|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
3-348 |
1.85e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.86 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 3 LEKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEftlkedltklktltvmfvdERKT 82
Cdd:PRK03918 233 LEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK-------------------EKAE 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 83 MSEKLKKTEDKLQAASSQLQVEQNKVttvtEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLkAEEEKGNDLLSRVN 162
Cdd:PRK03918 294 EYIKLSEFYEEYLDELREIEKRLSRL----EEEINGIEERIKELEEKEERLEELKKKLKELEKRL-EELEERHELYEEAK 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 163 MLKNRLQSLEAIEKDFLKNKLNQDSGKSTTALHQENNKIKELSQEVERLKLKLKDMKAIEDDLMK------------TED 230
Cdd:PRK03918 369 AKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelTEE 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 231 EYETLERRY-------ANERDKAQFLSKELEHVKMELAKyKLAEKTETSHEQWLFKRLQEEEAKSGHLSREvdALKEKIH 303
Cdd:PRK03918 449 HRKELLEEYtaelkriEKELKEIEEKERKLRKELRELEK-VLKKESELIKLKELAEQLKELEEKLKKYNLE--ELEKKAE 525
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 544346093 304 EYMATEDLICHLQGDHSVLQ---KKLNQQENRNRDLGREIENLTKELE 348
Cdd:PRK03918 526 EYEKLKEKLIKLKGEIKSLKkelEKLEELKKKLAELEKKLDELEEELA 573
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
25-362 |
1.07e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.54 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 25 EKERMTTKQLSQELESLKvriKELEAIESRLEKTEFTLKEDLTKLKTLTVMFVDERKTMSEKlkktEDKLQAASSQLQVE 104
Cdd:TIGR02168 666 AKTNSSILERRREIEELE---EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL----SRQISALRKDLARL 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 105 QNKVttvtEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAIEKDFLK--NK 182
Cdd:TIGR02168 739 EAEV----EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAelTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 183 LNQDSGKSTTALHQENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERRyanerdkaqfLSKELEHVKMELAK 262
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE----------LESELEALLNERAS 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 263 YKLAEKTETSHEQWLFKRLQEEEAKSGHLSREVDALKEKIHEYMATEDlicHLQGDHSVLQKKLNQQENRN-RDLGREIE 341
Cdd:TIGR02168 885 LEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE---GLEVRIDNLQERLSEEYSLTlEEAEALEN 961
|
330 340
....*....|....*....|.
gi 544346093 342 NLTKELERYRHFSKSLRPSLN 362
Cdd:TIGR02168 962 KIEDDEEEARRRLKRLENKIK 982
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
32-349 |
6.87e-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: 65.85 E-value: 6.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 32 KQLSQELESLKVRI---------KELEAIESRLEKTEFTLKEDLTKLKTLTVMFVDERKTMSEkLKKTEDKLQAASSQLQ 102
Cdd:TIGR02168 216 KELKAELRELELALlvlrleelrEELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE-LEEEIEELQKELYALA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 103 VEQNKVTTVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAIEKDflknk 182
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE----- 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 183 LNQDSGKSTTALHQENNKIKELSQEVERLKLKLKDMkaieddlmktEDEYETLERRYANERDKAQFLSKELEHVKMELAK 262
Cdd:TIGR02168 370 LESRLEELEEQLETLRSKVAQLELQIASLNNEIERL----------EARLERLEDRRERLQQEIEELLKKLEEAELKELQ 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 263 YKLAEKtetshEQWLFKRLQEEEAKSGHLSREVDALKEKIHEYMATEDLICHLQGdhsvLQKKLNQQENRNRDLGREIEN 342
Cdd:TIGR02168 440 AELEEL-----EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA----RLDSLERLQENLEGFSEGVKA 510
|
....*..
gi 544346093 343 LTKELER 349
Cdd:TIGR02168 511 LLKNQSG 517
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
107-348 |
7.89e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.47 E-value: 7.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 107 KVTTVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAI-----EKDFLKN 181
Cdd:PRK03918 169 EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELkeeieELEKELE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 182 KLNQDSGKSTTALHQENNKIKELSQEVERLKLKLKDMKAIEddlmKTEDEYETLERRYANERDKAQFLSKELEHVKMELA 261
Cdd:PRK03918 249 SLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK----EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 262 --KYKLAEKTETSheqwlfKRLQEEEAKSGHLSREVDALKEKIHEYmatedlichlqgdHSVLQKKLNQQENRNRDLGRE 339
Cdd:PRK03918 325 giEERIKELEEKE------ERLEELKKKLKELEKRLEELEERHELY-------------EEAKAKKEELERLKKRLTGLT 385
|
....*....
gi 544346093 340 IENLTKELE 348
Cdd:PRK03918 386 PEKLEKELE 394
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
19-284 |
2.32e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 64.32 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 19 SLKCNLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLTVmfvDERKTMSEKLKKTE---DKLQ 95
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGE---EEQLRVKEKIGELEaeiASLE 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 96 AASSQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSL---- 171
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETrdel 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 172 --EAIEKDFLKNKLN----------QDSGKSTTALHQENNKIKELSQEV----ERLKLKLKDMKAIEDDLMKTEDEYETL 235
Cdd:TIGR02169 388 kdYREKLEKLKREINelkreldrlqEELQRLSEELADLNAAIAGIEAKIneleEEKEDKALEIKKQEWKLEQLAADLSKY 467
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 544346093 236 ERRYANERDKAQFLSKELEHVKMELAKyKLAEKTETSHEQWLFKRLQEE 284
Cdd:TIGR02169 468 EQELYDLKEEYDRVEKELSKLQRELAE-AEAQARASEERVRGGRAVEEV 515
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
21-343 |
3.03e-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: 63.92 E-value: 3.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 21 KCNLEKERMTTK--QLSQELESLKvriKELEAIESRLEKTEfTLKEDLTKLKTLTVMFVDERKTMSEKLKKTEDKLQAAS 98
Cdd:TIGR02168 681 ELEEKIEELEEKiaELEKALAELR---KELEELEEELEQLR-KELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 99 SQLQVEQNKVTTVTEKLIEETKRAlksktdvEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAIEKDF 178
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEA-------EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 179 LKNKlnQDSGKSTTALHQEnnkIKELSQEVERLKLKLKDMKA----IEDDLMKTEDEYETLERRYANERDKAQFLS---K 251
Cdd:TIGR02168 830 ERRI--AATERRLEDLEEQ---IEELSEDIESLAAEIEELEElieeLESELEALLNERASLEEALALLRSELEELSeelR 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 252 ELEHVKMELakYKLAEKTETSHEQWlfkRLQEEEAKSghlsrEVDALKEKIHE-YMATEDLIchlQGDHSVLQKKLNQQE 330
Cdd:TIGR02168 905 ELESKRSEL--RRELEELREKLAQL---ELRLEGLEV-----RIDNLQERLSEeYSLTLEEA---EALENKIEDDEEEAR 971
|
330
....*....|...
gi 544346093 331 NRNRDLGREIENL 343
Cdd:TIGR02168 972 RRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3-267 |
5.19e-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: 63.15 E-value: 5.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 3 LEKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLTVMFVDERKT 82
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 83 MSEKLKKTEDKLQAASSqlqvEQNKVTTVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLL---- 158
Cdd:TIGR02168 843 LEEQIEELSEDIESLAA----EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRrele 918
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 159 ---SRVNMLKNRLQSLEAiEKDFLKNKLNQDsGKSTTALHQEN-----NKIKELSQEVERLKLKLKDMKAIEddlMKTED 230
Cdd:TIGR02168 919 elrEKLAQLELRLEGLEV-RIDNLQERLSEE-YSLTLEEAEALenkieDDEEEARRRLKRLENKIKELGPVN---LAAIE 993
|
250 260 270
....*....|....*....|....*....|....*..
gi 544346093 231 EYETLERRYanerdkaQFLSKELEHVkmELAKYKLAE 267
Cdd:TIGR02168 994 EYEELKERY-------DFLTAQKEDL--TEAKETLEE 1021
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3-305 |
1.28e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.62 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 3 LEKLEDAFNKSKQEcyslkcnLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLK-TLTVMFVDERK 81
Cdd:TIGR02169 725 IEQLEQEEEKLKER-------LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEaRLSHSRIPEIQ 797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 82 TMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRV 161
Cdd:TIGR02169 798 AELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL 877
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 162 NMLKNRLQSLEAiEKDFLKNKLNqdsgksttalhQENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERR--- 238
Cdd:TIGR02169 878 RDLESRLGDLKK-ERDELEAQLR-----------ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdee 945
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544346093 239 YANERDKAQFLSKELEHVKMELAKYK-LAEKTETSHEQWLfKRLQEEEAKSGHLSREVDALKEKIHEY 305
Cdd:TIGR02169 946 IPEEELSLEDVQAELQRVEEEIRALEpVNMLAIQEYEEVL-KRLDELKEKRAKLEEERKAILERIEEY 1012
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
32-332 |
2.78e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 32 KQLSQELESLKV--RIKELEAIESRLEKTEFTLKEDLTKLKTLTVMfVDERKTMSEKLKKTEDKLQAASSQLQVEQNKVT 109
Cdd:COG1196 216 RELKEELKELEAelLLLKLRELEAELEELEAELEELEAELEELEAE-LAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 110 TVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAIEKDFLKNKLNQDSgk 189
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA-- 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 190 sttalhQENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKAQFLSKELEHVKMELAKYKLAEKT 269
Cdd:COG1196 373 ------ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544346093 270 ETSHEQwlfkRLQEEEAKSghLSREVDALKEKIHEYMATEDLICHLQGDHSVLQKKLNQQENR 332
Cdd:COG1196 447 AAEEEA----ELEEEEEAL--LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
3-348 |
9.87e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 9.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 3 LEKLEDAFNKSKQECYSLKCNLEKERMTtKQLSQELESLKVRIK--ELEAIESRLEKTEFTLKEDLTKLKTLTVMF---- 76
Cdd:PRK03918 340 LEELKKKLKELEKRLEELEERHELYEEA-KAKKEELERLKKRLTglTPEKLEKELEELEKAKEEIEEEISKITARIgelk 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 77 --VDERKTMSEKLKKTEDKLQAASSQLQVEQNKvtTVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEE-- 152
Cdd:PRK03918 419 keIKELKKAIEELKKAKGKCPVCGRELTEEHRK--ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEli 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 153 KGNDLLSRVNMLKNRLQS--LEAIEKDF-----LKNKLNQDSGKSTTaLHQENNKIKELSQEVERLKLKLKDMKAIEDDL 225
Cdd:PRK03918 497 KLKELAEQLKELEEKLKKynLEELEKKAeeyekLKEKLIKLKGEIKS-LKKELEKLEELKKKLAELEKKLDELEEELAEL 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 226 MKTEDE-----YETLERR------YANERDKAQFLSKELEHVKMELAKykLAEKTETSheqwlFKRLQEEEAKSGHLSRE 294
Cdd:PRK03918 576 LKELEElgfesVEELEERlkelepFYNEYLELKDAEKELEREEKELKK--LEEELDKA-----FEELAETEKRLEELRKE 648
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 544346093 295 VDALKEKI--HEYMATEDLICHLQGDHSVLQKKLNQQENRNRDLGREIENLTKELE 348
Cdd:PRK03918 649 LEELEKKYseEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE 704
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2-361 |
1.39e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 2 ALEKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLTVMFVDERK 81
Cdd:PRK03918 297 KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELER 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 82 TMS-------EKLKKTEDKLQAASSQLQVEQNKVTTVT----------EKLIEETKRAlKSKTDV----------EEKMY 134
Cdd:PRK03918 377 LKKrltgltpEKLEKELEELEKAKEEIEEEISKITARIgelkkeikelKKAIEELKKA-KGKCPVcgrelteehrKELLE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 135 SVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAIEK-----DFLKN---KLNQDSGKSTTALHQENNKIKE--- 203
Cdd:PRK03918 456 EYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKlkelaEQLKEleeKLKKYNLEELEKKAEEYEKLKEkli 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 204 -LSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERRYAN-ERDKAQFLSKELEHVKMELakyklaEKTETSHEQWL---- 277
Cdd:PRK03918 536 kLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAElLKELEELGFESVEELEERL------KELEPFYNEYLelkd 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 278 -FKRLQEEEAKSGHLSREVDALKEKIHEymaTEDLICHLQGDHSVLQKKLNQQENRN-----RDLGREIENLTKELERYR 351
Cdd:PRK03918 610 aEKELEREEKELKKLEEELDKAFEELAE---TEKRLEELRKELEELEKKYSEEEYEElreeyLELSRELAGLRAELEELE 686
|
410
....*....|
gi 544346093 352 HFSKSLRPSL 361
Cdd:PRK03918 687 KRREEIKKTL 696
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
121-349 |
1.67e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 121 RALKSKTDVEEKMYSVtKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAiEKDFLKNKLNQDSGKSTTALHQENNK 200
Cdd:COG1196 216 RELKEELKELEAELLL-LKLRELEAELEELEAELEELEAELEELEAELAELEA-ELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 201 IKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKAQFLSKELEHVKMELAKYKLAEKTETsheqwlfKR 280
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE-------EA 366
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544346093 281 LQEEEAKSGHLSREVDALKEKIHEymatedlichLQGDHSVLQKKLNQQENRNRDLGREIENLTKELER 349
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLE----------ALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
3-384 |
1.73e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 57.81 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 3 LEKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLKVRIKEL----EAIESRLEKTEFTLKEDLTKLKTLTVMFVD 78
Cdd:pfam05483 284 LKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLteekEAQMEELNKAKAAHSFVVTEFEATTCSLEE 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 79 ERKTMSEKLKKTEDKLQAASSQLQV------EQNKVTTVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNK------ 146
Cdd:pfam05483 364 LLRTEQQRLEKNEDQLKIITMELQKksseleEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKeqelif 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 147 -LKAEEEKGNDLLSRVNMLKNRLQSLEAIEKDfLKNKLNQDSGKStTALHQENNKI----KELSQEVERLKLKLKDMKAI 221
Cdd:pfam05483 444 lLQAREKEIHDLEIQLTAIKTSEEHYLKEVED-LKTELEKEKLKN-IELTAHCDKLllenKELTQEASDMTLELKKHQED 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 222 EDDLMKTED----EYETLERRYANERDKAQFLSKEL----EHVKMELAKYKLAEKTETSHEQWLFKRLQEEEAKSGHLSR 293
Cdd:pfam05483 522 IINCKKQEErmlkQIENLEEKEMNLRDELESVREEFiqkgDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKK 601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 294 EVDALKEKIHEYMATEDLichLQGDHSVLQKKLNQQENRNRDLGREIENLTKELERyrhFSKSLRPSLNGRRISDPQVFS 373
Cdd:pfam05483 602 QIENKNKNIEELHQENKA---LKKKGSAENKQLNAYEIKVNKLELELASAKQKFEE---IIDNYQKEIEDKKISEEKLLE 675
|
410
....*....|.
gi 544346093 374 KEVQTEAVDNE 384
Cdd:pfam05483 676 EVEKAKAIADE 686
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
2-254 |
2.39e-08 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 57.24 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 2 ALEKLEDAFNKSKqecyslkcnLEKERMTTKQLSQELESLKVRIKELEAIESRLEKteftLKEDLTKLKtltvmfvDERK 81
Cdd:PRK05771 58 ALDKLRSYLPKLN---------PLREEKKKVSVKSLEELIKDVEEELEKIEKEIKE----LEEEISELE-------NEIK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 82 TMSEKLKKTEdKLQAASSQLQVEQN-KVTTVTEKLIEETKralksktdveekmYSVTKERDDLKNKLKAEEEKGNDLLSR 160
Cdd:PRK05771 118 ELEQEIERLE-PWGNFDLDLSLLLGfKYVSVFVGTVPEDK-------------LEELKLESDVENVEYISTDKGYVYVVV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 161 VNmLKNRLQSLEAI--EKDFLKNKLNqDSGKSTTALHQENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYetlerr 238
Cdd:PRK05771 184 VV-LKELSDEVEEElkKLGFERLELE-EEGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEY------ 255
|
250
....*....|....*.
gi 544346093 239 YANERDKAQFLSKELE 254
Cdd:PRK05771 256 LEIELERAEALSKFLK 271
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
4-375 |
2.51e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.84 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 4 EKLEDAFNKSKQEcyslKCNLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTltvmfvDERKTM 83
Cdd:PTZ00121 1377 KKKADAAKKKAEE----KKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKA------EEAKKA 1446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 84 SEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNM 163
Cdd:PTZ00121 1447 DEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE 1526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 164 LKNRLQSLEAIEKDFLKNKLNQDSGKSTTALH--QENNKIKELSQEVERLKLKLK---DMKAIE----DDLMKTEDEYET 234
Cdd:PTZ00121 1527 AKKAEEAKKADEAKKAEEKKKADELKKAEELKkaEEKKKAEEAKKAEEDKNMALRkaeEAKKAEeariEEVMKLYEEEKK 1606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 235 LE----RRYANERDKAQFLSKElEHVKMELAKYKLAEKTETSHEQWLFKRLQEEEAKSGHLSREVDALKEKIHEYMATED 310
Cdd:PTZ00121 1607 MKaeeaKKAEEAKIKAEELKKA-EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEE 1685
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544346093 311 lichlqgdhsvLQKKLNQQENRNRDLGREIENLTKELERYRHFSKSLRPSLNGRRISDPQVFSKE 375
Cdd:PTZ00121 1686 -----------DEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEA 1739
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
4-348 |
3.02e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.46 E-value: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 4 EKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLKvriKELEAIESRLEKTEFTLKEDLTKLKTLTVMFVDERKTM 83
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAA---DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAD 1394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 84 SEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEKmysvtKERDDLKNklKAEEEKGNDLLSRVNM 163
Cdd:PTZ00121 1395 EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEA-----KKADEAKK--KAEEAKKAEEAKKKAE 1467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 164 LKNRLQSL-----EAIEKDFLKNKLNQDSGKSTTALHQENNKIK-------ELSQEVERLKLKLKDMKAIE----DDLMK 227
Cdd:PTZ00121 1468 EAKKADEAkkkaeEAKKADEAKKKAEEAKKKADEAKKAAEAKKKadeakkaEEAKKADEAKKAEEAKKADEakkaEEKKK 1547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 228 TEDEYETLERRYANERDKAQFLSKELEHVKMELAKYKLAEKTETSHEQWLFKRLQEEEAKSGHLSREVDALKEKIHEYMA 307
Cdd:PTZ00121 1548 ADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK 1627
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 544346093 308 TEDlichlqgdhsvLQKKLNQQENRNRDLGREIENLTKELE 348
Cdd:PTZ00121 1628 AEE-----------EKKKVEQLKKKEAEEKKKAEELKKAEE 1657
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
47-343 |
3.72e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.00 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 47 ELEAIESRLEKTEFTLKEDLTKLKTLTvmfvDERKTmSEKLKKTEDKLQAASSQLQVEQNKVTtvtEKLIEETKRALKSK 126
Cdd:TIGR02169 178 ELEEVEENIERLDLIIDEKRQQLERLR----REREK-AERYQALLKEKREYEGYELLKEKEAL---ERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 127 TDVEEKmysVTKERDDLKNKLKAEEEKGNDLLSRVNmlknRLQSLEAIEkdfLKNKLnqdsGKSTTALHQENNKIKELSQ 206
Cdd:TIGR02169 250 EEELEK---LTEEISELEKRLEEIEQLLEELNKKIK----DLGEEEQLR---VKEKI----GELEAEIASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 207 EVERLKLKLKDmkaIEDDLMKTEDEYETLERRYANERDKAQFLSKELEHVKMELAKyklaektetsheqwLFKRLQEEEA 286
Cdd:TIGR02169 316 ELEDAEERLAK---LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELED--------------LRAELEEVDK 378
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 544346093 287 KSGHLSREVDALKEKIHEYmatEDLICHLQGDHSVLQKKLNQQENRNRDLGREIENL 343
Cdd:TIGR02169 379 EFAETRDELKDYREKLEKL---KREINELKRELDRLQEELQRLSEELADLNAAIAGI 432
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
32-262 |
4.49e-08 |
|
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: 55.93 E-value: 4.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 32 KQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKtltvmfvDERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTV 111
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALE-------RRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 112 TEKLiEETKRALKSKTDVEEKMysvtKERDDLKNKLKAEEekGNDLLSRVNMLK----NRLQSLEAIEKDflKNKLNQds 187
Cdd:COG4942 96 RAEL-EAQKEELAELLRALYRL----GRQPPLALLLSPED--FLDAVRRLQYLKylapARREQAEELRAD--LAELAA-- 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544346093 188 gkSTTALHQENNKIKELSQEVERLKLKLKDMKAIEDDLMKT-EDEYETLERRYANERDKAQFLSKELEHVKMELAK 262
Cdd:COG4942 165 --LRAELEAERAELEALLAELEEERAALEALKAERQKLLARlEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
3-391 |
5.00e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 56.45 E-value: 5.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 3 LEKLEDAFNKSKQECYSLKCNLE-----KERMTTKQLsqELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLTVMFV 77
Cdd:PRK01156 161 INSLERNYDKLKDVIDMLRAEISnidylEEKLKSSNL--ELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLK 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 78 DERKTMS---EKLKKTEDKLQAASSQLQVEQNKVTTVTEklieetkralksktdVEEKMYSVTKerddlkNKLKAEEEKG 154
Cdd:PRK01156 239 SALNELSsleDMKNRYESEIKTAESDLSMELEKNNYYKE---------------LEERHMKIIN------DPVYKNRNYI 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 155 NDLLSRVNMLKNRLQSLEAIEKDFLKNklnQDSGKSTTALHQENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYET 234
Cdd:PRK01156 298 NDYFKYKNDIENKKQILSNIDAEINKY---HAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIES 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 235 LERRYANERDKAQFLSKELEHVkmeLAKYKLAEKTETSHEQWLFKRLQEEEAKSGHLSREVDALKEK---IHEYMA---- 307
Cdd:PRK01156 375 LKKKIEEYSKNIERMSAFISEI---LKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENldeLSRNMEmlng 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 308 ---------------TEDLICHLQGDHSVLQKKLNQQENRNRDLGREIENLTKELER-----------YRHFSKSLRPSL 361
Cdd:PRK01156 452 qsvcpvcgttlgeekSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYleseeinksinEYNKIESARADL 531
|
410 420 430
....*....|....*....|....*....|
gi 544346093 362 NGRRISDPQVFSKEVQTEAVDNEppdYKSL 391
Cdd:PRK01156 532 EDIKIKINELKDKHDKYEEIKNR---YKSL 558
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
79-304 |
1.20e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 79 ERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKlIEETKRALKSKTDVEEkmysVTKERDDLKNKlkAEEEKGNDLL 158
Cdd:PTZ00121 1275 EEARKADELKKAEEKKKADEAKKAEEKKKADEAKKK-AEEAKKADEAKKKAEE----AKKKADAAKKK--AEEAKKAAEA 1347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 159 SRVNMlKNRLQSLEAIEKDFLKNKLNQDSGKSTTalhQENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLE-- 236
Cdd:PTZ00121 1348 AKAEA-EAAADEAEAAEEKAEAAEKKKEEAKKKA---DAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADea 1423
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544346093 237 RRYANERDKAQFLSKELEHV-KMELAKYKLAE--KTETSHEQWLFKRLQEEEAKSGHLSREVDALKEKIHE 304
Cdd:PTZ00121 1424 KKKAEEKKKADEAKKKAEEAkKADEAKKKAEEakKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEE 1494
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
23-355 |
1.23e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 23 NLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLtvmfVDERKTMSEKLKKTEDKLQAASSQLQ 102
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEV----LREINEISSELPELREELEKLEKEVK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 103 vEQNKVTTVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKgndlLSRVNMLKNRLQSLEAIEKdfLKNK 182
Cdd:PRK03918 232 -ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK----VKELKELKEKAEEYIKLSE--FYEE 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 183 LNQDSGKSTTALHQENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERRyANERDKAQFLSKELEHVKMELA- 261
Cdd:PRK03918 305 YLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEER-HELYEEAKAKKEELERLKKRLTg 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 262 --------KYKLAEKTETSHEqwlfKRLQEEEAKSGHLSREVDALKEKIHEYMAT----------------EDLICHLQG 317
Cdd:PRK03918 384 ltpeklekELEELEKAKEEIE----EEISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgrelteehrKELLEEYTA 459
|
330 340 350
....*....|....*....|....*....|....*...
gi 544346093 318 DHSVLQKKLNQQENRNRDLGREIENLTKELERYRHFSK 355
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIK 497
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
25-310 |
4.03e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 25 EKERMTTKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLTVMFVDERKTMSEKLKKTEDKLQAASSQLQVE 104
Cdd:PTZ00121 1246 EEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAE 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 105 QNKVTT-VTEKLIEETKRALKSKTDVEEKmysVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQslEAIEKDFLKNKL 183
Cdd:PTZ00121 1326 EAKKKAdAAKKKAEEAKKAAEAAKAEAEA---AADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE--EKKKADEAKKKA 1400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 184 NQDSGKSttalhQENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLE-RRYANERDKAQFLSKELEHVKMELAK 262
Cdd:PTZ00121 1401 EEDKKKA-----DELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEaKKKAEEAKKAEEAKKKAEEAKKADEA 1475
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 544346093 263 YKLAEKTETSHEqwlFKRLQEEEAKSGHLSREVDALKEKIHEYMATED 310
Cdd:PTZ00121 1476 KKKAEEAKKADE---AKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE 1520
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
157-363 |
4.12e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.53 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 157 LLSRVNMLKNRLQSLEaIEKDFLKNKLNqdsgksttalHQENnKIKELSQEVERLKLKLKDmkaIEDDLMKTEDEYETLE 236
Cdd:TIGR02169 672 EPAELQRLRERLEGLK-RELSSLQSELR----------RIEN-RLDELSQELSDASRKIGE---IEKEIEQLEQEEEKLK 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 237 RRYANERDKAQFLSKELEHVKMELAKY--KLAEKTETSHEqwLFKRLQEEEAK-SGHLSREVDALKEKIHEYMA------ 307
Cdd:TIGR02169 737 ERLEELEEDLSSLEQEIENVKSELKELeaRIEELEEDLHK--LEEALNDLEARlSHSRIPEIQAELSKLEEEVSriearl 814
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544346093 308 --TEDLICHLQGDHSVLQKKLNQQENRNRDL-------GREIENLTK-------ELERYRHFSKSLRPSLNG 363
Cdd:TIGR02169 815 reIEQKLNRLTLEKEYLEKEIQELQEQRIDLkeqiksiEKEIENLNGkkeeleeELEELEAALRDLESRLGD 886
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
91-286 |
5.57e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 5.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 91 EDKLQAASSQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQS 170
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 171 LEAI-EKDFLKNKLNQDSGKsTTALHQENNKIKELSQEVERLKLKLKDMKAIEDDLMK-----TEDEYETLERRYANERD 244
Cdd:COG4717 128 LPLYqELEALEAELAELPER-LEELEERLEELRELEEELEELEAELAELQEELEELLEqlslaTEEELQDLAEELEELQQ 206
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 544346093 245 KAQFLSKELEHVKMEL--AKYKLAEKTETSHEQWLFKRLQEEEA 286
Cdd:COG4717 207 RLAELEEELEEAQEELeeLEEELEQLENELEAAALEERLKEARL 250
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2-358 |
7.32e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 52.67 E-value: 7.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 2 ALEKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLTVMFVDERK 81
Cdd:pfam02463 174 ALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 82 TMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEETKRALKSKtdvEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRV 161
Cdd:pfam02463 254 ESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEEL---KSELLKLERRKVDDEEKLKESEKEKKKAEKEL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 162 NMLKNRLQSLEAIEKDFLKNKLNQDSGKSTTALHQENNKIKElsqevERLKLKLKDMKAIEDDLMKTEDEYETLERRYAN 241
Cdd:pfam02463 331 KKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLE-----EELLAKKKLESERLSSAAKLKEEELELKSEEEK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 242 ERDKAQFLSKELEHVKMELAKYKLAEKTETSHEQWLFKR--------LQEEEAKSGHLSREVDALKEKIHEYMATEDLIC 313
Cdd:pfam02463 406 EAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGklteekeeLEKQELKLLKDELELKKSEDLLKETQLVKLQEQ 485
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 544346093 314 HLQGDHSVLQKKLNQQENRNRDLGREIENLTKELERYRHFSKSLR 358
Cdd:pfam02463 486 LELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGR 530
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
168-351 |
8.94e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 8.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 168 LQSLEAIEKDFLKNKLNQ---DSGKSTTALHQEnnkIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERRYANERD 244
Cdd:COG4717 40 LAFIRAMLLERLEKEADElfkPQGRKPELNLKE---LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 245 KAQFLSKELEHVKMELAKYKLAEKTETSHEQWlfKRLQEEEAKSGHLSREVDALKEKIHEY------------MATEDLI 312
Cdd:COG4717 117 ELEKLEKLLQLLPLYQELEALEAELAELPERL--EELEERLEELRELEEELEELEAELAELqeeleelleqlsLATEEEL 194
|
170 180 190
....*....|....*....|....*....|....*....
gi 544346093 313 CHLQGDHSVLQKKLNQQENRNRDLGREIENLTKELERYR 351
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
30-261 |
1.55e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.56 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 30 TTKQLSQELESLKvriKELEAIESRLEktEFTLKEDLTKLKtltvmfvDERKTMSEKLKKTEDKLQAASSQLQVEQNKVT 109
Cdd:COG3206 176 ALEFLEEQLPELR---KELEEAEAALE--EFRQKNGLVDLS-------EEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 110 TVTEKLieETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAiekdflknKLNQDSGK 189
Cdd:COG3206 244 ALRAQL--GSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRA--------QLQQEAQR 313
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544346093 190 STTALHQEnnkIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKAQFLSKELEHVKMELA 261
Cdd:COG3206 314 ILASLEAE---LEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEA 382
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
11-413 |
2.06e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 51.23 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 11 NKSKQECYS-LKCNLEKeRMTTKQLSQELESLKVRIKELEAiESRLEKTEFTLkEDLTKLKTLTVmfvDERKTMSEKLKK 89
Cdd:COG5022 923 LEFKTELIArLKKLLNN-IDLEEGPSIEYVKLPELNKLHEV-ESKLKETSEEY-EDLLKKSTILV---REGNKANSELKN 996
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 90 TEDKLQAASSQLQVEQNKVttvteKLIEETKRALKSKTDVEEKMYSVTKErddLKNKLKAEEEKGNDLLSrVNMLKNRLQ 169
Cdd:COG5022 997 FKKELAELSKQYGALQEST-----KQLKELPVEVAELQSASKIISSESTE---LSILKPLQKLKGLLLLE-NNQLQARYK 1067
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 170 SLEaIEKDFLKNKLNQDSGKSTTalhqeNNKIKElsqeverlkLKLKDMKAIEDDLMKTEDEYETL---ERRYANERDKA 246
Cdd:COG5022 1068 ALK-LRRENSLLDDKQLYQLEST-----ENLLKT---------INVKDLEVTNRNLVKPANVLQFIvaqMIKLNLLQEIS 1132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 247 QFLSKELEHVKMELAKYKLAEKT-----------ETSHEQWlFKRLQEEEAKSGH---------------LSREVDALKE 300
Cdd:COG5022 1133 KFLSQLVNTLEPVFQKLSVLQLEldglfweanleALPSPPP-FAALSEKRLYQSAlydeksklsssevndLKNELIALFS 1211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 301 KIHEYMATEDLICHL--QGDHSVLQKKLNQQENRNRDLGREIENLTKelERYRHFSKSLRPSLNGRRISdPQVFSKEVQT 378
Cdd:COG5022 1212 KIFSGWPRGDKLKKLisEGWVPTEYSTSLKGFNNLNKKFDTPASMSN--EKLLSLLNSIDNLLSSYKLE-EEVLPATINS 1288
|
410 420 430
....*....|....*....|....*....|....*
gi 544346093 379 EAVDNEPPDYKSLIPLERAVINGQLYEESENQDED 413
Cdd:COG5022 1289 LLQYINVGLFNALRTKASSLRWKSATEVNYNSEEL 1323
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
3-284 |
2.07e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 3 LEKLEDAFNKSKQECYSLKCNLEKER--MTTKQLSQELESLKVRIKELEAIESRLEKTEF-TLKEDLTKLKTLTVMFVDE 79
Cdd:PRK03918 468 LKEIEEKERKLRKELRELEKVLKKESelIKLKELAEQLKELEEKLKKYNLEELEKKAEEYeKLKEKLIKLKGEIKSLKKE 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 80 RKTMSE---KLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEETKRALK----------SKTDVEEKMYSVTKERDDLKNK 146
Cdd:PRK03918 548 LEKLEElkkKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKelepfyneylELKDAEKELEREEKELKKLEEE 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 147 LKAEEEKGNDLLSRVNMLKNRLQSLEAIEKDFLKNKLNQDSGKSTTALHQENNKIKELSQEVERLKLKLKDMKAIEDDLM 226
Cdd:PRK03918 628 LDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 544346093 227 KTEDEYETLERryanERDKAQFLSKELEHVKMELAKYKLAEKTETSHEqwLFKRLQEE 284
Cdd:PRK03918 708 KAKKELEKLEK----ALERVEELREKVKKYKALLKERALSKVGEIASE--IFEELTEG 759
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
25-384 |
3.77e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.49 E-value: 3.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 25 EKERMTTKQLSQELESLKVRIKELEAIESRLEK---TEFTLKEDLTKLKTLTVMFVDERKTMSEKLKKTEdklqaASSQL 101
Cdd:pfam05483 275 EKTKLQDENLKELIEKKDHLTKELEDIKMSLQRsmsTQKALEEDLQIATKTICQLTEEKEAQMEELNKAK-----AAHSF 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 102 QVEQNKVTTVTeklIEETKRALKSKTDveekmysvtKERDDLKnKLKAEEEKGNDLLSRVNMLKNRlqslEAIEKDFLKN 181
Cdd:pfam05483 350 VVTEFEATTCS---LEELLRTEQQRLE---------KNEDQLK-IITMELQKKSSELEEMTKFKNN----KEVELEELKK 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 182 KLNQDSgksttALHQENNKIKELSQEVERLKLKLKDMkaieddLMKTEDEYETLERRYANERDKAQFLSKELEHVKMELA 261
Cdd:pfam05483 413 ILAEDE-----KLLDEKKQFEKIAEELKGKEQELIFL------LQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 262 KYKLAEKTETSHEQWLFKRLQEEEAKSGHLSREVDALKEKIHEYMATEDLichlqgdhsvLQKKLNQQENRNRDLGREIE 341
Cdd:pfam05483 482 KEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEER----------MLKQIENLEEKEMNLRDELE 551
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 544346093 342 NLTKELERYRHFSK-SLRPSLNGRRISDPQVFSKEVQTEAVDNE 384
Cdd:pfam05483 552 SVREEFIQKGDEVKcKLDKSEENARSIEYEVLKKEKQMKILENK 595
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
4-353 |
9.06e-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: 49.45 E-value: 9.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 4 EKLEDAFNKSKQECYSLKCNLEKERMTTKQL---SQELESLKVRIKELEAIESRLEKTeFTLKEDLTklktltvmfvDER 80
Cdd:pfam12128 426 EQLEAGKLEFNEEEYRLKSRLGELKLRLNQAtatPELLLQLENFDERIERAREEQEAA-NAEVERLQ----------SEL 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 81 KTMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEETKRAL----KSKTDVEEKMYSVTKE----RDDLKNKLKAEEE 152
Cdd:pfam12128 495 RQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLhflrKEAPDWEQSIGKVISPellhRTDLDPEVWDGSV 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 153 KGNDLLSRVNMlknRLQSLEAIEKDFLKNKLNQDSGKSTTALHQENNKIKELSQ-------EVERLKLKLKDMKAI---- 221
Cdd:pfam12128 575 GGELNLYGVKL---DLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEqlvqangELEKASREETFARTAlkna 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 222 EDDLMKTEDEYETLERR----YANERDKAQFLSKELEHVKMELA---KYKLAEKTETSHE---QWLFKRLQEEEAKSGHL 291
Cdd:pfam12128 652 RLDLRRLFDEKQSEKDKknkaLAERKDSANERLNSLEAQLKQLDkkhQAWLEEQKEQKREartEKQAYWQVVEGALDAQL 731
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544346093 292 SReVDALKEKIHEYMATEDLICHLQGDHSVlqKKLNQQENRNRDLGREIENLTKELERYRHF 353
Cdd:pfam12128 732 AL-LKAAIAARRSGAKAELKALETWYKRDL--ASLGVDPDVIAKLKREIRTLERKIERIAVR 790
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1-347 |
1.08e-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: 48.96 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 1 MALEKLEDAFNKSKQECYSL-----------KCNLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEFTLKE----- 64
Cdd:pfam15921 426 MEVQRLEALLKAMKSECQGQmerqmaaiqgkNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDltasl 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 65 ------------DLTKLKTLtvmfVDERKTMSEKLKKTEDKLQAASSQLQ------VEQNKVTTVTEKLIEETKRAL--- 123
Cdd:pfam15921 506 qekeraieatnaEITKLRSR----VDLKLQELQHLKNEGDHLRNVQTECEalklqmAEKDKVIEILRQQIENMTQLVgqh 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 124 -KSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEaIEKDFLKNklnqdsgksttALHQENNKIK 202
Cdd:pfam15921 582 gRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLE-LEKVKLVN-----------AGSERLRAVK 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 203 ELSQEVERLklkLKDMKAIEDDLMKTEDEYETLERRYANErdkaqflSKELEhvkMELAKYKLAEKTETSHEQWLFKRLQ 282
Cdd:pfam15921 650 DIKQERDQL---LNEVKTSRNELNSLSEDYEVLKRNFRNK-------SEEME---TTTNKLKMQLKSAQSELEQTRNTLK 716
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544346093 283 EEEAKSGHLSREVDALKEKIheyMATEDLICHLQGDHSVLQKKLNQQENRNRDLGREIENLTKEL 347
Cdd:pfam15921 717 SMEGSDGHAMKVAMGMQKQI---TAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQEL 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
112-351 |
1.24e-05 |
|
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: 48.90 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 112 TEKLIEETKRALksktdveEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAIEKDFLKNKL---NQDSG 188
Cdd:TIGR02168 177 TERKLERTRENL-------DRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELeelQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 189 KSTTALHQENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERRYanERDKaQFLSKELEHVKMELAKYKLAEK 268
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL--EQQK-QILRERLANLERQLEELEAQLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 269 TETSHEQWLFKRLQEEEAKSGHLSREVDALKEKIHEYMAT-EDLICHLQGdhsvLQKKLNQQENRNRDLGREIENLTKEL 347
Cdd:TIGR02168 327 ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAElEELESRLEE----LEEQLETLRSKVAQLELQIASLNNEI 402
|
....
gi 544346093 348 ERYR 351
Cdd:TIGR02168 403 ERLE 406
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-233 |
1.37e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 2 ALEKLEDAFNKSKQECYSLK---------CNLEKERMttKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTl 72
Cdd:COG1196 275 ELEELELELEEAQAEEYELLaelarleqdIARLEERR--RELEERLEELEEELAELEEELEELEEELEELEEELEEAEE- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 73 tvmfvdERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEKMysvTKERDDLKNKLKAEEE 152
Cdd:COG1196 352 ------ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE---EAEEALLERLERLEEE 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 153 KGNDLLSRVNMLKNRLQSLEAIEKDFLK-NKLNQDSGKSTTALHQENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDE 231
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEeAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
..
gi 544346093 232 YE 233
Cdd:COG1196 503 YE 504
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
4-357 |
1.48e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 48.63 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 4 EKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLkvrikELE-AIESRLEKTEFTLKEDLTKLKTLTVMFVD---- 78
Cdd:pfam01576 243 EELQAALARLEEETAQKNNALKKIRELEAQISELQEDL-----ESErAARNKAEKQRRDLGEELEALKTELEDTLDttaa 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 79 ------ERKTMSEKLKKT-EDKLQAASSQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEE 151
Cdd:pfam01576 318 qqelrsKREQEVTELKKAlEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQ 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 152 EKGNDLLSRVNMLKNRLQSLEA--IEKDFLKNKLNQDSGKS-------TTALHQENNKIKELSQEVERLKLKLKDMK--- 219
Cdd:pfam01576 398 QAKQDSEHKRKKLEGQLQELQArlSESERQRAELAEKLSKLqselesvSSLLNEAEGKNIKLSKDVSSLESQLQDTQell 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 220 --------AIEDDLMKTEDEYETLERRYANERDKAQFLSKELEHVKMELA--KYKLAEKTETSHeqwlfkrlQEEEAKSg 289
Cdd:pfam01576 478 qeetrqklNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSdmKKKLEEDAGTLE--------ALEEGKK- 548
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544346093 290 HLSREVDALKEKIHEYMATEDlichlqgdhsvlqkKLNQQENRnrdLGREIENLTKELERYRHFSKSL 357
Cdd:pfam01576 549 RLQRELEALTQQLEEKAAAYD--------------KLEKTKNR---LQQELDDLLVDLDHQRQLVSNL 599
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
32-349 |
1.92e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 32 KQLSQELESLKVRIKELEAIESRLEK-------------TEFTLKEDLTKLKTLTVMfVDERKTMSEKLKKTEDKLQAAS 98
Cdd:COG4717 98 EELEEELEELEAELEELREELEKLEKllqllplyqeleaLEAELAELPERLEELEER-LEELRELEEELEELEAELAELQ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 99 SQLQVEQNKVTTVTEKLIEETKRALKS-----------KTDVEEKMYSVTKERDDLKNKLKAEEEK-------------- 153
Cdd:COG4717 177 EELEELLEQLSLATEEELQDLAEELEElqqrlaeleeeLEEAQEELEELEEELEQLENELEAAALEerlkearlllliaa 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 154 --------GNDLLSRVNMLKNRLQSLEAI------EKDFLKNKLNQDSGKSTTALHQENNKIKELSQEVERLKLKLKDMK 219
Cdd:COG4717 257 allallglGGSLLSLILTIAGVLFLVLGLlallflLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSP 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 220 AIEDDLMKTEDEYETLERRYANERDKAQFlsKELEHVKMELAKYKLAEkTETSHEQWL--FKRLQEEEAKSGHLSREVDA 297
Cdd:COG4717 337 EELLELLDRIEELQELLREAEELEEELQL--EELEQEIAALLAEAGVE-DEEELRAALeqAEEYQELKEELEELEEQLEE 413
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 544346093 298 LKEKIHEYMATEDLIcHLQGDHSVLQKKLNQQENRNRDLGREIENLTKELER 349
Cdd:COG4717 414 LLGELEELLEALDEE-ELEEELEELEEELEELEEELEELREELAELEAELEQ 464
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
55-300 |
2.09e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 55 LEKTEFTLKEDLTKLKTLTVMFVDERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEKMY 134
Cdd:PTZ00121 1295 AKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKE 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 135 SVTKERDDLKNKLKaEEEKGNDLLSRVNMLKNRLQSLEAIEKDflKNKLNQDSGKSTTALHQENNKIK-ELSQEVERLKL 213
Cdd:PTZ00121 1375 EAKKKADAAKKKAE-EKKKADEAKKKAEEDKKKADELKKAAAA--KKKADEAKKKAEEKKKADEAKKKaEEAKKADEAKK 1451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 214 KLKDMKAIEDDLMKTEDEYETLE-RRYANERDKAQFLSKELEHV--KMELAKYKLAEKTETSHEQWLFKRLQEEEAKSGH 290
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKAEEAKKADEaKKKAEEAKKADEAKKKAEEAkkKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAE 1531
|
250
....*....|
gi 544346093 291 LSREVDALKE 300
Cdd:PTZ00121 1532 EAKKADEAKK 1541
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2-349 |
2.14e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 2 ALEKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLKvRIKELEAIESRLEKTEFTLKEDLTKLKTLTVMfVDERK 81
Cdd:COG4717 82 EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE-KLLQLLPLYQELEALEAELAELPERLEELEER-LEELR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 82 TMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEETKRALKS-----------KTDVEEKMYSVTKERDDLKNKLKAE 150
Cdd:COG4717 160 ELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEElqqrlaeleeeLEEAQEELEELEEELEQLENELEAA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 151 EEK----------------------GNDLLSRVNMLKNRLQSLEAI------EKDFLKNKLNQDSGKSTTALHQENNKIK 202
Cdd:COG4717 240 ALEerlkearlllliaaallallglGGSLLSLILTIAGVLFLVLGLlallflLLAREKASLGKEAEELQALPALEELEEE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 203 ELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKAQFlsKELEHVKMELAKYKLAEkTETSHEQWL--FKR 280
Cdd:COG4717 320 ELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL--EELEQEIAALLAEAGVE-DEEELRAALeqAEE 396
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544346093 281 LQEEEAKSGHLSREVDALKEKIHEYMATEDLichlqgdhSVLQKKLNQQENRNRDLGREIENLTKELER 349
Cdd:COG4717 397 YQELKEELEELEEQLEELLGELEELLEALDE--------EELEEELEELEEELEELEEELEELREELAE 457
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
3-348 |
3.64e-05 |
|
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: 47.32 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 3 LEKLEDAFNKSKQECYSLKCNLEKERmttKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLTvmfvderkT 82
Cdd:TIGR04523 150 KEKELEKLNNKYNDLKKQKEELENEL---NLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLE--------S 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 83 MSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVN 162
Cdd:TIGR04523 219 QISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEIS 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 163 MLKN-RLQSLEAIEKDFLKNKLNQDSgKSTTALHQENNKIKELSQEVERLKLKLKDM----KAIEDDLMKTEDEYETLER 237
Cdd:TIGR04523 299 DLNNqKEQDWNKELKSELKNQEKKLE-EIQNQISQNNKIISQLNEQISQLKKELTNSesenSEKQRELEEKQNEIEKLKK 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 238 RYANERDKAQFLSKELEHVKMELAKYKLAE-------KTETSHEQWLFKRLQEEEAKSGHLSREVDALKEKIHE----YM 306
Cdd:TIGR04523 378 ENQSYKQEIKNLESQINDLESKIQNQEKLNqqkdeqiKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVkeliIK 457
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 544346093 307 ATEDLICHLQGDHSVLQKKLNQQENRNRDLGREIENLTKELE 348
Cdd:TIGR04523 458 NLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELK 499
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
54-368 |
3.95e-05 |
|
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: 47.35 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 54 RLEKTEFTLKEDLTKLKTLTVMFVDERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEKM 133
Cdd:TIGR00606 685 RVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLK 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 134 YSVTKERDDLKNkLKAEEEKGNDLLSRVNMLKNRLQSLEAIEKDFLKNKLNQDSGKSTTALHQENNKIKE-------LSQ 206
Cdd:TIGR00606 765 NDIEEQETLLGT-IMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEkqheldtVVS 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 207 EVERLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKAQFLSKELEHVKMEL----AKYKLAEKTETSHEQWLFKRLQ 282
Cdd:TIGR00606 844 KIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVqsliREIKDAKEQDSPLETFLEKDQQ 923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 283 EEEA--KSGHLSR-----EVDALKEK---IHEYMatEDLICHLQGDHsvlQKKLNQQENRNRDLGREIENLTKELERYRH 352
Cdd:TIGR00606 924 EKEEliSSKETSNkkaqdKVNDIKEKvknIHGYM--KDIENKIQDGK---DDYLKQKETELNTVNAQLEECEKHQEKINE 998
|
330
....*....|....*.
gi 544346093 353 FSKSLRPSLNGRRISD 368
Cdd:TIGR00606 999 DMRLMRQDIDTQKIQE 1014
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
21-386 |
4.26e-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: 4.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 21 KCNLEKERMTTKQLSQELESLK----VRIKELEAIESRLEKTEFTL----KEDLTKLKTLTvmfvDERKTMSEKLKKTED 92
Cdd:pfam15921 592 KAQLEKEINDRRLELQEFKILKdkkdAKIRELEARVSDLELEKVKLvnagSERLRAVKDIK----QERDQLLNEVKTSRN 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 93 KLQAASSQLQVEQNKVTTVTEKLiEETKRALKSKtdveekMYSVTKERDDLKNKLKAEEEKGNDLLS------------- 159
Cdd:pfam15921 668 ELNSLSEDYEVLKRNFRNKSEEM-ETTTNKLKMQ------LKSAQSELEQTRNTLKSMEGSDGHAMKvamgmqkqitakr 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 160 -RVNMLKNRLQSLEAI------EKDFLKNKLNQDSGKSTTALHQENNKIKEL----SQEvERLKLKLKDMKAIEDDLMKT 228
Cdd:pfam15921 741 gQIDALQSKIQFLEEAmtnankEKHFLKEEKNKLSQELSTVATEKNKMAGELevlrSQE-RRLKEKVANMEVALDKASLQ 819
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 229 EDEYETLERRYANE--RDKAQFL--SKELE---HVKMELAKYKLAEKTETSHEQWLFKRLQEEEAKSGHLSREVDALKEK 301
Cdd:pfam15921 820 FAECQDIIQRQEQEsvRLKLQHTldVKELQgpgYTSNSSMKPRLLQPASFTRTHSNVPSSQSTASFLSHHSRKTNALKED 899
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 302 iheymATEDLICHLQGDHSVLQKKLNQQENRNRDLGRE---------IENLTKELERYRHFSKSLRPSLNGRRISDPQVF 372
Cdd:pfam15921 900 -----PTRDLKQLLQELRSVINEEPTVQLSKAEDKGRApslgalddrVRDCIIESSLRSDICHSSSNSLQTEGSKSSETC 974
|
410
....*....|....*
gi 544346093 373 SKE-VQTEAVDNEPP 386
Cdd:pfam15921 975 SREpVLLHAGELEDP 989
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
91-348 |
5.60e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 46.71 E-value: 5.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 91 EDKLQAASSQLQVEQNKVTTVTEKLieetkralkskTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQS 170
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESEL-----------KELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 171 LEAIEKDfLKNKLNQDSGKStTALHQENNKIKELSQEVE---------RLKLKLK------DMKAIEDDLMKTED----- 230
Cdd:pfam01576 73 LEEILHE-LESRLEEEEERS-QQLQNEKKKMQQHIQDLEeqldeeeaaRQKLQLEkvtteaKIKKLEEDILLLEDqnskl 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 231 --EYETLERR-------YANERDKAQFLSK----------ELE---------HVKMELAKYKLAEKTETSHEQWLFKRLQ 282
Cdd:pfam01576 151 skERKLLEERiseftsnLAEEEEKAKSLSKlknkheamisDLEerlkkeekgRQELEKAKRKLEGESTDLQEQIAELQAQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 283 EEEAKsGHLSR---EVDALKEKIHEYMATEDL----ICHLQGDHSVLQKKL-------NQQENRNRDLGREIENLTKELE 348
Cdd:pfam01576 231 IAELR-AQLAKkeeELQAALARLEEETAQKNNalkkIRELEAQISELQEDLeseraarNKAEKQRRDLGEELEALKTELE 309
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
32-357 |
5.62e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.50 E-value: 5.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 32 KQLSQELESLKVRIKELEAIESRLEKTEFTL-------KEDLTKLKTLTVMFVDERKTMSEKLKKTEDKLQAASSQLQVE 104
Cdd:TIGR00618 545 EDVYHQLTSERKQRASLKEQMQEIQQSFSILtqcdnrsKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPE 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 105 QNKV-TTVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAIekdflKNKL 183
Cdd:TIGR00618 625 QDLQdVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYW-----KEML 699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 184 NQdsgkSTTALHQENNKIKELSQEVERLKLKLKDMKAiedDLMKTEDEYETLERRYANERDKAQFLSKELEHVKMELAKY 263
Cdd:TIGR00618 700 AQ----CQTLLRELETHIEEYDREFNEIENASSSLGS---DLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTA 772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 264 KLAEKTETSH-EQWLFKRLQEEEAKSGHLSREVDALKEKIHEYMATEDLICHLqgdhsvLQKKLNQQENRNRDLGREIEN 342
Cdd:TIGR00618 773 ALQTGAELSHlAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCET------LVQEEEQFLSRLEEKSATLGE 846
|
330
....*....|....*
gi 544346093 343 LTKELERYRHFSKSL 357
Cdd:TIGR00618 847 ITHQLLKYEECSKQL 861
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
111-312 |
8.38e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.00 E-value: 8.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 111 VTEKLIEEtkralksKTDVEEKMYSVTKERDDlkNKLKAEEEKGNDLLSRVNMLKNRLQSLEaiekdflknklnqdsgks 190
Cdd:COG2433 381 ALEELIEK-------ELPEEEPEAEREKEHEE--RELTEEEEEIRRLEEQVERLEAEVEELE------------------ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 191 ttalhqenNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERRYANerdkaqfLSKELEHVKMELAkyKLAEKTE 270
Cdd:COG2433 434 --------AELEEKDERIERLERELSEARSEERREIRKDREISRLDREIER-------LERELEEERERIE--ELKRKLE 496
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 544346093 271 tsheqwLFKRLQEEEAKSGHLSREV------DALKEKIHEY-MATEDLI 312
Cdd:COG2433 497 ------RLKELWKLEHSGELVPVKVvekftkEAIRRLEEEYgLKEGDVV 539
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
110-351 |
9.26e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.90 E-value: 9.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 110 TVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAiekdfLKNKLNQDSGK 189
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELRE-----KRDELNEKVKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 190 STTALHQENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERRY-------ANER---DKAQFLSKELEHVKME 259
Cdd:COG1340 76 LKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQqtevlspEEEKelvEKIKELEKELEKAKKA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 260 LAKYKLAEKTETSHEQW------LFKRLQEEEAKSGHLSREVDALKEKIHEYMATEDLichLQGDHSVLQKKLNQQENRN 333
Cdd:COG1340 156 LEKNEKLKELRAELKELrkeaeeIHKKIKELAEEAQELHEEMIELYKEADELRKEADE---LHKEIVEAQEKADELHEEI 232
|
250
....*....|....*...
gi 544346093 334 RDLGREIENLTKELERYR 351
Cdd:COG1340 233 IELQKELRELRKELKKLR 250
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
4-347 |
1.34e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 4 EKLEDAFNKS--KQECYSLKCNLEKERmTTKQLSQELESLKVRIKELEAIESRLEKTEfTLKEDLTKLKTLTVMFVDERK 81
Cdd:PTZ00121 1457 KKAEEAKKKAeeAKKADEAKKKAEEAK-KADEAKKKAEEAKKKADEAKKAAEAKKKAD-EAKKAEEAKKADEAKKAEEAK 1534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 82 TmSEKLKKTEDKLQAASSQLQVEQNKVTTVteKLIEETKRALKSKT----------DVEEKMYSVTKERDDLKNKLKAEE 151
Cdd:PTZ00121 1535 K-ADEAKKAEEKKKADELKKAEELKKAEEK--KKAEEAKKAEEDKNmalrkaeeakKAEEARIEEVMKLYEEEKKMKAEE 1611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 152 EKGNDLlSRVNMLKNRLQSLEAIEKDFLKNKLNQDSGKSTTALH-QENNKIK--ELSQEVERLKLKLKDMKAIEDDLMKT 228
Cdd:PTZ00121 1612 AKKAEE-AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKaEEENKIKaaEEAKKAEEDKKKAEEAKKAEEDEKKA 1690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 229 EDEYetleRRYANERDKAQFLSKELEHVKMELAKYKLAEKTETSHEQWLfKRLQEEEAKSGHLSREVDALKEKIHEYMAT 308
Cdd:PTZ00121 1691 AEAL----KKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEA-KKEAEEDKKKAEEAKKDEEEKKKIAHLKKE 1765
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 544346093 309 EDLICH--LQGDHSVLQKKLNQQENRNRdlgREIENLTKEL 347
Cdd:PTZ00121 1766 EEKKAEeiRKEKEAVIEEELDEEDEKRR---MEVDKKIKDI 1803
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
34-277 |
1.55e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 34 LSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKL---KTLTVMFVDERKTMSEKLKKTEDKLQAASSQLQVEQnkvtt 110
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEELEELLAALglpPDLSPEELLELLDRIEELQELLREAEELEEELQLEE----- 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 111 vteklIEETKRALKSKTDVEEkmysvtkeRDDLKNKLKAEEEKgNDLLSRVNMLKNRLQSL----EAIEKDFLKNKLNQD 186
Cdd:COG4717 368 -----LEQEIAALLAEAGVED--------EEELRAALEQAEEY-QELKEELEELEEQLEELlgelEELLEALDEEELEEE 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 187 SGKSTTALHQENNKIKELSQEVERLKLKLKDMKAiEDDLMKTEDEYETLerryanerdKAQFLSKELEHVKMELAKYKLA 266
Cdd:COG4717 434 LEELEEELEELEEELEELREELAELEAELEQLEE-DGELAELLQELEEL---------KAELRELAEEWAALKLALELLE 503
|
250
....*....|.
gi 544346093 267 EKTETSHEQWL 277
Cdd:COG4717 504 EAREEYREERL 514
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-412 |
1.76e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.06 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 2 ALEKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLKVRIKELEAIESRL--EKTEFT-----LKEDLTKLKTLTV 74
Cdd:TIGR02169 358 EYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLqeELQRLSeeladLNAAIAGIEAKIN 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 75 MFVDERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLieetkralkskTDVEEKMYSVTKERDDLKNKLKAEEEKG 154
Cdd:TIGR02169 438 ELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY-----------DRVEKELSKLQRELAEAEAQARASEERV 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 155 NDLLSRVNMLKNRLQ------------------SLEAIEKDFLKNKLNQDSGKSTTA---LHQEN---------NKIKEL 204
Cdd:TIGR02169 507 RGGRAVEEVLKASIQgvhgtvaqlgsvgeryatAIEVAAGNRLNNVVVEDDAVAKEAielLKRRKagratflplNKMRDE 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 205 SQEVERLKLKLKDMKAIedDLMKTEDEYE-----------------------------TLE------------------- 236
Cdd:TIGR02169 587 RRDLSILSEDGVIGFAV--DLVEFDPKYEpafkyvfgdtlvvedieaarrlmgkyrmvTLEgelfeksgamtggsraprg 664
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 237 --RRYANERDKAQFLSKELEHVKMELA--KYKLAEKTETSHEqwLFKRLQEEEAKSGHLSREVDALKEKIHeymATEDLI 312
Cdd:TIGR02169 665 giLFSRSEPAELQRLRERLEGLKRELSslQSELRRIENRLDE--LSQELSDASRKIGEIEKEIEQLEQEEE---KLKERL 739
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 313 CHLQGDHSVLQKKLNQQENRNRDLGREIENLTKELERYRHFSKSLRPSLNGRRISDPQVFSKEVQTEAVDNEppdyKSLI 392
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIE----ARLR 815
|
490 500
....*....|....*....|...
gi 544346093 393 PLERAVINGQL---YEESENQDE 412
Cdd:TIGR02169 816 EIEQKLNRLTLekeYLEKEIQEL 838
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
200-351 |
2.01e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.06 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 200 KIKELSQEVERL---KLKLKDMKAIEDDLMKTEdEYETLERRYANERDKAQfLSKELEHVKMELAKY--KLAEKTETSHE 274
Cdd:TIGR02169 192 IIDEKRQQLERLrreREKAERYQALLKEKREYE-GYELLKEKEALERQKEA-IERQLASLEEELEKLteEISELEKRLEE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 275 qwLFKRLQEEEAKSGHL-SREVDALKEKIHEYMA----TEDLICHLQGDHSVLQKKLNQQENRNRDLGREIENLTKELER 349
Cdd:TIGR02169 270 --IEQLLEELNKKIKDLgEEEQLRVKEKIGELEAeiasLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEE 347
|
..
gi 544346093 350 YR 351
Cdd:TIGR02169 348 ER 349
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
4-264 |
2.56e-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: 44.24 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 4 EKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLTVMFVDERKTM 83
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVL 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 84 SEKLKKTEDKLQaassQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNM 163
Cdd:TIGR04523 474 SRSINKIKQNLE----QKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNK 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 164 LKNRLQSlEAIEKDFLKN-----KLNQDSGKSTTALHQENNKIKELSQEVERL--KLKLKDMKA--IEDDLMKTEDEYET 234
Cdd:TIGR04523 550 DDFELKK-ENLEKEIDEKnkeieELKQTQKSLKKKQEEKQELIDQKEKEKKDLikEIEEKEKKIssLEKELEKAKKENEK 628
|
250 260 270
....*....|....*....|....*....|
gi 544346093 235 LERRYANERDKAQFLSKELEHVKMELAKYK 264
Cdd:TIGR04523 629 LSSIIKNIKSKKNKLKQEVKQIKETIKEIR 658
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2-177 |
2.84e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 2 ALEKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKL------------ 69
Cdd:COG4942 42 ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlralyrlgrqpp 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 70 --------------KTLTVM--FVDERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEKM 133
Cdd:COG4942 122 lalllspedfldavRRLQYLkyLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLL 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 544346093 134 ysvtkerDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAIEKD 177
Cdd:COG4942 202 -------ARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
15-361 |
3.07e-04 |
|
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: 43.73 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 15 QECYSLKCNLEKERMTTKQLSQELESlkvRIKELEAIESRLEKTEFTLKEDLTKLKTLTVMFVDERKTMSEKlKKTEDKL 94
Cdd:pfam07888 48 QAQEAANRQREKEKERYKRDREQWER---QRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEE-KDALLAQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 95 QAASSQLQVE---------QNKVTTVTE--KLIEETKRALKSKTDVEEkmysvtkERDDLKNKLKAEEEKGNDLLSRVNM 163
Cdd:pfam07888 124 RAAHEARIREleediktltQRVLERETEleRMKERAKKAGAQRKEEEA-------ERKQLQAKLQQTEEELRSLSKEFQE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 164 LKNRLQSLEAiEKDFLKNKLNQDSGKSTTAlhqennkikelSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERRYAN-- 241
Cdd:pfam07888 197 LRNSLAQRDT-QVLQLQDTITTLTQKLTTA-----------HRKEAENEALLEELRSLQERLNASERKVEGLGEELSSma 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 242 -ERDKAQflsKELEHVKMELAKY--KLAEKTETSHE---QWlfkrLQEEEAksghLSREVDALKEKIheymatEDLICHL 315
Cdd:pfam07888 265 aQRDRTQ---AELHQARLQAAQLtlQLADASLALREgraRW----AQERET----LQQSAEADKDRI------EKLSAEL 327
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 544346093 316 QGDHSVLQKKLNQQENRNRDLGREIENLTKELERYRHFSKSLRPSL 361
Cdd:pfam07888 328 QRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASL 373
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
62-300 |
3.40e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 62 LKEDLTKLKTLTVMfvderktmsEKLKKteDKLQAASSQLQVEQNKVTTVTEKL------IEETKRalKSKTDVEEKMYS 135
Cdd:PHA02562 155 LVEDLLDISVLSEM---------DKLNK--DKIRELNQQIQTLDMKIDHIQQQIktynknIEEQRK--KNGENIARKQNK 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 136 VTKERDDLKNkLKAEEEKGNDLLSRVNM------------------LKNRLQSLEAIEKDFLKNklnQDSGKSTTALHQE 197
Cdd:PHA02562 222 YDELVEEAKT-IKAEIEELTDELLNLVMdiedpsaalnklntaaakIKSKIEQFQKVIKMYEKG---GVCPTCTQQISEG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 198 NNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEY--------------ETLERRYANERDKAQFLSKELEHVKMELAKY 263
Cdd:PHA02562 298 PDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFneqskkllelknkiSTNKQSLITLVDKAKKVKAAIEELQAEFVDN 377
|
250 260 270
....*....|....*....|....*....|....*..
gi 544346093 264 KLAEKTETSHEQWLFKRLQEEEAKSGHLSREVDALKE 300
Cdd:PHA02562 378 AEELAKLQDELDKIVKTKSELVKEKYHRGIVTDLLKD 414
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
83-247 |
3.94e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 83 MSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKlIEETKRALKS-KTDVEEKMYSVTKERDDLKNKLKAEEEKGN------ 155
Cdd:COG3883 28 LQAELEAAQAELDALQAELEELNEEYNELQAE-LEALQAEIDKlQAEIAEAEAEIEERREELGERARALYRSGGsvsyld 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 156 ---------DLLSRVNMLK----NRLQSLEAIEKDflKNKLNQDSGKSTTALHQENNKIKELSQEVERLKLKLKDMKAIE 222
Cdd:COG3883 107 vllgsesfsDFLDRLSALSkiadADADLLEELKAD--KAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALL 184
|
170 180
....*....|....*....|....*
gi 544346093 223 DDLMKTEDEYETLERRYANERDKAQ 247
Cdd:COG3883 185 AQLSAEEAAAEAQLAELEAELAAAE 209
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
34-377 |
5.37e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 43.14 E-value: 5.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 34 LSQELESLKVRIKELEAIESRLEKTEFTLK------EDLTKLKTlTVMFVDERKTM--------SEKLKKTedklQAASS 99
Cdd:pfam05622 109 LAEEAQALKDEMDILRESSDKVKKLEATVEtykkklEDLGDLRR-QVKLLEERNAEymqrtlqlEEELKKA----NALRG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 100 QLQVEQNKVTTVTEKLIEETKRALKSKTD---VEEKMYSVTK-------ERDDLK---NKLKAEEEKGNDLLSRVNMLKN 166
Cdd:pfam05622 184 QLETYKRQVQELHGKLSEESKKADKLEFEykkLEEKLEALQKekerliiERDTLRetnEELRCAQLQQAELSQADALLSP 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 167 RLQSLEAIEKDFLKNKLnqdsgKSTTALHQENNKIKELSQEvERLKLKLKDMKAIEDDLMKTEDEYETlERRYANERdka 246
Cdd:pfam05622 264 SSDPGDNLAAEIMPAEI-----REKLIRLQHENKMLRLGQE-GSYRERLTELQQLLEDANRRKNELET-QNRLANQR--- 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 247 qflSKELEHvkmelakyklaektetsHEQWLFKRLQEEEAK---SGHLSREVDALKEKIHEYmatedlichlqgdHSVLQ 323
Cdd:pfam05622 334 ---ILELQQ-----------------QVEELQKALQEQGSKaedSSLLKQKLEEHLEKLHEA-------------QSELQ 380
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544346093 324 KKLNQQENR----NRDLGREIENLTKEL-----------ERYRHFS-------KSLRPSLNGRRISDPQVFSKEVQ 377
Cdd:pfam05622 381 KKKEQIEELepkqDSNLAQKIDELQEALrkkdedmkameERYKKYVekaksviKTLDPKQNPASPPEIQALKNQLL 456
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
23-373 |
5.78e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.19 E-value: 5.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 23 NLEKERmttkqLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLTV---MFVD---ERKTMSEKLKKTEDkLQA 96
Cdd:pfam05557 131 NSELEE-----LQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFeiqSQEQdseIVKNSKSELARIPE-LEK 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 97 ASSQLQVEQNKVTTVTEK--LIEETKRALKSKTDVEEKMYS------VTKER----------------------DDLKNK 146
Cdd:pfam05557 205 ELERLREHNKHLNENIENklLLKEEVEDLKRKLEREEKYREeaatleLEKEKleqelqswvklaqdtglnlrspEDLSRR 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 147 LKAEEEKGNDLLSRVNMLKNRLQSLEAIEKDfLKNKLNQDSGKSTtalhQENNKIKELSQEVERLKLKL------KD-MK 219
Cdd:pfam05557 285 IEQLQQREIVLKEENSSLTSSARQLEKARRE-LEQELAQYLKKIE----DLNKKLKRHKALVRRLQRRVllltkeRDgYR 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 220 AI----EDDLMKTEDEYETLERRYANER--DKAQFLSKELEH----VKMELAKYKLAEKTETSHEQWLfkRLQEEEAKSG 289
Cdd:pfam05557 360 AIlesyDKELTMSNYSPQLLERIEEAEDmtQKMQAHNEEMEAqlsvAEEELGGYKQQAQTLERELQAL--RQQESLADPS 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 290 HLSREVDALKEKIHEYMAT-----------EDLICH--LQGD-----HSVLQKKLNQQENRNRDLGREIENLTKELERYR 351
Cdd:pfam05557 438 YSKEEVDSLRRKLETLELErqrlreqknelEMELERrcLQGDydpkkTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLK 517
|
410 420
....*....|....*....|..
gi 544346093 352 HFSKSLRPSLNGRRISDPQVFS 373
Cdd:pfam05557 518 RLLKKLEDDLEQVLRLPETTST 539
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
23-217 |
6.14e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 6.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 23 NLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKtltvmfvDERKTMSEKLKKTEDKLQAASSQLQ 102
Cdd:COG4913 672 ELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLE-------KELEQAEEELDELQDRLEAAEDLAR 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 103 VEQnkvttvtEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVN------------------ML 164
Cdd:COG4913 745 LEL-------RALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNrewpaetadldadleslpEY 817
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 544346093 165 KNRLQSLEAI-----EKDFlKNKLNQDSGKSTTALHQE-NNKIKELSQEVERLKLKLKD 217
Cdd:COG4913 818 LALLDRLEEDglpeyEERF-KELLNENSIEFVADLLSKlRRAIREIKERIDPLNDSLKR 875
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
25-236 |
6.57e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 6.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 25 EKERMTTKQLSQELESLKVRIKELEAIESRLEKTEfTLKEDLTKLKtltvmfvDERKTMSEKLKKTEDKLQAAS---SQL 101
Cdd:PRK02224 568 EEAREEVAELNSKLAELKERIESLERIRTLLAAIA-DAEDEIERLR-------EKREALAELNDERRERLAEKRerkREL 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 102 --QVEQNKVttvtEKLIEETKRALKSKTDVEEKMYSVTKERDDLknklkaeeekgndlLSRVNMLKNRLQSLEAI--EKD 177
Cdd:PRK02224 640 eaEFDEARI----EEAREDKERAEEYLEQVEEKLDELREERDDL--------------QAEIGAVENELEELEELreRRE 701
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544346093 178 FLKNKLnqdsgKSTTALHQENNKIKEL---------SQEVERLKLKLKDMKaiedDLMKTEDEYETLE 236
Cdd:PRK02224 702 ALENRV-----EALEALYDEAEELESMygdlraelrQRNVETLERMLNETF----DLVYQNDAYSHIE 760
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
36-239 |
6.80e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 6.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 36 QELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTltvmfvdERKTMSEKLKKTEDKLQAAssqlqveqnkvttvtEKL 115
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKT-------ELEDLEKEIKRLELEIEEV---------------EAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 116 IEETKRALKSKTDVEEkMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAIEKDfLKNKLNQDSGKSTTALH 195
Cdd:COG1579 75 IKKYEEQLGNVRNNKE-YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAE-LEAELEEKKAELDEELA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 544346093 196 QENNKIKELSQEVERLKlklkdmKAIEDDLMKtedEYETLERRY 239
Cdd:COG1579 153 ELEAELEELEAEREELA------AKIPPELLA---LYERIRKRK 187
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
84-302 |
7.21e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 7.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 84 SEKLKKTEDKLQAASSQLQVEQNKVttvtEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNM 163
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKEL----AALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 164 LKNRLQSLEAIEKDFLKN-KLNQDSGKSTTALHQEN-----NKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLER 237
Cdd:COG4942 95 LRAELEAQKEELAELLRAlYRLGRQPPLALLLSPEDfldavRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544346093 238 RYANERDKAQFLSKELEHVKMELAKY-KLAEKTETSHEQwlfkRLQEEEAKSGHLSREVDALKEKI 302
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLlARLEKELAELAA----ELAELQQEAEELEALIARLEAEA 236
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2-395 |
7.49e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.03 E-value: 7.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 2 ALEKLEDAFNKSKQECYSLKCNLEKERMTTKQL---SQELESLKVRIKELEAIESRLEK---TEFTLKEDLTKLKTLTvm 75
Cdd:TIGR00618 301 AVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHvkqQSSIEEQRRLLQTLHSQEIHIRDaheVATSIREISCQQHTLT-- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 76 fvDERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEEtkRALKSKTDVEEKMYSVTKERDDLK--------NKL 147
Cdd:TIGR00618 379 --QHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAF--RDLQGQLAHAKKQQELQQRYAELCaaaitctaQCE 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 148 KAEEEKGNDLLSRVNMLKNRLQSLEAIEKDFLKNKLNQDSGKSTTALHQENNKIKELSQEVERLKLKLKD-----MKAIE 222
Cdd:TIGR00618 455 KLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGpltrrMQRGE 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 223 DDLMKTEDEYETLERRYANERDKAQFLSKELEHVKMELAK-------YKLAEKTETSHEQWLFKRLQEEEAKSGHLSREV 295
Cdd:TIGR00618 535 QTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSIltqcdnrSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQ 614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 296 DALKEKIHEYMATEDLICHLQGDHSVLQKKLNQqenrnrdLGREIENLTKELERYRHFSKSLRPSLNG-RRISDPQVFSK 374
Cdd:TIGR00618 615 HALLRKLQPEQDLQDVRLHLQQCSQELALKLTA-------LHALQLTLTQERVREHALSIRVLPKELLaSRQLALQKMQS 687
|
410 420
....*....|....*....|.
gi 544346093 375 EVQTEAVDNEPPDYKSLIPLE 395
Cdd:TIGR00618 688 EKEQLTYWKEMLAQCQTLLRE 708
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
51-299 |
8.13e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 8.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 51 IESRLEKTEFTLKEDLTKLKTLTVMFVDERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLIE---ETKRALKSKT 127
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQarsELEQLEEELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 128 DVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAIEKDF--LKNKLNQDSGKSTTALHQENNKIKELS 205
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLeaQIAELQSEIAEREEELKELEEQLESLQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 206 QEVERLKLKLKDMKAIE-----DDLMKTEDEYETLERRYANERDKAQFLSKELEHVKMELAKYKLAEKTETSHEQWLFKR 280
Cdd:COG4372 164 EELAALEQELQALSEAEaeqalDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALE 243
|
250
....*....|....*....
gi 544346093 281 LQEEEAKSGHLSREVDALK 299
Cdd:COG4372 244 LEEDKEELLEEVILKEIEE 262
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
3-233 |
9.12e-04 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 41.55 E-value: 9.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 3 LEKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLKVRIKELeaiESRLEKTEFTLKEDLTKLKTLTVMfVDE--- 79
Cdd:pfam00261 3 MQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLL---EEELERTEERLAEALEKLEEAEKA-ADEser 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 80 -RKTMSEKLKKTEDKLQAASSQLqveqnkvttvtEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLL 158
Cdd:pfam00261 79 gRKVLENRALKDEEKMEILEAQL-----------KEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELE 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544346093 159 SRVNMLKNRLQSLEAIEKdflknKLNQDSGKSTTALHQENNKIKEL---SQEVERLKLKL-KDMKAIEDDLMKTEDEYE 233
Cdd:pfam00261 148 EELKVVGNNLKSLEASEE-----KASEREDKYEEQIRFLTEKLKEAetrAEFAERSVQKLeKEVDRLEDELEAEKEKYK 221
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2-211 |
1.00e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 2 ALEKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTltvmfvdERK 81
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-------EIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 82 TMSEKLKKTEDKL--QAASSQLQVEQNKVTTV--------TEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEE 151
Cdd:COG4942 94 ELRAELEAQKEELaeLLRALYRLGRQPPLALLlspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 152 EKGNDLLSRVNMLKNRLQSLEAiEKDFLKNKLNQDSGKSTTALHQENNKIKELSQEVERL 211
Cdd:COG4942 174 AELEALLAELEEERAALEALKA-ERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
36-370 |
1.11e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 36 QELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLTVMFVDE---------------------RKTMSEKLKKTEDKL 94
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEErddllaeaglddadaeavearREELEDRDEELRDRL 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 95 QAASSQLQVEQNKVTTVTEKL--------------------IEETKRALKSK----TDVEEKMYSVTKERDDLKNKLKAE 150
Cdd:PRK02224 331 EECRVAAQAHNEEAESLREDAddleeraeelreeaaeleseLEEAREAVEDRreeiEELEEEIEELRERFGDAPVDLGNA 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 151 EEKGNDLLSRVNMLKNRLQSLEA----IEKDFLKNKLNQDSGKSTT------------ALHQENNKIKELSQEVERLKLK 214
Cdd:PRK02224 411 EDFLEELREERDELREREAELEAtlrtARERVEEAEALLEAGKCPEcgqpvegsphveTIEEDRERVEELEAELEDLEEE 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 215 ----------LKDMKAIEDDLMKTEDEYETLERRYANERDKAQFLSKELEHVKMElaKYKLAEKTETSHEQWLFKRLQEE 284
Cdd:PRK02224 491 veeveerlerAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER--AAELEAEAEEKREAAAEAEEEAE 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 285 EAKS--GHLSREVDALKEKIHEYMATEDL---ICHLQGDHSVLQKKLNQQENRNrDLGReiENLTKELERYRhfskSLRP 359
Cdd:PRK02224 569 EAREevAELNSKLAELKERIESLERIRTLlaaIADAEDEIERLREKREALAELN-DERR--ERLAEKRERKR----ELEA 641
|
410
....*....|.
gi 544346093 360 SLNGRRISDPQ 370
Cdd:PRK02224 642 EFDEARIEEAR 652
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
32-348 |
1.34e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.93 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 32 KQLSQELESLKVRIK----ELEAIESRLEKTEFTLKEDLTKLKTLTvmfvDERKTMSEKLKKTEDKLQAASSQLQVEQNK 107
Cdd:TIGR04523 36 KQLEKKLKTIKNELKnkekELKNLDKNLNKDEEKINNSNNKIKILE----QQIKDLNDKLKKNKDKINKLNSDLSKINSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 108 VTTVTE---KLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDllsrvnmLKNRLQSLEAIEKDFLKNKLN 184
Cdd:TIGR04523 112 IKNDKEqknKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYND-------LKKQKEELENELNLLEKEKLN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 185 QdsgksttalhqeNNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKAQFLSKELEHVKMELAKYK 264
Cdd:TIGR04523 185 I------------QKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 265 LAEKTETSHEQWLFKRLQEEEaksghlsREVDALKEKIHEymaTEDLICHLQGDHSVLQKKlnQQENRNRDLGREIENLT 344
Cdd:TIGR04523 253 TQLNQLKDEQNKIKKQLSEKQ-------KELEQNNKKIKE---LEKQLNQLKSEISDLNNQ--KEQDWNKELKSELKNQE 320
|
....
gi 544346093 345 KELE 348
Cdd:TIGR04523 321 KKLE 324
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
147-352 |
1.43e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 147 LKAEEEKgnDLLSRVNMLKNRLQSL--EAIEKDFLKNKLNQDsgKSTTALHQENNKIKELSQEVERLKLKLKDMKAIEDD 224
Cdd:COG4913 245 EDAREQI--ELLEPIRELAERYAAAreRLAELEYLRAALRLW--FAQRRLELLEAELEELRAELARLEAELERLEARLDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 225 LmktEDEYETLERRYA-NERDKAQFLSKELEHVKMELAKyklAEKTETSHEQWLfKRLQEEEAKSghlSREVDALKEKIH 303
Cdd:COG4913 321 L---REELDELEAQIRgNGGDRLEQLEREIERLERELEE---RERRRARLEALL-AALGLPLPAS---AEEFAALRAEAA 390
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 544346093 304 EYMATedlichLQGDHSVLQKKLNQQENRNRDLGREIENLTKELERYRH 352
Cdd:COG4913 391 ALLEA------LEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
21-233 |
1.54e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 21 KCNLEKERMTTKQLSQEL-ESLKVRIKELEAIESRLEKteftLKEDLTKLKTltvmfvdERKTMSEKLKKTEDKLQAASS 99
Cdd:COG4372 12 RLSLFGLRPKTGILIAALsEQLRKALFELDKLQEELEQ----LREELEQARE-------ELEQLEEELEQARSELEQLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 100 QLQVEQNKVTTVTEKLI---EETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAIEK 176
Cdd:COG4372 81 ELEELNEQLQAAQAELAqaqEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 544346093 177 DFLKNKLNQDSGKSTTALHQENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYE 233
Cdd:COG4372 161 SLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELA 217
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2-133 |
1.67e-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: 40.68 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 2 ALEKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLKVRI-------------KELEAIESRLEktefTLKEDLTK 68
Cdd:COG1579 32 ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIkkyeeqlgnvrnnKEYEALQKEIE----SLKRRISD 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544346093 69 LKTLTVMFVDERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEKM 133
Cdd:COG1579 108 LEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
46-346 |
2.08e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 41.74 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 46 KELEAIESRLEKTEFT-----LKEDLTKLKTLTVMFVDERKTMSEKLKKTED-------KLQAASSQLQVEQNKVTTVT- 112
Cdd:PTZ00440 940 KEKEKIEKQLSDTKINnlkmqIEKTLEYYDKSKENINGNDGTHLEKLDKEKDewehfksEIDKLNVNYNILNKKIDDLIk 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 113 ---EKLIEETKRALKSK-TDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAIEKDFLKNklnqdsg 188
Cdd:PTZ00440 1020 kqhDDIIELIDKLIKEKgKEIEEKVDQYISLLEKMKTKLSSFHFNIDIKKYKNPKIKEEIKLLEEKVEALLKK------- 1092
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 189 ksttalhqennkIKELSQEVERLKLKLKDMKAIEDDLM-KTEDEYET----LERRYANERDkaqfLSKELEHVKMELAKY 263
Cdd:PTZ00440 1093 ------------IDENKNKLIEIKNKSHEHVVNADKEKnKQTEHYNKkkksLEKIYKQMEK----TLKELENMNLEDITL 1156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 264 KLAEKTETSHEQWLF----KRLQEEEAKSGHLSREVDALKEKIHEYMAteDLICHLQGDHSVLqkKLNQQENRNRDLGRE 339
Cdd:PTZ00440 1157 NEVNEIEIEYERILIdhivEQINNEAKKSKTIMEEIESYKKDIDQVKK--NMSKERNDHLTTF--EYNAYYDKATASYEN 1232
|
....*..
gi 544346093 340 IENLTKE 346
Cdd:PTZ00440 1233 IEELTTE 1239
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
22-243 |
2.19e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 22 CNLEKERMTTKQLSQELESLKVRIKELEAIESRLE---KTEFTLKEDLTKLKTLTVMFVDERKTMSEKLKKTEdKLQAAS 98
Cdd:PRK02224 468 ETIEEDRERVEELEAELEDLEEEVEEVEERLERAEdlvEAEDRIERLEERREDLEELIAERRETIEEKRERAE-ELRERA 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 99 SQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLkNKLKAEEEKGNDLLSRVNMLKNRLQSLEAIE--- 175
Cdd:PRK02224 547 AELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIADAEDEIERLREKREALAELNder 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 176 KDFLKNK------------------LNQDSGKSTTALHQENNKIKELS-----------------QEVERLKLKLKDMKA 220
Cdd:PRK02224 626 RERLAEKrerkreleaefdearieeAREDKERAEEYLEQVEEKLDELReerddlqaeigavenelEELEELRERREALEN 705
|
250 260
....*....|....*....|...
gi 544346093 221 IEDDLMKTEDEYETLERRYANER 243
Cdd:PRK02224 706 RVEALEALYDEAEELESMYGDLR 728
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
8-250 |
2.27e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 8 DAFNKSK--------QECYSLKCNLEKERMTTKQLSQELESL-KVRIKELEAIESRLEKTEFTLKEDLTKLKTLTVMFVD 78
Cdd:PHA02562 169 DKLNKDKirelnqqiQTLDMKIDHIQQQIKTYNKNIEEQRKKnGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVM 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 79 ERKTMSEKLKKTEDKLQAASSQLQ--------VEQNKVT-TVTEKLIEETKRAlkskTDVEEKMYSVTKERDDLKNKLKA 149
Cdd:PHA02562 249 DIEDPSAALNKLNTAAAKIKSKIEqfqkvikmYEKGGVCpTCTQQISEGPDRI----TKIKDKLKELQHSLEKLDTAIDE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 150 EEEKGNDLlsrvNMLKNRLQSleaiekdfLKNKLNQDSGksttALHQENNKIKELSQEVERLKLKLKDmkaIEDDLMKTE 229
Cdd:PHA02562 325 LEEIMDEF----NEQSKKLLE--------LKNKISTNKQ----SLITLVDKAKKVKAAIEELQAEFVD---NAEELAKLQ 385
|
250 260
....*....|....*....|....
gi 544346093 230 DEYETLERRYAN---ERDKAQFLS 250
Cdd:PHA02562 386 DELDKIVKTKSElvkEKYHRGIVT 409
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
138-302 |
2.29e-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: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 138 KERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAiEKDFLKNKLNQDSGKSTTAlhqENNK-IKELSQEVERLKLKLK 216
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLEL-EIEEVEARIKKYEEQLGNV---RNNKeYEALQKEIESLKRRIS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 217 DmkaIEDDLMKTEDEYETLERRYANERDKAQFLSKELEHVKMELAKyKLAEktetsheqwlfkrLQEEEAKsghLSREVD 296
Cdd:COG1579 107 D---LEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE-ELAE-------------LEAELEE---LEAERE 166
|
....*.
gi 544346093 297 ALKEKI 302
Cdd:COG1579 167 ELAAKI 172
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
86-310 |
3.49e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 86 KLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEKmysvTKERDDLKNKLKAEEEKgndLLSRVNMLK 165
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL----QAEIDKLQAEIAEAEAE---IEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 166 NRLQSLeaiekdflknklnQDSGKSTTALHQ--ENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERRYANER 243
Cdd:COG3883 90 ERARAL-------------YRSGGSVSYLDVllGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 544346093 244 DKAQFLSKELEHVKMELAKyKLAEKTETSHEqwLFKRLQEEEAKSGHLSREVDALKEKIHEYMATED 310
Cdd:COG3883 157 AELEALKAELEAAKAELEA-QQAEQEALLAQ--LSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
32-122 |
3.54e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 32 KQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLtvmfVDERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTV 111
Cdd:COG4942 153 EELRADLAELAALRAELEAERAELEALLAELEEERAALEAL----KAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
90
....*....|.
gi 544346093 112 TEKLIEETKRA 122
Cdd:COG4942 229 IARLEAEAAAA 239
|
|
| CortBP2 |
pfam09727 |
Cortactin-binding protein-2; This entry is the first approximately 250 residues of ... |
22-81 |
3.84e-03 |
|
Cortactin-binding protein-2; This entry is the first approximately 250 residues of cortactin-binding protein 2. In addition to being a positional candidate for autism this protein is expressed at highest levels in the brain in humans. The human protein has six associated ankyrin repeat domains pfam00023 towards the C-terminus which act as protein-protein interaction domains.
Pssm-ID: 462860 [Multi-domain] Cd Length: 187 Bit Score: 39.12 E-value: 3.84e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 22 CNLEKERmttKQLSQELESLKVRIKELEAiesRLEKTEFTLKEDLTKLKTLTVMFVDERK 81
Cdd:pfam09727 133 YLLEKER---ERLKQELEQEKAQQKRLEK---ELKKLLEKLEEELSKQKQIALLLVKERK 186
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
86-349 |
3.91e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.39 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 86 KLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEkmysVTKERDDLKNKLKAEEEKGNDLLSRVNMLK 165
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKI----LEQQIKDLNDKLKKNKDKINKLNSDLSKIN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 166 NRLQSleaieKDFLKNKLNQDSGKSTTALHQENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDK 245
Cdd:TIGR04523 110 SEIKN-----DKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 246 AQflsKELEHVKMELAK--YKLAE-KTETSHEQWLFKRLQEEEAKSGHLSREVDALKEKIHEymatedlichLQGDHSVL 322
Cdd:TIGR04523 185 IQ---KNIDKIKNKLLKleLLLSNlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINE----------KTTEISNT 251
|
250 260
....*....|....*....|....*..
gi 544346093 323 QKKLNQQENRNRDLGREIENLTKELER 349
Cdd:TIGR04523 252 QTQLNQLKDEQNKIKKQLSEKQKELEQ 278
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
31-460 |
4.03e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.80 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 31 TKQLSQELESLKVRIKELEAIESRLEKTeftLKEDLTKLKTLTVMFVDERKTMSEKLKKTEDKLQAASSQLQVEQNKVTT 110
Cdd:TIGR00606 446 KEILEKKQEELKFVIKELQQLEGSSDRI---LELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQ 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 111 VTEKLIEETkralksktDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRV-------NMLKNRLQSLEA---IEKDFLK 180
Cdd:TIGR00606 523 EMEQLNHHT--------TTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLlgyfpnkKQLEDWLHSKSKeinQTRDRLA 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 181 nKLNQDSGKSTTALHQENNKIKELSQEVERLKLKLKDM---KAIEDDLMKTEDEYETLERRYANERDKAQFLSKELEHVK 257
Cdd:TIGR00606 595 -KLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVcgsQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLT 673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 258 ME------LAKYKLAEKTETsheQWLFKRLQEEEAKSGHLSREVDALKEKIHEymATEDLICHLQGDHSVLQ---KKLNQ 328
Cdd:TIGR00606 674 DEnqsccpVCQRVFQTEAEL---QEFISDLQSKLRLAPDKLKSTESELKKKEK--RRDEMLGLAPGRQSIIDlkeKEIPE 748
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 329 QENRNRDLGREIENLTKELERYRHFSKSLRPSLNGRRISDPQV-FSKEVQTEAVDNEpPDYKSLIPLERAVINGQLYEES 407
Cdd:TIGR00606 749 LRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVtIMERFQMELKDVE-RKIAQQAAKLQGSDLDRTVQQV 827
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 544346093 408 ENQDEDPNDEGSVLSFKCSQSTPCPVNRKLWIPWMKSKEGHLQNGKMQTKPNA 460
Cdd:TIGR00606 828 NQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNL 880
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
151-347 |
4.88e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 39.88 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 151 EEKGNDLL---SRVNMLKNRLQSLEAIEKDFLK------NKLNQDSGKSTTALHQENNKIKELSQEVERLKLKLKDMKAI 221
Cdd:pfam07888 16 EEGGTDMLlvvPRAELLQNRLEECLQERAELLQaqeaanRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 222 EDDLMKTEDEYETLERRYANERD-------KAQFLSKELEHVKMELAKYKLAEKTEtsheqwlFKRLQEEEAKSGHLSRE 294
Cdd:pfam07888 96 HEELEEKYKELSASSEELSEEKDallaqraAHEARIRELEEDIKTLTQRVLERETE-------LERMKERAKKAGAQRKE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 544346093 295 VDALKEKIHEYM-ATEDLICHLQGDHSVLQKKLNQQENRNRDLGREIENLTKEL 347
Cdd:pfam07888 169 EEAERKQLQAKLqQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKL 222
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
3-228 |
5.65e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.00 E-value: 5.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 3 LEKLEDAFNKSKQecyslkcNLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLTVMFVDERKT 82
Cdd:TIGR04523 470 LKVLSRSINKIKQ-------NLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISD 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 83 MSEKLKKTEDKLQaaSSQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVN 162
Cdd:TIGR04523 543 LEDELNKDDFELK--KENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELE 620
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544346093 163 MLKNRLQSLEAIEK--DFLKNKLNQdsgkSTTALHQENNKIKELSQEVERlklKLKDMKAIEDDLMKT 228
Cdd:TIGR04523 621 KAKKENEKLSSIIKniKSKKNKLKQ----EVKQIKETIKEIRNKWPEIIK---KIKESKTKIDDIIEL 681
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
24-361 |
5.86e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.03 E-value: 5.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 24 LEKERMTTKQLSQELESLKVRIKELEAIESRLEK--------TEFTLKeDLTKLKTLTVMFVDERKTMS----EKLKKTE 91
Cdd:TIGR00606 257 IEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELkmekvfqgTDEQLN-DLYHNHQRTVREKERELVDCqrelEKLNKER 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 92 DKLQAASSQLQVEQNKVTTVTEKLIEETKR--------ALKSKTDVEEKMYSVTKErddLKNKLKAEEEKGNDLLSRVNM 163
Cdd:TIGR00606 336 RLLNQEKTELLVEQGRLQLQADRHQEHIRArdsliqslATRLELDGFERGPFSERQ---IKNFHTLVIERQEDEAKTAAQ 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 164 LKNRLQSLEAIEKDFLKNKLNQDSGKSTT------ALHQENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLER 237
Cdd:TIGR00606 413 LCADLQSKERLKQEQADEIRDEKKGLGRTielkkeILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEK 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 238 RYANERDKAQFLSKELEHVKMELAKYKLAEKTE------TSHEQWLF---KRLQEEEAKSGHLSREVDALKEKIHEYMAT 308
Cdd:TIGR00606 493 NSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEqlnhhtTTRTQMEMltkDKMDKDEQIRKIKSRHSDELTSLLGYFPNK 572
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 544346093 309 EDLICHLqgdHSvLQKKLNQQENRNRDLGREIENLTKELERYRHFSKSLRPSL 361
Cdd:TIGR00606 573 KQLEDWL---HS-KSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQL 621
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
32-288 |
6.05e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.16 E-value: 6.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 32 KQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLTVMFVDERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTV 111
Cdd:pfam01576 99 KKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 112 TEklieetkraLKSK-----TDVEEKMYSVTKERDDL-KNKLKAEEEKGN------DLLSRVNMLKNRLQSLEAiEKDFL 179
Cdd:pfam01576 179 SK---------LKNKheamiSDLEERLKKEEKGRQELeKAKRKLEGESTDlqeqiaELQAQIAELRAQLAKKEE-ELQAA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 180 KNKLNQDSGKSTTALhqenNKIKELSQEVERLklklkdmkaiEDDLmktEDEYETLERRYANERDkaqfLSKELEHVKME 259
Cdd:pfam01576 249 LARLEEETAQKNNAL----KKIRELEAQISEL----------QEDL---ESERAARNKAEKQRRD----LGEELEALKTE 307
|
250 260 270
....*....|....*....|....*....|....*..
gi 544346093 260 L--------AKYKLAEKTETshEQWLFKRLQEEEAKS 288
Cdd:pfam01576 308 LedtldttaAQQELRSKREQ--EVTELKKALEEETRS 342
|
|
| GrpE |
pfam01025 |
GrpE; |
189-247 |
6.17e-03 |
|
GrpE;
Pssm-ID: 425996 [Multi-domain] Cd Length: 165 Bit Score: 37.97 E-value: 6.17e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 544346093 189 KSTTALHQENNKIKELSQEVERLKLKLKDMKaieDDLMKTEDEYETLERRYANERDKAQ 247
Cdd:pfam01025 1 EEKKNEEALTDEIESLEEEIEELEKKIEELK---EKLLRALAEFENLRKRTEKEKEEAK 56
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
33-273 |
6.22e-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: 39.67 E-value: 6.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 33 QLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLktltvmfvderktmSEKLKKTEDKLQAASSQLQVEQNKVTTvT 112
Cdd:pfam19220 38 AILRELPQAKSRLLELEALLAQERAAYGKLRRELAGL--------------TRRLSAAEGELEELVARLAKLEAALRE-A 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 113 EKLIEETKRALKSKTDVEEkmysvtkerdDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEA--IEKDFLKNKLNQDSGKS 190
Cdd:pfam19220 103 EAAKEELRIELRDKTAQAE----------ALERQLAAETEQNRALEEENKALREEAQAAEKalQRAEGELATARERLALL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 191 TTALHQENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYET--LERRYANERDKAQFlskELEHVKMELAKYKLAEK 268
Cdd:pfam19220 173 EQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGqlAAEQAERERAEAQL---EEAVEAHRAERASLRMK 249
|
....*
gi 544346093 269 TETSH 273
Cdd:pfam19220 250 LEALT 254
|
|
| MPS2 |
pfam17060 |
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component ... |
156-303 |
7.19e-03 |
|
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component of the spindle pole body (SPB) required for the insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. It seems that Mps2-Spc24 interaction may contribute to the localization of Spc24 and other kinetochore components to the inner plaque of the SPB.
Pssm-ID: 407228 [Multi-domain] Cd Length: 340 Bit Score: 39.19 E-value: 7.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 156 DLLSRVNMLKNRLQSleAIEKDFLKNKLNQDSGKSTTalhQENNKIKELSQEVERLKLKLKDMkaiEDDLMKTEDEYETL 235
Cdd:pfam17060 109 DVKSSPRSEADSLGT--PIKVDLLRNLKPQESPETPR---RINRKYKSLELRVESMKDELEFK---DETIMEKDRELTEL 180
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544346093 236 ERRYANERDKAQFLSKELEHVKME-LAKYKLAEKTETSHE---QWLFKRLQEEEAKSGHLSREVDALKEKIH 303
Cdd:pfam17060 181 TSTISKLKDKYDFLSREFEFYKQHhEHGGNNSIKTATKHEfiiSELKRKLQEQNRLIRILQEQIQFDPGALH 252
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
13-152 |
7.58e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 39.66 E-value: 7.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 13 SKQECYSLKcnLEKERMTT--KQLSQELESLKVRIKELEaiesrleKTEFTLKEDLTKLKTLTVMFVDERKTMSEKLKKT 90
Cdd:pfam05911 686 LKEEFEQLK--SEKENLEVelASCTENLESTKSQLQESE-------QLIAELRSELASLKESNSLAETQLKCMAESYEDL 756
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544346093 91 EDKLQAASSQLQVEQNKVTTVTEKLIEETK---RALKSKTDVEEKMYSVTKER------DDLKNKLKAEEE 152
Cdd:pfam05911 757 ETRLTELEAELNELRQKFEALEVELEEEKNcheELEAKCLELQEQLERNEKKEssncdaDQEDKKLQQEKE 827
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
37-214 |
8.76e-03 |
|
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: 38.85 E-value: 8.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 37 ELESLKV----RIKELEAIESRLEKTEFTLKEDLTKLKtltvmfvDERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTVT 112
Cdd:smart00787 127 RLEAKKMwyewRMKLLEGLKEGLDENLEGLKEDYKLLM-------KELELLNSIKPKLRDRKDALEEELRQLKQLEDELE 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 113 EKLIEETKRA-LKSKTDVEEKMYSVtKERDDLKNKLKAEEEKGNDLlsrVNMLKNRLQSLEAIEKDFLKNKlnqdsgkst 191
Cdd:smart00787 200 DCDPTELDRAkEKLKKLLQEIMIKV-KKLEELEEELQELESKIEDL---TNKKSELNTEIAEAEKKLEQCR--------- 266
|
170 180
....*....|....*....|...
gi 544346093 192 talHQENNKIKELSQEVERLKLK 214
Cdd:smart00787 267 ---GFTFKEIEKLKEQLKLLQSL 286
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
117-199 |
9.52e-03 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 39.42 E-value: 9.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 117 EETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKgnDLLSRVNMLKNRLQS--LEAIeKDFLKnKLNQDSGKSTTAL 194
Cdd:PTZ00400 561 EKKKELVDAKNEAETLIYSVEKQLSDLKDKISDADKD--ELKQKITKLRSTLSSedVDSI-KDKTK-QLQEASWKISQQA 636
|
....*
gi 544346093 195 HQENN 199
Cdd:PTZ00400 637 YKQGN 641
|
|
| |
