|
Name |
Accession |
Description |
Interval |
E-value |
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
1-249 |
2.16e-132 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 397.86 E-value: 2.16e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 1 MTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKSLTERNTFLEEQLEHIREEVSQLRHDLLMKDELLQFYTSAAEE 80
Cdd:pfam04849 61 MTKTYNDIEAVTRLLEEKERDLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEILQLRHELSKKDDLLQIYSNDAEE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 81 SDGESASTTPIHRNDTSFTVPNYLPLDSLQKKLKDLEEENIVLRSEANHLETETISYEEKEQQLVNDCVKELRDANIQIS 160
Cdd:pfam04849 141 SETESSCSTPLRRNESFSSLHGCVQLDALQEKLRGLEEENLKLRSEASHLKTETDTYEEKEQQLMSDCVEQLSEANQQMA 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 161 TIAEELAKKTEDASRQQEEITHLLSQIVDLQKKAKSYALENEELTQHLGAAKDAQRALTAELRELEDKYAECMEMLHEAQ 240
Cdd:pfam04849 221 ELSEELARKMEENLRQQEEITSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLGMLHEAQ 300
|
....*....
gi 688589783 241 EELKNFRNK 249
Cdd:pfam04849 301 EELKELRKK 309
|
|
| Milton |
pfam12448 |
Kinesin associated protein; This domain family is found in eukaryotes, and is typically ... |
311-477 |
1.70e-70 |
|
Kinesin associated protein; This domain family is found in eukaryotes, and is typically between 143 and 173 amino acids in length. The family is found in association with pfam04849. This family is a region of the protein milton. Milton recruits the heavy chain of kinesin to mitochondria to allow the motor movement function of kinesin.
Pssm-ID: 463588 Cd Length: 171 Bit Score: 229.86 E-value: 1.70e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 311 RQRSMGPSPMNIPGSNQTSSMNSRRSSCMSTPRSSMYGGDG--VEIDNRTNSLLLETQSPQDGSNDSNRKPGTPGTPGSH 388
Cdd:pfam12448 1 RQRSLTPSPMNIPGSNQSSSLTSMRSSSSSTPRSSYYGGDGssISLDNRTNSILSETSSSQDSGYDRPKKPGTPGTPGAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 389 DLQAALRRLSLRRDNYLSERRFFEEERERKLNALAedKSQFYEDSEdGGGPLTPADSIMSLGLNSV-----FSIYSSRSY 463
Cdd:pfam12448 81 DLEAALRRLSLRRQNYLSERRFFEEERERKLLALA--GTYNYDEGE-HGGSLTPNDSIMSLGSNHSgssshSSGFSSRSY 157
|
170
....*....|....
gi 688589783 464 LPEKLQIVKPLEGS 477
Cdd:pfam12448 158 LPEKLQIVKPLEGS 171
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
8-249 |
9.93e-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: 9.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 8 IDAVTRLLEEKERDLELAARIGQSLLKKNKSLTERNTFLEEQLEHIREEVSQLRHDLLmkdELLQFYTSAAEESDGESAS 87
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT---ELEAEIEELEERLEEAEEE 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 88 TTPIHRNdtsftvpnylpLDSLQKKLKDLEEENIVLRSEANHLETETISYEEKEQQL---VNDCVKELRDANIQISTIAE 164
Cdd:TIGR02168 777 LAEAEAE-----------IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLrerLESLERRIAATERRLEDLEE 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 165 ELAKKTEDASRQQEEITHLLSQIVDLQKKAKSYALENEELTQHLGAAKDAQRALTAELRELEDK-------YAECMEMLH 237
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKrselrreLEELREKLA 925
|
250
....*....|..
gi 688589783 238 EAQEELKNFRNK 249
Cdd:TIGR02168 926 QLELRLEGLEVR 937
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
106-245 |
1.63e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 106 LDSLQKKLKDLEEENIVLRSEANHLETEtisYEEKEQqlvndcvkELRDANIQISTIAEELAKKTEDASRQQEEITHLLS 185
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAE---LEELRL--------ELEELELELEEAQAEEYELLAELARLEQDIARLEE 309
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 186 QIVDLQKKAKSYALENEELTQHLGAAKDAQRALTAELRELEDKYAECMEMLHEAQEELKN 245
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
6-244 |
1.69e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 6 NDIDAVTRLLEEKERDLELA----ARIGQSLLKKNKSLTERNTFLEEQLEHIREEVSQLRHDLLMKDELLQfytsAAEES 81
Cdd:COG1196 246 AELEELEAELEELEAELAELeaelEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE----RLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 82 DGEsasttpihrndtsftvpnylpLDSLQKKLKDLEEENIVLRSEANHLETETISYEEKEQQLvndcVKELRDANIQIST 161
Cdd:COG1196 322 EEE---------------------LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA----EEALLEAEAELAE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 162 IAEELAKKTEDASRQQEEITHLLSQIVDLQKKAKSYALENEELTQHLGAAKDAQRALTAELRELEDKYAECMEMLHEAQE 241
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
...
gi 688589783 242 ELK 244
Cdd:COG1196 457 EEE 459
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
8-249 |
3.66e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.84 E-value: 3.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 8 IDAVTRLLEEKE-RDLELAARIgQSLLKKNKSLTERNTFLEEQLEHIREEVSQLRHDLLMKDELLQFYTSAAEESDGESA 86
Cdd:TIGR02168 262 LQELEEKLEELRlEVSELEEEI-EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELA 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 87 STTPIhrndtsftvpnylpLDSLQKKLKDLEEENIVLRSEANHLETETISYEEKEQQL---VNDCVKELRDANIQISTIA 163
Cdd:TIGR02168 341 ELEEK--------------LEELKEELESLEAELEELEAELEELESRLEELEEQLETLrskVAQLELQIASLNNEIERLE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 164 EELAKKTEDASRQQEEITHLLSQIVDLQKKAKSYALenEELTQHLGAAKDAQRALTAELRELEDKYAECMEMLHEAQEEL 243
Cdd:TIGR02168 407 ARLERLEDRRERLQQEIEELLKKLEEAELKELQAEL--EELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL 484
|
....*.
gi 688589783 244 KNFRNK 249
Cdd:TIGR02168 485 AQLQAR 490
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
13-244 |
5.39e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 5.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 13 RLLEEKERDLELAARIGQsLLKKNKSLTERNTFLEEQLEHIREEVSQLRHDLLMKDELLQFYTSAAEESDGEsasttpih 92
Cdd:COG1196 282 ELEEAQAEEYELLAELAR-LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE-------- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 93 rndtsftvpnylpLDSLQKKLKDLEEENIVLRSEANHLETETISYEEKEQQLVND---CVKELRDANIQISTIAEELAKK 169
Cdd:COG1196 353 -------------LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAaaeLAAQLEELEEAEEALLERLERL 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688589783 170 TEDASRQQEEITHLLSQIVDLQKKAKSYALENEELTQHLGAAKDAQRALTAELRELEDKYAECMEMLHEAQEELK 244
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
15-244 |
1.02e-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: 58.96 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 15 LEEKERDLELAARIGQSLLKKNKSLTERNTFLEEQLEHIREEVSQLRHDLLMKDELLQFYTSAAEESDGESASTTPIHRN 94
Cdd:pfam05483 515 LKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILEN 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 95 DTsftvpNYL--PLDSLQKKLKDLEEENIVLRSEA--------------NHLETETISYEEKEQQLVNDCVKELRDANIQ 158
Cdd:pfam05483 595 KC-----NNLkkQIENKNKNIEELHQENKALKKKGsaenkqlnayeikvNKLELELASAKQKFEEIIDNYQKEIEDKKIS 669
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 159 ISTIAEELAKK---TEDASRQQEEI----THLLSQIVDLQKKAK-SYALENEELTQHLGAAKD-------AQRALTAELR 223
Cdd:pfam05483 670 EEKLLEEVEKAkaiADEAVKLQKEIdkrcQHKIAEMVALMEKHKhQYDKIIEERDSELGLYKNkeqeqssAKAALEIELS 749
|
250 260
....*....|....*....|....
gi 688589783 224 ELEDKYAEC---MEMLHEAQEELK 244
Cdd:pfam05483 750 NIKAELLSLkkqLEIEKEEKEKLK 773
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3-295 |
2.22e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 3 KTYNDIDAVTRLLEEKERDLELaarigqslLKKNKSLTERNTFLEEQLEHIREEVSQLRhdLLMKDELLQFYTSAAEESD 82
Cdd:TIGR02168 183 RTRENLDRLEDILNELERQLKS--------LERQAEKAERYKELKAELRELELALLVLR--LEELREELEELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 83 GEsasttpihrndtsftvpnylpLDSLQKKLKDLEEENIVLRSEANHLETEtisyEEKEQQLVNDCVKELRDANIQISTI 162
Cdd:TIGR02168 253 EE---------------------LEELTAELQELEEKLEELRLEVSELEEE----IEELQKELYALANEISRLEQQKQIL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 163 AEELAKKTEDASRQQEEITHLLSQIVDLQKKAKSYALENEELTQHLGAAKDAQRALTAELRELEDKyaecmemLHEAQEE 242
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESR-------LEELEEQ 380
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 688589783 243 LKNFRNKtvplstprrFHSLGLfPMDSLAAEIEgtmRKEIQMSDPDVEEQRLQ 295
Cdd:TIGR02168 381 LETLRSK---------VAQLEL-QIASLNNEIE---RLEARLERLEDRRERLQ 420
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
15-249 |
1.24e-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: 55.84 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 15 LEEKERDLELAARIGQslLKKNKSlterntFLEEQLEHIREEVSQLR---------HDLLMKD-ELLQFYTSAAEESDGE 84
Cdd:TIGR02169 670 RSEPAELQRLRERLEG--LKRELS------SLQSELRRIENRLDELSqelsdasrkIGEIEKEiEQLEQEEEKLKERLEE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 85 SASTtpihrndtsftvpnylpLDSLQKKLKDLEEENIVLRSEANHLETETISYEEKE---------------QQLVNDCV 149
Cdd:TIGR02169 742 LEED-----------------LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALndlearlshsripeiQAELSKLE 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 150 KELRDANIQISTIAEELAKKTEDASRQQEEITHLLSQIVDLQKKAKSYALENEELTQHLGAAKDAQRALTAELRELEDKY 229
Cdd:TIGR02169 805 EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL 884
|
250 260
....*....|....*....|
gi 688589783 230 AECMEMLHEAQEELKNFRNK 249
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERK 904
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
15-202 |
1.62e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 15 LEEKERDLELAARIGQSLLKKNKSLTErntfLEEQLEHIREEVSQLRHDLLMKDELLQFYTSAAEESDGESASTTPIHRn 94
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEE----LEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPER- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 95 dtsftvpnylpLDSLQKKLKDLEEenivLRSEANHLETETISYEEKEQQLVNDC----VKELRDANIQISTIAEELAKKT 170
Cdd:COG4717 148 -----------LEELEERLEELRE----LEEELEELEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELE 212
|
170 180 190
....*....|....*....|....*....|..
gi 688589783 171 EDASRQQEEITHLLSQIVDLQKKAKSYALENE 202
Cdd:COG4717 213 EELEEAQEELEELEEELEQLENELEAAALEER 244
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
16-243 |
2.61e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 16 EEKERDLELAARIGQSLLKKNKSLTERNTFLEEQLEHIREEVSQLRHDLlmkdELLQFYTSAAEESdgesasttpihrnd 95
Cdd:COG1196 221 ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL----EELRLELEELELE-------------- 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 96 tsftvpnylpLDSLQKKLKDLEEENIVLRSEANHLETETISYEEKEQQLvndcVKELRDANIQISTIAEELAKKTEDASR 175
Cdd:COG1196 283 ----------LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL----EEELAELEEELEELEEELEELEEELEE 348
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688589783 176 QQEEITHLLSQIVDLQKKAKSYALENEELTQHLGAAKDAQRALTAELRELEDKYAECMEMLHEAQEEL 243
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
106-285 |
3.07e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 53.37 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 106 LDSLQKKLKDLEEENIVLRSEANHLETEtISYEEKEQQLVNDCVKE----LRDANIQISTIAEELAKKTEDASRQQEEIT 181
Cdd:COG4372 40 LDKLQEELEQLREELEQAREELEQLEEE-LEQARSELEQLEEELEElneqLQAAQAELAQAQEELESLQEEAEELQEELE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 182 HLLSQIVDLQKKAKSYALENEELTQHLGAAKDAQRALTAELRELEDKYAECME-----MLHEAQEELKNFRNKTVPLSTP 256
Cdd:COG4372 119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQelqalSEAEAEQALDELLKEANRNAEK 198
|
170 180
....*....|....*....|....*....
gi 688589783 257 RRFHSLGLFPMDSLAAEIEGTMRKEIQMS 285
Cdd:COG4372 199 EEELAEAEKLIESLPRELAEELLEAKDSL 227
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
3-293 |
4.06e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 4.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 3 KTYNDIDAvtrLLEEKER-DLELAARIGQSLLKKNKSLTERNTFLEEQLEHIREEVSQLRHDLLMKDELLQFYTSAAEES 81
Cdd:PRK03918 362 ELYEEAKA---KKEELERlKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKC 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 82 DGESASTTPIHRND--TSFTvpnyLPLDSLQKKLKDLEEENIVLRSEANHLETETIsyEEKEQQLVNDCVKELRDANIQI 159
Cdd:PRK03918 439 PVCGRELTEEHRKEllEEYT----AELKRIEKELKEIEEKERKLRKELRELEKVLK--KESELIKLKELAEQLKELEEKL 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 160 STI-AEELAKKTEDASRQQEEITHLLSQIVDLQKKAKSYALENEELTQHLGAAKDAQRALTAELRELEDKYAECMEMLHE 238
Cdd:PRK03918 513 KKYnLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEE 592
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 688589783 239 AQEELKNFRNKTVPL-STPRRFHSLgLFPMDSLAAEIEGTmRKEIQMSDPDVEEQR 293
Cdd:PRK03918 593 RLKELEPFYNEYLELkDAEKELERE-EKELKKLEEELDKA-FEELAETEKRLEELR 646
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
6-230 |
4.10e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 4.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 6 NDIDAVTRLLEEKERDLELAARIGQSLLKKNKSLTERNTFLEEQLEHIREEVSQLRHDLLMKDELLQFYTSAAEESDGES 85
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 86 ASttpiHRNDTsftvpnylpLDSLQKKLKDLEEENIVLRSEANHLETETISYEEKEQQLvndcvKELRDANIQISTIAEE 165
Cdd:COG1196 382 EE----LAEEL---------LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE-----EALAELEEEEEEEEEA 443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688589783 166 LAKKTEDASRQQEEITHLLSQIVDLQKKAKSYALENEELTQHLGAAKDAQRALTAELRELEDKYA 230
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
12-251 |
5.10e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.49 E-value: 5.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 12 TRLLEEKERDLELAARIGQSLLKKNKSLTERNTFLEEQLEHIrEEVSQLrhdllmKDELLQFYTSAAEESDGEsasttpi 91
Cdd:TIGR04523 362 QRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQ-EKLNQQ------KDEQIKKLQQEKELLEKE------- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 92 HRNDTSFTVPNylpldslQKKLKDLEEENIVLRSEANHLETETisyEEKEQQLvndcvKELrdaNIQISTIAEELAKKTE 171
Cdd:TIGR04523 428 IERLKETIIKN-------NSEIKDLTNQDSVKELIIKNLDNTR---ESLETQL-----KVL---SRSINKIKQNLEQKQK 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 172 DASRQQEEITHLLSQIVDLQKKAKsyaleneELTQHLGAAKDAQRALTAELRELEDKYAECMEMLHEAQEELKNFRNKTV 251
Cdd:TIGR04523 490 ELKSKEKELKKLNEEKKELEEKVK-------DLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKE 562
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
106-251 |
5.65e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.52 E-value: 5.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 106 LDSLQKKLKDLEEENIVLRSEANHLETETISYEEKEQQLVndcvKELRDANIQISTIAEELAKKTEDASRQQEEITHLLS 185
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLR----KELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 186 QIVDLQKKAKSYALENEELTQHLGAAKD-----------AQRALTA---ELRELEDKYAECMEMLHEAQEELKNFRNKTV 251
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAeieeleaqieqLKEELKAlreALDELRAELTLLNEEAANLRERLESLERRIA 834
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6-245 |
7.41e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.14 E-value: 7.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 6 NDIDAVTRLLEEKERDLELAARIGQSLLKKNKSLTERNTFLEEQLEHIREEVSQLRHDLLMKDELLQfytsaaeESDGES 85
Cdd:TIGR02168 712 EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA-------EAEAEI 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 86 ASTTPIHRNDTSFTVPNYLPLDSLQKKLKDLEEENIVLRSEANHLETETISYE----------EKEQQLVNDCVKELRDA 155
Cdd:TIGR02168 785 EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATErrledleeqiEELSEDIESLAAEIEEL 864
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 156 NIQISTIAEELAKKTEDASRQQEEITHLLSQIVDLQKKAKSYALEN-------EELTQHLGAAKDAQRALTAELRELEDK 228
Cdd:TIGR02168 865 EELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRselrrelEELREKLAQLELRLEGLEVRIDNLQER 944
|
250
....*....|....*..
gi 688589783 229 YAECMEMLHEAQEELKN 245
Cdd:TIGR02168 945 LSEEYSLTLEEAEALEN 961
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
37-283 |
7.41e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.14 E-value: 7.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 37 KSLTERNTFLEEQLEHIREEVSQLRHDL-LMKDELLQFYTSAAEESDGESASTTPIHRNDTsfTVPNYLP-LDSLQKKLK 114
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELeELEEELEQLRKELEELSRQISALRKDLARLEA--EVEQLEErIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 115 DLEEENIVLRSEANHLETETISYEEKEQQLVndcvKELRDANIQISTIAEELAKKTEDASRQQEEITHLLSQIVDLQKKA 194
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELE----AQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 195 KSYALENEELTQHLGAAKDAQRALTAELRELEdkyaecmEMLHEAQEELKNFRNKTVPLSTPRRFHSLGLFPMDSLAAEI 274
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELE-------ELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
|
....*....
gi 688589783 275 EGTMRKEIQ 283
Cdd:TIGR02168 907 ESKRSELRR 915
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
106-267 |
8.20e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 8.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 106 LDSLQKKLKDLEEENIVLRSEANHLEtetisyeeKEQQLVNDcVKELRDANIQISTIAEELakktEDASRQQEEITHLLS 185
Cdd:COG4717 97 LEELEEELEELEAELEELREELEKLE--------KLLQLLPL-YQELEALEAELAELPERL----EELEERLEELRELEE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 186 QIVDLQKKAKSYALENEELTQHLGAAKDAQ--------RALTAELRELEDKYAECMEMLHEAQEELKNFRNKTVPLSTPR 257
Cdd:COG4717 164 ELEELEAELAELQEELEELLEQLSLATEEElqdlaeelEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
170
....*....|
gi 688589783 258 RFHSLGLFPM 267
Cdd:COG4717 244 RLKEARLLLL 253
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2-249 |
1.69e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 2 TKTYN--DIDAVTRLLEE-KERDLELAARIG--QSLLKKNKSLTERNTFLEEQLEHIREEVSQLrhdllmKDELLQFYTS 76
Cdd:PRK03918 512 LKKYNleELEKKAEEYEKlKEKLIKLKGEIKslKKELEKLEELKKKLAELEKKLDELEEELAEL------LKELEELGFE 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 77 AAEESDGESASTTPIHRndtsftvpNYLPLDSLQKKLKDLEEEnivLRSEAnhletETISYEEKEQQLVNDCVKELRDan 156
Cdd:PRK03918 586 SVEELEERLKELEPFYN--------EYLELKDAEKELEREEKE---LKKLE-----EELDKAFEELAETEKRLEELRK-- 647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 157 iQIstiaEELAKK--TEDASRQQEEITHLLSQIVDLQKkaksyalENEELTQHLGAAKDAQRALTAELRELEdKYAECME 234
Cdd:PRK03918 648 -EL----EELEKKysEEEYEELREEYLELSRELAGLRA-------ELEELEKRREEIKKTLEKLKEELEERE-KAKKELE 714
|
250
....*....|....*
gi 688589783 235 MLHEAQEELKNFRNK 249
Cdd:PRK03918 715 KLEKALERVEELREK 729
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
106-249 |
1.32e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 106 LDSLQKKLKDLEEENIVLRSEANHLETETISYEEkeqqlvndcvkELRDANIQISTIAEELAKKTEDASRQQEEITHLLS 185
Cdd:COG4372 33 LRKALFELDKLQEELEQLREELEQAREELEQLEE-----------ELEQARSELEQLEEELEELNEQLQAAQAELAQAQE 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688589783 186 QIVDLQKKAKSYALENEELTQHLGAAKDAQRALTAELRELEDKYAECMEMLHEAQEELKNFRNK 249
Cdd:COG4372 102 ELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
5-242 |
1.69e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.60 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 5 YNDIDAVTRLLEE-KERDLELaarigQSLLKKNKSltERNTfLEEQLEHIREEVSQLRHdllMKDELLQFYTSAAEESD- 82
Cdd:COG1340 14 EEKIEELREEIEElKEKRDEL-----NEELKELAE--KRDE-LNAQVKELREEAQELRE---KRDELNEKVKELKEERDe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 83 -----GESASTTPIHRNDTSFTVPNYLPLDSLQKKLKDLE------------EENIVLRSEAnhLETEtisYEEKEQQL- 144
Cdd:COG1340 83 lneklNELREELDELRKELAELNKAGGSIDKLRKEIERLEwrqqtevlspeeEKELVEKIKE--LEKE---LEKAKKALe 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 145 ----VNDCVKELRDANIQISTIAEELAKKTEDASRQQEEITHLLSQIVDLQKKAKSYALENEELTQHLGAAKDAQRALTA 220
Cdd:COG1340 158 knekLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQK 237
|
250 260
....*....|....*....|..
gi 688589783 221 ELRELEDKYAECMEMLHEAQEE 242
Cdd:COG1340 238 ELRELRKELKKLRKKQRALKRE 259
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
3-249 |
1.90e-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: 48.48 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 3 KTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKSLTERNTFL---EEQLE----HIREEVSQLRHDLLMKDELLQfYT 75
Cdd:TIGR04523 479 KIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLkekIEKLEsekkEKESKISDLEDELNKDDFELK-KE 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 76 SAAEESDGESASTTPIHRNDTSFTVPNylplDSLQKKLKDLEEENIVLRSEanhLETETISYEEKEQQLvNDCVKELRDA 155
Cdd:TIGR04523 558 NLEKEIDEKNKEIEELKQTQKSLKKKQ----EEKQELIDQKEKEKKDLIKE---IEEKEKKISSLEKEL-EKAKKENEKL 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 156 NIQISTIAEELAKKTEDASRQQEEI-----------------THLLSQIVDLQKKAKSYAL--ENEELTQHLGaakdaqr 216
Cdd:TIGR04523 630 SSIIKNIKSKKNKLKQEVKQIKETIkeirnkwpeiikkikesKTKIDDIIELMKDWLKELSlhYKKYITRMIR------- 702
|
250 260 270
....*....|....*....|....*....|....*.
gi 688589783 217 alTAELRELEDKYAECMEMLHEAQE---ELKNFRNK 249
Cdd:TIGR04523 703 --IKDLPKLEEKYKEIEKELKKLDEfskELENIIKN 736
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
18-249 |
2.00e-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: 48.48 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 18 KERDLELAARIGQSLLKKNKSLT-------ERNTFLEEQLEHIREEVSQLRHDLL-MKDELLQFYTSAAEESDGESASTT 89
Cdd:TIGR04523 195 KLLKLELLLSNLKKKIQKNKSLEsqiselkKQNNQLKDNIEKKQQEINEKTTEISnTQTQLNQLKDEQNKIKKQLSEKQK 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 90 PIHRNDTSftvpnylpLDSLQKKLKDLEEENIVLRSEA-----NHLETETISYEEKEQQLVNDCV---KELRDANIQIST 161
Cdd:TIGR04523 275 ELEQNNKK--------IKELEKQLNQLKSEISDLNNQKeqdwnKELKSELKNQEKKLEEIQNQISqnnKIISQLNEQISQ 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 162 IAEELAKKTEDASRQQEEITHLLSQIVDLQKKAKSYALENEELT-------QHLGAAKDAQRALTAELRELEDKYaecmE 234
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLEsqindleSKIQNQEKLNQQKDEQIKKLQQEK----E 422
|
250
....*....|....*
gi 688589783 235 MLHEAQEELKNFRNK 249
Cdd:TIGR04523 423 LLEKEIERLKETIIK 437
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
3-249 |
2.92e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 3 KTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKSLTERNTFLEEQLEHIREEVSQLRHDLLMKDELLQFytsaAEESD 82
Cdd:PRK03918 300 EFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAK----KEELE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 83 GESASTTPihrndtsftvpnyLPLDSLQKKLKDLEEENIVLRSEANHLETETISYEEKEQQLvNDCVKELRDA------- 155
Cdd:PRK03918 376 RLKKRLTG-------------LTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL-KKAIEELKKAkgkcpvc 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 156 ----------------NIQISTIAEELAK---KTEDASRQQEEITHLLS-------------QIVDLQKKAKSYALEN-- 201
Cdd:PRK03918 442 grelteehrkelleeyTAELKRIEKELKEieeKERKLRKELRELEKVLKkeseliklkelaeQLKELEEKLKKYNLEEle 521
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 688589783 202 ------EELTQHLGAAKDAQRALTAELR---ELEDKYAECMEMLHEAQEELKNFRNK 249
Cdd:PRK03918 522 kkaeeyEKLKEKLIKLKGEIKSLKKELEkleELKKKLAELEKKLDELEEELAELLKE 578
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
3-304 |
4.36e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 3 KTYNDIDAVTRLLEEKERDLElaarigqSLLKKNKSLTERNTFLEEQLEHIREEVSQLRHDL-----LMKD-----ELLQ 72
Cdd:PRK03918 228 KEVKELEELKEEIEELEKELE-------SLEGSKRKLEEKIRELEERIEELKKEIEELEEKVkelkeLKEKaeeyiKLSE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 73 FYTSAAEESDgESASTTPIHRNDTSFTVPNYLPLDSLQKKLKDLEEENIVLRSEANHLETETISYEEKEQQLVNdcVKEL 152
Cdd:PRK03918 301 FYEEYLDELR-EIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEE--LERL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 153 RdANIQISTIaEELAKKTEDASRQQEEITHLLSQIVD----LQKKAKSY--ALE------------NEELTQHlgAAKDA 214
Cdd:PRK03918 378 K-KRLTGLTP-EKLEKELEELEKAKEEIEEEISKITArigeLKKEIKELkkAIEelkkakgkcpvcGRELTEE--HRKEL 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 215 QRALTAELRELEDKYAECMEMLHEAQEELKNFRNKtvpLSTPRRfhslgLFPMDSLAAEIEGTmrkEIQMSDPDVEEQRl 294
Cdd:PRK03918 454 LEEYTAELKRIEKELKEIEEKERKLRKELRELEKV---LKKESE-----LIKLKELAEQLKEL---EEKLKKYNLEELE- 521
|
330
....*....|
gi 688589783 295 QPKRVFETVR 304
Cdd:PRK03918 522 KKAEEYEKLK 531
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
150-312 |
5.16e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 5.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 150 KELRDANIQISTIAEELAKKTEDASRQQEEITHLLSQIVDLQKKAKSYALENEELTQHLGAAKDAQRALTAELRELEDKY 229
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 230 AECMEML--HEAQEELKNFRNKTVPLSTPRRFHSLGLFpMDSLAAEIEG--TMRKEIQMSDPDVEEQRLQPKRVFETVRN 305
Cdd:COG4942 107 AELLRALyrLGRQPPLALLLSPEDFLDAVRRLQYLKYL-APARREQAEElrADLAELAALRAELEAERAELEALLAELEE 185
|
....*..
gi 688589783 306 VNQSVRQ 312
Cdd:COG4942 186 ERAALEA 192
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
106-244 |
6.01e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 6.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 106 LDSLQKKLKDLEEENIVLRSEANHLETEtisYEEKEQQLvNDCVKELRDANIQISTIAEELAKKTE--DASRQQEEITHL 183
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEAR---LEAAKTEL-EDLEKEIKRLELEIEEVEARIKKYEEqlGNVRNNKEYEAL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 184 LSQIvDLQKKAKSyALEN---------EELTQHLGAAKDAQRALTAELRELEDKYAECMEMLHEAQEELK 244
Cdd:COG1579 95 QKEI-ESLKRRIS-DLEDeilelmeriEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
23-243 |
6.33e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 6.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 23 ELAARIGQSLLK---------KNKSLTERNTFLEEQLEHIREEVSQLRhdllmkDELLQF-----YTSAAEESDGESASt 88
Cdd:COG3206 148 ELAAAVANALAEayleqnlelRREEARKALEFLEEQLPELRKELEEAE------AALEEFrqkngLVDLSEEAKLLLQQ- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 89 tpihrndtsftvpnylpLDSLQKKLKDLEEENIVLRSEANHLETETISYEEKEQQLVNDcvKELRDANIQISTIAEELAK 168
Cdd:COG3206 221 -----------------LSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQS--PVIQQLRAQLAELEAELAE 281
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688589783 169 KTEDASRQQEEITHLLSQIVDLQKKAKSyalENEELTQHLGAAKDAQRALTAELRELEDKYAECMEMLHEAQEEL 243
Cdd:COG3206 282 LSARYTPNHPDVIALRAQIAALRAQLQQ---EAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAEL 353
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
108-250 |
9.86e-05 |
|
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: 45.39 E-value: 9.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 108 SLQKKLKDLEEENI-VLRSEANHLEtetisyeeKEQQLVNDCVKELRDANIQISTIAEELAK--------KTEDASRQQE 178
Cdd:smart00787 140 KLLEGLKEGLDENLeGLKEDYKLLM--------KELELLNSIKPKLRDRKDALEEELRQLKQledeledcDPTELDRAKE 211
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688589783 179 EITHLLSQIVDLQKKAKSYALENEELTQHLGAAKDAQRALTAELRELEDKYAECMEM-LHEA---QEELKNFRNKT 250
Cdd:smart00787 212 KLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFtFKEIeklKEQLKLLQSLT 287
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2-307 |
1.01e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 2 TKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKSLTeRNTFLEEQLEHIREEVSQLRHDLLMKDEllQFYTSAAEES 81
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELI-KLKELAEQLKELEEKLKKYNLEELEKKA--EEYEKLKEKL 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 82 DGESASTtpihrndtsftvpnyLPLDSLQKKLKDLEEENIVLRSEANHLETETISYEEKEQQLVNDCVKELrdaniqist 161
Cdd:PRK03918 535 IKLKGEI---------------KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEEL--------- 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 162 iaEELAKKTEDASRQQEEITHLLSQIVDLQKKAKSYALENEELTQHLGAAKDAQRALTAELRELEDKYAEcmemlheaqE 241
Cdd:PRK03918 591 --EERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE---------E 659
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688589783 242 ELKNFRNKTVPLStprRFHSlglfpmdSLAAEIEG--TMRKEIQMSDPDVEEQRLQPKRVFETVRNVN 307
Cdd:PRK03918 660 EYEELREEYLELS---RELA-------GLRAELEEleKRREEIKKTLEKLKEELEEREKAKKELEKLE 717
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
6-249 |
1.77e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 6 NDIDAVTRLLEEKERDLELAARIG--------QSLLKKNKSLTERNTFLEEQLEHIREEVSQLRHDLlmkDELLQFYTSA 77
Cdd:COG4717 163 EELEELEAELAELQEELEELLEQLslateeelQDLAEELEELQQRLAELEEELEEAQEELEELEEEL---EQLENELEAA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 78 AEESDGESASTTPI-------------HRNDTSFTVPN-----------YLPLDSLQKKLKDLEEENIVLRSEANHLETE 133
Cdd:COG4717 240 ALEERLKEARLLLLiaaallallglggSLLSLILTIAGvlflvlgllalLFLLLAREKASLGKEAEELQALPALEELEEE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 134 TISYEEKEQQLVNDC-----------VKELRDANIQISTIAEELAKKTEDASRQQ----------EEITHLLSQIVDLQK 192
Cdd:COG4717 320 ELEELLAALGLPPDLspeellelldrIEELQELLREAEELEEELQLEELEQEIAAllaeagvedeEELRAALEQAEEYQE 399
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688589783 193 KAKSYALENEELTQHLGAAKDAQRA-----LTAELRELEDKYAECMEMLHEAQEELKNFRNK 249
Cdd:COG4717 400 LKEELEELEEQLEELLGELEELLEAldeeeLEEELEELEEELEELEEELEELREELAELEAE 461
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
106-244 |
1.82e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 106 LDSLQKKLKDLEEENIVLRSEANHLETETISYEEKEQQLVNDCVKELRDANIQ-------------------------IS 160
Cdd:COG3883 46 LEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSggsvsyldvllgsesfsdfldrlsaLS 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 161 TIAEELAKKTEDASRQQEEITHLLSQIVDLQKKAKSYALENEELTQHLGAAKDAQRALTAELRELEDKYAECMEMLHEAQ 240
Cdd:COG3883 126 KIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
|
....
gi 688589783 241 EELK 244
Cdd:COG3883 206 AAAE 209
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1-249 |
1.93e-04 |
|
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: 45.35 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 1 MTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKSLTERNTFLEEQLEHIREEVSQLRHDLLMKdellqfytSAAEE 80
Cdd:pfam02463 179 IEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQEL--------LRDEQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 81 SDGESASTTPIHRNDTSFTVPNYLPLDSLQKKLKD--------LEEEnivLRSEANHLETETISYEEKEQQLVNDcVKEL 152
Cdd:pfam02463 251 EEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEeelkllakEEEE---LKSELLKLERRKVDDEEKLKESEKE-KKKA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 153 RDANIQISTIAEELAKKTEDASRQQEEithLLSQIVDLQKKaksYALENEELTQHLGAAKDAQRALTAELRELEDKYAEC 232
Cdd:pfam02463 327 EKELKKEKEEIEELEKELKELEIKREA---EEEEEEELEKL---QEKLEQLEEELLAKKKLESERLSSAAKLKEEELELK 400
|
250
....*....|....*..
gi 688589783 233 MEMLHEAQEELKNFRNK 249
Cdd:pfam02463 401 SEEEKEAQLLLELARQL 417
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
43-229 |
2.72e-04 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 44.30 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 43 NTFLEEQLEHIREEVSQLRHDLLMKDELLQfytsaaeesDGESASTTPIHRNDTSFTVPNYLpldslqKKLKDLEEEnIV 122
Cdd:pfam04108 118 RDALKELIDELQAAQESLDSDLKRFDDDLR---------DLQKELESLSSPSESISLIPTLL------KELESLEEE-MA 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 123 --LRSEANHLET-------------ETISYEEKEQQLVNDCVKELRDANIQISTIAEELAKKTEDASRQQEEITHLLSQI 187
Cdd:pfam04108 182 slLESLTNHYDQcvtavklteggraEMLEVLENDARELDDVVPELQDRLDEMENNYERLQKLLEQKNSLIDELLSALQLI 261
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 688589783 188 VDLQKKAKSYALENEELTQHLGAAKDAQRALTAELRELEDKY 229
Cdd:pfam04108 262 AEIQSRLPEYLAALKEFEERWEEEKETIEDYLSELEDLREFY 303
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
46-246 |
2.94e-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: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 46 LEEQLEHIREEVSQLRHDLLMKDELLQFYTSAAEESDGE-SASTTPIHRNDTSftvpnylpLDSLQKKLKDLEEENIVLR 124
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRiAALARRIRALEQE--------LAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 125 SEANHLETE---------TISYEEKEQQLVN--DCVKELRDANIqISTIAEELAKKTEDASRQQEEITHLLSQIVDLQKK 193
Cdd:COG4942 97 AELEAQKEElaellralyRLGRQPPLALLLSpeDFLDAVRRLQY-LKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 688589783 194 AKSYALENEELTQHLGAAKDAQRALTAELRELEDKYAECMEMLHEAQEELKNF 246
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
150-249 |
3.15e-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: 43.37 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 150 KELRDANIQISTIAEELAKKTEDASRQQEEITHLLSQIVDLQKKAKSYaleneelTQHLGAAKDA--QRALTAEL----- 222
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY-------EEQLGNVRNNkeYEALQKEIeslkr 103
|
90 100
....*....|....*....|....*....
gi 688589783 223 --RELEDKYAECMEMLHEAQEELKNFRNK 249
Cdd:COG1579 104 riSDLEDEILELMERIEELEEELAELEAE 132
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
9-238 |
5.23e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 5.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 9 DAVTRLLEEKERDLELAARIGQSLLKknksLTERNTFLEEQLEHIREEVSQLRHDLLmkdELLQFYTSAAEESDGESAST 88
Cdd:PRK02224 237 DEADEVLEEHEERREELETLEAEIED----LRETIAETEREREELAEEVRDLRERLE---ELEEERDDLLAEAGLDDADA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 89 TPIHrndtsftvpnyLPLDSLQKKLKDLEEENIVLRSEANHLETETISYEEKEQQLvNDCVKELRDaniQISTIAEELAK 168
Cdd:PRK02224 310 EAVE-----------ARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDL-EERAEELRE---EAAELESELEE 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 169 KTEDASRQQEEITHLLSQIVDLQK----------KAKSYaleNEELTQHLGAAKDAQRALTAELRELEDKYAECMEMLHE 238
Cdd:PRK02224 375 AREAVEDRREEIEELEEEIEELRErfgdapvdlgNAEDF---LEELREERDELREREAELEATLRTARERVEEAEALLEA 451
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
104-244 |
5.76e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 5.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 104 LPLDSLQKKLKDLEEENIVLRSEANHLETEtisYEEKEQQLvNDCVKELRDANIQISTIA----EELAKKTEDASRQQEE 179
Cdd:COG4913 281 LRLWFAQRRLELLEAELEELRAELARLEAE---LERLEARL-DALREELDELEAQIRGNGgdrlEQLEREIERLERELEE 356
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688589783 180 ITHLLSQIVDLQKKAK-SYALENEELTQHLGAAKDAQRALTAELRELEDKYAECMEMLHEAQEELK 244
Cdd:COG4913 357 RERRRARLEALLAALGlPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR 422
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
131-245 |
6.20e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 131 ETETISYEEKEQQLVNDCVKELRDANIQISTIAEELAKKTEDASRQQEEITHLLSQIVDLQKKAKSYALENEELTQHLGA 210
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA 91
|
90 100 110
....*....|....*....|....*....|....*
gi 688589783 211 AKDAQRALTAELRELEDKYAECMEMLHEAQEELKN 245
Cdd:COG4372 92 AQAELAQAQEELESLQEEAEELQEELEELQKERQD 126
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
108-245 |
8.52e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 8.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 108 SLQKKLKDLEEENIVLRSEANhLETETISYE------EKEQQLVNDCVKELRDANiqistiaEELAKKtEDASRQQEEIt 181
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAK-KEAEAIKKEalleakEEIHKLRNEFEKELRERR-------NELQKL-EKRLLQKEEN- 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688589783 182 hllsqivdLQKKAKSYALENEELTQHlgaakdaQRALTAELRELEDKYAECMEMLHEAQEELKN 245
Cdd:PRK12704 98 --------LDRKLELLEKREEELEKK-------EKELEQKQQELEKKEEELEELIEEQLQELER 146
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
10-245 |
1.30e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 10 AVTRLLEEKERDLE-LAARIGQsllKKNKSLTER-NTF------LEEQLEHIREEVSQLRHDLLMKDELLQFYTSAAEES 81
Cdd:PRK02224 177 GVERVLSDQRGSLDqLKAQIEE---KEEKDLHERlNGLeselaeLDEEIERYEEQREQARETRDEADEVLEEHEERREEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 82 DgESASTTPIHRNDTSFTVPNYlplDSLQKKLKDLEEENIVLRSEANHLETETiSYEEKEQQLVNDCVKELRDaniQIST 161
Cdd:PRK02224 254 E-TLEAEIEDLRETIAETERER---EELAEEVRDLRERLEELEEERDDLLAEA-GLDDADAEAVEARREELED---RDEE 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 162 IAEELAKKTEDASRQQEEITHLLSQIVDLQKKAKSYALENEELTQHLGAAKDAQRALTAELRELEDKYAECMEMLHEAQE 241
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPV 405
|
....
gi 688589783 242 ELKN 245
Cdd:PRK02224 406 DLGN 409
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
13-247 |
1.32e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.65 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 13 RLLEEKERDLElAARIGQSLLKKNKSLTERntfLEEQLEHIREEVSQLRHDLLMKDELLQFYTSAAEESDGESASTTpIH 92
Cdd:TIGR00618 504 CPLCGSCIHPN-PARQDIDNPGPLTRRMQR---GEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILT-QC 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 93 RNDTSFTVPNYL-PLDSLQKKLKDLEEENIVLRsEANHLEtetisyEEKEQQLVNDCVKELRDANIQISTIAEELAKKTE 171
Cdd:TIGR00618 579 DNRSKEDIPNLQnITVRLQDLTEKLSEAEDMLA-CEQHAL------LRKLQPEQDLQDVRLHLQQCSQELALKLTALHAL 651
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688589783 172 DASRQQEEITHLLSQIVDLQKKAKSYALENEELTQHLgaakdaQRALTAELRELEdkyaECMEMLHEAQEELKNFR 247
Cdd:TIGR00618 652 QLTLTQERVREHALSIRVLPKELLASRQLALQKMQSE------KEQLTYWKEMLA----QCQTLLRELETHIEEYD 717
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
107-253 |
1.41e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 107 DSLQKKLKDLEEENIVLRSEANHLET-------ETISYEEKEQQLVNDcVKELRDA-----------NIQISTIAEELAK 168
Cdd:COG1340 4 DELSSSLEELEEKIEELREEIEELKEkrdelneELKELAEKRDELNAQ-VKELREEaqelrekrdelNEKVKELKEERDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 169 KTEDASRQQEEITHLLSQIVDLQKKAKSY--------ALENEELTQHLGaaKDAQRALTAELRELEDKYAEcMEMLHEAQ 240
Cdd:COG1340 83 LNEKLNELREELDELRKELAELNKAGGSIdklrkeieRLEWRQQTEVLS--PEEEKELVEKIKELEKELEK-AKKALEKN 159
|
170
....*....|...
gi 688589783 241 EELKNFRNKTVPL 253
Cdd:COG1340 160 EKLKELRAELKEL 172
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
106-275 |
1.50e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 106 LDSLQK-KLKDLEEENIVLRSEANHLETETISYEE--KEQQLVND------------CVKELRDANIQISTIAEELAKKT 170
Cdd:PHA02562 168 MDKLNKdKIRELNQQIQTLDMKIDHIQQQIKTYNKniEEQRKKNGeniarkqnkydeLVEEAKTIKAEIEELTDELLNLV 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 171 EDASRQQEEITHLLSQIVDLQKKAKSYALENEELTQH----------------LGAAKDAQRALTAELRELEDKYAECME 234
Cdd:PHA02562 248 MDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGgvcptctqqisegpdrITKIKDKLKELQHSLEKLDTAIDELEE 327
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 688589783 235 MLHEAQEELKNFRNKTVPLSTPRRFHSLGLFPMDSLAAEIE 275
Cdd:PHA02562 328 IMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIE 368
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
3-295 |
1.60e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.34 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 3 KTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKSLTERNTFLEEQ-------------LEHIREEVSQLRHDLLMKDE 69
Cdd:TIGR00606 581 SKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKlfdvcgsqdeesdLERLKEEIEKSSKQRAMLAG 660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 70 LLQFYTSAAEESDGESASTTPIHRNDTSFTVPNYLPLDSLQKKLKDLEEENIVLRSEANHLETET------ISYEEKEQQ 143
Cdd:TIGR00606 661 ATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRdemlglAPGRQSIID 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 144 LVNDCVKELRDANIQISTIAEELAKKTEDASRQ------QEEITHLLSQIVDLQKKAKSYALENEELTQHLGA---AKDA 214
Cdd:TIGR00606 741 LKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLlgtimpEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAklqGSDL 820
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 215 QRALTA----------ELRELEDKYAECMEMLHEAQEELKNFRNKTVPLSTPRRFHSLGLFPMDSLAAEIEgTMRKEIQM 284
Cdd:TIGR00606 821 DRTVQQvnqekqekqhELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLV-ELSTEVQS 899
|
330
....*....|.
gi 688589783 285 SDPDVEEQRLQ 295
Cdd:TIGR00606 900 LIREIKDAKEQ 910
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
8-245 |
2.24e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.98 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 8 IDAVTRLLEEKERDLELAArigqslLKKNKSLTErNTFLEEQLEHIREEVSQLRHDLLMKDELLQFYTSAAEESDGESAS 87
Cdd:TIGR02169 197 RQQLERLRREREKAERYQA------LLKEKREYE-GYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 88 ttpihRNDTsftvpnylpLDSLQKKLKDL-EEENIVLRSEANHLETETISYE----EKEQQLvNDCVKELRDANIQISTI 162
Cdd:TIGR02169 270 -----IEQL---------LEELNKKIKDLgEEEQLRVKEKIGELEAEIASLErsiaEKEREL-EDAEERLAKLEAEIDKL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 163 AEELAKKTEDASRQQEEITHLLSQIVDLQKKAKSYALENEELTQHLGAAKDAQRALTAELREL----------EDKYAEC 232
Cdd:TIGR02169 335 LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLkreinelkreLDRLQEE 414
|
250
....*....|...
gi 688589783 233 MEMLHEAQEELKN 245
Cdd:TIGR02169 415 LQRLSEELADLNA 427
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
106-242 |
2.34e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 106 LDSLQKKLKDLEEENIVLRSEANHLETETISYEEKEQQLVNdcVKELRDANIQISTIAEELAkktedasRQQEEITHLL- 184
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQR--LAEYSWDEIDVASAEREIA-------ELEAELERLDa 682
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 185 --SQIVDLQKKAKSYALENEELTQHLGAAKDAQRALTAELRELEDKYAECMEMLHEAQEE 242
Cdd:COG4913 683 ssDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
3-244 |
2.46e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 3 KTYNDIDAVTRLLEEKERDLElaarigqSLLKKNKSLTERNTFLEEQLEHIREEVSQLRHDLLMKDELLQFYTSAAEESD 82
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLE-------KFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 83 GESASTTPIHRNdtsftvpnylpLDSLQKKLKDLEEENIVLRSEANHLETETISYEEKEQQLvndcvKELRDANIQISTI 162
Cdd:PRK03918 235 ELKEEIEELEKE-----------LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-----KELKEKAEEYIKL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 163 AEELAKKTEDASRQQEEITHLLSQIVDLQKKAKSYALENEELtqhlgaakdaqRALTAELRELEDKYAEcMEMLHEAQEE 242
Cdd:PRK03918 299 SEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL-----------EELKKKLKELEKRLEE-LEERHELYEE 366
|
..
gi 688589783 243 LK 244
Cdd:PRK03918 367 AK 368
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
8-249 |
2.94e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 8 IDAVTRLLEEKERDLELAARIGQSLLKKNKSLTERNTFLEEQLEHIREEVSQLRHDLLMKDELLQFYTSAAEESDGEsas 87
Cdd:PRK02224 316 REELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEE--- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 88 ttpIHRNDTSFtvpNYLP--LDSLQKKLKDLEEENIVLRSEANHLETETISYE---EKEQQLVN-----DCVKELRDANI 157
Cdd:PRK02224 393 ---IEELRERF---GDAPvdLGNAEDFLEELREERDELREREAELEATLRTARervEEAEALLEagkcpECGQPVEGSPH 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 158 qISTIAE------ELAKKTEDASRQQEEITHLLSQIVDLQKKAK--SYALENEEL------TQHLGAAKDAQRA------ 217
Cdd:PRK02224 467 -VETIEEdrerveELEAELEDLEEEVEEVEERLERAEDLVEAEDriERLEERREDleeliaERRETIEEKRERAeelrer 545
|
250 260 270
....*....|....*....|....*....|....*
gi 688589783 218 ---LTAELRELEDKYAECMEMLHEAQEELKNFRNK 249
Cdd:PRK02224 546 aaeLEAEAEEKREAAAEAEEEAEEAREEVAELNSK 580
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
109-245 |
3.09e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 39.89 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 109 LQKKLKDLEEEnivLRSEANHLETETISYEEKEQQLVndcvKELRDANIQIstiaEELAKKTEDASRQQEEITHLLSQIV 188
Cdd:pfam13851 27 LIKSLKEEIAE---LKKKEERNEKLMSEIQQENKRLT----EPLQKAQEEV----EELRKQLENYEKDKQSLKNLKARLK 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 688589783 189 DLQKKAKSYALENEELTQHLgaakdaqRALTAELRELEDKYAecmEMLHEAQE--ELKN 245
Cdd:pfam13851 96 VLEKELKDLKWEHEVLEQRF-------EKVERERDELYDKFE---AAIQDVQQktGLKN 144
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
113-243 |
3.10e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 113 LKDLEEEnivLRSEANHLETE--------TIS--YEEKEQQLVndcVKELRDANIQISTIAEELAKKTEDASRQQEEITH 182
Cdd:COG1196 191 LEDILGE---LERQLEPLERQaekaeryrELKeeLKELEAELL---LLKLRELEAELEELEAELEELEAELEELEAELAE 264
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688589783 183 LLSQIVDLQkkaksyaLENEELTQHLGAAKDAQRALTAELRELEDKYAECMEMLHEAQEEL 243
Cdd:COG1196 265 LEAELEELR-------LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
110-248 |
3.34e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 110 QKKLKDLEEENIVLRSEANHLETETISYEEKEQQLV------NDCVKELRDANIQISTIAEELAKKTEDASRQQEEITHL 183
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARetrdeaDEVLEEHEERREELETLEAEIEDLRETIAETEREREEL 277
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688589783 184 LSQIVDLQKKAKSYALENEELTQHLGAAKDAQRALTAELRELEDKYAECMEMLHEAQEELKNFRN 248
Cdd:PRK02224 278 AEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNE 342
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
106-249 |
4.52e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 106 LDSLQKKLKDLEEENIVLRSEANHLETEtisYEEKEQQLvNDCVKELRDANIQISTIAEELAKKTEDASRQQEEITHlls 185
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAE---LEELNEEY-NELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE--- 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688589783 186 QIVDLQKK------------AKSYA--LENEELTQHLGaakDAQRALTAELRELEDKYAECMEMLHEAQEELKNFRNK 249
Cdd:COG3883 91 RARALYRSggsvsyldvllgSESFSdfLDRLSALSKIA---DADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
12-315 |
4.70e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 12 TRLLEEKERDLELAARIGQSLLKKNKSLTErntfLEEQLEHIREEVSQLRHDLLMKDELLQFYTSAAEESDGEsasttpi 91
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRK----ALFELDKLQEELEQLREELEQAREELEQLEEELEQARSE------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 92 hrndtsftvpnylpLDSLQKKLKDLEEENIVLRSEANHLETETISYEEKEQQL---VNDCVKELRDANIQISTIAEELAK 168
Cdd:COG4372 75 --------------LEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELqeeLEELQKERQDLEQQRKQLEAQIAE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 169 KTEDASRQQEEITHLLSQIVDLQKKAKSYALENEELTQHlgaakDAQRALTAELRELEDKYaecmemlhEAQEELKNFRN 248
Cdd:COG4372 141 LQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA-----EAEQALDELLKEANRNA--------EKEEELAEAEK 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688589783 249 KTVPLSTPRRFHSLGLFPMDsLAAEIEGTMRKEIQMSDPDVEEQRLQPKRVFETVRNVNQSVRQRSM 315
Cdd:COG4372 208 LIESLPRELAEELLEAKDSL-EAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDT 273
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
13-307 |
5.33e-03 |
|
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: 40.73 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 13 RLLEEKERDLELAARIGQSLLKKNKSLTERNTFLEEQLEHIREEvSQLRHDLLMKDELLQFYTSAAEESDGESASTTPIH 92
Cdd:pfam02463 697 RQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKL-LKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKE 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 93 RNDTSFTVPNYLPLDSLQKKLKDLEEENIVLRSEANHLETETISYEEKEQQLVNDCVKELRDANIQISTIAEELAKKTED 172
Cdd:pfam02463 776 LAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEE 855
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 173 ASRQQEEIT------HLLSQIVDLQKKAKSYALENEELTQHlgAAKDAQRALTAELRELEDKYAECMEMLHEAQEELKNF 246
Cdd:pfam02463 856 LERLEEEITkeellqELLLKEEELEEQKLKDELESKEEKEK--EEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKY 933
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688589783 247 RNKTvplstprrfhslglfPMDSLAAEIEgtmrKEIQMSDPDVEEQRL-QPKRVFETVRNVN 307
Cdd:pfam02463 934 EEEP---------------EELLLEEADE----KEKEENNKEEEEERNkRLLLAKEELGKVN 976
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
106-231 |
5.88e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.14 E-value: 5.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 106 LDSLQKKLKDLEEENIVLRSEANHLETETISYEEK----EQQL--VNDcVKELRDANIQISTIAEELAKKTEDASRQQEE 179
Cdd:COG1579 40 LAALEARLEAAKTELEDLEKEIKRLELEIEEVEARikkyEEQLgnVRN-NKEYEALQKEIESLKRRISDLEDEILELMER 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 688589783 180 ITHLLSQIVDLQKKAksyalenEELTQHLGAAKDAQRALTAELRELEDKYAE 231
Cdd:COG1579 119 IEELEEELAELEAEL-------AELEAELEEKKAELDEELAELEAELEELEA 163
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
29-256 |
6.62e-03 |
|
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: 40.06 E-value: 6.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 29 GQSLLKKNKSLT-ERNTFLEEQlEHIREEVSQLRHDLLMKDELLQFYTSAAEESDGESASTTPIHRNDTSFTVpnyLPLD 107
Cdd:pfam05622 213 YKKLEEKLEALQkEKERLIIER-DTLRETNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKL---IRLQ 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 108 SLQKKLKDLEEENIVLRSEA--NHLE--TETISYEEKEQQLVNDCVKELRDANIQISTIAEELAKKTEDASRQQEEITHL 183
Cdd:pfam05622 289 HENKMLRLGQEGSYRERLTElqQLLEdaNRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKAEDSSLLKQKLEEH 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 184 LSQIVDLQKKAKSYALENEELTQHLGAAKDA-----QRALTA---ELRELEDKYAECMEmlhEAQEELKNFRNKTVPLST 255
Cdd:pfam05622 369 LEKLHEAQSELQKKKEQIEELEPKQDSNLAQkidelQEALRKkdeDMKAMEERYKKYVE---KAKSVIKTLDPKQNPASP 445
|
.
gi 688589783 256 P 256
Cdd:pfam05622 446 P 446
|
|
| PRK14160 |
PRK14160 |
heat shock protein GrpE; Provisional |
129-238 |
6.65e-03 |
|
heat shock protein GrpE; Provisional
Pssm-ID: 237629 [Multi-domain] Cd Length: 211 Bit Score: 38.97 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 129 HLETETISYEEKEQQLVNDCVKELRDANIQiSTIAEELAKKTEDASRQQEEITHLLSQIVDLQKKAKSyalENEELTQHL 208
Cdd:PRK14160 2 EKECKDAKHENMEEDCCKENENKEEDKGKE-EDLEFEEIEKEEIIEDSEESNEVKIEELKDENNKLKE---ENKKLENEL 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 688589783 209 GAAKDAQRALTAEL--------RELEDKYAE-CMEMLHE 238
Cdd:PRK14160 78 EALKDRLLRTVAEYdnyrkrtaKEKEGIYSDaCEDVLKE 116
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
150-245 |
7.52e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.75 E-value: 7.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 150 KELRDANIQISTIAEELAKKTEDASRQQEEITHLLSQIVDLQKKAKsyaleneELTQHLGAAKDAQRALTAELRELEDKY 229
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA-------ALARRIRALEQELAALEAELAELEKEI 92
|
90
....*....|....*.
gi 688589783 230 AECMEMLHEAQEELKN 245
Cdd:COG4942 93 AELRAELEAQKEELAE 108
|
|
| Uso1_p115_C |
pfam04871 |
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ... |
108-206 |
8.93e-03 |
|
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.
Pssm-ID: 461461 [Multi-domain] Cd Length: 121 Bit Score: 36.99 E-value: 8.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 108 SLQKKLKDLEEENIVLRSEANHLETETISYEEKEQQL--VNDCVKELRDAniqISTIAEELAKKTEDASRQQEEITHLLS 185
Cdd:pfam04871 5 ELESEASSLKNENTELKAELQELSKQYNSLEQKESQAkeLEAEVKKLEEA---LKKLKAELSEEKQKEKEKQSELDDLLL 81
|
90 100
....*....|....*....|.
gi 688589783 186 QIVDLQKKAKSYALENEELTQ 206
Cdd:pfam04871 82 LLGDLEEKVEKYKARLKELGE 102
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
106-231 |
9.90e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 9.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688589783 106 LDSLQKKLKDLEEENIVLRSEANHLETEtisYEEKEQQLVNDCVKELRDANIQISTIAEELAKKTEDASRQQEEITHL-- 183
Cdd:COG4913 297 LEELRAELARLEAELERLEARLDALREE---LDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALgl 373
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 688589783 184 -----LSQIVDLQKKAK----SYALENEELTQHLGAAKDAQRALTAELRELEDKYAE 231
Cdd:COG4913 374 plpasAEEFAALRAEAAalleALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| |
