|
Name |
Accession |
Description |
Interval |
E-value |
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
122-447 |
8.96e-110 |
|
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: 333.02 E-value: 8.96e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 122 RPMDELVTLEEA----DGGSDILLVVPKATVLQNQLDESQQERNDLMQL------------------KLQLEDQVTELRS 179
Cdd:pfam07888 1 KPLDELVTLEEEshgeEGGTDMLLVVPRAELLQNRLEECLQERAELLQAqeaanrqrekekerykrdREQWERQRRELES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 180 RVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGDHVARILELEDDIQTMSDKVLMKEVELDRVRDTVK 259
Cdd:pfam07888 81 RVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 260 altreqeKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELE 339
Cdd:pfam07888 161 -------KAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 340 PLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSRLEVAEVNGRLAELSLHMKEEKCQWSKERTGLLQSM 419
Cdd:pfam07888 234 ALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSA 313
|
330 340
....*....|....*....|....*...
gi 148672009 420 EAEKDKILKLSAEILRLEKTVQEERTQK 447
Cdd:pfam07888 314 EADKDRIEKLSAELQRLEERLQEERMER 341
|
|
| SKICH |
pfam17751 |
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The ... |
15-118 |
9.21e-41 |
|
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The functions of the SKICH domains of NDP52 and CALCOCO1 are not known.
Pssm-ID: 465482 Cd Length: 102 Bit Score: 140.84 E-value: 9.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 15 VNFLNVARTYIPNTKVECHYTLPPGTMPSASDWIGIFKVEAACVRDYHTFVWssVPESTTDGSPTHASVQFQASYLPKPG 94
Cdd:pfam17751 1 VVFQNVGEWYPPDEDIECSYTLTPDFTPSSWDWIGLFKVGWKSVNDYVTYVW--AKDDEVEGSNSVRQVLFKASYLPKEP 78
|
90 100
....*....|....*....|....
gi 148672009 95 AQLYQFRYVNRQGRVCGQSPPFQF 118
Cdd:pfam17751 79 EGFYQFCYVSNLGSVVGISTPFQF 102
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
145-437 |
7.54e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 80.37 E-value: 7.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 145 KATVLQNQLDESQQErndLMQLKLQ-LEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQ 223
Cdd:COG1196 214 RYRELKEELKELEAE---LLLLKLReLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 224 GDHVARILELEDDIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREEncclnteLEEA 303
Cdd:COG1196 291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE-------LAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 304 KSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRS 383
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 148672009 384 RLEVAEVNGRLAELSLHMKEEKCQWSKERTGLLQSMEAEKDKILKLSAEILRLE 437
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
145-434 |
2.79e-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: 75.48 E-value: 2.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 145 KATVLQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSelteqykglsrshgELSEERDILSQQQG 224
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS--------------ELEEEIEELQKELY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 225 DHVARILELEDDIQtmsdkvlMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTV-------REENCCLN 297
Cdd:TIGR02168 292 ALANEISRLEQQKQ-------ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELkeeleslEAELEELE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 298 TELEEAKSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQL-----RGVQELAASSQQKAALLGEELASAAGA 372
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLedrreRLQQEIEELLKKLEEAELKELQAELEE 444
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148672009 373 RDRTIAEL------HRSRLEVAEVNGRLAELSLHMKEEKCQWSKERTGLLQSMEAEKDKILKLSAEIL 434
Cdd:TIGR02168 445 LEEELEELqeelerLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALL 512
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
150-397 |
7.03e-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: 74.32 E-value: 7.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 150 QNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATAR-------QEHSELTEQYKGLSRSHGELSEERDILSQQ 222
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRkeleelsRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 223 QGDHVARILELEDDIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEE 302
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 303 AKSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAE----LEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIA 378
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEEleseLEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915
|
250
....*....|....*....
gi 148672009 379 ELHRSRLEVAEVNGRLAEL 397
Cdd:TIGR02168 916 ELEELREKLAQLELRLEGL 934
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
170-446 |
8.80e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.82 E-value: 8.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 170 LEDQVTELRSRVQELE--AALATARQEHSELTEQYKGLSRSHgelseERDILSQQQGDHVARILELEDDIQTMSDKVLMK 247
Cdd:COG1196 191 LEDILGELERQLEPLErqAEKAERYRELKEELKELEAELLLL-----KLRELEAELEELEAELEELEAELEELEAELAEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 248 EVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQEEQGAQVQRLKDKLAHMKDT 327
Cdd:COG1196 266 EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 328 LGQAQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSRLEVAEVNGRLAELSLHMKEEKCQ 407
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
250 260 270
....*....|....*....|....*....|....*....
gi 148672009 408 WSKERTGLLQSMEAEKDKILKLSAEILRLEKTVQEERTQ 446
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
167-444 |
1.69e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 72.79 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 167 KLQLEDQVTELRSRVQELEAALATARQEHS-------ELTEQYKGLSRSHGELSEERDILSQQQGDHVARILELEDDIQT 239
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKRELSSLQSELRrienrldELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 240 MSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADK-----EQSEAELQTVREENCCLNTELEEAKSRQEEQGAQV 314
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLshsriPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 315 QRLKDKLAHMKDTLGQAQQKV----AELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSRLEVAEV 390
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIksieKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEL 908
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 148672009 391 NGRLAELSLHMKEEKCQWSkERTGLLQSMEAEKDKILKLSAEILRLEKtVQEER 444
Cdd:TIGR02169 909 EAQIEKKRKRLSELKAKLE-ALEEELSEIEDPKGEDEEIPEEELSLED-VQAEL 960
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
149-391 |
2.24e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.40 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGDHVA 228
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 229 RILELEDDIQTMSDKVLMKEVELDRvrdtvkaLTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQE 308
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAEIEE-------LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 309 EQGAQVQRLKDKLAHMKDTLGQAQQKVAElepLKEQLRGVQELAAssQQKAALLGEELASAAGARDRtIAELHRSRLEVA 388
Cdd:TIGR02168 912 ELRRELEELREKLAQLELRLEGLEVRIDN---LQERLSEEYSLTL--EEAEALENKIEDDEEEARRR-LKRLENKIKELG 985
|
...
gi 148672009 389 EVN 391
Cdd:TIGR02168 986 PVN 988
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
149-397 |
1.74e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.58 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGDHVA 228
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 229 RILELEDDIQTmsdkvlmKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQE 308
Cdd:COG1196 394 AAAELAAQLEE-------LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 309 EQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQ----LRGVQELAASSQQK------AALLGEELASAAGARDRTIA 378
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADyegfLEGVKAALLLAGLRglagavAVLIGVEAAYEAALEAALAA 546
|
250
....*....|....*....
gi 148672009 379 ELHRSRLEVAEVNGRLAEL 397
Cdd:COG1196 547 ALQNIVVEDDEVAAAAIEY 565
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
145-375 |
5.85e-12 |
|
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: 67.10 E-value: 5.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 145 KATVLQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQG 224
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 225 DHVARILELEDDIQTMSDKVLMKEV-------ELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREEnccLN 297
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLALLlspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE---LE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148672009 298 TELEEAKSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLrgvQELAASSQQKAALLGEELASAAGARDR 375
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL---EALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
169-451 |
1.42e-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: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 169 QLEDQVTELRSRVQELEAAlATARQEHSELTEQYKGLSRS---------HGELSEERDILSQQQGDHV---ARILELEDD 236
Cdd:TIGR02168 190 RLEDILNELERQLKSLERQ-AEKAERYKELKAELRELELAllvlrleelREELEELQEELKEAEEELEeltAELQELEEK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 237 IQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTvreenccLNTELEEAKSRQEEQGAQVQR 316
Cdd:TIGR02168 269 LEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE-------LEAQLEELESKLDELAEELAE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 317 LKDKLA----HMKDTLGQAQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSRLEV----A 388
Cdd:TIGR02168 342 LEEKLEelkeELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRerlqQ 421
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148672009 389 EVNGRLAELSLH-MKEEKCQWSKERTGLLQSMEAEKDKILKLSAEILRLEKTVQEERTQKSRVQ 451
Cdd:TIGR02168 422 EIEELLKKLEEAeLKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
149-354 |
1.63e-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: 66.63 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGDHVA 228
Cdd:TIGR02169 341 LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 229 RILELEDDIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQE 308
Cdd:TIGR02169 421 ELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAR 500
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 148672009 309 EQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRGVQELAAS 354
Cdd:TIGR02169 501 ASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAG 546
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
155-345 |
1.88e-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: 66.63 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 155 ESQQERNDLMQLKLQLED-QVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGDHVARILEL 233
Cdd:TIGR02169 766 RIEELEEDLHKLEEALNDlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 234 EDDIqtmsdkvlmkevelDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQEEQGAQ 313
Cdd:TIGR02169 846 KEQI--------------KSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ 911
|
170 180 190
....*....|....*....|....*....|..
gi 148672009 314 VQRLKDKLAHMKDTLGQAQQKVAELEPLKEQL 345
Cdd:TIGR02169 912 IEKKRKRLSELKAKLEALEEELSEIEDPKGED 943
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
197-397 |
6.52e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.47 E-value: 6.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 197 ELTEQYKGLSRSHGELSEERdilsqQQGDHVARILELEDDIQTMSDKVLmkevELDRVRDTVKALTREQEKLL--RQLKE 274
Cdd:COG4913 229 ALVEHFDDLERAHEALEDAR-----EQIELLEPIRELAERYAAARERLA----ELEYLRAALRLWFAQRRLELleAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 275 FQADKEQSEAELQTVREENCCLNTELEEAK-SRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELE--------PLKEQL 345
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREELDELEaQIRGNGGDRLEQLEREIERLERELEERERRRARLEallaalglPLPASA 379
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 148672009 346 RGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSRLEVAEVNGRLAEL 397
Cdd:COG4913 380 EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL 431
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
251-452 |
9.40e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.23 E-value: 9.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 251 LDRVRDTVKALTREQEKLLRQ-------------LKEFQ-----ADKEQSEAELQTVREENCCLNTELEEAKSRQEEQGA 312
Cdd:TIGR02168 188 LDRLEDILNELERQLKSLERQaekaerykelkaeLRELElallvLRLEELREELEELQEELKEAEEELEELTAELQELEE 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 313 QVQRLKDKLAHMKDTLGQAQQK----VAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSRLEVA 388
Cdd:TIGR02168 268 KLEELRLEVSELEEEIEELQKElyalANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE 347
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148672009 389 EVNGRLAELSLHMKEEKCQWSKERTGLLQS---MEAEKDKILKLSAEILRLEKTVQEERTQKSRVQD 452
Cdd:TIGR02168 348 ELKEELESLEAELEELEAELEELESRLEELeeqLETLRSKVAQLELQIASLNNEIERLEARLERLED 414
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
145-372 |
3.40e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 58.30 E-value: 3.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 145 KATVLQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRShgelseerdilSQQQG 224
Cdd:COG3883 31 ELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA-----------LYRSG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 225 DHVARILEL--EDDIQTMsdkvlmkeveLDRVrDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREEnccLNTELEE 302
Cdd:COG3883 100 GSVSYLDVLlgSESFSDF----------LDRL-SALSKIADADADLLEELKADKAELEAKKAELEAKLAE---LEALKAE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 303 AKSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGA 372
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
149-372 |
5.85e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.53 E-value: 5.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 149 LQNQLDESQQERNDL-------MQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRShgelseerdilSQ 221
Cdd:COG3883 28 LQAELEAAQAELDALqaeleelNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA-----------LY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 222 QQGDHVARILEL--EDDIQTMSDKVLMkeveLDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREEnccLNTE 299
Cdd:COG3883 97 RSGGSVSYLDVLlgSESFSDFLDRLSA----LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE---LEAA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148672009 300 LEEAKSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGA 372
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
155-449 |
1.01e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.74 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 155 ESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGDHVARILELE 234
Cdd:PRK02224 248 ERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELR 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 235 DDIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQEEQGAQV 314
Cdd:PRK02224 328 DRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 315 QRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRGVQELAASSQQKAA-------LLGEELASAAGARDRTIAELHRS---- 383
Cdd:PRK02224 408 GNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpVEGSPHVETIEEDRERVEELEAEledl 487
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 384 RLEVAEVNGRLAEL-SLHMKEEKCQWSKERTGLLQSMEAEKDKIL---KLSAEILRLEKTVQEERTQKSR 449
Cdd:PRK02224 488 EEEVEEVEERLERAeDLVEAEDRIERLEERREDLEELIAERRETIeekRERAEELRERAAELEAEAEEKR 557
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
149-442 |
1.65e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.97 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALAT---ARQEHSELTEQYKGLSRSHGELSEERDILSQQQGD 225
Cdd:PRK02224 204 LHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEheeRREELETLEAEIEDLRETIAETEREREELAEEVRD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 226 HVARILELEDDIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKS 305
Cdd:PRK02224 284 LRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELRE 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 306 RQEEqgaqvqrLKDKLAHMKDTLGQAQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASaagARDRTIAELHRSRL 385
Cdd:PRK02224 364 EAAE-------LESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELRE---ERDELREREAELEA 433
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 386 EVAEVNGRLAELSLHMKEEK---CQWSKERTGLLQSMEAEKDKILKLSAEILRLEKTVQE 442
Cdd:PRK02224 434 TLRTARERVEEAEALLEAGKcpeCGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEE 493
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
147-361 |
3.57e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.79 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 147 TVLQNQLDESQQERNDLMQLKLQ-LEDQVTELRSRVQELEAALATARQEHS--ELTEQYKGLSRSHGELSEERDILSQQQ 223
Cdd:COG3206 156 ALAEAYLEQNLELRREEARKALEfLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 224 GDHVARILELEDDIQTMSDKV--LMKEVELDRVRDTVKALTREQEKLLRQL-----------KEFQADKEQSEAELQTVR 290
Cdd:COG3206 236 AEAEARLAALRAQLGSGPDALpeLLQSPVIQQLRAQLAELEAELAELSARYtpnhpdvialrAQIAALRAQLQQEAQRIL 315
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148672009 291 EEnccLNTELEEAKSRQEEQGAQVQRLKDKLAhmkdTLGQAQQKVAELEPLKEQLRGVQELAASSQQKAAL 361
Cdd:COG3206 316 AS---LEAELEALQAREASLQAQLAQLEARLA----ELPELEAELRRLEREVEVARELYESLLQRLEEARL 379
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
149-435 |
4.73e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 55.51 E-value: 4.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 149 LQNQLDESQQERNDLMQLKLQ-----LEDQVTELRSRVQELEAALATARQEHSELTEQYKGL--------SRSHGELSEE 215
Cdd:pfam15921 243 VEDQLEALKSESQNKIELLLQqhqdrIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIqeqarnqnSMYMRQLSDL 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 216 RDILSQQQGDHVARILELEDDIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCC 295
Cdd:pfam15921 323 ESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKR 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 296 L-------NTELEEAKSRQEEQGAQVQRLKDKLAHMK-DTLGQAQQKV-----------------AELEPLKEQLRG-VQ 349
Cdd:pfam15921 403 LwdrdtgnSITIDHLRRELDDRNMEVQRLEALLKAMKsECQGQMERQMaaiqgkneslekvssltAQLESTKEMLRKvVE 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 350 ELAA------SSQQKAALLGEELASAAGARDRTIAELHRSRlevAEVNGRLAELS-LHMKEEKCQWSKERTGLLQSMEAE 422
Cdd:pfam15921 483 ELTAkkmtleSSERTVSDLTASLQEKERAIEATNAEITKLR---SRVDLKLQELQhLKNEGDHLRNVQTECEALKLQMAE 559
|
330
....*....|...
gi 148672009 423 KDKILklsaEILR 435
Cdd:pfam15921 560 KDKVI----EILR 568
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
170-350 |
1.50e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 170 LEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILS-----QQQGDHVARILELEDDIQTMSDKV 244
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASaereiAELEAELERLDASSDDLAALEEQL 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 245 LMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQEEQGAQVQRLKDKLAhm 324
Cdd:COG4913 695 EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLE-- 772
|
170 180
....*....|....*....|....*.
gi 148672009 325 kdtlGQAQQKVAELEPLKEQLRGVQE 350
Cdd:COG4913 773 ----ERIDALRARLNRAEEELERAMR 794
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
228-452 |
1.62e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.91 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 228 ARILELEDDIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQlkEFQADKEQSEAELQTVREENcclntELEEAKSRQ 307
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKE--LEELSRQISALRKDLARLEA-----EVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 308 EEQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRGV-----QELAASSQQKAAL------LGEELASAAGARDRT 376
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQieqlkEELKALREALDELraeltlLNEEAANLRERLESL 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 377 IAELHRSRLEVAEVNGRLAELSLHMKE-----EKCQ------------WSKERTGLLQSMEAEKDKILKLSAEILRLEKT 439
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIESlaaeiEELEelieeleseleaLLNERASLEEALALLRSELEELSEELRELESK 909
|
250
....*....|...
gi 148672009 440 VQEERTQKSRVQD 452
Cdd:TIGR02168 910 RSELRRELEELRE 922
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
181-449 |
1.94e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.53 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 181 VQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQgDHVARILELEDDIQTMSDKVLMKEVEldrvrdtvkA 260
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRER-EKAERYQALLKEKREYEGYELLKEKE---------A 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 261 LTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQEEQGAQVQ-RLKDKLAHMKDTLGQAQQKVA--- 336
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQlRVKEKIGELEAEIASLERSIAeke 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 337 -ELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSRLEVAEVNGRLAELSLHMKEEKCQWSKERTGL 415
Cdd:TIGR02169 315 rELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
|
250 260 270
....*....|....*....|....*....|....
gi 148672009 416 lqsmEAEKDKILKLSAEILRLEKTVQEERTQKSR 449
Cdd:TIGR02169 395 ----EKLKREINELKRELDRLQEELQRLSEELAD 424
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
260-452 |
2.01e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 260 ALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELE 339
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 340 --------PLKEQLRGVQE----------LAASSQQKAALLGEELASAAGARDRTIAELHRSRLEVAEVNGRLAELSLHM 401
Cdd:COG4942 97 aeleaqkeELAELLRALYRlgrqpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 148672009 402 KEEKCQWSKERTGLLQSMEAEKDKILKLSAEILRLEKTVQEERTQKSRVQD 452
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
179-389 |
4.59e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.69 E-value: 4.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 179 SRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGDHVARILELEDDIQTMSDKVLMKEVELDRVRDTV 258
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 259 KALTREQEKLLRQLKEF-----------QADKEQSEAELQTVREENCCLNTELEEAKSRQEEQGAQVQRLKDKLAHMKDT 327
Cdd:COG4942 100 EAQKEELAELLRALYRLgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148672009 328 LGQAQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSRLEVAE 389
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
145-449 |
4.91e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.35 E-value: 4.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 145 KATVLQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQqqg 224
Cdd:PRK02224 350 DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRE--- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 225 dhvaRILELEDDIQTMSDKVlmkeVELDRVRDTVKALTREQE----KLLRQLKEFQADKEQSEAELQTVREENCCLNTEL 300
Cdd:PRK02224 427 ----REAELEATLRTARERV----EEAEALLEAGKCPECGQPvegsPHVETIEEDRERVEELEAELEDLEEEVEEVEERL 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 301 EEAK------SRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARD 374
Cdd:PRK02224 499 ERAEdlveaeDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELN 578
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148672009 375 RTIAELHRSRLEVAEVNGRLAELSlhMKEEKCQWSKERTGLLQSMEAE-KDKILKLSAEILRLEKTVQEERTQKSR 449
Cdd:PRK02224 579 SKLAELKERIESLERIRTLLAAIA--DAEDEIERLREKREALAELNDErRERLAEKRERKRELEAEFDEARIEEAR 652
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
149-346 |
5.87e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.94 E-value: 5.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQY---KGLSRSHGELSEERDILSQQQGd 225
Cdd:TIGR04523 150 KEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLsnlKKKIQKNKSLESQISELKKQNN- 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 226 hvarilELEDDIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKS 305
Cdd:TIGR04523 229 ------QLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNN 302
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 148672009 306 rQEEQG------AQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLR 346
Cdd:TIGR04523 303 -QKEQDwnkelkSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLK 348
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
149-407 |
6.97e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.99 E-value: 6.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQY-----KGLSRSHGELSEERDILS--- 220
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEqlrvkEKIGELEAEIASLERSIAeke 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 221 QQQGDHVARILELEDDIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTEL 300
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 301 EEAKSRQEEQGAQVQRLKDKLAHMKDTLGQAQqkvAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAEL 380
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELADLN---AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQEL 471
|
250 260
....*....|....*....|....*..
gi 148672009 381 HRSRLEVAEVNGRLAELSLHMKEEKCQ 407
Cdd:TIGR02169 472 YDLKEEYDRVEKELSKLQRELAEAEAQ 498
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
152-323 |
8.12e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 8.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 152 QLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLS-RSHGELSEERDILSQQQGDHVARI 230
Cdd:COG4913 282 RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRR 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 231 LELEDDIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREEnccLNTELEEAKSRQEEQ 310
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE---LEAEIASLERRKSNI 438
|
170
....*....|...
gi 148672009 311 GAQVQRLKDKLAH 323
Cdd:COG4913 439 PARLLALRDALAE 451
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
185-380 |
1.15e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 185 EAALATARQEHSELTEQYKGLSRSHGELSEERDILsQQQGDHVARILELEDDiqtmsdkvlmkEVELDRVRDTVKALTRE 264
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDAL-QERREALQRLAEYSWD-----------EIDVASAEREIAELEAE 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 265 QEKLLR---QLKEFQADKEQSEAELQTVREencclntELEEAKSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKV-AELEP 340
Cdd:COG4913 677 LERLDAssdDLAALEEQLEELEAELEELEE-------ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLArLELRA 749
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 148672009 341 LKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAEL 380
Cdd:COG4913 750 LLEERFAAALGDAVERELRENLEERIDALRARLNRAEEEL 789
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
145-452 |
1.65e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.40 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 145 KATVLQNQLDESQQERNdlmqlklQLEDQVTELRSRVQELEAalatarqEHSELTEQYKglsrshGELSEERDILSQQQG 224
Cdd:TIGR04523 322 KLEEIQNQISQNNKIIS-------QLNEQISQLKKELTNSES-------ENSEKQRELE------EKQNEIEKLKKENQS 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 225 dHVARILELEDDIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAK 304
Cdd:TIGR04523 382 -YKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLD 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 305 SRQEEQGAQVQRLKDKLAHMKDTLGQAQQ----KVAELEPLKEQLRGVQELAASSQQKAALLG---EELASAAGARDRTI 377
Cdd:TIGR04523 461 NTRESLETQLKVLSRSINKIKQNLEQKQKelksKEKELKKLNEEKKELEEKVKDLTKKISSLKekiEKLESEKKEKESKI 540
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148672009 378 AELHRSRLEVAEVNGR--LAELSLHMKEEKCQWSKERTGLLQSMEAEKDKILKLSAEILRLEKTVQEERTQKSRVQD 452
Cdd:TIGR04523 541 SDLEDELNKDDFELKKenLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEK 617
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
130-397 |
2.02e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 50.22 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 130 LEEADGGSDILLVVPKATVLQNQ-----------------------LDESQQER-----NDLMQLKLQLEDQVTE----L 177
Cdd:pfam12128 227 IRDIQAIAGIMKIRPEFTKLQQEfntlesaelrlshlhfgyksdetLIASRQEErqetsAELNQLLRTLDDQWKEkrdeL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 178 RSRVQELEAALATARQEHSELTEQYK-----GLSRSHGELSEERDIlsQQQGDHVARILE-LEDDIQTMSDK-----VLM 246
Cdd:pfam12128 307 NGELSAADAAVAKDRSELEALEDQHGafldaDIETAAADQEQLPSW--QSELENLEERLKaLTGKHQDVTAKynrrrSKI 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 247 KEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELqtvREENCCLNTELEEAKSRQEEQGAQVQRLKDKLAHMKD 326
Cdd:pfam12128 385 KEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESEL---REQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPE 461
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148672009 327 TLGQAQQKVAELEPLKEQlrgvQELAASSQQKAALlgeELASAAGARDRTIAELHRSRLEVAEVNGRLAEL 397
Cdd:pfam12128 462 LLLQLENFDERIERAREE----QEAANAEVERLQS---ELRQARKRRDQASEALRQASRRLEERQSALDEL 525
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
124-447 |
2.80e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 2.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 124 MDELVTLEEADGGSDILLVVPKATVLQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYK 203
Cdd:PRK03918 371 KEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHR 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 204 G--LSRSHGELSeerDILSQqqgdhVARILELEDDIQ---TMSDKVLMKEVELDRVRDTVKALTREQEKllrqLKEFQAD 278
Cdd:PRK03918 451 KelLEEYTAELK---RIEKE-----LKEIEEKERKLRkelRELEKVLKKESELIKLKELAEQLKELEEK----LKKYNLE 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 279 K-EQSEAELQTVREENCCLNTELEEAKSRQEEqgaqVQRLKDKLAHMKDTLGQAQQKVAEL---------EPLKEQLRGV 348
Cdd:PRK03918 519 ElEKKAEEYEKLKEKLIKLKGEIKSLKKELEK----LEELKKKLAELEKKLDELEEELAELlkeleelgfESVEELEERL 594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 349 QELAASSQQKAALLG--EELASAAGARDRTIAELHRSRLEVAEVNGRLAELSLHMKEEKCQWSKERtgllqsMEAEKDKI 426
Cdd:PRK03918 595 KELEPFYNEYLELKDaeKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEE------YEELREEY 668
|
330 340
....*....|....*....|.
gi 148672009 427 LKLSAEILRLEKTVQEERTQK 447
Cdd:PRK03918 669 LELSRELAGLRAELEELEKRR 689
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
149-292 |
3.14e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDI--LSQQQGDH 226
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYeaLQKEIESL 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148672009 227 VARILELEDDIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREE 292
Cdd:COG1579 102 KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
232-450 |
4.19e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 232 ELEDDIQTMSDkvLMKEveLDRVRDTVKAlTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLN-----TELEEAKSR 306
Cdd:COG4913 222 DTFEAADALVE--HFDD--LERAHEALED-AREQIELLEPIRELAERYAAARERLAELEYLRAALRlwfaqRRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 307 QEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELEplkEQLR--GVQELAASSQQKAALlGEELASAAGARDRTIAELHRSR 384
Cdd:COG4913 297 LEELRAELARLEAELERLEARLDALREELDELE---AQIRgnGGDRLEQLEREIERL-ERELEERERRRARLEALLAALG 372
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148672009 385 LEVAEVNGRLAELSLHMKEEKCQWSKERTGLLQSMEAEKDKILKLSAEILRLEKTVQEERTQKSRV 450
Cdd:COG4913 373 LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNI 438
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
152-445 |
4.21e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 4.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 152 QLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAAlatarqeHSELTEQYKGLSRSHGELSEERDILSQQQgdhvARIL 231
Cdd:PRK03918 201 ELEEVLREINEISSELPELREELEKLEKEVKELEEL-------KEEIEELEKELESLEGSKRKLEEKIRELE----ERIE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 232 ELEDDIQTMSDKVlmKEV-ELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREEncclNTELEEAKSRQEEQ 310
Cdd:PRK03918 270 ELKKEIEELEEKV--KELkELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEER----IKELEEKEERLEEL 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 311 GAQVQRLKDKLAHMKD---TLGQAQQKVAELEPLKEQLRG------VQELAASSQQKAALLGE--ELASAAGARDRTIAE 379
Cdd:PRK03918 344 KKKLKELEKRLEELEErheLYEEAKAKKEELERLKKRLTGltpeklEKELEELEKAKEEIEEEisKITARIGELKKEIKE 423
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148672009 380 LHRSRLEVAEVNGRL----AELSLHMKEE-KCQWSKERTGLLQSMEAEKDKILKLSAEILRLEKTVQEERT 445
Cdd:PRK03918 424 LKKAIEELKKAKGKCpvcgRELTEEHRKElLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESE 494
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
145-313 |
4.68e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 4.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 145 KATVLQNQLDESQQERNDLMQLK---LQLEDQVTELRSRVQELEAALATARQEHSELtEQYKGLSRSHGELSEERDILSQ 221
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKL-EKLLQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 222 QQG------DHVARILELEDDIQTMSDKVLMKEVELDRVRDTVKALTREQ-EKLLRQLKEFQADKEQSEAELQTVREENC 294
Cdd:COG4717 144 LPErleeleERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170
....*....|....*....
gi 148672009 295 CLNTELEEAKSRQEEQGAQ 313
Cdd:COG4717 224 ELEEELEQLENELEAAALE 242
|
|
| COG4192 |
COG4192 |
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ... |
149-397 |
1.03e-05 |
|
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal transduction mechanisms];
Pssm-ID: 443346 [Multi-domain] Cd Length: 640 Bit Score: 47.76 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELeaALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGDHVA 228
Cdd:COG4192 39 LSNQIRYILDDSLPKLQASLKLEENSNELVAALPEF--AAATNTTERSQLRNQLNTQLADIEELLAELEQLTQDAGDLRA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 229 RILELEDDIQtmsdkvlmkevELDRVRDTVKALTREQEKLLRQLKEFQAD-KEQSEAELQTVREENCCLNTELEEAKSRQ 307
Cdd:COG4192 117 AVADLRNLLQ-----------QLDSLLTQRIALRRRLQELLEQINWLHQDfNSELTPLLQEASWQQTRLLDSVETTESLR 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 308 EEQGA--QVQRLKDKLAHMKDTLGQ--AQQKVAELEPLKEQLrgvQELAASSQQKAALLGEelASAAGARDRTIAELhrs 383
Cdd:COG4192 186 NLQNElqLLLRLLAIENQIVSLLREvaAARDQADVDNLFDRL---QYLKDELDRNLQALKN--YPSTITLRQLIDEL--- 257
|
250
....*....|....
gi 148672009 384 rLEVAEVNGRLAEL 397
Cdd:COG4192 258 -LAIGSGEGGLPSL 270
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
170-450 |
1.06e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.89 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 170 LEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSrshGELSEERDILSQQQgdhvARILELEDDIQTMSDKVLMKEV 249
Cdd:pfam10174 343 LQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLA---GEIRDLKDMLDVKE----RKINVLQKKIENLQEQLRDKDK 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 250 ELDRVRDTVK-----------ALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSR------------ 306
Cdd:pfam10174 416 QLAGLKERVKslqtdssntdtALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKvsalqpelteke 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 307 ------QEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRGVQELAASSQ-------------QKAALLGEELA 367
Cdd:pfam10174 496 sslidlKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRtnpeindrirlleQEVARYKEESG 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 368 SAAGARDRTIAELHRSRLEVAEVNGRLAEL----SLHMKEE----------KCQWSKERTGLLQSMEAEKDKILKLSAEI 433
Cdd:pfam10174 576 KAQAEVERLLGILREVENEKNDKDKKIAELesltLRQMKEQnkkvanikhgQQEMKKKGAQLLEEARRREDNLADNSQQL 655
|
330 340
....*....|....*....|...
gi 148672009 434 L------RLEKTVQEERTQKSRV 450
Cdd:pfam10174 656 QleelmgALEKTRQELDATKARL 678
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
151-338 |
1.36e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.83 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 151 NQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGDHVARI 230
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 231 LELEDDIQTMSDKVLM---KEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREenccLNTELEEAKsRQ 307
Cdd:COG1340 81 DELNEKLNELREELDElrkELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKE----LEKELEKAK-KA 155
|
170 180 190
....*....|....*....|....*....|.
gi 148672009 308 EEQGAQVQRLKDKLAHMKDTLGQAQQKVAEL 338
Cdd:COG1340 156 LEKNEKLKELRAELKELRKEAEEIHKKIKEL 186
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
151-350 |
1.40e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 151 NQLDESQQERNDLMQLKLQ-LEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILsqqqgdhvAR 229
Cdd:PRK02224 522 EELIAERRETIEEKRERAEeLRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL--------ER 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 230 ILELEDDIQTMSDkvlmkevELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENccLNTELEEAKSRQEE 309
Cdd:PRK02224 594 IRTLLAAIADAED-------EIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEE--AREDKERAEEYLEQ 664
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 148672009 310 QGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRGVQE 350
Cdd:PRK02224 665 VEEKLDELREERDDLQAEIGAVENELEELEELRERREALEN 705
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
154-446 |
2.46e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 46.76 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 154 DESQQERNDLMQLKLQLE--------DQVTELRSRVQELEAALATARQEHSELTEQykgLSRSHGELSEerdiLSQQQGD 225
Cdd:pfam12128 571 DGSVGGELNLYGVKLDLKridvpewaASEEELRERLDKAEEALQSAREKQAAAEEQ---LVQANGELEK----ASREETF 643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 226 HVARILELEDDIQTMSDKvlmKEVELDRVRdtvKALTREQEKLLRQLKEFQADKEQSEAELQTVREENccLNTELEEAKS 305
Cdd:pfam12128 644 ARTALKNARLDLRRLFDE---KQSEKDKKN---KALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQ--KEQKREARTE 715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 306 RQEEQGAQVQRLKDKLAHMKdtlgqaQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASaagaRDRTIAELHRsRL 385
Cdd:pfam12128 716 KQAYWQVVEGALDAQLALLK------AAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAK----LKREIRTLER-KI 784
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148672009 386 EVAEVNG-RLAELSLHMKEekcQWSKERTGLLQSMEAEKDKILKLSAEILRLEKTVQEERTQ 446
Cdd:pfam12128 785 ERIAVRRqEVLRYFDWYQE---TWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAK 843
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
149-451 |
2.52e-05 |
|
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: 47.04 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 149 LQNQLDESQQERNDLMQLKLQ----LEDQVTELRSRVQELEAALATAR---QEHSELTEQYKGLSRSH-GELSEERDILS 220
Cdd:pfam15921 115 LQTKLQEMQMERDAMADIRRResqsQEDLRNQLQNTVHELEAAKCLKEdmlEDSNTQIEQLRKMMLSHeGVLQEIRSILV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 221 QQQGDHVARILElEDDIQTMSDKVLMKEV-----ELDR-----------VRDTVKALTRE-QEKLLRQLKEFQADKEQ-- 281
Cdd:pfam15921 195 DFEEASGKKIYE-HDSMSTMHFRSLGSAIskilrELDTeisylkgrifpVEDQLEALKSEsQNKIELLLQQHQDRIEQli 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 282 SEAELQ---------TVREENCCLNTELEEAKSRQEEQGA----QVQRLKDKLAHMKDTLGQAQQKVAE-LEPLKEQLrg 347
Cdd:pfam15921 274 SEHEVEitgltekasSARSQANSIQSQLEIIQEQARNQNSmymrQLSDLESTVSQLRSELREAKRMYEDkIEELEKQL-- 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 348 vqELAASSQQKAALLGEELASAAGARDRTIAELhrsrleVAEVNGRLAELSLHMKEEKCQWSKErTGLLQSMEAEKDKIL 427
Cdd:pfam15921 352 --VLANSELTEARTERDQFSQESGNLDDQLQKL------LADLHKREKELSLEKEQNKRLWDRD-TGNSITIDHLRRELD 422
|
330 340
....*....|....*....|....
gi 148672009 428 KLSAEILRLEKTVqeeRTQKSRVQ 451
Cdd:pfam15921 423 DRNMEVQRLEALL---KAMKSECQ 443
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
169-445 |
2.58e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 169 QLEDQVTELRSRvqELEAALATARQEHSELTEQYKglsrshgELSEERDILSQQQGDHVARILELEDDIQTMSDkvlmKE 248
Cdd:PRK02224 191 QLKAQIEEKEEK--DLHERLNGLESELAELDEEIE-------RYEEQREQARETRDEADEVLEEHEERREELET----LE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 249 VELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREEncclnTELEEAKsrQEEQGAQVQRLKDKLAHMKDTL 328
Cdd:PRK02224 258 AEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAE-----AGLDDAD--AEAVEARREELEDRDEELRDRL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 329 GQ----AQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSRLEVAEVNGRLAELSLHMKEE 404
Cdd:PRK02224 331 EEcrvaAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNA 410
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 148672009 405 kcqwSKERTGLLQSMEAEKDKILKLSAEILRLEKTVQEERT 445
Cdd:PRK02224 411 ----EDFLEELREERDELREREAELEATLRTARERVEEAEA 447
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
169-355 |
2.63e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 169 QLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRshgelseerdilsqqqgdhvaRILELEDDIQTMSDKVLMKE 248
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEK---------------------EIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 249 VELDRVRDtvkalTREQEKLLRQLKEFQADKEQSEAELQTVREencclntELEEAKSRQEEQGAQVQRLKDKLAHMKDTL 328
Cdd:COG1579 80 EQLGNVRN-----NKEYEALQKEIESLKRRISDLEDEILELME-------RIEELEEELAELEAELAELEAELEEKKAEL 147
|
170 180
....*....|....*....|....*..
gi 148672009 329 gqaQQKVAELEPLKEQLRGVQELAASS 355
Cdd:COG1579 148 ---DEELAELEAELEELEAEREELAAK 171
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
159-451 |
4.39e-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: 45.87 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 159 ERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGDHVARILEL--EDD 236
Cdd:pfam05483 416 EDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELtaHCD 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 237 IQTMSDKVLMKE-----VELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREE--------NCCLNTELEEA 303
Cdd:pfam05483 496 KLLLENKELTQEasdmtLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEfiqkgdevKCKLDKSEENA 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 304 KSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRGVQ----------------------ELAASSQQKAAL 361
Cdd:pfam05483 576 RSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKkkgsaenkqlnayeikvnklelELASAKQKFEEI 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 362 LG---EELASAAGARDRTIAELHRSRLEVAEV-----------NGRLAELSLHMKEEKCQWSK------ERTGLLQSMEA 421
Cdd:pfam05483 656 IDnyqKEIEDKKISEEKLLEEVEKAKAIADEAvklqkeidkrcQHKIAEMVALMEKHKHQYDKiieerdSELGLYKNKEQ 735
|
330 340 350
....*....|....*....|....*....|....*...
gi 148672009 422 EKD--------KILKLSAEILRLEKTVQEERTQKSRVQ 451
Cdd:pfam05483 736 EQSsakaaleiELSNIKAELLSLKKQLEIEKEEKEKLK 773
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
125-446 |
6.56e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 6.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 125 DELVTLEEADGGSDILLvvpkaTVLQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATAR----------QE 194
Cdd:PRK02224 391 EEIEELRERFGDAPVDL-----GNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpvegSP 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 195 HSELTEQYKGlsrSHGELSEERDILSQQQGDHVARI------LELEDDIQTMSDKVLMKEVELDRVRDTVKALTREQEKL 268
Cdd:PRK02224 466 HVETIEEDRE---RVEELEAELEDLEEEVEEVEERLeraedlVEAEDRIERLEERREDLEELIAERRETIEEKRERAEEL 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 269 LRQLKEFQADKEQSEAELQTVREENcclNTELEEAKSRQEEQGAQVQRLkDKLAHMKDTLGQAQQKVAELEPLKEQLRGV 348
Cdd:PRK02224 543 RERAAELEAEAEEKREAAAEAEEEA---EEAREEVAELNSKLAELKERI-ESLERIRTLLAAIADAEDEIERLREKREAL 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 349 QELAASSQQKAALLGEELASAAGARDRTIAELHRSRLEVAE-----VNGRLAELslhmKEEKCQWSKERTGL---LQSME 420
Cdd:PRK02224 619 AELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEeyleqVEEKLDEL----REERDDLQAEIGAVeneLEELE 694
|
330 340
....*....|....*....|....*.
gi 148672009 421 AEKDKILKLSAEILRLEkTVQEERTQ 446
Cdd:PRK02224 695 ELRERREALENRVEALE-ALYDEAEE 719
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
187-425 |
9.27e-05 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 44.90 E-value: 9.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 187 ALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGDHVARILE-LEDDIQTMSDKVLMKEVELDRVrdtvkalTREQ 265
Cdd:pfam15964 354 ALIQCEQLKSELERQKERLEKELASQQEKRAQEKEALRKEMKKEREeLGATMLALSQNVAQLEAQVEKV-------TREK 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 266 EKLLRQLKEFQADKEQSEAELQTVREEnccLNTELEEAKSRQEEQGAQVQRLKDKlahmkdTLGQAQQKVAELEPLKEQL 345
Cdd:pfam15964 427 NSLVSQLEEAQKQLASQEMDVTKVCGE---MRYQLNQTKMKKDEAEKEHREYRTK------TGRQLEIKDQEIEKLGLEL 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 346 RGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSRLEVAEVNGRLAELSLHMKEEKCQWSKERTGLLQSMEAEKDK 425
Cdd:pfam15964 498 SESKQRLEQAQQDAARAREECLKLTELLGESEHQLHLTRLEKESIQQSFSNEAKAQALQAQQREQELTQKMQQMEAQHDK 577
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
149-449 |
9.68e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 9.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATArQEHSELTEQYKGLSRSHGELSEERDILSQQQGDHVA 228
Cdd:PRK03918 243 LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEE 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 229 RILELEDDIQTMSDKvlmkEVELDRVRDTVKALTREQEKLLRQLKEFQaDKEQSEAELQTVREENCCLNTE-----LEEA 303
Cdd:PRK03918 322 EINGIEERIKELEEK----EERLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGLTPEklekeLEEL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 304 KSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELE-----------PLKEQLRGvqELAASSQQKAALLGEELAsaaga 372
Cdd:PRK03918 397 EKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgkcpvcgrELTEEHRK--ELLEEYTAELKRIEKELK----- 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 373 rdRTIAELHRSRLEVAEVNGRLAE----LSLHMKEEKCQWSKERTGLLQSMEAEKD---------KILKLSAEILRLEKT 439
Cdd:PRK03918 470 --EIEEKERKLRKELRELEKVLKKeselIKLKELAEQLKELEEKLKKYNLEELEKKaeeyeklkeKLIKLKGEIKSLKKE 547
|
330
....*....|
gi 148672009 440 VQEERTQKSR 449
Cdd:PRK03918 548 LEKLEELKKK 557
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
147-347 |
1.27e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 43.98 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 147 TVLQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALA----TARQEHSELTEQYKGLSRSHGELSEErdiLSQQ 222
Cdd:pfam09787 43 TALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQeeaeSSREQLQELEEQLATERSARREAEAE---LERL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 223 QGDHVARILELEDDIQTMSDKVLMKEVELDRVRDTVKALTR------EQEKLLRQLKEFQADKeqsEAELQTVREENCCL 296
Cdd:pfam09787 120 QEELRYLEEELRRSKATLQSRIKDREAEIEKLRNQLTSKSQssssqsELENRLHQLTETLIQK---QTMLEALSTEKNSL 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 148672009 297 NTELEEA-KSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRG 347
Cdd:pfam09787 197 VLQLERMeQQIKELQGEGSNGTSINMEGISDGEGTRLRNVPGLFSESDSDRA 248
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
149-335 |
1.35e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.23 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHgELSEERDI---LSQQQGD 225
Cdd:PHA02562 218 KQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVI-KMYEKGGVcptCTQQISE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 226 HVARILELEDDIQTMSDKVlmkeVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKS 305
Cdd:PHA02562 297 GPDRITKIKDKLKELQHSL----EKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQA 372
|
170 180 190
....*....|....*....|....*....|
gi 148672009 306 RQEEQGAQVQRLKDKLAHMKDTLGQAQQKV 335
Cdd:PHA02562 373 EFVDNAEELAKLQDELDKIVKTKSELVKEK 402
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
160-309 |
1.37e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.85 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 160 RNDLMQ-LKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELseerdilsqqqgdhvariLELEDDIQ 238
Cdd:smart00787 138 RMKLLEgLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQL------------------KQLEDELE 199
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148672009 239 TMsdkvlmKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQEE 309
Cdd:smart00787 200 DC------DPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQ 264
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
149-350 |
3.44e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGDHVA 228
Cdd:COG1340 34 LNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 229 ---RILELEDDIQTmsdKVLMKEVElDRVRDTVKALTREQEKLLRQLKEFQADKEqSEAELQTVREencclntELEEAKS 305
Cdd:COG1340 114 lrkEIERLEWRQQT---EVLSPEEE-KELVEKIKELEKELEKAKKALEKNEKLKE-LRAELKELRK-------EAEEIHK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 148672009 306 RQEEQGAQVQRLKDKlahMKDTLGQAQQKVAELEPLKEQLRGVQE 350
Cdd:COG1340 182 KIKELAEEAQELHEE---MIELYKEADELRKEADELHKEIVEAQE 223
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
151-278 |
3.77e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 151 NQLDESQQERNDLMQLK---LQLEDQVTELR---SRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQg 224
Cdd:COG4913 651 QRLAEYSWDEIDVASAEreiAELEAELERLDassDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL- 729
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 225 DHVARILE---------LEDDIQTMSDKVLMKEVEL-------DRVRDTVKALTREQEKLLRQLKEFQAD 278
Cdd:COG4913 730 DELQDRLEaaedlarleLRALLEERFAAALGDAVERelrenleERIDALRARLNRAEEELERAMRAFNRE 799
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
150-448 |
3.85e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.09 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 150 QNQLDESQQERNDLMQLKLQLEDQVTELRSRVQEL--EAALATARQEHSELTEQYKGLSRSHGELSEERDILSQqqgdhv 227
Cdd:TIGR04523 266 KKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLnnQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQ------ 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 228 arileLEDDIQtmsdkvlmkeveldRVRDTVKALTREQEKLLRQLKEfqadKEQseaELQTVREENCCLNTELEEAKSrq 307
Cdd:TIGR04523 340 -----LNEQIS--------------QLKKELTNSESENSEKQRELEE----KQN---EIEKLKKENQSYKQEIKNLES-- 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 308 eeqgaQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSRlev 387
Cdd:TIGR04523 392 -----QINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTR--- 463
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148672009 388 AEVNGRLAELSLHMKEEKCQWSKertgLLQSMEAEKDKILKLSAEILRLEKTVQEERTQKS 448
Cdd:TIGR04523 464 ESLETQLKVLSRSINKIKQNLEQ----KQKELKSKEKELKKLNEEKKELEEKVKDLTKKIS 520
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
145-325 |
3.98e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.70 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 145 KATVLQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQG 224
Cdd:TIGR04523 448 QDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIE 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 225 DHVARILELEDDIQTMSDKVLMKEVELDrvRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREEnccLNTELEEAK 304
Cdd:TIGR04523 528 KLESEKKEKESKISDLEDELNKDDFELK--KENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQ---KEKEKKDLI 602
|
170 180
....*....|....*....|.
gi 148672009 305 SRQEEQGAQVQRLKDKLAHMK 325
Cdd:TIGR04523 603 KEIEEKEKKISSLEKELEKAK 623
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
230-347 |
4.70e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.93 E-value: 4.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 230 ILELEDDIQTMSDKVLMKEVEL-----DRVRDTVKALTREQEkLLRQLKEFQADKEQSEaeLQTVREENCCLNTELEEAK 304
Cdd:smart00787 148 GLDENLEGLKEDYKLLMKELELlnsikPKLRDRKDALEEELR-QLKQLEDELEDCDPTE--LDRAKEKLKKLLQEIMIKV 224
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 148672009 305 SRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRG 347
Cdd:smart00787 225 KKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRG 267
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
126-339 |
6.43e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.41 E-value: 6.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 126 ELVTLEEADGGSDILLVVPKATVLQNQL-DESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEhselteqykg 204
Cdd:pfam15921 631 ELEKVKLVNAGSERLRAVKDIKQERDQLlNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQ---------- 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 205 LSRSHGELSEERDILSQQQGD--HVARIleleddIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQS 282
Cdd:pfam15921 701 LKSAQSELEQTRNTLKSMEGSdgHAMKV------AMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKL 774
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 148672009 283 EAELQTVREENCCLNTELEEAKSrqeeqgaQVQRLKDKLAHMKDTLGQAQQKVAELE 339
Cdd:pfam15921 775 SQELSTVATEKNKMAGELEVLRS-------QERRLKEKVANMEVALDKASLQFAECQ 824
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
176-326 |
8.92e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.77 E-value: 8.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 176 ELRSRV---QELEAALATARQEHSELTEQYKGLSRSHGElseerdilsQQQGDHVARILELEDDIQTMSDKVLMKEVELD 252
Cdd:COG2433 367 EVKARVirgLSIEEALEELIEKELPEEEPEAEREKEHEE---------RELTEEEEEIRRLEEQVERLEAEVEELEAELE 437
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148672009 253 RVRDTVKALTREqeklLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQEEQGAQVQRLKD--KLAHMKD 326
Cdd:COG2433 438 EKDERIERLERE----LSEARSEERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKElwKLEHSGE 509
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
145-445 |
1.03e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 41.21 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 145 KATVLQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKglsrshgELSEERDILSQQQG 224
Cdd:pfam19220 77 RLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNR-------ALEEENKALREEAQ 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 225 DHVARILELEDDIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQAdkeQSEAELQTVREENCCLNTELEEAK 304
Cdd:pfam19220 150 AAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELET---QLDATRARLRALEGQLAAEQAERE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 305 SRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSR 384
Cdd:pfam19220 227 RAEAQLEEAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADL 306
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148672009 385 LEVAEVNGRLAELSLHMKEEKCQWSKERTGLLQSMEAEKDKILKLSAEILRLEKTVQEERT 445
Cdd:pfam19220 307 ERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDRIAELTKRFEVERA 367
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
149-451 |
1.04e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 149 LQNQLDESQQERNDLMQLKLQ-LEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDIlsqQQGDHV 227
Cdd:COG4717 175 LQEELEELLEQLSLATEEELQdLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERL---KEARLL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 228 ARILELEDDIQTMSDKVLMKEVELDRVRDTVKALtreqekLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQ 307
Cdd:COG4717 252 LLIAAALLALLGLGGSLLSLILTIAGVLFLVLGL------LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 308 EEQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRgVQELAASSQQKAALLGEELASAAGARDRTIAELHRSRLEV 387
Cdd:COG4717 326 AALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ-LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEEL 404
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148672009 388 AEVNGRLAELSLHMKEEKCQWSKERTgllqsmeaeKDKILKLSAEILRLEKTVQEERTQKSRVQ 451
Cdd:COG4717 405 EELEEQLEELLGELEELLEALDEEEL---------EEELEELEEELEELEEELEELREELAELE 459
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
215-389 |
1.21e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 215 ERDILSQQQGDHVARILELEDDIQTMSDkvlmkevELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREenc 294
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEA-------RLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 295 clNTELEEAKSRQEEQGAQVQRLKDKLAHMKDtlgqaqqkvaELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARD 374
Cdd:COG1579 88 --NKEYEALQKEIESLKRRISDLEDEILELME----------RIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
170
....*....|....*
gi 148672009 375 RTIAELHRSRLEVAE 389
Cdd:COG1579 156 AELEELEAEREELAA 170
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
125-351 |
1.24e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 125 DELVTLEEADGGSDILLVVPKATVLQNQLDESQQERNDLMQLKLQLEdQVTELRSRVQELEAALATARQEHSELTEQYKG 204
Cdd:PRK03918 503 EQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAELLKELEE 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 205 LSRSHGELSEERDILSQQQGDHVARILELEDDIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQadKEQSEA 284
Cdd:PRK03918 582 LGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELE--KKYSEE 659
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148672009 285 ELQTVREENCCLNTELEEAKSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRGVQEL 351
Cdd:PRK03918 660 EYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEEL 726
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
149-356 |
1.93e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.87 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELE--------------AALATARQEHSELTEQYKGLSRSHGELSE 214
Cdd:pfam15921 595 LEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLElekvklvnagserlRAVKDIKQERDQLLNEVKTSRNELNSLSE 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 215 ERDILSQQQGDHvarilelEDDIQTMSDKVLMK----EVELDRVRDTVKALTREQEKLLR----QLKEFQADKEQSEAEL 286
Cdd:pfam15921 675 DYEVLKRNFRNK-------SEEMETTTNKLKMQlksaQSELEQTRNTLKSMEGSDGHAMKvamgMQKQITAKRGQIDALQ 747
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148672009 287 QTVReencclntELEEAKSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVA-ELEPLKEQLRGVQELAASSQ 356
Cdd:pfam15921 748 SKIQ--------FLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAgELEVLRSQERRLKEKVANME 810
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
234-422 |
2.13e-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: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 234 EDDIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQEEQGAQ 313
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 314 VQR--------------------------LKDKLAHMKDTLGQAQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELA 367
Cdd:COG3883 95 LYRsggsvsyldvllgsesfsdfldrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 148672009 368 SAAGARDRTIAELhrsRLEVAEVNGRLAELSLHMKEEKCQWSKERTGLLQSMEAE 422
Cdd:COG3883 175 AQQAEQEALLAQL---SAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
232-356 |
2.34e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.42 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 232 ELEDDIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQEEQG 311
Cdd:TIGR00606 692 ELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQE 771
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 148672009 312 AQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRGVQELAASSQ 356
Cdd:TIGR00606 772 TLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQ 816
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
248-357 |
2.44e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 39.74 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 248 EVELDRVRDTVKALTREQEKLLRQLK----EFQADKEQSEAELQTVREENCCLNTELEEAKSRQEEQGAQVQRLKDKLAH 323
Cdd:pfam09787 46 TLELEELRQERDLLREEIQKLRGQIQqlrtELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRY 125
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 148672009 324 MKDTL--------GQAQQKVAELEPLKEQLRgVQELAASSQQ 357
Cdd:pfam09787 126 LEEELrrskatlqSRIKDREAEIEKLRNQLT-SKSQSSSSQS 166
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
240-397 |
2.89e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.56 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 240 MSDKVLMKEVELDRVRDTVKALTrEQEKLLRQLKE-FQADKEQSEAELQTVREENCCLNTELEEAKSRQEEQGAQVQRLK 318
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAELA-DLLSLERQGNQdLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 319 DKLAHMKDTLGQAQQKVAEL----EPLKEQLRGVQEL-------AASSQQKAALLGEELASAAGARdrtIAELHRSRlev 387
Cdd:PRK09039 123 QELDSEKQVSARALAQVELLnqqiAALRRQLAALEAAldasekrDRESQAKIADLGRRLNVALAQR---VQELNRYR--- 196
|
170
....*....|
gi 148672009 388 AEVNGRLAEL 397
Cdd:PRK09039 197 SEFFGRLREI 206
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
165-379 |
3.56e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.50 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 165 QLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQykgLSRSHGELSEERDILSQQQgdhvARILELEDDIQTMSDKV 244
Cdd:COG4372 24 ILIAALSEQLRKALFELDKLQEELEQLREELEQAREE---LEQLEEELEQARSELEQLE----EELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 245 LMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQEEQGAQVQRLKDKLAHM 324
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 148672009 325 KDTlgQAQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAE 379
Cdd:COG4372 177 SEA--EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEA 229
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
149-442 |
3.65e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 39.70 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQqqgdhva 228
Cdd:pfam05483 224 IQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTK------- 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 229 rilELEDdiqtmsdkvlmKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQE 308
Cdd:pfam05483 297 ---ELED-----------IKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 309 E-QGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRG----VQELAASSQQKAALLG-----EELASAAGARDRTIA 378
Cdd:pfam05483 363 ElLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNkeveLEELKKILAEDEKLLDekkqfEKIAEELKGKEQELI 442
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148672009 379 ELHRSRLEvaEVNGRLAELSLHMKEEKcQWSKERTGLLQSMEAEKDKILKLSAE----ILRLEKTVQE 442
Cdd:pfam05483 443 FLLQAREK--EIHDLEIQLTAIKTSEE-HYLKEVEDLKTELEKEKLKNIELTAHcdklLLENKELTQE 507
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
228-452 |
3.84e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 39.61 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 228 ARILELEDDIQTMSdkvlmkeVELDRVRDTVKALTREQEKLLRQLKEFQADKE----QSEAELQTVREENCCLNTELEEA 303
Cdd:PHA02562 174 DKIRELNQQIQTLD-------MKIDHIQQQIKTYNKNIEEQRKKNGENIARKQnkydELVEEAKTIKAEIEELTDELLNL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 304 KSRQEEQGAQVQRLKDKLAHMKDTLGQAQ------QKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDrti 377
Cdd:PHA02562 247 VMDIEDPSAALNKLNTAAAKIKSKIEQFQkvikmyEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAID--- 323
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148672009 378 aelhrsrlEVAEVNGRLAELSLHMKEEKCQWSKERtgllQSMEAEKDKILKLSAEILRLEKTVQEERTQKSRVQD 452
Cdd:PHA02562 324 --------ELEEIMDEFNEQSKKLLELKNKISTNK----QSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQD 386
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
155-366 |
4.08e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.77 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 155 ESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRshgELSEERDILSQQQGDHV---ARIL 231
Cdd:pfam01576 58 EAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEE---QLDEEEAARQKLQLEKVtteAKIK 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 232 ELEDDIQTMSDK--VLMKEVEL--DRVRDTVKALTREQEKL--LRQLK----------------------EFQADKEQSE 283
Cdd:pfam01576 135 KLEEDILLLEDQnsKLSKERKLleERISEFTSNLAEEEEKAksLSKLKnkheamisdleerlkkeekgrqELEKAKRKLE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 284 AELQTVREENCCLNTELEEAKSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELEP----LKEQLRGVQELAASSQQKA 359
Cdd:pfam01576 215 GESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAqiseLQEDLESERAARNKAEKQR 294
|
....*..
gi 148672009 360 ALLGEEL 366
Cdd:pfam01576 295 RDLGEEL 301
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
280-373 |
4.18e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 39.55 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 280 EQSEAELQTVREENCCLNTELEEAKSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRgVQELAASSQQKA 359
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQ-EKAAETSQERKQ 216
|
90
....*....|....
gi 148672009 360 ALlgEELASAAGAR 373
Cdd:PRK11448 217 KR--KEITDQAAKR 228
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
149-397 |
4.59e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.12 E-value: 4.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGDHVA 228
Cdd:COG4372 57 AREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 229 RILELEDDIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQE 308
Cdd:COG4372 137 QIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPREL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 309 EQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSRLEVA 388
Cdd:COG4372 217 AEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELK 296
|
....*....
gi 148672009 389 EVNGRLAEL 397
Cdd:COG4372 297 LLALLLNLA 305
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
250-320 |
4.73e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 38.94 E-value: 4.73e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148672009 250 ELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQEEQGAQVQRLKDK 320
Cdd:COG4026 136 ELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELLKK 206
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
226-339 |
4.81e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 38.94 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 226 HVARI-LELEDDIQTMSDKVLMKEVELDRVRDTVKALTREQE--KLLRQLKEFQADKEQSEAELQTVREENCCLNTELEE 302
Cdd:COG4026 88 HVERMkLPLGHDVEYVDVELVRKEIKNAIIRAGLKSLQNIPEynELREELLELKEKIDEIAKEKEKLTKENEELESELEE 167
|
90 100 110
....*....|....*....|....*....|....*..
gi 148672009 303 AKSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELE 339
Cdd:COG4026 168 LREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELL 204
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
150-344 |
5.35e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 39.24 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 150 QNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERdilsqqqgdhvAR 229
Cdd:pfam05667 334 EEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKKTLDLLPDAE-----------EN 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 230 ILELEDDIQTMSDKVLMKEVELDRVRdtvKALTREqeklLRQLKEFQADKEqSEAELQtvreencclnteLEEAKSRQEE 309
Cdd:pfam05667 403 IAKLQALVDASAQRLVELAGQWEKHR---VPLIEE----YRALKEAKSNKE-DESQRK------------LEEIKELREK 462
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 148672009 310 qgaqvqrlkdklahMKDTLGQAQQK-------VAELEPLKEQ 344
Cdd:pfam05667 463 --------------IKEVAEEAKQKeelykqlVAEYERLPKD 490
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
149-369 |
5.71e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.39 E-value: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSrshGELSEERDILSQQQGDHVA 228
Cdd:pfam01576 248 ALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALK---TELEDTLDTTAAQQELRSK 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 229 RILELEDDIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQS----EAELQTVREENCCLNTELEEAK 304
Cdd:pfam01576 325 REQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAkqalESENAELQAELRTLQQAKQDSE 404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148672009 305 SRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELEplkEQLRGVQELAASSQQKAALLGEELASA 369
Cdd:pfam01576 405 HKRKKLEGQLQELQARLSESERQRAELAEKLSKLQ---SELESVSSLLNEAEGKNIKLSKDVSSL 466
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
150-344 |
6.20e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 38.95 E-value: 6.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 150 QNQLDESQQERNDLMQLKLQLEDQVTELrSRVQELEAaLATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGDHVAR 229
Cdd:pfam17380 347 ERELERIRQEERKRELERIRQEEIAMEI-SRMRELER-LQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQ 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 230 ILELEDDIQTMSDKVLMKE--VELDRVRDTVKALTREQEKLLRQLKEFQADK---EQSEAELQTVREEN-CCLNTELEEA 303
Cdd:pfam17380 425 IRAEQEEARQREVRRLEEEraREMERVRLEEQERQQQVERLRQQEEERKRKKlelEKEKRDRKRAEEQRrKILEKELEER 504
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 148672009 304 KSRQEEQGAQVQRLKDKLAHMKDTLGQAQQ-KVAELEPLKEQ 344
Cdd:pfam17380 505 KQAMIEEERKRKLLEKEMEERQKAIYEEERrREAEEERRKQQ 546
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
130-361 |
6.44e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 6.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 130 LEEADGGSDILlvvpkaTVLQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSH 209
Cdd:COG4913 677 LERLDASSDDL------AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 210 GE-----------LSEERDILSQQQGDHVARILELEDDI-QTMSDKVLMKEVELDRVRDTVKALtREQEKLLRQLK---- 273
Cdd:COG4913 751 LEerfaaalgdavERELRENLEERIDALRARLNRAEEELeRAMRAFNREWPAETADLDADLESL-PEYLALLDRLEedgl 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 274 -EFQAD-----KEQSEAELQTVREEnccLNTELEEAKSR-----------------------QEEQGAQVQRLKDKL--- 321
Cdd:COG4913 830 pEYEERfkellNENSIEFVADLLSK---LRRAIREIKERidplndslkripfgpgrylrleaRPRPDPEVREFRQELrav 906
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 148672009 322 --AHMKDTLGQAQQKVAELEPLKEQLRGVQELAASSQQKAAL 361
Cdd:COG4913 907 tsGASLFDEELSEARFAALKRLIERLRSEEEESDRRWRARVL 948
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
165-451 |
7.08e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.00 E-value: 7.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 165 QLKLQLEDQVTELRSRVQELEAalatarqEHSELTEQYKGLSRSHGELSEERDILsqqqgdhVARILELEDDIQTMsdkv 244
Cdd:pfam01576 19 ERQQKAESELKELEKKHQQLCE-------EKNALQEQLQAETELCAEAEEMRARL-------AARKQELEEILHEL---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 245 lmkEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNT---ELEEAKSRQEEQGAQVQR----L 317
Cdd:pfam01576 81 ---ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAkikKLEEDILLLEDQNSKLSKerklL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 318 KDKLAHMKDTLGQAQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRsrlEVAEVNGRLAEL 397
Cdd:pfam01576 158 EERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQE---QIAELQAQIAEL 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 148672009 398 --SLHMKEEKCQWSKERTG--LLQSMEAEKdKILKLSAEILRLEKTVQEERTQKSRVQ 451
Cdd:pfam01576 235 raQLAKKEEELQAALARLEeeTAQKNNALK-KIRELEAQISELQEDLESERAARNKAE 291
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
247-366 |
8.18e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 38.04 E-value: 8.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 247 KEVELDRVRDTVKALTrEQEKllrQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQEEqgaQVQRLKDKLAHMKD 326
Cdd:pfam02841 185 KEAVEEAILQTDQALT-AKEK---AIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQE---HVKQLIEKMEAERE 257
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 148672009 327 TLGQAQQKVAELEpLKEQLRGVQElaaSSQQKAALLGEEL 366
Cdd:pfam02841 258 QLLAEQERMLEHK-LQEQEELLKE---GFKTEAESLQKEI 293
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
149-289 |
8.40e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 38.46 E-value: 8.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 149 LQNQLDESQQERNDLMQLKLQLEDQ----------------VTELRSRVQELEAALATARQEHSELTEQYKGL------- 205
Cdd:COG3206 224 LESQLAEARAELAEAEARLAALRAQlgsgpdalpellqspvIQQLRAQLAELEAELAELSARYTPNHPDVIALraqiaal 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 206 --------SRSHGELSEERDILSQQQGDHVARILELEDDIQTMSDKvlmkEVELDRVRDTVKALTREQEKLLRQLKEFQA 277
Cdd:COG3206 304 raqlqqeaQRILASLEAELEALQAREASLQAQLAQLEARLAELPEL----EAELRRLEREVEVARELYESLLQRLEEARL 379
|
170
....*....|..
gi 148672009 278 DKEQSEAELQTV 289
Cdd:COG3206 380 AEALTVGNVRVI 391
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
176-361 |
8.65e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 38.78 E-value: 8.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 176 ELRSRVQELEAALATARQEHSEltEQYKglsrsHGELSEERDILSQQQGDhvarileLEDDIQTMSDkvlmkevELDRVR 255
Cdd:COG3096 282 ELSERALELRRELFGARRQLAE--EQYR-----LVEMARELEELSARESD-------LEQDYQAASD-------HLNLVQ 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672009 256 DTVkaltREQEKLLRqlkeFQADkeqseaelqtvreencclnteLEEAKSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKV 335
Cdd:COG3096 341 TAL----RQQEKIER----YQED---------------------LEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEV 391
|
170 180
....*....|....*....|....*.
gi 148672009 336 AElepLKEQLRGVQElAASSQQKAAL 361
Cdd:COG3096 392 DS---LKSQLADYQQ-ALDVQQTRAI 413
|
|
| |
