFDQMLAEEKAISARYAEE----RDRAEAEAREKETRALSLARALEEal 649
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907069530 419 ---EEYERQDREQRLTAAD---------------EKVVLAAE-EVKTYKRRIEEMEEELQKTE 462
Cdd:pfam01576 650 eakEELERTNKQLRAEMEDlvsskddvgknvhelERSKRALEqQVEEMKTQLEELEDELQATE 712
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
90-509 |
1.01e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.65 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 90 TEKQISEKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKQNmilsdeavKYKDKIKILEETNVSLGDKAKSLRLQLE 169
Cdd:TIGR00618 227 ELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIE--------ELRAQEAVLEETQERINRARKAAPLAAH 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 170 SER-EQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALNEAKLSEENVKSECHRVQEENARLKKKKEQLQQQVEEW 248
Cdd:TIGR00618 299 IKAvTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLT 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 249 S--------KSHAELTEQIKSFEKSQEDLEIALTH---------KDDNISALTNCITQLNRLE-CELESEDPDKGGNESD 310
Cdd:TIGR00618 379 QhihtlqqqKTTLTQKLQSLCKELDILQREQATIDtrtsafrdlQGQLAHAKKQQELQQRYAElCAAAITCTAQCEKLEK 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 311 DLANgetggDRSEKIRNRIKQMMDV-------SRTQTAVSIVEEDLKLLQLKLRASMSTKCNLEDQIKKLEDDRSSLQta 383
Cdd:TIGR00618 459 IHLQ-----ESAQSLKEREQQLQTKeqihlqeTRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQ-- 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 384 kaGLEDECKTLRQKVEILNELYQQKEMALQKKLSQEEYERQDrEQRLTAADEKVVLAAEEVKTYKRRIEEMEEELQKTER 463
Cdd:TIGR00618 532 --RGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQS-FSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAED 608
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1907069530 464 SFKNQIAAHEKKAHDNWLKARAAERAMAEEKREAANLRHK---LLEMTQ 509
Cdd:TIGR00618 609 MLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALhalQLTLTQ 657
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
77-466 |
1.25e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.50 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 77 RTILVVKSRVYQVTEKqiseKLENikkenaeLMQKLSSYEQKIKESKKYVQ--ETKKQNmilSDEAvkykdkIKILEEtn 154
Cdd:pfam10174 386 KDMLDVKERKINVLQK----KIEN-------LQEQLRDKDKQLAGLKERVKslQTDSSN---TDTA------LTTLEE-- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 155 vSLGDKAKSL-RLQLESEREQNVKnQDLILENKKSIEKLKDVISMNASELSEVQVALNEAK-----LSEENVKSECH--- 225
Cdd:pfam10174 444 -ALSEKERIIeRLKEQREREDRER-LEELESLKKENKDLKEKVSALQPELTEKESSLIDLKehassLASSGLKKDSKlks 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 226 -----RVQEENARLKKKKEQLQQQVEEWSKSHAELTEQIKSFEKsqedlEIALtHKDDNisalTNCITQLNRL-----EC 295
Cdd:pfam10174 522 leiavEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRIRLLEQ-----EVAR-YKEES----GKAQAEVERLlgilrEV 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 296 ELESEDPDKGGNESDDLANGEtGGDRSEKIRNrIKQMMDVSRTQTAvsiveedlKLLQLKLRASMSTKCN-----LEDQI 370
Cdd:pfam10174 592 ENEKNDKDKKIAELESLTLRQ-MKEQNKKVAN-IKHGQQEMKKKGA--------QLLEEARRREDNLADNsqqlqLEELM 661
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 371 KKLEDDRSSLQTAKAGLEDECKTLRQKVEILNELYQQKEMALQKKLSQeeyerqdREQRLTAA----DEKVVL------- 439
Cdd:pfam10174 662 GALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEM-------KQEALLAAisekDANIALlelsssk 734
|
410 420 430
....*....|....*....|....*....|.
gi 1907069530 440 ---AAEEVKTYKRRIEEMEEEL-QKTERSFK 466
Cdd:pfam10174 735 kkkTQEEVMALKREKDRLVHQLkQQTQNRMK 765
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
287-462 |
1.90e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 287 ITQLNRLECELESEDPDKGGNES--DDLANGETGGDRSEKIRNRIKQMMDVSRTQTAVSIVEEDLKLLQLKLRASMSTKC 364
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAElqEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 365 NLEDQIKKLEDdrssLQTAKAGLEDECKTLRQKveiLNELYQQKEMALQKKLSQEEYERQDREQRLTAADEKVVLAAEEV 444
Cdd:COG4717 150 ELEERLEELRE----LEEELEELEAELAELQEE---LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL 222
|
170
....*....|....*...
gi 1907069530 445 KTYKRRIEEMEEELQKTE 462
Cdd:COG4717 223 EELEEELEQLENELEAAA 240
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
88-460 |
2.08e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 88 QVTEKQISEKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKQNMILSDEAVKYKDKIKILEETNVSLGDKAKSLRLQ 167
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 168 LESEREQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALNEAK-------LSEENVKSECHRVQEENA------RL 234
Cdd:COG1196 472 AALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGlrglagaVAVLIGVEAAYEAALEAAlaaalqNI 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 235 KKKKEQLQQQVEEWSKSHAELTEQIKSFEKSQEDLEIALTHKDDNISALTNCITQLNRLECELESEDPDKGGNESDDLAN 314
Cdd:COG1196 552 VVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAAR 631
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 315 GETGGDRSEKIRNRIKQM---MDVSRTQTAVSIVEEDLKLLQLKLRASMSTKcnLEDQIKKLEDDRSSLQTAKAGLEDEC 391
Cdd:COG1196 632 LEAALRRAVTLAGRLREVtleGEGGSAGGSLTGGSRRELLAALLEAEAELEE--LAERLAEEELELEEALLAEEEEEREL 709
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907069530 392 KTLRQKVEILNELYQQKEMALQKKLSQEEYERQDREQRLTAADEKVVLAAEEVKTYKRRIEEMEEELQK 460
Cdd:COG1196 710 AEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
102-519 |
2.85e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 102 KKENAELMQKLSSYEQ--KIKESKKYVQETKKQNMILSDEAVKYKDKIKILEET-NVSLGDKAKSLRLQLESEREQNVKn 178
Cdd:PTZ00121 1195 KAEDARKAEAARKAEEerKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEErNNEEIRKFEEARMAHFARRQAAIK- 1273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 179 qdliLENKKSIEKLKdvismnasELSEVQVAlNEAKLSEENVKSECHRVQEENARLkkkkeqlqqqVEEWSKSHAELTEQ 258
Cdd:PTZ00121 1274 ----AEEARKADELK--------KAEEKKKA-DEAKKAEEKKKADEAKKKAEEAKK----------ADEAKKKAEEAKKK 1330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 259 IKSFEKSQEdleialthkddnisaltncitqlnrlecelESEDPDKGGNESDDLANGETGGDRSEKIRNRIKQMMDVSRT 338
Cdd:PTZ00121 1331 ADAAKKKAE------------------------------EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKA 1380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 339 QTAVSIVEEDLKLLQLKLRASMSTKcnLEDQIKKLEDDRSSLQTAKAGLEDECKT--LRQKVEILNELYQQKEMALQKKL 416
Cdd:PTZ00121 1381 DAAKKKAEEKKKADEAKKKAEEDKK--KADELKKAAAAKKKADEAKKKAEEKKKAdeAKKKAEEAKKADEAKKKAEEAKK 1458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 417 SQEEYERQDREQRLTAADEKVVLA--AEEVKTYKRRIEEMEEELQKTERSFKNqiAAHEKKAHDnwlKARAAERAMAEEK 494
Cdd:PTZ00121 1459 AEEAKKKAEEAKKADEAKKKAEEAkkADEAKKKAEEAKKKADEAKKAAEAKKK--ADEAKKAEE---AKKADEAKKAEEA 1533
|
410 420
....*....|....*....|....*
gi 1907069530 495 REAANLRhKLLEMTQKMAMRQDEPV 519
Cdd:PTZ00121 1534 KKADEAK-KAEEKKKADELKKAEEL 1557
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
91-271 |
3.39e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 91 EKQISEKLENIKKENAELmqklssyEQKIKESKKYVQETKKQNmilsdeavkykDKIKILEETNVSLGDKAKSLRL---Q 167
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNL-------EQKQKELKSKEKELKKLN-----------EEKKELEEKVKDLTKKISSLKEkieK 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 168 LESEREQnvKNQDlILENKKSIEKLKDVISMNA--SELSEVQVALNEAKLSEENVKSECHRVQEENARLKKKKEQLQQQV 245
Cdd:TIGR04523 529 LESEKKE--KESK-ISDLEDELNKDDFELKKENleKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEI 605
|
170 180
....*....|....*....|....*.
gi 1907069530 246 EEWSKSHAELTEQIKSFEKSQEDLEI 271
Cdd:TIGR04523 606 EEKEKKISSLEKELEKAKKENEKLSS 631
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
96-464 |
3.43e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.93 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 96 EKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKQNMILSDEAVKYKDKI----KILEETNVSLGDKAKSLR-LQLES 170
Cdd:pfam01576 173 EKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIaelqAQIAELRAQLAKKEEELQaALARL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 171 EREQNVKNQDLilenkKSIEKLKDVISMNASELSEVQVALNEAK-----LSEE--NVKSECHRV-------QEENARLKK 236
Cdd:pfam01576 253 EEETAQKNNAL-----KKIRELEAQISELQEDLESERAARNKAEkqrrdLGEEleALKTELEDTldttaaqQELRSKREQ 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 237 KKEQLQQQVEEWSKSHA---------------ELTEQIKSFEKSQEDLE---IALTHKDDNISALTNCITQlNRLECE-- 296
Cdd:pfam01576 328 EVTELKKALEEETRSHEaqlqemrqkhtqaleELTEQLEQAKRNKANLEkakQALESENAELQAELRTLQQ-AKQDSEhk 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 297 ---LESEDPDKGGNESDDLANGETGGDRSEKIRNRIKQMMDV--------SRTQTAVSIVEEDLKLLQLKLRASMSTKCN 365
Cdd:pfam01576 407 rkkLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLlneaegknIKLSKDVSSLESQLQDTQELLQEETRQKLN 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 366 LEDQIKKLEDDRSSLQTAkagLEDECKTlRQKVEILNELYQQKEMALQKKLSQEeyerqdrEQRLTAADEKVVLAAEEVK 445
Cdd:pfam01576 487 LSTRLRQLEDERNSLQEQ---LEEEEEA-KRNVERQLSTLQAQLSDMKKKLEED-------AGTLEALEEGKKRLQRELE 555
|
410
....*....|....*....
gi 1907069530 446 TYKRRIEEMEEELQKTERS 464
Cdd:pfam01576 556 ALTQQLEEKAAAYDKLEKT 574
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
253-441 |
4.04e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 40.81 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 253 AELTEQIKSFEKSQEDLEIALthkDDNISALTNCitqLNRLECELESEDPDKGGNESDDLANG-ETGGDRSEKIRNRIKQ 331
Cdd:pfam05911 647 AQVDNGCSEIDNLSSDPEIPS---DGPLVSGSND---LKTEENKRLKEEFEQLKSEKENLEVElASCTENLESTKSQLQE 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 332 MmdvsrtqtavsivEEDLKLLQLKLRASMSTKCNLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEILN--------- 402
Cdd:pfam05911 721 S-------------EQLIAELRSELASLKESNSLAETQLKCMAESYEDLETRLTELEAELNELRQKFEALEveleeeknc 787
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1907069530 403 ---------ELYQQKEMALQKKLS-----QEEYE-RQDREqrLTAADEKvvLAA 441
Cdd:pfam05911 788 heeleakclELQEQLERNEKKESSncdadQEDKKlQQEKE--ITAASEK--LAE 837
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
92-441 |
4.36e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 40.26 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 92 KQISEKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKQNMILSDEAVKYKDKIKILEETNVSLGDKAKSLRLQLESE 171
Cdd:pfam07888 76 RELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 172 REQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALNEAKLSEENVKSECHRVQEENARLKKKKEQLQQQVEEWSKS 251
Cdd:pfam07888 156 KERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 252 HAELTEQIKSFEKSQ-------EDLEIALTHKDDNISALTNCITQLNRLECELES------EDPDKGGNESDDL-ANGET 317
Cdd:pfam07888 236 LEELRSLQERLNASErkveglgEELSSMAAQRDRTQAELHQARLQAAQLTLQLADaslalrEGRARWAQERETLqQSAEA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 318 GGDRSEKIRNRIKQMMDvsrtqtavSIVEEDLKLLQLKLRASMSTKCNLedqiKKLEDDRSSLQTAKAGLEdecktLRQK 397
Cdd:pfam07888 316 DKDRIEKLSAELQRLEE--------RLQEERMEREKLEVELGREKDCNR----VQLSESRRELQELKASLR-----VAQK 378
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1907069530 398 veilnelyqQKEMALQKKLSQEEYERQdREQRL-TAADEKVVLAA 441
Cdd:pfam07888 379 ---------EKEQLQAEKQELLEYIRQ-LEQRLeTVADAKWSEAA 413
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
97-463 |
4.65e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 97 KLENIKKENAELMQKLSSYEQKIKESKKYVQETKKQNMILSDEAVKYKDKIKILEETNVSLGDkakslrlqlesereQNV 176
Cdd:pfam01576 83 RLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLED--------------QNS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 177 KnqdLILENKKSIEKLKDVISmNASELSEVQVALNEAKLSEENVKS--ECHRVQEENARLKKKKEQLQQQVE--EWSKSH 252
Cdd:pfam01576 149 K---LSKERKLLEERISEFTS-NLAEEEEKAKSLSKLKNKHEAMISdlEERLKKEEKGRQELEKAKRKLEGEstDLQEQI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 253 AELTEQIK----SFEKSQEDLEIALTHKDDNISALTNCITQLNRLEC-------ELESEDPDKGGNESD--DLangetgG 319
Cdd:pfam01576 225 AELQAQIAelraQLAKKEEELQAALARLEEETAQKNNALKKIRELEAqiselqeDLESERAARNKAEKQrrDL------G 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 320 DRSEKIRNRIKQMMDVSRTQTAV-SIVEEDLKLLQLKLR----------ASMSTKCN-----LEDQIKKLEDDRSSLQTA 383
Cdd:pfam01576 299 EELEALKTELEDTLDTTAAQQELrSKREQEVTELKKALEeetrsheaqlQEMRQKHTqaleeLTEQLEQAKRNKANLEKA 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 384 KAGLEDECKTLRQKVEILNELYQQKE----------MALQKKLSQEEYERQDREQR--------------LTAADEKVVL 439
Cdd:pfam01576 379 KQALESENAELQAELRTLQQAKQDSEhkrkklegqlQELQARLSESERQRAELAEKlsklqselesvsslLNEAEGKNIK 458
|
410 420
....*....|....*....|....
gi 1907069530 440 AAEEVKTYKRRIEEMEEELQKTER 463
Cdd:pfam01576 459 LSKDVSSLESQLQDTQELLQEETR 482
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
367-468 |
4.71e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 367 EDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEILNELYQQKEmalqkklsqeeyerqdreQRLTAADEKVVLAAEEVKT 446
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQ------------------AELEALQAEIDKLQAEIAE 76
|
90 100
....*....|....*....|..
gi 1907069530 447 YKRRIEEMEEELQKTERSFKNQ 468
Cdd:COG3883 77 AEAEIEERREELGERARALYRS 98
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
95-428 |
5.56e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 95 SEKLENIKKENAELMQKLSSYEQKIK--ESKKYVQETKKQNMILSDEAVKYK-DKIKILEETNVSlgdKAKSLRlqlESE 171
Cdd:PTZ00121 1583 AEEAKKAEEARIEEVMKLYEEEKKMKaeEAKKAEEAKIKAEELKKAEEEKKKvEQLKKKEAEEKK---KAEELK---KAE 1656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 172 REQNVKNQDlilENKKSIEKLKDVISMNASELSEVQVALNEAKLSEENVKSEchRVQEENARLKKKKEQLQQQVEEWSKS 251
Cdd:PTZ00121 1657 EENKIKAAE---EAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE--ELKKKEAEEKKKAEELKKAEEENKIK 1731
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 252 HAELTEQIKSFEKSQEDL--------EIALTHKDDNISALTNCITQLNRLECELESEDPDKGGNES-------DDLANGE 316
Cdd:PTZ00121 1732 AEEAKKEAEEDKKKAEEAkkdeeekkKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDkkikdifDNFANII 1811
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 317 TGGDRSEKIRNRIKQMMDVSRTQTAVS---IVEEDLKLLQLKLRA-------------SMSTKCNLEDQIKKLEDDRSSL 380
Cdd:PTZ00121 1812 EGGKEGNLVINDSKEMEDSAIKEVADSknmQLEEADAFEKHKFNKnnengedgnkeadFNKEKDLKEDDEEEIEEADEIE 1891
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1907069530 381 QTAKAGLEDecktlrqkvEILNELYQQKEM-ALQKKLSQEEYERQDREQ 428
Cdd:PTZ00121 1892 KIDKDDIER---------EIPNNNMAGKNNdIIDDKLDKDEYIKRDAEE 1931
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
381-469 |
5.82e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 37.94 E-value: 5.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 381 QTAKAGLEDECKTLRQKVEILNELYQQKEMALQKKLSQEEYERQDREQRLtaadekvvlaAEEVKTYKRRIEEMEEELQK 460
Cdd:pfam03938 18 KAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQEL----------QKKEQELQQLQQKAQQELQK 87
|
....*....
gi 1907069530 461 TERSFKNQI 469
Cdd:pfam03938 88 KQQELLQPI 96
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
92-469 |
6.34e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 40.20 E-value: 6.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 92 KQISEKLENIKKENAELmqkLSSYEQKIKESKkyvQETKKQNMILSDEAV----KYKDKIKILEETNvslgDKAKSLRLQ 167
Cdd:PTZ00440 399 EYFISKYTNIISLSEHT---LKAAEDVLKENS---QKIADYALYSNLEIIeikkKYDEKINELKKSI----NQLKTLISI 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 168 LESEreqnvknQDLILENKKSIEKLKDVISMNASELSEVQVALNeaklSEENVKSECHRVQEEnarlKKKKEQLQQQVEE 247
Cdd:PTZ00440 469 MKSF-------YDLIISEKDSMDSKEKKESSDSNYQEKVDELLQ----IINSIKEKNNIVNNN----FKNIEDYYITIEG 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 248 WSKSHAELTEQIKSFEKSQEDL----EIALTHKDD------NISALTNCITQLNRLECELESEDPDKGGNESDDLANGET 317
Cdd:PTZ00440 534 LKNEIEGLIELIKYYLQSIETLikdeKLKRSMKNDiknkikYIEENVDHIKDIISLNDEIDNIIQQIEELINEALFNKEK 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 318 GGDRSEKIRNRIKQMMDvsrtqtavSIVEEDLKLLQLKLRASMSTKCNLEDQIKKLEDDRSSLQTAKAgledECKTLRQK 397
Cdd:PTZ00440 614 FINEKNDLQEKVKYILN--------KFYKGDLQELLDELSHFLDDHKYLYHEAKSKEDLQTLLNTSKN----EYEKLEFM 681
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907069530 398 V-----EILNELYQ--QKEMALQKKLSQEEYErqDREQRLTAADEKVVlaaEEVKTYKRRIEEMEEELQKTErSFKNQI 469
Cdd:PTZ00440 682 KsdnidNIIKNLKKelQNLLSLKENIIKKQLN--NIEQDISNSLNQYT---IKYNDLKSSIEEYKEEEEKLE-VYKHQI 754
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
91-390 |
6.55e-03 |
|
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: 39.94 E-value: 6.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 91 EKQISEKLENIKKENAELMQKLSSYEQKIKESKKYVQetkKQNMILSDEAVK-YKDKIKILEEtnvslgdKAKSLRLQLE 169
Cdd:COG5185 277 SKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATES---LEEQLAAAEAEQeLEESKRETET-------GIQNLTAEIE 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 170 SEREQNVKNQDLILENKKSIEKLKDvISMNASELSEVQVALNEAKLSEENVKSECHRVQEENARLKKkkeqlqqqveews 249
Cdd:COG5185 347 QGQESLTENLEAIKEEIENIVGEVE-LSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLE------------- 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 250 kshAELTEQIKSFEKSQEDLEIALTHKDDNISALTNCITQLNRLECELESEDPDKGGNESDDLAN-GETGGDRSEKIRNR 328
Cdd:COG5185 413 ---DTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRsVRSKKEDLNEELTQ 489
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907069530 329 IKQmmdvsrtqtAVSIVEEDLKLLQLKLRASMSTKCNLEDQIKKLEDDRSSLQTAKAGLEDE 390
Cdd:COG5185 490 IES---------RVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALE 542
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
201-442 |
6.84e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 6.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 201 SELSEVQVALNEAKLSEENVKSECHRVQEENARLKKKKEQLQQQVEEWSKSHAELTEQIKSFEKSQEDLEIALthkDDNI 280
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL---GERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 281 SALTNCITQLNRLECELESEDPdkggnesDDLAngetggdrsekirNRIKQMMDVSRTQTAvsIVEEdLKLLQLKLRAsm 360
Cdd:COG3883 93 RALYRSGGSVSYLDVLLGSESF-------SDFL-------------DRLSALSKIADADAD--LLEE-LKADKAELEA-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 361 sTKCNLEDQIKKLEDDRSSLQTAKAGLEdecKTLRQKVEILNELyQQKEMALQKKLSQEEYERQDREQRLTAADEKVVLA 440
Cdd:COG3883 148 -KKAELEAKLAELEALKAELEAAKAELE---AQQAEQEALLAQL-SAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
..
gi 1907069530 441 AE 442
Cdd:COG3883 223 AA 224
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
92-375 |
7.12e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.50 E-value: 7.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 92 KQISEKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKQNMILSDEAVKYKDKIKILEETNVSLGDKAKSLRLQLESE 171
Cdd:COG4372 55 EQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 172 REQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALNEAKLSE-ENVKSECHRVQEENARLKKKKEQLQQQVEEWSK 250
Cdd:COG4372 135 EAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 251 SHAELTEQIKSFEKSQEDLEIALTHKDDNISALTNCITQLNRLECELESEDPD--KGGNESDDLANGETGGDRSEKIRNR 328
Cdd:COG4372 215 ELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIlvEKDTEEEELEIAALELEALEEAALE 294
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1907069530 329 IKQMMDVSRTQTAVSIVEEDLKLLQLKLRASMSTKCNLEDQIKKLED 375
Cdd:COG4372 295 LKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELAD 341
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
63-179 |
7.38e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 37.84 E-value: 7.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 63 TAVLGIVSFAIFSWRTILVVKSRVYQVTE---KQISEKLENIKKENAELMQKLSSYEQKIKESKKyvqetKKQNMIlsDE 139
Cdd:COG0711 2 TLFWQLINFLILVLLLKKFAWPPILKALDerqEKIADGLAEAERAKEEAEAALAEYEEKLAEARA-----EAAEII--AE 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1907069530 140 AVKYKDKIK--ILEETNVSLGDKAKSLRLQLESEREQ---NVKNQ 179
Cdd:COG0711 75 ARKEAEAIAeeAKAEAEAEAERIIAQAEAEIEQERAKalaELRAE 119
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
401-475 |
7.57e-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: 39.36 E-value: 7.57e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907069530 401 LNELyQQKEMALQKKLSQEEYERQDREQRLTAADEKVVLAAEEVKTYKRRIEEMEEELQKTERsfknQIAAHEKK 475
Cdd:COG4942 29 LEQL-QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK----EIAELRAE 98
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
91-218 |
7.85e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.12 E-value: 7.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 91 EKQISEKLENIKKEnAELMQKLSSYEQKIKESKKYVQETKKQNMILSDEAVKYKDKIKILEETNVSLGDKAKSLRLQLES 170
Cdd:COG1340 135 EKELVEKIKELEKE-LEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADE 213
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1907069530 171 EREQNVKNQD-------LILENKKSIEKLKDVISMNASELSEVQVALNEAKLSEE 218
Cdd:COG1340 214 LHKEIVEAQEkadelheEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEK 268
|
|
| cc_LAMB4_C |
cd22301 |
C-terminal coiled-coil domain found in laminin subunit beta-4 (LAMB4); LAMB4, also called ... |
92-147 |
7.98e-03 |
|
C-terminal coiled-coil domain found in laminin subunit beta-4 (LAMB4); LAMB4, also called laminin beta-1-related protein, is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Mutations or loss of LAMB4 may be features of gastric and colorectal cancers. Reduced LAMB4 levels may contribute to colonic dysmotility associated with diverticulitis. This model corresponds to the C-terminal coiled-coil domain of LAMB4, which may be involved in the integrin binding activity.
Pssm-ID: 411972 [Multi-domain] Cd Length: 70 Bit Score: 35.79 E-value: 7.98e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069530 92 KQISEKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKQNMILSDEAVKYKDKI 147
Cdd:cd22301 5 KNIKKEAENLAKEIEDKMKRIEDLEKRIQDLNKRKEDKANQLARLEKQVISLRKEI 60
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| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
351-478 |
8.94e-03 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 37.68 E-value: 8.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 351 LLQLKLRaSMSTKCNLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEilneLYQQKEMALQKKLSQEEyeRQDREQRl 430
Cdd:pfam11559 43 LLQQRDR-DLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLERELA----LLQAKERQLEKKLKTLE--QKLKNEK- 114
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90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1907069530 431 taadekvvlaaeevktykrrieemeEELQKTER---SFKNQiAAHEKKAHD 478
Cdd:pfam11559 115 -------------------------EELQRLKNalqQIKTQ-FAHEVKKRD 139
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| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
525-805 |
9.20e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 39.92 E-value: 9.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 525 PGRPN-----TQNPPRRGLLSQNGSFGPSpvsggeCSPPLPAEPPGRPLSATLSRRDTPRSEFGSLDRHLPRPRWPS-EA 598
Cdd:PHA03247 2670 LGRAAqasspPQRPRRRAARPTVGSLTSL------ADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPApPA 2743
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 599 SGKHSASDPGPAPVVNSSSRSSSPAKAVDEGKQTVPQE----PEGPSASSMAPLAGHPVAVNMAPKG-PPPFPGVPLMGG 673
Cdd:PHA03247 2744 VPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRrltrPAVASLSESRESLPSPWDPADPPAAvLAPAAALPPAAS 2823
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 674 PVPPPIRYGPPPQLCGGPFGPRPLPPPFVPGMHPPLG--VREYAPGVLPGKRDLPLDPR-EFLPGHTPFRPPGS--LGPR 748
Cdd:PHA03247 2824 PAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGdvRRRPPSRSPAAKPAAPARPPvRRLARPAVSRSTESfaLPPD 2903
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250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907069530 749 EFFIPGTRLPPPTHGPQEYPPPPPAVRDSLPSGPREEAKPASPSSVQDRSQASKPTP 805
Cdd:PHA03247 2904 QPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVP 2960
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| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
92-230 |
9.60e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.42 E-value: 9.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069530 92 KQISEKLENIKkenaELMQKLSS----YEQKIKESKKYVQETKKQNMILSDEAVKYKDKIkileetnvslgdkaKSLRLQ 167
Cdd:PRK00409 509 KLIGEDKEKLN----ELIASLEElereLEQKAEEAEALLKEAEKLKEELEEKKEKLQEEE--------------DKLLEE 570
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90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907069530 168 LESEREQNVKN----QDLILENKKSIEKLKDViSMNASELSEVQVALNEAKLSEENVKSECHRVQEE 230
Cdd:PRK00409 571 AEKEAQQAIKEakkeADEIIKELRQLQKGGYA-SVKAHELIEARKRLNKANEKKEKKKKKQKEKQEE 636
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