|
Name |
Accession |
Description |
Interval |
E-value |
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
35-348 |
1.70e-142 |
|
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: 427.52 E-value: 1.70e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 35 DSLY-LYEGQDWVI--SPSCSPDEPSAISPMLAEETFRYMtflavgssfpqngsnslskVLSADRVEQMTKTYNDIDVVT 111
Cdd:pfam04849 12 DTLGtGYANQDWKIpsPAGRPPEVSLPLSPEQIRETLNYF-------------------LLCSDRVSQMTKTYNDIEAVT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 112 HLLSERDRDLELAARIGQSLLQRNHVLQERNESLEEQLAQALDQVHQLQHELAKKDELLRMVASASEESETDSSCSTPLR 191
Cdd:pfam04849 73 RLLEEKERDLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEILQLRHELSKKDDLLQIYSNDAEESETESSCSTPLR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 192 HPVPAGAALALSQLEALQSKLQDLEEENLTLRSEACHLKKETITYEEKEQQLVNDCVKELRESNSQMVSLTDELSQKNED 271
Cdd:pfam04849 153 RNESFSSLHGCVQLDALQEKLRGLEEENLKLRSEASHLKTETDTYEEKEQQLMSDCVEQLSEANQQMAELSEELARKMEE 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 326668399 272 LMRHQEEIAQLLSQIVELQHRVKELALEKEELRIHLQASKEAQRQLTNELKELSDRNAECVGMLHESQEEIKDLRSK 348
Cdd:pfam04849 233 NLRQQEEITSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLGMLHEAQEELKELRKK 309
|
|
| Milton |
pfam12448 |
Kinesin associated protein; This domain family is found in eukaryotes, and is typically ... |
394-549 |
9.59e-26 |
|
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: 104.67 E-value: 9.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 394 SSQKRVFQTVRSVNQSVMRAAAAGPPipGSGVIMTPVPYQSHTHNTADEDASRGReNSRLGQPGSPGGSALTSALNRLSL 473
Cdd:pfam12448 15 SNQSSSLTSMRSSSSSTPRSSYYGGD--GSSISLDNRTNSILSETSSSQDSGYDR-PKKPGTPGTPGARDLEAALRRLSL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 474 RRQNFLCERQFFQAERERKLQDL--TAAESEGGASGCSSPMGSTVSSFTNLSEFSISSSCFKT--FLPEKLQIVKPMEGS 549
Cdd:pfam12448 92 RRQNYLSERRFFEEERERKLLALagTYNYDEGEHGGSLTPNDSIMSLGSNHSGSSSHSSGFSSrsYLPEKLQIVKPLEGS 171
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
107-346 |
4.26e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.94 E-value: 4.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 107 IDVVTHLLSERDRDLELAARIGQSLLQRNHVLQERNESLEEQLAQALDQVHQLQHELAKKDELLRMVASASEESETDssc 186
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE--- 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 187 stplrhpvpagAALALSQLEALQSKLQDLEEENLTLRSEACHLKKETITYEEKEQQL---VNDCVKELRESNSQMVSLTD 263
Cdd:TIGR02168 777 -----------LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLrerLESLERRIAATERRLEDLEE 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 264 ELSQKNEDLMRHQEEIAQLLSQIVELQHRVKELALEKEELRIHLQASKEAQRQLTNELKELSDRNAECVGMLHESQEEIK 343
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925
|
...
gi 326668399 344 DLR 346
Cdd:TIGR02168 926 QLE 928
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
116-348 |
7.64e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.58 E-value: 7.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 116 ERDRDLELAARIGQSLLQRNHVLQERNESLEEQLAQALDQVHQLQHELAK-KDELLRMVASASEESETDSSCSTPLRHPV 194
Cdd:COG1196 222 LKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEElRLELEELELELEEAQAEEYELLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 195 pAGAALALSQLEALQSKLQDLEEENLTLRSEACHLKKETITYEEKEQQL----------VNDCVKELRESNSQMVSLTDE 264
Cdd:COG1196 302 -QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAeeeleeaeaeLAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 265 LSQKNEDLMRHQEEIAQLLSQIVELQHRVKELALEKEELRIHLQASKEAQRQLTNELKELSDRNAECVGMLHESQEEIKD 344
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
....
gi 326668399 345 LRSK 348
Cdd:COG1196 461 LLEL 464
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
88-387 |
1.05e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.94 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 88 LSKVLSADRVEqmtKTYNDIDVVTHLLSERDRDLElaarigqSLLQRNHVLQERNESLEEQLAQALDQVHQLQHELAKKD 167
Cdd:PRK03918 151 VRQILGLDDYE---NAYKNLGEVIKEIKRRIERLE-------KFIKRTENIEELIKEKEKELEEVLREINEISSELPELR 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 168 ELLRMVASASEESETDSSCSTPLRhpvpagaalalSQLEALQSKLQDLEEENLTLRSEACHLKKETITYEEKEQQLvndc 247
Cdd:PRK03918 221 EELEKLEKEVKELEELKEEIEELE-----------KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL---- 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 248 vKELRESNSQMVSLTDELSQKNEDLMRHQEEIAQLLSQIVELQHRVKELALEKEELrihlqaskeaqRQLTNELKELSDR 327
Cdd:PRK03918 286 -KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL-----------EELKKKLKELEKR 353
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 328 NAEcvgmLHESQEEIKDLRSKNTPSAGLRrhTSYGLYPMDSIAAEIEGTMRREMSVEEEI 387
Cdd:PRK03918 354 LEE----LEERHELYEEAKAKKEELERLK--KRLTGLTPEKLEKELEELEKAKEEIEEEI 407
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
128-413 |
1.49e-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: 65.46 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 128 GQSLLQRNHVLQERNES--LEEQLAQALDQVHQLQHELAKkdellrmvasaseesetdsscstplrhpvpagaalALSQL 205
Cdd:TIGR02168 663 GGSAKTNSSILERRREIeeLEEKIEELEEKIAELEKALAE-----------------------------------LRKEL 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 206 EALQSKLQDLEEENLTLRSEACHLKKETITYEEKEQQL---VNDCVKELRESNSQMVSLTDELSQKNEDLMRHQEEIAQL 282
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLeerIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL 787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 283 LSQIVELQHRVKELALEKEELRIHLQASKEAQRQLTNELKELSDRNAECVGMLHESQEEIKDLRSKNTPSAGLRRHTSyg 362
Cdd:TIGR02168 788 EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE-- 865
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 326668399 363 lYPMDSIAAEIEGTMRREMSVEEEIAfeDQRSSQKRVFQTVRSVNQSVMRA 413
Cdd:TIGR02168 866 -ELIEELESELEALLNERASLEEALA--LLRSELEELSEELRELESKRSEL 913
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
114-330 |
1.39e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 114 LSERDRDLELAARIGQSLLQRNHVLQERNESLEEQLAQALDQVHQLQHELAKKDELLRMVASASEESETDsscstplrhp 193
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD---------- 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 194 vpagAALALSQLEALQSKLQDLEEENLTLRSEACHLKKETITYEEKEQQL----------VNDCVKELRESNSQMVSLTD 263
Cdd:COG1196 304 ----IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAeeeleeaeaeLAEAEEALLEAEAELAEAEE 379
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 326668399 264 ELSQKNEDLMRHQEE-------IAQLLSQIVELQHRVKELALEKEELRIHLQASKEAQRQLTNELKELSDRNAE 330
Cdd:COG1196 380 ELEELAEELLEALRAaaelaaqLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
114-348 |
4.36e-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: 60.85 E-value: 4.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 114 LSERDRDLELAARIGQSLLQRNHVLQERN--ESLEEQLAQALDQVHQLQHELAKKDELLRMVASASEEsetdsscstplr 191
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRriENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKE------------ 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 192 hpvpagaalalsQLEALQSKLQDLEEENLTLRSEACHLKKETITYEEKEQQL------------------VNDCVKELRE 253
Cdd:TIGR02169 738 ------------RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLeealndlearlshsripeIQAELSKLEE 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 254 SNSQMVSLTDELSQKNEDLMRH----QEEIAQLLSQIVELQHRVKELALEKEELRIHLQASKEAQRQLTNELKELSDRNA 329
Cdd:TIGR02169 806 EVSRIEARLREIEQKLNRLTLEkeylEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG 885
|
250
....*....|....*....
gi 326668399 330 ECVGMLHESQEEIKDLRSK 348
Cdd:TIGR02169 886 DLKKERDELEAQLRELERK 904
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
143-346 |
5.38e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 5.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 143 ESLEEQLAQALdQVHQLQHELAKKDELLRMVA--SASEESETDSscstplrhpvpAGAALALSQLEALQSKLQDLEEENL 220
Cdd:COG1196 203 EPLERQAEKAE-RYRELKEELKELEAELLLLKlrELEAELEELE-----------AELEELEAELEELEAELAELEAELE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 221 TLRSEAchlkketityeEKEQQLVNDCVKELRESNSQMVSLTDELSQKNEDLMRHQEEIAQLLSQIVELQHRVKELALEK 300
Cdd:COG1196 271 ELRLEL-----------EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 326668399 301 EELRIHLQASKEAQRQLTNELKELSDRNAECVGMLHESQEEIKDLR 346
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
97-329 |
5.96e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 5.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 97 VEQMTKTYNDIDVVTHLLSERDRDLELAARIGQSLLQRNHVLQERNESLEEQLAQALDQVHQLQHELAKKDELLRMVASA 176
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 177 SEESETDSscstplrhpvpagAALALSQLEALQSKLQDLEEENLTLRSEAcHLKKETITYEEKEQQLvndcVKELRESNS 256
Cdd:COG1196 374 LAEAEEEL-------------EELAEELLEALRAAAELAAQLEELEEAEE-ALLERLERLEEELEEL----EEALAELEE 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 326668399 257 QMVSLTDELSQKNEDLMRHQEEIAQLLSQIVELQHRVKELALEKEELRIHLQASKEAQRQLTNELKELSDRNA 329
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
97-347 |
9.15e-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: 59.69 E-value: 9.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 97 VEQMTKTYNDIDVVTHLLSE-RDRDLELAARIgQSLLQRNHVLQERNESLEEQLAQALDQVHQLQHELAKKDELLRMVAS 175
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEElRLEVSELEEEI-EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 176 ASEESETDsscstplrhpvpagAALALSQLEALQSKLQDLEEENLTLRSEACHLKKETITYEEKEQQLVNDcVKELRES- 254
Cdd:TIGR02168 331 KLDELAEE--------------LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK-VAQLELQi 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 255 ---NSQMVSLTDELSQKNEDLMRHQEEIAQLLSQIV-----ELQHRVKELALEKEELRIHLQASKEAQRQLTNELKELSD 326
Cdd:TIGR02168 396 aslNNEIERLEARLERLEDRRERLQQEIEELLKKLEeaelkELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
|
250 260
....*....|....*....|.
gi 326668399 327 RNAECVGMLHESQEEIKDLRS 347
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLER 496
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
118-335 |
2.23e-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: 58.53 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 118 DRDLELAARIGQSLLQRNHVLQERNESLEEQLAQALDQVHQLQHELAKKDELLRMVASASEESETdsscstplrhpvpag 197
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE--------------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 198 aalalsQLEALQSKLQDLEEENLTLRSEachlkketITYEEKEQQLVNDCVKELRESNSQMvsltdELSQKNEDLMRHQE 277
Cdd:TIGR02168 380 ------QLETLRSKVAQLELQIASLNNE--------IERLEARLERLEDRRERLQQEIEEL-----LKKLEEAELKELQA 440
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 326668399 278 EIAQLLSQIVELQHRVKELALEKEELRIHLQASKEAQRQLTNELKELSDRNAECVGML 335
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQ 498
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
190-348 |
3.37e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 56.83 E-value: 3.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 190 LRHPVPAGAALALSQLEALQSKLQDLEEENLTLRSEachLKKETityEEKEQQlvndcVKELRESNSQMVSLTDELSQKN 269
Cdd:COG4372 18 LRPKTGILIAALSEQLRKALFELDKLQEELEQLREE---LEQAR---EELEQL-----EEELEQARSELEQLEEELEELN 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 326668399 270 EDLMRHQEEIAQLLSQIvelqhrvKELALEKEELRIHLQASKEAQRQLTNELKELSDRNAECVGMLHESQEEIKDLRSK 348
Cdd:COG4372 87 EQLQAAQAELAQAQEEL-------ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
105-346 |
3.61e-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: 57.77 E-value: 3.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 105 NDIDVVTHLLSERDRDLELAARIGQSLLQRNHVLQERNESLEEQLA---QALDQVHQLQHELAKKDELLRMVASASEESE 181
Cdd:TIGR02169 702 NRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSsleQEIENVKSELKELEARIEELEEDLHKLEEAL 781
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 182 TDSSCStPLRHPVPAGAALA----------LSQLEALQSKLQDLEEENLTLRSEACHLKKETITYEEKE---QQLVNDCV 248
Cdd:TIGR02169 782 NDLEAR-LSHSRIPEIQAELskleeevsriEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIksiEKEIENLN 860
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 249 KELRESNSQMVSLTDELSQKNEDLMRHQEEIAQLLSQIVELQHRVKELALEKEELRIHLQASKEAQRQLTNELKELSDRN 328
Cdd:TIGR02169 861 GKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPK 940
|
250
....*....|....*...
gi 326668399 329 AECVgmlhESQEEIKDLR 346
Cdd:TIGR02169 941 GEDE----EIPEEELSLE 954
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
117-330 |
3.95e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.33 E-value: 3.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 117 RDRDLELAARIGQSLLQ---------RNHVLQERNESLEEQLAQALDQVHQLQHELAKKDELLRMVASASEesetdsscs 187
Cdd:COG3206 143 TSPDPELAAAVANALAEayleqnlelRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEE--------- 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 188 tplrhpvpagAALALSQLEALQSKLQDLEEENLTLRSEACHLKKETITYEEKEQQLVNDCV-----KELRESNSQMVSLT 262
Cdd:COG3206 214 ----------AKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPViqqlrAQLAELEAELAELS 283
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 326668399 263 DELSQKNEDLMRHQEEIAQLLSQI-VELQHRVKELALEKEELRIHLQASKEAQRQLTNELKELSDRNAE 330
Cdd:COG3206 284 ARYTPNHPDVIALRAQIAALRAQLqQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAE 352
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
202-348 |
5.96e-08 |
|
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: 55.41 E-value: 5.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 202 LSQLEALQSKLqdleEENL-TLRSEACHLKKEtityeekeQQLVNDCVKELRE----SNSQMVSLT---DELSQKNEDLM 273
Cdd:smart00787 139 MKLLEGLKEGL----DENLeGLKEDYKLLMKE--------LELLNSIKPKLRDrkdaLEEELRQLKqleDELEDCDPTEL 206
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 326668399 274 -RHQEEIAQLLSQIVELQHRVKELALEKEELRIHLQASKEAQRQLTNELKELSDRNAECVGMlheSQEEIKDLRSK 348
Cdd:smart00787 207 dRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGF---TFKEIEKLKEQ 279
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
134-348 |
1.93e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 134 RNHVLQERN---------------ESLEEQLAQALDQVHQLQHELAKKDELLRMVASASEESEtdsscstpLRHPVPAGA 198
Cdd:COG4913 214 REYMLEEPDtfeaadalvehfddlERAHEALEDAREQIELLEPIRELAERYAAARERLAELEY--------LRAALRLWF 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 199 A-----LALSQLEALQSKLQDLEEENLTLRSEACHLKKETITYEEKEQQLVNDCVKELREsnsQMVSLTDELSQKNEDLM 273
Cdd:COG4913 286 AqrrleLLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLER---EIERLERELEERERRRA 362
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 326668399 274 RHQEEIAQLLsqiVELQHRVKELALEKEELRIHLQASKEAQRQLTNELKELSDRNAECVGMLHESQEEIKDLRSK 348
Cdd:COG4913 363 RLEALLAALG---LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
114-348 |
2.18e-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: 55.07 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 114 LSERDRDLE---LAARIGQSLLQRNHVLQERnESLEEQLAQALDQVHQLQHELAKKDELLRMVASA-SEESETDSSCSTP 189
Cdd:TIGR02169 216 LLKEKREYEgyeLLKEKEALERQKEAIERQL-ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKiKDLGEEEQLRVKE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 190 LRHPVPAGAALALSQLEALQSKLQDLEE----------------ENLTLRSEACHLKKETIT--YEEKEQQLvNDCVKEL 251
Cdd:TIGR02169 295 KIGELEAEIASLERSIAEKERELEDAEErlakleaeidkllaeiEELEREIEEERKRRDKLTeeYAELKEEL-EDLRAEL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 252 RESNSQMVSLTDELSQKNEDLMRHQEEIAQLLSQIVELQHRVKELALEKEELRIHLQASKEAQRQLTNELKELSDRNAEC 331
Cdd:TIGR02169 374 EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ 453
|
250
....*....|....*..
gi 326668399 332 VGMLHESQEEIKDLRSK 348
Cdd:TIGR02169 454 EWKLEQLAADLSKYEQE 470
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
114-348 |
3.84e-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: 54.26 E-value: 3.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 114 LSERDRDLELAARIGQSLLQRNHVLQERNESLE------EQLAQALD-QVHQLQHELAKKDE----LLRMVASASEE--- 179
Cdd:TIGR04523 365 LEEKQNEIEKLKKENQSYKQEIKNLESQINDLEskiqnqEKLNQQKDeQIKKLQQEKELLEKeierLKETIIKNNSEikd 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 180 -SETDSSCSTPLRHpvpagaalaLSQL-EALQSKLQDLEEENLTLRSEACHLKKEtitYEEKEQQL--VNDCVKELRESN 255
Cdd:TIGR04523 445 lTNQDSVKELIIKN---------LDNTrESLETQLKVLSRSINKIKQNLEQKQKE---LKSKEKELkkLNEEKKELEEKV 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 256 SQMVSLTDELSQKNEDLmrhQEEIAQLLSQIVELQHRVKEL--ALEKEELRIHLQASKEAQRQLTNELKELSDRNAECVG 333
Cdd:TIGR04523 513 KDLTKKISSLKEKIEKL---ESEKKEKESKISDLEDELNKDdfELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQE 589
|
250
....*....|....*
gi 326668399 334 MLHESQEEIKDLRSK 348
Cdd:TIGR04523 590 LIDQKEKEKKDLIKE 604
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
127-348 |
4.14e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 127 IGQSLLQRNHVLQERNESLEEQLAQA---LDQVHQLQHELAKKDELLRMVASASEEsETDsscstplrhpvpagAALALS 203
Cdd:COG4913 604 LGFDNRAKLAALEAELAELEEELAEAeerLEALEAELDALQERREALQRLAEYSWD-EID--------------VASAER 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 204 QLEALQSKLQDLEEENLTLRseacHLKKEtitYEEKEQQLvndcvKELREsnsqmvsltdELSQKNEDLMRHQEEIAQLL 283
Cdd:COG4913 669 EIAELEAELERLDASSDDLA----ALEEQ---LEELEAEL-----EELEE----------ELDELKGEIGRLEKELEQAE 726
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 326668399 284 SQIVELQHRVKEL-ALEKEELRIHLQA--SKEAQRQLTNELKE-LSDRNAECVGMLHESQEEIKDLRSK 348
Cdd:COG4913 727 EELDELQDRLEAAeDLARLELRALLEErfAAALGDAVERELREnLEERIDALRARLNRAEEELERAMRA 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
204-348 |
1.04e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.14 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 204 QLEALQSKLQDLEEENLTLRSEachLKKETITYEEKEQQLVNDcVKELRESNSQMVSLTDELSQKNEDLMRHQEEIAQLL 283
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAE---LQELEEKLEELRLEVSEL-EEEIEELQKELYALANEISRLEQQKQILRERLANLE 315
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 326668399 284 SQIVELQHRVKELALEKEELRIHLQASKEAQRQLTNELKELSDRNAECVGML-------HESQEEIKDLRSK 348
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELeelesrlEELEEQLETLRSK 387
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
113-298 |
1.09e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 113 LLSERDRDLELAARIGQSLLQRNHVLQERNESLEEQLAQALDQVHQLQHELAKKDELLRMVASASEESETDSScstplRH 192
Cdd:COG4717 68 LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAE-----LA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 193 PVPAGAALALSQLEALQSKLQDLEEENLTLRSEACHLKKETITYEEKEQQLVNDCVKELRESNSQMVSLTDELSQKNEDL 272
Cdd:COG4717 143 ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL 222
|
170 180
....*....|....*....|....*...
gi 326668399 273 MRHQEEIAQLLSQIV--ELQHRVKELAL 298
Cdd:COG4717 223 EELEEELEQLENELEaaALEERLKEARL 250
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
203-348 |
1.28e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.45 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 203 SQLEALQSKLQDLEEENLTLRSEACHLKKETITYEEKEQQLVNDcVKELRESNSQMVSLTDELsqkNEDLMRHQEEIAQL 282
Cdd:COG1340 8 SSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQ-VKELREEAQELREKRDEL---NEKVKELKEERDEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 283 LSQIVELQHRVKEL---------------ALEK--EELRIHLQA---SKEAQRQLTNELKELSDRnAECVGMLHESQEEI 342
Cdd:COG1340 84 NEKLNELREELDELrkelaelnkaggsidKLRKeiERLEWRQQTevlSPEEEKELVEKIKELEKE-LEKAKKALEKNEKL 162
|
....*.
gi 326668399 343 KDLRSK 348
Cdd:COG1340 163 KELRAE 168
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
142-348 |
2.87e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.17 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 142 NESLEEQLAQALDQVHQLQHELA-KKDELLRMVasaseesetdsscstplrhpvpagaalalSQLEALQSKLQDLEEENL 220
Cdd:TIGR04523 358 NSEKQRELEEKQNEIEKLKKENQsYKQEIKNLE-----------------------------SQINDLESKIQNQEKLNQ 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 221 TLRSEACHLKKEtitYEEKEQQLVNdcVKELRE-SNSQMVSLTDELSQKNEDLMRHQEEIAQLLSQIVELQHRVKELALE 299
Cdd:TIGR04523 409 QKDEQIKKLQQE---KELLEKEIER--LKETIIkNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQN 483
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 326668399 300 KEELRIHLqASKEAQ-RQLTNELKELSDRNAECVGMLHESQEEIKDLRSK 348
Cdd:TIGR04523 484 LEQKQKEL-KSKEKElKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESE 532
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
96-337 |
5.95e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 5.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 96 RVEQMTKTYNDIDVVTHLLSERDRDL--ELAARIGQSLlqrnHVLQERNESLEEQLAQALDQVHQLQHELAKKDELLRMV 173
Cdd:TIGR02169 259 EISELEKRLEEIEQLLEELNKKIKDLgeEEQLRVKEKI----GELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKL 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 174 ASASEESETDSSCSTPLRHPVPAGAALALSQLEALQSKLQDLEEENLTLRseachlkKETITYEEKEQQLVNdcvkELRE 253
Cdd:TIGR02169 335 LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR-------DELKDYREKLEKLKR----EINE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 254 SNSQMVSLTDELSQKNEDLMRHQEEIAQLLSQIVELQHRVK--------------------------------------- 294
Cdd:TIGR02169 404 LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEdkaleikkqewkleqlaadlskyeqelydlkeeydrvek 483
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 326668399 295 ---ELALEKEELRIHLQASKEAQRQLTNELKELSDRNAECVGMLHE 337
Cdd:TIGR02169 484 elsKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQ 529
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
204-350 |
6.74e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.02 E-value: 6.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 204 QLEALQSKLQDLE---EENLT--LRSEACHLKKETITYE----EKEQQL------VNDCVKELRESNSQMVSLTDELSQK 268
Cdd:TIGR04523 289 QLNQLKSEISDLNnqkEQDWNkeLKSELKNQEKKLEEIQnqisQNNKIIsqlneqISQLKKELTNSESENSEKQRELEEK 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 269 N---EDLMRHQE----EIAQLLSQIVELQHRVKELALEKEELRIHLQASKEAQRQLTNELKELSDRNAecvgmlhESQEE 341
Cdd:TIGR04523 369 QneiEKLKKENQsykqEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETII-------KNNSE 441
|
....*....
gi 326668399 342 IKDLRSKNT 350
Cdd:TIGR04523 442 IKDLTNQDS 450
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
129-404 |
1.36e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 129 QSLLQRNHVLQERNESLEEQLAQALDQVHQLQHELAKKDELLRMVASASEESETDsscstplrhpvpagAALALSQLEAL 208
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQ--------------LQAAQAELAQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 209 QSKLQDLEEENLTLRSEACHLKKETITYEEKEQQLvndcvkelRESNSQmvsLTDELSQKNEDLMRHQEEIAQLLSQIVE 288
Cdd:COG4372 100 QEELESLQEEAEELQEELEELQKERQDLEQQRKQL--------EAQIAE---LQSEIAEREEELKELEEQLESLQEELAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 289 LQHRVKELALEKEELRIHlQASKEAQRQLTNELKELSDRNAEcVGMLHESQEEIKDLRSKNTPSAGLRRHTSYGLYPMDS 368
Cdd:COG4372 169 LEQELQALSEAEAEQALD-ELLKEANRNAEKEEELAEAEKLI-ESLPRELAEELLEAKDSLEAKLGLALSALLDALELEE 246
|
250 260 270
....*....|....*....|....*....|....*.
gi 326668399 369 IAAEIEGTMRREMSVEEEIAFEDQRSSQKRVFQTVR 404
Cdd:COG4372 247 DKEELLEEVILKEIEELELAILVEKDTEEEELEIAA 282
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
203-348 |
1.38e-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: 49.25 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 203 SQLEALQSKLQDLEEENLTLRSEACHLKketityeEKEQQLVNdcvkELRESNSQMVSLTDELSQKNEDLMRH------- 275
Cdd:TIGR04523 496 KELKKLNEEKKELEEKVKDLTKKISSLK-------EKIEKLES----EKKEKESKISDLEDELNKDDFELKKEnlekeid 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 276 --QEEIAQ-------LLSQIVELQHRVKELALEKEELRIHLQASKEAQRQLTNELKELSDRNAECVgmlhesqEEIKDLR 346
Cdd:TIGR04523 565 ekNKEIEElkqtqksLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLS-------SIIKNIK 637
|
..
gi 326668399 347 SK 348
Cdd:TIGR04523 638 SK 639
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
203-347 |
1.38e-05 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 46.82 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 203 SQLEALQSKLQDLEEENLTLRSEACHLKKETITYEEKE---QQLVN---------------------DCVKELRESNSQM 258
Cdd:pfam15619 18 NELAELQSKLEELRKENRLLKRLQKRQEKALGKYEGTEselPQLIArhneevrvlrerlrrlqekerDLERKLKEKEAEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 259 VSLTDELsQKNEDLM--RHQEEIAQLLSQIVELQHRVKELALEKEELRIHLQ-ASKEAQRQLTNELKelsdrnaecvgML 335
Cdd:pfam15619 98 LRLRDQL-KRLEKLSedKNLAEREELQKKLEQLEAKLEDKDEKIQDLERKLElENKSFRRQLAAEKK-----------KH 165
|
170
....*....|..
gi 326668399 336 HESQEEIKDLRS 347
Cdd:pfam15619 166 KEAQEEVKILQE 177
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
230-349 |
1.48e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 230 KKETITYEEKEQQLVNDCVKELRESNSQMVSLTDELSQKNEDLMRHQEEIAQLLSQIVELQHRVKELALEKEELRIHLQA 309
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA 91
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 326668399 310 SKEAQRQLTNELKELSDRNAECVGMLHESQEEIKDLRSKN 349
Cdd:COG4372 92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQR 131
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
140-348 |
1.53e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 140 ERNESLEEQLAQALDQVHQLQHELAKKDELlRMVASASEESETDSSCSTPLRHPVPAGAALALSQLEALQSKLQDLEEEN 219
Cdd:PRK02224 475 ERVEELEAELEDLEEEVEEVEERLERAEDL-VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEA 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 220 LTLRSEAchlkketityEEKEQQlVNDCVKELRESNSQMVSLTDELSQKNeDLMRHQEEIAQLLSQIVELQHRVKELALE 299
Cdd:PRK02224 554 EEKREAA----------AEAEEE-AEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEDEIERLREKREALAEL 621
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 326668399 300 KEELRIHLQASKEAQRQLTNE-----LKELSDRNAECVGMLHESQEEIKDLRSK 348
Cdd:PRK02224 622 NDERRERLAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREE 675
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
139-348 |
1.85e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 139 QERNESLEEQLAQALDQVHQLQHELAKKDELLRMVASASEESETDsscstplrhpvpagAALALSQLEALQSKLQDLEEE 218
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR--------------IAALARRIRALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 219 NLTLRSEACHLKKETITYEEKEQQLVNDCVKELRESNSQMVSLTDELSQKNEDLMRHQEEIAQLLSQIVELQHRVKELAL 298
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 326668399 299 EKEELRIHLQASKEAQRQLTNELKELSDRNAECVGMLHESQEEIKDLRSK 348
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE 214
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
128-348 |
1.98e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 128 GQSLLQRNHVLQERN----ESLEEQLAQALDQVHQLQHELAKKDELLRmvasaseesetdsscstplrhpvpagaalALS 203
Cdd:COG4913 594 DRRRIRSRYVLGFDNraklAALEAELAELEEELAEAEERLEALEAELD-----------------------------ALQ 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 204 QLEALQSKLQDLEEENLTLRSeachLKKEtitYEEKEQQLvndcvKELRESNSQMVSLTDELSQKNEDLMRHQEEIAQLL 283
Cdd:COG4913 645 ERREALQRLAEYSWDEIDVAS----AERE---IAELEAEL-----ERLDASSDDLAALEEQLEELEAELEELEEELDELK 712
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 284 SQIVELQHRVKELALEKEELRIHLQASKEAQRQ-----LTNELKELSDRNAEcVGMLHESQEEIKDLRSK 348
Cdd:COG4913 713 GEIGRLEKELEQAEEELDELQDRLEAAEDLARLelralLEERFAAALGDAVE-RELRENLEERIDALRAR 781
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
113-325 |
2.81e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 47.76 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 113 LLSERDRdLELAARIGQSLLQRNHVLQERNESLEEQLAQALDQVHQLQHELAKKDELLRMVASASEESEtDsscstplrh 192
Cdd:COG0497 211 LEEERRR-LSNAEKLREALQEALEALSGGEGGALDLLGQALRALERLAEYDPSLAELAERLESALIELE-E--------- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 193 pvpagaalALSQLEALQSKLqDLEEENLtlrseachlkketityEEKEQQL--VNDCVKELRESNSQMVSLTDELSQKNE 270
Cdd:COG0497 280 --------AASELRRYLDSL-EFDPERL----------------EEVEERLalLRRLARKYGVTVEELLAYAEELRAELA 334
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 326668399 271 DLMRHQEEIAQLLSQIVELQHRVKELALEKEELRIhlQASKEAQRQLTNELKELS 325
Cdd:COG0497 335 ELENSDERLEELEAELAEAEAELLEAAEKLSAARK--KAAKKLEKAVTAELADLG 387
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
114-330 |
2.85e-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: 47.45 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 114 LSERDRDLELAARIGQSLLQRNHVLQERNESLEEQLAQALDQVHQLQHELAKKDELLRMVASASEESETDSscstplrhp 193
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL--------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 194 vpAGAALALSQLEALQSKLQDLEEENLTLRSEACHLKKETITY----EEKEQQLVNDCVKELRESNSQMVSLTDELSQKN 269
Cdd:COG4942 100 --EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYlkylAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 326668399 270 EDLMRHQEEIAQLLSQIVELQHRVKELALEKEELRIHLQASKEAQRQLTNELKELSDRNAE 330
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
138-350 |
3.40e-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: 47.71 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 138 LQERNESLEEQLAQALDQVHQLQHELAKKDELLRMVASASEESETDSSCSTplrhpvpagaalalSQLEALQSKLQDLEE 217
Cdd:TIGR04523 223 LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQ--------------KELEQNNKKIKELEK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 218 ENLTLRSEACHLKKEtityeeKEQQLVNDCVKELRESNSQMVSLTDELSQKNEDLMRHQEEIAQLLSQI-------VELQ 290
Cdd:TIGR04523 289 QLNQLKSEISDLNNQ------KEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELtnsesenSEKQ 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 291 HRVKE---------------------LALEKEELRIHLQASKEAQRQLTNELKEL-SDRNaecvgmlhESQEEIKDLRSK 348
Cdd:TIGR04523 363 RELEEkqneieklkkenqsykqeiknLESQINDLESKIQNQEKLNQQKDEQIKKLqQEKE--------LLEKEIERLKET 434
|
..
gi 326668399 349 NT 350
Cdd:TIGR04523 435 II 436
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
145-348 |
3.52e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 47.97 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 145 LEEQLAQALDQVHQLQHE--------------LAKKDELLRMVASASEESETDSSCSTPLRHPVPAGAALALSQLEALQS 210
Cdd:PLN02939 147 LNQARLQALEDLEKILTEkealqgkinilemrLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSK 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 211 KLQDLEEENLTLRSEACHLKKETITYE---------EKEQQLVNDCVKEL-------RESNSQMVSLT-DELSQKNEDL- 272
Cdd:PLN02939 227 ELDVLKEENMLLKDDIQFLKAELIEVAeteervfklEKERSLLDASLRELeskfivaQEDVSKLSPLQyDCWWEKVENLq 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 273 ------MRHQEEIAQLLSQIVELQHRVKELALEKEELRIHlQASKEAQRQLTNELKELSDRNAEC-------VGMLHESQ 339
Cdd:PLN02939 307 dlldraTNQVEKAALVLDQNQDLRDKVDKLEASLKEANVS-KFSSYKVELLQQKLKLLEERLQASdheihsyIQLYQESI 385
|
....*....
gi 326668399 340 EEIKDLRSK 348
Cdd:PLN02939 386 KEFQDTLSK 394
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
139-349 |
3.55e-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: 47.71 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 139 QERNESLEEQLAQALDQVHQLQHELAKK----DELLRMVASASEE---SETD-SSCSTPLRHPVpagaalalSQLEALQS 210
Cdd:TIGR04523 306 QDWNKELKSELKNQEKKLEEIQNQISQNnkiiSQLNEQISQLKKEltnSESEnSEKQRELEEKQ--------NEIEKLKK 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 211 KLQDLEEENLTLRSEACHLKKETITYEEKEQQLVNDcVKELRESNSQMVSLTDELSQKNEDLmrhQEEIAQLLSQIVELQ 290
Cdd:TIGR04523 378 ENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQ-IKKLQQEKELLEKEIERLKETIIKN---NSEIKDLTNQDSVKE 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 291 HRVKELALEKEELRIHL-----------QASKEAQRQLTNELKELSDRNAEcvgmLHESQEEIKDLRSKN 349
Cdd:TIGR04523 454 LIIKNLDNTRESLETQLkvlsrsinkikQNLEQKQKELKSKEKELKKLNEE----KKELEEKVKDLTKKI 519
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
194-467 |
3.60e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 194 VPAGAALALSQLEALQSKLQDLEEENLTLRseachlkketityeekeqqlvndcvKELRESNSQMVSLTDELSQKNEDLM 273
Cdd:COG3883 7 AAPTPAFADPQIQAKQKELSELQAELEAAQ-------------------------AELDALQAELEELNEEYNELQAELE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 274 RHQEEIAQLLSQIVELQHRVKELaleKEELRIHLQAS------------------------------------------- 310
Cdd:COG3883 62 ALQAEIDKLQAEIAEAEAEIEER---REELGERARALyrsggsvsyldvllgsesfsdfldrlsalskiadadadlleel 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 311 KEAQRQLTNELKELSDRNAECVGMLHESQEEIKDLRSKNTPSAGLrrhtsyglypMDSIAAEIEGTMRREMSVEEEIAFE 390
Cdd:COG3883 139 KADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAL----------LAQLSAEEAAAEAQLAELEAELAAA 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 326668399 391 DQRSSQKRVFQTVRSVNQSVMRAAAAGPPIPGSGVIMTPVPYQSHTHNTADEDASRGRENSRLGQPGSPGGSALTSA 467
Cdd:COG3883 209 EAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGG 285
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
204-348 |
3.65e-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: 46.07 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 204 QLEALQSKLQDLEEENLTLRSEachLKKETITYEEKEQQLvNDCVKELRESNSQMVSLTDELSQ--KNEDLMRHQEEIAQ 281
Cdd:COG1579 25 RLKELPAELAELEDELAALEAR---LEAAKTELEDLEKEI-KRLELEIEEVEARIKKYEEQLGNvrNNKEYEALQKEIES 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 326668399 282 LLSQIVELQHRVKELALEKEELRIHLQASKEAQRQLTNELKELSDRNAEcvgMLHESQEEIKDLRSK 348
Cdd:COG1579 101 LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE---ELAELEAELEELEAE 164
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
121-413 |
3.79e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.79 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 121 LELAARIGQSLLQRNH--------VLQERNESLEEQLAQALD---QVHQLQHELAKKDELL---RMVASASEESETDSSC 186
Cdd:pfam05483 361 LEELLRTEQQRLEKNEdqlkiitmELQKKSSELEEMTKFKNNkevELEELKKILAEDEKLLdekKQFEKIAEELKGKEQE 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 187 STPLrhpvpagaalalsqLEALQSKLQDLEEENLTLRSEACHLKKETityEEKEQQLVNDCVKELR-ESNSQMVSLTD-E 264
Cdd:pfam05483 441 LIFL--------------LQAREKEIHDLEIQLTAIKTSEEHYLKEV---EDLKTELEKEKLKNIElTAHCDKLLLENkE 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 265 LSQKNED----LMRHQEEI-------AQLLSQIV-----------ELQHRVKELALEKEELRIHLQASKEAQRQLTNEL- 321
Cdd:pfam05483 504 LTQEASDmtleLKKHQEDIinckkqeERMLKQIEnleekemnlrdELESVREEFIQKGDEVKCKLDKSEENARSIEYEVl 583
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 322 ---KELSDRNAECVGM----------LHESQEEIKDLRSKNTpsAGLRRHTSYGLyPMDSIAAEIEGTMRR--EMSVEEE 386
Cdd:pfam05483 584 kkeKQMKILENKCNNLkkqienknknIEELHQENKALKKKGS--AENKQLNAYEI-KVNKLELELASAKQKfeEIIDNYQ 660
|
330 340
....*....|....*....|....*..
gi 326668399 387 IAFEDQRSSQKRVFQTVRSVNQSVMRA 413
Cdd:pfam05483 661 KEIEDKKISEEKLLEEVEKAKAIADEA 687
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
204-347 |
4.79e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 4.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 204 QLEALQSKLQDLEEENLTLRSEACHLkkETITYEEKEQQLVNDCVKELRESNSQMVSLT-DELSQKNEDLMRHQEEIAQL 282
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELREL--EKVLKKESELIKLKELAEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKL 537
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 326668399 283 LSQIVELQHRVKELALEKEELRIHLQASKEAQRQLTNELKELSDRNAECVgmlHESQEEIKDLRS 347
Cdd:PRK03918 538 KGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESV---EELEERLKELEP 599
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
110-346 |
4.86e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 110 VTHLLSERDRDLELAARIGQSLLQRNHVLQERNESLEEQLAQAldqvhQLQHELAKKDELLRMVASASEESetdsscstp 189
Cdd:COG4717 321 LEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL-----QLEELEQEIAALLAEAGVEDEEE--------- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 190 LRHpvpagAALALSQLEALQSKLQDLEEEnLTLRSEACHLKKETITYEEkeqqlvndcvkelresnsqmvsLTDELSQKN 269
Cdd:COG4717 387 LRA-----ALEQAEEYQELKEELEELEEQ-LEELLGELEELLEALDEEE----------------------LEEELEELE 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 270 EDLMRHQEEIAQLLSQIVELQHRVKELALEKEelrihLQASKEAQRQLTNELKELSDRNAE---CVGMLHESQEEIKDLR 346
Cdd:COG4717 439 EELEELEEELEELREELAELEAELEQLEEDGE-----LAELLQELEELKAELRELAEEWAAlklALELLEEAREEYREER 513
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
203-348 |
5.84e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.93 E-value: 5.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 203 SQLEALQSKLQDLEE--ENLT-----LRSEACHL--KKETITYEEK---EQQLVNDCVKELRESNSQMVSLTDELSQ--- 267
Cdd:PHA02562 234 AEIEELTDELLNLVMdiEDPSaalnkLNTAAAKIksKIEQFQKVIKmyeKGGVCPTCTQQISEGPDRITKIKDKLKElqh 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 268 KNEDLMRHQEEIAQLLSQIVELQHRVKELALEKEELRIHLQASKEAQRQLTNELKELSDRNAECVGMLHESQEEIKDLRS 347
Cdd:PHA02562 314 SLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVK 393
|
.
gi 326668399 348 K 348
Cdd:PHA02562 394 T 394
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
122-348 |
5.99e-05 |
|
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: 47.27 E-value: 5.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 122 ELAARIGQSLLQRNHVLQERNESLEEQLAQA----------LDQVHQLQHELAKKDELLRMVASA-SEESETDSSCSTPL 190
Cdd:pfam02463 226 LLYLDYLKLNEERIDLLQELLRDEQEEIESSkqeiekeeekLAQVLKENKEEEKEKKLQEEELKLlAKEEEELKSELLKL 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 191 RHPVpagaALALSQLEALQS---KLQDLEEENLTLRSEACHLKKETITYEEKEQQLVNDCVKELRESNSQMVSLTDELSQ 267
Cdd:pfam02463 306 ERRK----VDDEEKLKESEKekkKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 268 KNEDLMRHQEEIAQLLSQIVELQhrvKELALEKEELRIHLQASKEAQRQLTNELKELSDRNAECVGMLHESQEEIKDLRS 347
Cdd:pfam02463 382 ESERLSSAAKLKEEELELKSEEE---KEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQEL 458
|
.
gi 326668399 348 K 348
Cdd:pfam02463 459 K 459
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
98-304 |
6.14e-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: 6.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 98 EQMTKTYNDIDVVTHLLSERDRDLELAARIGQSLLQRNHVLQERNESLEEQLAQALDQVHQLQHELAK---------KDE 168
Cdd:COG4942 41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEllralyrlgRQP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 169 LLRMVASASEESETDSScSTPLRHPVPAGAAlalsQLEALQSKLQDLEEENLTLRSEachlkKETITYEEKEQQlvndcv 248
Cdd:COG4942 121 PLALLLSPEDFLDAVRR-LQYLKYLAPARRE----QAEELRADLAELAALRAELEAE-----RAELEALLAELE------ 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 326668399 249 KELRESNSQMVSLTDELSQKNEDLMRHQEEIAQLLSQIVELQHRVKELALEKEELR 304
Cdd:COG4942 185 EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
95-347 |
6.21e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 46.75 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 95 DRVEQMTKTYNDI-DVVTHLLS--ERDRDLELAAR-----IGQSLLQRNHVLQERNESLEEQLAQ--------------- 151
Cdd:PRK04778 112 SLLDLIEEDIEQIlEELQELLEseEKNREEVEQLKdlyreLRKSLLANRFSFGPALDELEKQLENleeefsqfveltesg 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 152 ----ALDQVHQLQHELAKKDELLRMVASASEESETDsscstplrhpVPAgaalalsQLEALQSKLQDLEEENLtlrseac 227
Cdd:PRK04778 192 dyveAREILDQLEEELAALEQIMEEIPELLKELQTE----------LPD-------QLQELKAGYRELVEEGY------- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 228 HLKKETItyeEKEQQLVNdcvKELRESNSQMVSLT-DELSQKNEDLmrhQEEIAQLLSQI---VELQHRVKElalEKEEL 303
Cdd:PRK04778 248 HLDHLDI---EKEIQDLK---EQIDENLALLEELDlDEAEEKNEEI---QERIDQLYDILereVKARKYVEK---NSDTL 315
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 326668399 304 RIHLQASKEAQRQLTNELKELSDR---NAECVGMLHESQEEIKDLRS 347
Cdd:PRK04778 316 PDFLEHAKEQNKELKEEIDRVKQSytlNESELESVRQLEKQLESLEK 362
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
122-404 |
7.17e-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: 47.09 E-value: 7.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 122 ELAARigqsLLQRNHVLQERNESLEEQLAQALDQVHQLQHELAKKDELLRMVASASEESEtdsscstplrhpvpagAALA 201
Cdd:pfam01576 61 EMRAR----LAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEE----------------AARQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 202 LSQLE--ALQSKLQDLEEENLTLRSEACHLKKETITYEEKEQQLVNDCVKE---------LRESNSQMVSLTDELSQKNE 270
Cdd:pfam01576 121 KLQLEkvTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEeekakslskLKNKHEAMISDLEERLKKEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 271 DLMRHQEEIA-QLLSQIVELQHRVKELALEKEELRIHLQA-SKEAQRQLTNELKELSDRNA------ECVGMLHESQEEI 342
Cdd:pfam01576 201 KGRQELEKAKrKLEGESTDLQEQIAELQAQIAELRAQLAKkEEELQAALARLEEETAQKNNalkkirELEAQISELQEDL 280
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 326668399 343 KDLRSKNTPSAGLRRHTSYGLYPM--------DSIAAEIEGTMRREMSVEE-EIAFEDQRSSQKRVFQTVR 404
Cdd:pfam01576 281 ESERAARNKAEKQRRDLGEELEALkteledtlDTTAAQQELRSKREQEVTElKKALEEETRSHEAQLQEMR 351
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
209-343 |
8.06e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 8.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 209 QSKLQDLEEE-NLTL---RSEACHLKKETIT-YEEKEQQLVNDCVKELRESNSQMVSLTDELSQKNEDLMRHQEEI---- 279
Cdd:PRK12704 30 EAKIKEAEEEaKRILeeaKKEAEAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLekre 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 326668399 280 AQLLSQIVELQHRVKELALEKEEL-RIHLQASKEAQR--QLTNE------LKELSDR-NAECVGMLHESQEEIK 343
Cdd:PRK12704 110 EELEKKEKELEQKQQELEKKEEELeELIEEQLQELERisGLTAEeakeilLEKVEEEaRHEAAVLIKEIEEEAK 183
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
133-327 |
1.04e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 133 QRNHVLQERNESLEEQLAQALDQVHQLQHELAKKDELLRMVASASEESETDsscstplrhpvpagaalalsQLEALQSKL 212
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGD--------------------RLEQLEREI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 213 QDLEEEnltlrseachlkKETItyEEKEQQLVNDCvkelresnsQMVSLTDELSQknEDLMRHQEEIAQLLSQIVELQHR 292
Cdd:COG4913 348 ERLERE------------LEER--ERRRARLEALL---------AALGLPLPASA--EEFAALRAEAAALLEALEEELEA 402
|
170 180 190
....*....|....*....|....*....|....*
gi 326668399 293 VKElalEKEELRIHLQASKEAQRQLTNELKELSDR 327
Cdd:COG4913 403 LEE---ALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
140-346 |
1.10e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 140 ERNESLEEQLAQALDQVHQLQHELAKKDELLRMVASASEESETDsscstplrhpvpagAALALSQLEALQSKLQDLEEEN 219
Cdd:PRK02224 223 ERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRET--------------IAETEREREELAEEVRDLRERL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 220 LTLRSEACHLKKETiTYEEKEQQLVNDCVKELRESNSQmvsLTDELSQKNEDLMRHQEEIAQLLSQIVELQHRVKELALE 299
Cdd:PRK02224 289 EELEEERDDLLAEA-GLDDADAEAVEARREELEDRDEE---LRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREE 364
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 326668399 300 KEELRIHLQASKEAQRQLTNELKELSDR---NAECVGMLHESQEEIKDLR 346
Cdd:PRK02224 365 AAELESELEEAREAVEDRREEIEELEEEieeLRERFGDAPVDLGNAEDFL 414
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
138-345 |
1.25e-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: 45.53 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 138 LQERNESLEEQLAQALDQVHQLQHELAKKDEllRMVASASEESETDsscstplrhpvpAGAALALSQLEALQSKLQDLEE 217
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALER--RIAALARRIRALE------------QELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 218 ENLTLRSEachLKKETITYEEKEQQ------LVNDCVKELRESNSQMVSLTDELSQKNEDLMRHQEEIAQLLSQIVELQH 291
Cdd:COG4942 98 ELEAQKEE---LAELLRALYRLGRQpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 326668399 292 RVKELALEKEELRIHLQASKEAQRQLTNELKELSDRNAECVGMLHESQEEIKDL 345
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
122-313 |
1.73e-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: 45.14 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 122 ELAARIGQsLLQRNHVLQERNESLEEQLAQALDQVHQLQHELAK-KDELLRMVASASEESETDsscstPLRHPV-PAGAA 199
Cdd:COG4942 59 ALERRIAA-LARRIRALEQELAALEAELAELEKEIAELRAELEAqKEELAELLRALYRLGRQP-----PLALLLsPEDFL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 200 LALSQLEALQSKLQDLEEENLTLRSEACHLKKETITYEEKEQQLVndcvKELRESNSQMVSLTDELSQKNEDLMRHQEEI 279
Cdd:COG4942 133 DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE----ALLAELEEERAALEALKAERQKLLARLEKEL 208
|
170 180 190
....*....|....*....|....*....|....
gi 326668399 280 AQLLSQIVELQHRVKELALEKEELRIHLQASKEA 313
Cdd:COG4942 209 AELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
98-346 |
2.42e-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: 45.34 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 98 EQMTKTYNDIDVVTHLLSERDRDLELAARIGQSLLQRNHVLQERNESLEEQLAQALDQVHQLQHELAKKDELlrmvasas 177
Cdd:TIGR00618 211 PCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEET-------- 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 178 eESETDSSCSTplrhpvpagAALALSQlEALQSKLQDLEEENLTLrseachlkKETITYEEKEQQLVNDCVKELRESNSQ 257
Cdd:TIGR00618 283 -QERINRARKA---------APLAAHI-KAVTQIEQQAQRIHTEL--------QSKMRSRAKLLMKRAAHVKQQSSIEEQ 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 258 MVSLTDELSQKNEDLMRHQEE--IAQLLSQIVELQHRVKELALEKEELRIHLQASKEAQRQLTNE----LKELSDRNAEC 331
Cdd:TIGR00618 344 RRLLQTLHSQEIHIRDAHEVAtsIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREqatiDTRTSAFRDLQ 423
|
250
....*....|....*
gi 326668399 332 VGMLHESQEEIKDLR 346
Cdd:TIGR00618 424 GQLAHAKKQQELQQR 438
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
200-348 |
2.50e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 200 LALSQLEALQSKLQDLEEENLTLRSEACHLKKETITYEEKEQQLvndcvKELRESNSQM------VSLTDELSQKNEDLM 273
Cdd:COG4717 68 LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAEL-----EELREELEKLekllqlLPLYQELEALEAELA 142
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 326668399 274 RHQEEIAQLLSQIVELQHRVKELALEKEELRIHLQASKEAQRQLT----NELKELSDRNAECVGMLHESQEEIKDLRSK 348
Cdd:COG4717 143 ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlateEELQDLAEELEELQQRLAELEEELEEAQEE 221
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
201-348 |
2.94e-04 |
|
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: 45.05 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 201 ALSQLEALQ---SKLQDLEEEnltLRSEACHLKKE---TITYEEKEQQL-----------VNDCVKELRESNSQMVSLTD 263
Cdd:TIGR02168 177 TERKLERTRenlDRLEDILNE---LERQLKSLERQaekAERYKELKAELrelelallvlrLEELREELEELQEELKEAEE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 264 ELSQKNEDLMRHQEEIAQLLSQIVEL-------QHRVKELALEKEELRIHLQASKEAQRQLTNELKELSDRNAECVGMLH 336
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELeeeieelQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
|
170
....*....|..
gi 326668399 337 ESQEEIKDLRSK 348
Cdd:TIGR02168 334 ELAEELAELEEK 345
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
82-345 |
3.07e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.96 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 82 QNGSNSLSKVLSADRVEQMTKTYNDIDVvtHLLSERDRDLELaarigqslLQRNHVLQERNESLEEQLAQALDqvhqlqh 161
Cdd:TIGR00618 635 QQCSQELALKLTALHALQLTLTQERVRE--HALSIRVLPKEL--------LASRQLALQKMQSEKEQLTYWKE------- 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 162 ELAKKDELLRmvasaseESETDSSCSTPLRHPVPAGAALALSQLEALQSKLQDLEEENLTLRSEAChlKKETITYEEKEQ 241
Cdd:TIGR00618 698 MLAQCQTLLR-------ELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVL--KARTEAHFNNNE 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 242 QLVNDcvkelRESNSQMVSLTDELSQKNEDLMRHQEEIAQLLSQI-VELQHRVKELALEKEELRIHLQASK---EAQRQL 317
Cdd:TIGR00618 769 EVTAA-----LQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIgQEIPSDEDILNLQCETLVQEEEQFLsrlEEKSAT 843
|
250 260
....*....|....*....|....*...
gi 326668399 318 TNELKELSDRNAECVGMLHESQEEIKDL 345
Cdd:TIGR00618 844 LGEITHQLLKYEECSKQLAQLTQEQAKI 871
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
217-321 |
3.32e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 217 EENLTLRSEACHLKKETityeEKEQQLVNDCVKELRESNSQMVSLTDELSQKNEDL------MRHQEEIAQLLSQIVELQ 290
Cdd:PRK04863 286 EEALELRRELYTSRRQL----AAEQYRLVEMARELAELNEAESDLEQDYQAASDHLnlvqtaLRQQEKIERYQADLEELE 361
|
90 100 110
....*....|....*....|....*....|....*...
gi 326668399 291 HR-------VKELALEKEELRIHLQASKEAQRQLTNEL 321
Cdd:PRK04863 362 ERleeqnevVEEADEQQEENEARAEAAEEEVDELKSQL 399
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
143-326 |
3.32e-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: 43.92 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 143 ESLEEQLAQALDQVHQLQHEL--------AKKDELLRMVASASEESETDSSCSTPLRhpvpagaalALSQLEA-LQSKLQ 213
Cdd:pfam04108 115 EILRDALKELIDELQAAQESLdsdlkrfdDDLRDLQKELESLSSPSESISLIPTLLK---------ELESLEEeMASLLE 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 214 DLE---EENLTLRSEACHLKKETITYEEKEQQLVNDCVKELRESNSQMVSLTDELSQKNEDLMRHQEEIAQLLSQIVELQ 290
Cdd:pfam04108 186 SLTnhyDQCVTAVKLTEGGRAEMLEVLENDARELDDVVPELQDRLDEMENNYERLQKLLEQKNSLIDELLSALQLIAEIQ 265
|
170 180 190
....*....|....*....|....*....|....*.
gi 326668399 291 HRVKELALEKEELRIHLQASKEAQRQLTNELKELSD 326
Cdd:pfam04108 266 SRLPEYLAALKEFEERWEEEKETIEDYLSELEDLRE 301
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
139-442 |
3.33e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 44.56 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 139 QERNESLEEQLAQALDQVHQLQHELAKKDELLRMVASASEESETDSSC--STPLRHPVPAGAALALSQLEALQSKLQDLE 216
Cdd:COG5185 274 AESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAeaEQELEESKRETETGIQNLTAEIEQGQESLT 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 217 EENLTLRSEACHLKKETItYEEKEQQL--VNDCVKELRESNSQMV------------SLTDELSQKNEDLMRHQEEIAQL 282
Cdd:COG5185 354 ENLEAIKEEIENIVGEVE-LSKSSEELdsFKDTIESTKESLDEIPqnqrgyaqeilaTLEDTLKAADRQIEELQRQIEQA 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 283 LSQIVELQHRVKELALEKEelRIHLQASKEAQRQLTNELKELSDRNAEcvgMLHESQEEIKDLRSK-NTPSAGL---RRH 358
Cdd:COG5185 433 TSSNEEVSKLLNELISELN--KVMREADEESQSRLEEAYDEINRSVRS---KKEDLNEELTQIESRvSTLKATLeklRAK 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 359 TSYGLYPMDSIAAEIEGTMRREMsVEEEIAFEDQRSSQKRVFQTVRSVNQSVMRAAAAgppiPGSGVIMTPVPYQSHTHN 438
Cdd:COG5185 508 LERQLEGVRSKLDQVAESLKDFM-RARGYAHILALENLIPASELIQASNAKTDGQAAN----LRTAVIDELTQYLSTIES 582
|
....
gi 326668399 439 TADE 442
Cdd:COG5185 583 QQAR 586
|
|
| DUF4456 |
pfam14644 |
Domain of unknown function (DUF4456); This domain family is found in bacteria and eukaryotes, ... |
221-348 |
5.00e-04 |
|
Domain of unknown function (DUF4456); This domain family is found in bacteria and eukaryotes, and is approximately 210 amino acids in length. There is a single completely conserved residue E that may be functionally important.
Pssm-ID: 464232 Cd Length: 209 Bit Score: 42.66 E-value: 5.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 221 TLRSEACHLKKETITYEEKEQQLVNDCVKELREsnsQMVSLTDELSQKNEDLM-----RHQEEIAQLLSQIV-ELQHRVK 294
Cdd:pfam14644 26 TFEQCAENIQQKLLSYQEQADEYHNSCLQELRN---QVERLEELLPSVPELIFesllkRHLQKLERAMKNIAaEFSQKQK 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 326668399 295 ELALEKE----ELRIHLQASKEAQrqltnELKEL----SDRNAECVGMLHESQEEIKDLRSK 348
Cdd:pfam14644 103 QLEQLKQqheqQLRPTLGHPQNAQ-----ELEQLcdreEDRQKEHIELIQAHREALLEAVDK 159
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
202-348 |
5.09e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 202 LSQLEALQSKLQDLEEENLTLRSEACHLKKETITYEEKEQQLVNDCVKELRESNSQMVSLTDELSQKNEDLMRHQEEIAQ 281
Cdd:PRK03918 502 AEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEE 581
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 326668399 282 L-LSQIVELQHRVKELA------LE----KEELRIHLQASKEAQRQLTNELKELSDRNAEcvgmLHESQEEIKDLRSK 348
Cdd:PRK03918 582 LgFESVEELEERLKELEpfyneyLElkdaEKELEREEKELKKLEEELDKAFEELAETEKR----LEELRKELEELEKK 655
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
203-345 |
5.77e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 5.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 203 SQLEALQSKLQDLEEENLTLRSEACHLKKEtityeekeqqlvndcvkeLRESNSQMVSLTDELSQKNEDLMRHQEEIAQL 282
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEK------------------RDELNEELKELAEKRDELNAQVKELREEAQEL 62
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 326668399 283 LSQIVELQHRVKELALEKEELRIHLQASKEAQRQLTNELKELSDRNAEcvgmLHESQEEIKDL 345
Cdd:COG1340 63 REKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGS----IDKLRKEIERL 121
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
112-348 |
5.82e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 43.97 E-value: 5.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 112 HLLSERDR---DLELAARIGQSLLQRnhvLQERNESLEEQLAQAldqVHQLQHELAKKDELLRMVASaseesetdsscst 188
Cdd:pfam07111 485 QLREERNRldaELQLSAHLIQQEVGR---AREQGEAERQQLSEV---AQQLEQELQRAQESLASVGQ------------- 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 189 plrhpvpagaalalsQLEALQSKLQDLEEENLTLRSEachLKKETITYEEKEQQLVNDCVKELREsnsqmvsltdELSQK 268
Cdd:pfam07111 546 ---------------QLEVARQGQQESTEEAASLRQE---LTQQQEIYGQALQEKVAEVETRLRE----------QLSDT 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 269 NEDLMRHQEEIAQLLSQIVELQHRVKELALEKEEL-RIHLQASKEAQRQLTNELKELS-DRNAecvgMLHESQEEIKDLR 346
Cdd:pfam07111 598 KRRLNEARREQAKAVVSLRQIQHRATQEKERNQELrRLQDEARKEEGQRLARRVQELErDKNL----MLATLQQEGLLSR 673
|
..
gi 326668399 347 SK 348
Cdd:pfam07111 674 YK 675
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
197-416 |
7.60e-04 |
|
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: 43.51 E-value: 7.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 197 GAALALSQLEALQSKLQDLEEENLTLRSEACHLKKETITYEEKEQQLVNdcvkELRESNSQMVSLTDELSQKNEDLMRHQ 276
Cdd:TIGR02168 664 GSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEE----ELEQLRKELEELSRQISALRKDLARLE 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 277 EEIAQLLSQIVELQHRVKELALEKEELRIHLQASKEAqrqltnelkelsdrnaecvgmLHESQEEIKDLRskntpsaglr 356
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE---------------------LAEAEAEIEELE---------- 788
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 326668399 357 rhtsyglypmdsiaAEIEGTMRREMSVEEEI-AFEDQRSSQKRVFQTVRSVNQSVMRAAAA 416
Cdd:TIGR02168 789 --------------AQIEQLKEELKALREALdELRAELTLLNEEAANLRERLESLERRIAA 835
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
114-304 |
7.74e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 7.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 114 LSERDRDL-ELAARIGQSLLQRNHvLQERNESLEEQLAQALDQVHQLQHELAKKDELLRMVASASEESETDSscstplrh 192
Cdd:COG1579 12 LQELDSELdRLEHRLKELPAELAE-LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 193 pvpaGAALALSQLEALQSKLQDLEEENLTLRSEACHLKKEtityEEKEQQLVNDCVKELRESNSQMVSLTDELSQKNEDL 272
Cdd:COG1579 83 ----GNVRNNKEYEALQKEIESLKRRISDLEDEILELMER----IEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
|
170 180 190
....*....|....*....|....*....|...
gi 326668399 273 mrhQEEIAQLLSQIVELQHRVKELALEK-EELR 304
Cdd:COG1579 155 ---EAELEELEAEREELAAKIPPELLALyERIR 184
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
203-462 |
9.28e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 9.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 203 SQLEALQSKLQDLEEENLTLRSEACHLKKETITYEEKEQQLVNDCVKELR----------------ESNS-----QMVSL 261
Cdd:COG3883 44 AELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARalyrsggsvsyldvllGSESfsdflDRLSA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 262 TDELSQKNEDLMRH----QEEIAQLLSQIVELQHRVKELALEKEELRIHLQASKEAQRQLTNELKELSDRNAECVGMLHE 337
Cdd:COG3883 124 LSKIADADADLLEElkadKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 338 SQEEIKDLRSKNTPSAGLRRHTSYGLYPMDSIAAEIEGTMRREMSVEEEIAFEDQRSSQkrVFQTVRSVNQSVMRAAAAG 417
Cdd:COG3883 204 ELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSA--GAAGAAAGAAGAGAAAASA 281
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 326668399 418 PPIPGSGVIMTPVPYQSHTHNTADEDASRGRENSRLGQPGSPGGS 462
Cdd:COG3883 282 AGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGA 326
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
101-342 |
1.02e-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: 43.13 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 101 TKTYNDIDVVTHLLSERDRDLELAARIgqsllqrNHVLQERNESLEEQLAQALDQVHQLQHELAKkDELLRMvASASEES 180
Cdd:pfam05911 630 IKKHDCIDKVTLSENKVAQVDNGCSEI-------DNLSSDPEIPSDGPLVSGSNDLKTEENKRLK-EEFEQL-KSEKENL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 181 ETDSSCSTplrhpvpagaalalSQLEALQSKLQDLEE--ENLTLRSEAC---------HLKKETITYEEKEQQLVnDCVK 249
Cdd:pfam05911 701 EVELASCT--------------ENLESTKSQLQESEQliAELRSELASLkesnslaetQLKCMAESYEDLETRLT-ELEA 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 250 ELRESNSQMVSLTDELSQKNEDlmrHQEEIAQLLsqivELQHRVKelALEKEELRIHLQASKEAQRQLTNELKELSDRNA 329
Cdd:pfam05911 766 ELNELRQKFEALEVELEEEKNC---HEELEAKCL----ELQEQLE--RNEKKESSNCDADQEDKKLQQEKEITAASEKLA 836
|
250
....*....|...
gi 326668399 330 ECvgmlhesQEEI 342
Cdd:pfam05911 837 EC-------QETI 842
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
114-346 |
1.05e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 114 LSERDRDLElaarigqsllQRNHVLQERNESLEEQLAQALDQVHQLQHELAKKDELLRMVASASEESETDSSCSTPLRhp 193
Cdd:PRK02224 347 LREDADDLE----------ERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL-- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 194 vpagaALALSQLEALQSKLQDLE----------EENLTLRSEA--------------------CHLKKETITYEEKEQQL 243
Cdd:PRK02224 415 -----EELREERDELREREAELEatlrtarervEEAEALLEAGkcpecgqpvegsphvetieeDRERVEELEAELEDLEE 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 244 VNDCVKELRESNSQMVSLTDELSQKNEDLMRHQEEIAQLLSQIVELQHRVKELALEKEELRihlqASKEAQRQLTNELKE 323
Cdd:PRK02224 490 EVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELE----AEAEEKREAAAEAEE 565
|
250 260
....*....|....*....|...
gi 326668399 324 LSDRNAECVGMLHESQEEIKDLR 346
Cdd:PRK02224 566 EAEEAREEVAELNSKLAELKERI 588
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
119-360 |
1.08e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.14 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 119 RDLELAARIGQSLLQRNHVLQERNESLEEQLAQALDQVHQLQHELAKKDELLRMVASASEE-----SETDSSCSTPLRHP 193
Cdd:COG5022 843 KAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLEleseiIELKKSLSSDLIEN 922
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 194 VPAGAALAL--------SQLEALQSKLQDLEEENLTLRSEACHLKKETITYEEKEQQLvNDCVKELRESNSQMVSLTDEL 265
Cdd:COG5022 923 LEFKTELIArlkkllnnIDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKS-TILVREGNKANSELKNFKKEL 1001
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 266 SQKNEDLMRHQEEIAQL---LSQIVELQHRVKELALEKEELRIHLQASK------EAQRQLTNELKELSDRNAECVGMLH 336
Cdd:COG5022 1002 AELSKQYGALQESTKQLkelPVEVAELQSASKIISSESTELSILKPLQKlkglllLENNQLQARYKALKLRRENSLLDDK 1081
|
250 260 270
....*....|....*....|....*....|....*
gi 326668399 337 -----ESQE------EIKDLRSKNTPSAGLRRHTS 360
Cdd:COG5022 1082 qlyqlESTEnllktiNVKDLEVTNRNLVKPANVLQ 1116
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
168-348 |
1.27e-03 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 42.00 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 168 ELLRMVASASEESETDSSCSTPLRHPVPAGAALALS-QLEALQSKLQDLEEENLTLrseachlKKETITYEEKeqqlVND 246
Cdd:pfam15294 90 ELLEQIAEFEEREFTSSNKKPNFELNKPKLEPLNEGgGSALLHMEIERLKEENEKL-------KERLKTLESQ----ATQ 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 247 CVKELRESNSQMVSLTDELSQKNeDLMRHQEEIAQLLSQI----VELQHRVKELALEKEELRIHLQASK----EAQRQLT 318
Cdd:pfam15294 159 ALDEKSKLEKALKDLQKEQGAKK-DVKSNLKEISDLEEKMaalkSDLEKTLNASTALQKSLEEDLASTKhellKVQEQLE 237
|
170 180 190
....*....|....*....|....*....|....*.
gi 326668399 319 NELKELSDRNAECVG------MLHESQEEIKDLRSK 348
Cdd:pfam15294 238 MAEKELEKKFQQTAAyrnmkeMLTKKNEQIKELRKR 273
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
203-324 |
1.38e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 203 SQLEALQSKLQDLEEENLTLRSEACHLKKETITYEEKeQQLVNDcVKELRESNSQMVSLTDELSQKNEDLMRHQEEIAQL 282
Cdd:COG1579 45 ARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ-LGNVRN-NKEYEALQKEIESLKRRISDLEDEILELMERIEEL 122
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 326668399 283 LSQIVELQHRVK----ELALEKEELRIHLQASKEAQRQLTNELKEL 324
Cdd:COG1579 123 EEELAELEAELAeleaELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
203-343 |
1.41e-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: 42.70 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 203 SQLEALQSKLQDLEEENLTLRSEACHLKKETityeEKEQQLVNDCVKELRESNsQMVSLTDELSQKNEdlmrhqeeiaQL 282
Cdd:TIGR04523 152 KELEKLNNKYNDLKKQKEELENELNLLEKEK----LNIQKNIDKIKNKLLKLE-LLLSNLKKKIQKNK----------SL 216
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 326668399 283 LSQIVELQHRVKELALEKEELRIHLQASKEAQRQLTNELKELSDRNAECVGMLHESQEEIK 343
Cdd:TIGR04523 217 ESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELE 277
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
93-348 |
1.42e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 93 SADRVEQMTKTYNDIDVVTHLLSERDRDLELAARIGQSLLQRNHVLQERNESLEEQLAQALDQVHQLQhELAKKDELLRM 172
Cdd:PRK03918 291 KAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELE-ERHELYEEAKA 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 173 VASASEESETDSSCSTPlrhpvpagaalalsqlEALQSKLQDLEEENLTLRSEACHLKKETITYEEKEQQLvNDCVKELR 252
Cdd:PRK03918 370 KKEELERLKKRLTGLTP----------------EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL-KKAIEELK 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 253 ESNSQMVSLTDELSQKNE-DLMR-HQEEIAQLLSQIVELQHRVKELALEKEELRIHLQASKE--AQRQLTNELKELSDR- 327
Cdd:PRK03918 433 KAKGKCPVCGRELTEEHRkELLEeYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKl 512
|
250 260
....*....|....*....|....
gi 326668399 328 ---NAEcvgMLHESQEEIKDLRSK 348
Cdd:PRK03918 513 kkyNLE---ELEKKAEEYEKLKEK 533
|
|
| NIP100 |
COG5244 |
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ... |
117-401 |
1.58e-03 |
|
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227569 [Multi-domain] Cd Length: 669 Bit Score: 42.36 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 117 RDRDLELAARIGQSLLQRNHVLQERNESL--EEQLAQALDQVHQLQHELAkkdellrmvaSASEESETDSSCSTPLRhpv 194
Cdd:COG5244 57 KKRHGIFIRPDDDSLLNGNAAYEKIKGGLvcESKGMDKDGEIKQENHEDR----------IHFEESKIRRLEETIEA--- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 195 pagaalaLSQLEalqsklqdlEEENLTLRSEACHLKKETITYEEKEQQLVNDcvkelRESNSQMVSlTDELSQKNEDLMR 274
Cdd:COG5244 124 -------LKSTE---------KEEIVELRRENEELDKINLSLRERISSEEPE-----LNKDGSKLS-YDELKEFVEESRV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 275 HQEEIAQLLSQIVELQHRVKELALE--KEELRihlqasKEAQRQLTNE---LKELSDRNAecvGMLHESQEEIKDLRSKN 349
Cdd:COG5244 182 QVYDMVELVSDISETLNRNGSIQRSsvRECER------SNIHDVLFLVngiLDGVIDELN---GELERLRRQLVSLMSSH 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 326668399 350 tpsaglrrhtsyglypmdsiAAEIEGTMRREMSVEEEIAFEDQ-RSSQKRVFQ 401
Cdd:COG5244 253 --------------------GIEVEENSRLKATLEKFQSLELKvNTLQEELYQ 285
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
138-330 |
1.76e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 138 LQERNESLEEQLAQALDQVHQLQHELAKKDELLRMVASASEESETDSScstplrhpvpagaalALSQLeaLQSK-LQDLE 216
Cdd:COG3883 56 LQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVS---------------YLDVL--LGSEsFSDFL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 217 EENLTLRSEACHLKKETITYEEKEQQLVNDcVKELRESNSQMVSLTDELSQKNEDLMRHQEEIAQLLSQiveLQHRVKEL 296
Cdd:COG3883 119 DRLSALSKIADADADLLEELKADKAELEAK-KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQ---LSAEEAAA 194
|
170 180 190
....*....|....*....|....*....|....
gi 326668399 297 ALEKEELRIHLQASKEAQRQLTNELKELSDRNAE 330
Cdd:COG3883 195 EAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
143-373 |
2.41e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 143 ESLEEQLAQALDQVHQLQHELAKKDEL---LRMVASASEESETD-SSCSTPLRHpvpagaaLALSQLEALQSKLQDLEE- 217
Cdd:PRK03918 528 EKLKEKLIKLKGEIKSLKKELEKLEELkkkLAELEKKLDELEEElAELLKELEE-------LGFESVEELEERLKELEPf 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 218 --ENLTLRSeACHLKKETITYEEKEQQLVNDCVKELRESNSQMVSLTDELSQKN------------EDLMRHQEEIAQLL 283
Cdd:PRK03918 601 ynEYLELKD-AEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEkkyseeeyeelrEEYLELSRELAGLR 679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 284 SQIVELQHRVKELALEKEELRIHLQASKEAQRQLTNELKELSDrnaecvgmLHESQEEIKDLRSKntpsagLRRHtsyGL 363
Cdd:PRK03918 680 AELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALER--------VEELREKVKKYKAL------LKER---AL 742
|
250
....*....|
gi 326668399 364 YPMDSIAAEI 373
Cdd:PRK03918 743 SKVGEIASEI 752
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
139-350 |
2.54e-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: 41.88 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 139 QERNESLEEQLAqaLDQVHQLQHELAKKDELLRMVASA-SEESETDSSCSTPLRHPVPAgaalalsQLEALQSKLQDLEE 217
Cdd:TIGR00618 163 KEKKELLMNLFP--LDQYTQLALMEFAKKKSLHGKAELlTLRSQLLTLCTPCMPDTYHE-------RKQVLEKELKHLRE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 218 ENLTLRSEACHLKKETITYEEKE--QQLVNDCVKELRESNSQMVSLTD-----ELSQKNEDLMRHQEEIAQLLSQI---- 286
Cdd:TIGR00618 234 ALQQTQQSHAYLTQKREAQEEQLkkQQLLKQLRARIEELRAQEAVLEEtqeriNRARKAAPLAAHIKAVTQIEQQAqrih 313
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 326668399 287 VELQHRVKELALEKEELRIHL--QASKEAQRQLTNELKELSDRNAEcvgmLHESQEEIKDLRSKNT 350
Cdd:TIGR00618 314 TELQSKMRSRAKLLMKRAAHVkqQSSIEEQRRLLQTLHSQEIHIRD----AHEVATSIREISCQQH 375
|
|
| Kre28 |
pfam17097 |
Spindle pole body component; In Saccharomyces cerevisae Kre28 and Spc105 form a kinetochore ... |
144-360 |
2.57e-03 |
|
Spindle pole body component; In Saccharomyces cerevisae Kre28 and Spc105 form a kinetochore microtubule binding complex, which bridges between centromeric heterochromatin and kinetochore MAPs (microtubule associated protein, such as Bim1, Bik1 and SIk19) and motors (Cin8, Kar3). It may be regulated by sumoylation.
Pssm-ID: 407241 [Multi-domain] Cd Length: 360 Bit Score: 41.33 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 144 SLEEQLAQALDQV--HQLQHELAKKDELLRMVASASEES---ETDSSCSTPLRHPvpagaalalsqlEALQSKLQDLEEE 218
Cdd:pfam17097 15 ELEEQTAHSSEQVltEQDKRLLGALRELTQSVIQLIEENslvTVSGDAANLLIDP------------SGIEVKIRQLDQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 219 NLTLRSeaCHLKKETITYEEKEQQLVNDCVKELRESNSQMVSLTDELSQ-KNEDLMRHQEEIAQLLSQIVEL-------Q 290
Cdd:pfam17097 83 VELLKV--THLEQETLDNFLRYTISSTDLLQLESVSDPKYASLEDEVSQlEDDTLTVLNQEIDQIKGDILQVaqeiadkQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 291 HRVKELAL--------------EKEELRihlqaskeaqRQLTNELKELSDRNAECVGMLHESQEEIKDLRSKNTPSAGLR 356
Cdd:pfam17097 161 DQVNELCLetsneldecwellnELERLR----------DQRITVEEQTSNEKDTELDPVEETYEEWKSLQESLQQLEHLK 230
|
....
gi 326668399 357 RHTS 360
Cdd:pfam17097 231 EELD 234
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
213-406 |
2.63e-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: 41.42 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 213 QDLEEENLTLRSEACHLKKETITYEEKeqqlvndcVKELRESNSQMVSLTDELSQKNEDLMRHQEEIAQllsQIVELQHR 292
Cdd:pfam07888 69 EQWERQRRELESRVAELKEELRQSREK--------HEELEEKYKELSASSEELSEEKDALLAQRAAHEA---RIRELEED 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 293 VKELALEKEELRIHLQASKEAQRQLTNELKELSDRNAECVGMLHESQEEikdLRSKNTPSAGLRRH----TSYGLYPMDS 368
Cdd:pfam07888 138 IKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEE---LRSLSKEFQELRNSlaqrDTQVLQLQDT 214
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 326668399 369 IAA---EIEGTMRREmsVEEEIAFEDQRSSQKRVFQTVRSV 406
Cdd:pfam07888 215 ITTltqKLTTAHRKE--AENEALLEELRSLQERLNASERKV 253
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
204-352 |
2.94e-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: 41.59 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 204 QLEALQSKLQDLEEENLTLRSEACHLKKETITYeekeQQLVNDCVKELREsnsqmvsLTDELSQKNEDLMRHQEEIAQLL 283
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDEL----SQELSDASRKIGE-------IEKEIEQLEQEEEKLKERLEELE 743
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 326668399 284 SQIVELQHRVKELALEKEELRihlqaskeaqrqltnelKELSDRNAEcvgmLHESQEEIKDLRSKNTPS 352
Cdd:TIGR02169 744 EDLSSLEQEIENVKSELKELE-----------------ARIEELEED----LHKLEEALNDLEARLSHS 791
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
116-325 |
3.47e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 116 ERDRDlELAARIgqsllqrnHVLQERNESLEEQLAQALDQ----------VHQLQHELAKKDELLRmvaSASEESETDss 185
Cdd:PRK02224 271 ERERE-ELAEEV--------RDLRERLEELEEERDDLLAEaglddadaeaVEARREELEDRDEELR---DRLEECRVA-- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 186 cstplrhpvpagAALALSQLEALQSKLQDLEEENLTLRSEACHLKKEtityeekeqqlVNDCVKELRESnsqmvsltdel 265
Cdd:PRK02224 337 ------------AQAHNEEAESLREDADDLEERAEELREEAAELESE-----------LEEAREAVEDR----------- 382
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 266 sqknedlmrhQEEIAQLLSQIVELQHRVKELALEKEELRIHLQASKEAQRQLTNELKELS 325
Cdd:PRK02224 383 ----------REEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELE 432
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
84-305 |
3.65e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 84 GSNSLSKVLS--ADRVEQMTKTYNDI---------DVVTHLLSERDRDLELAARIGQSLLQRNHVLQERNESLEEQlAQA 152
Cdd:PHA02562 178 ELNQQIQTLDmkIDHIQQQIKTYNKNieeqrkkngENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDP-SAA 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 153 LDQVHQLQHELAKKDELLRMVASASEESETDSSCSTPLRHPVPAGAALALS------QLEALQSKLQDLEE---ENLTLR 223
Cdd:PHA02562 257 LNKLNTAAAKIKSKIEQFQKVIKMYEKGGVCPTCTQQISEGPDRITKIKDKlkelqhSLEKLDTAIDELEEimdEFNEQS 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 224 SEACHLKKEtitYEEKEQQLVNdcvkeLRESNSQMVSLTDELSQKNEDlmrHQEEIAQLLSQIVELQHRVKELALEKEEL 303
Cdd:PHA02562 337 KKLLELKNK---ISTNKQSLIT-----LVDKAKKVKAAIEELQAEFVD---NAEELAKLQDELDKIVKTKSELVKEKYHR 405
|
..
gi 326668399 304 RI 305
Cdd:PHA02562 406 GI 407
|
|
| ZapB |
COG3074 |
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ... |
237-296 |
3.70e-03 |
|
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442308 [Multi-domain] Cd Length: 79 Bit Score: 37.26 E-value: 3.70e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 326668399 237 EEKEQQLVNDC------VKELRESNSQMVSLTDELSQKNEDLmrhQEEIAQLLSQIVELQHRVKEL 296
Cdd:COG3074 10 EAKVQQAVDTIellqmeVEELKEKNEELEQENEELQSENEEL---QSENEQLKTENAEWQERIRSL 72
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
138-321 |
3.99e-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: 41.31 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 138 LQERNESLEEQLAQALDQVHQLQHELAKKDELLRMVASASEESETDSSCSTPLRHPVPAGAALALSQLEALQSKLQDLE- 216
Cdd:pfam01576 733 LQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQr 812
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 217 --EENLTLRSEACHLKKETityEEKEQQLVNDCVK---EL-------RESNSQMVSLTDELSQKNEDLMRHQEEIAQLLS 284
Cdd:pfam01576 813 elEEARASRDEILAQSKES---EKKLKNLEAELLQlqeDLaaserarRQAQQERDELADEIASGASGKSALQDEKRRLEA 889
|
170 180 190
....*....|....*....|....*....|....*..
gi 326668399 285 QIVELQHRVKELALEKEELRIHLQASKEAQRQLTNEL 321
Cdd:pfam01576 890 RIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTEL 926
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
114-417 |
3.99e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 114 LSERDRdlELAARIGQSLLQRNHVLQERNESLeeQLAQALDQVHQLQHE-LAKKDELLRMVASASEESETDSScstplRH 192
Cdd:PRK04863 846 RVELER--ALADHESQEQQQRSQLEQAKEGLS--ALNRLLPRLNLLADEtLADRVEEIREQLDEAEEAKRFVQ-----QH 916
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 193 pvpaGAALalSQLEALQSKLQDLEEENLTLRSEachlkketitYEEKEQQLVN-----DCVKELRE-----SNSQMVSLT 262
Cdd:PRK04863 917 ----GNAL--AQLEPIVSVLQSDPEQFEQLKQD----------YQQAQQTQRDakqqaFALTEVVQrrahfSYEDAAEML 980
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 263 DELSQKNEDLMRHQEEIAQLLSQIVELQHRVKELALEKEELRIHLQASKEAQRQLTNELK-ELSDrnaecVGMLHESQEE 341
Cdd:PRK04863 981 AKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKqELQD-----LGVPADSGAE 1055
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 342 IKDLRSKNTPSAGLRRH---TSYGLYPMDSIAAEIEGTMRREMSVEEEI-AFEDQRSSQKRVFqtvrsvnQSVMRAAAAG 417
Cdd:PRK04863 1056 ERARARRDELHARLSANrsrRNQLEKQLTFCEAEMDNLTKKLRKLERDYhEMREQVVNAKAGW-------CAVLRLVKDN 1128
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
205-398 |
4.25e-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: 41.11 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 205 LEALQSKLQDLEEENLTLRSEACHLKKETITYEEKEQ-----------QLVNDCVKELRESNSQMVSLTDELSQKNEDLM 273
Cdd:pfam02463 182 TENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKleleeeyllylDYLKLNEERIDLLQELLRDEQEEIESSKQEIE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 274 RHQEEIAQLLSQIVElqhrvKELALEKEELRIHLQASKEAQRQLTNELKELSDRNAECVGMLHESQEEIKDLRSKNTPSA 353
Cdd:pfam02463 262 KEEEKLAQVLKENKE-----EEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEE 336
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 326668399 354 GLRRHTSYGLYPMDSIAAEIEGTMRREMSVEEEIAFEDQRSSQKR 398
Cdd:pfam02463 337 IEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKL 381
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
138-343 |
4.31e-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: 40.83 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 138 LQERNESLEEQLAQALDQVHQLQHELAKKDELLrmvasasEESETDSSCSTPlrhpvpagAALALSQLealQSKLQDLEE 217
Cdd:pfam05622 12 LAQRCHELDQQVSLLQEEKNSLQQENKKLQERL-------DQLESGDDSGTP--------GGKKYLLL---QKQLEQLQE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 218 ENLTLRSEACHLKketITYEEKEQQLVndcvkelresnsqmvsltdELSQKNEDLMRHQEEIAQLLSQIVELQH---RVK 294
Cdd:pfam05622 74 ENFRLETARDDYR---IKCEELEKEVL-------------------ELQHRNEELTSLAEEAQALKDEMDILREssdKVK 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 326668399 295 ELALEKEELRIHLQASKEAQRQltneLKELSDRNAECVGMLHESQEEIK 343
Cdd:pfam05622 132 KLEATVETYKKKLEDLGDLRRQ----VKLLEERNAEYMQRTLQLEEELK 176
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
278-390 |
4.46e-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: 39.91 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 278 EIAQLLSQIVELQHRVKELALEKEELRIHLQASKEAQRQLTNELKELSDRNAECVGMLHESQEEIKDLRSKntpsagLRR 357
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ------LGN 84
|
90 100 110
....*....|....*....|....*....|...
gi 326668399 358 HTSYGLYpmDSIAAEIEgTMRREMSVEEEIAFE 390
Cdd:COG1579 85 VRNNKEY--EALQKEIE-SLKRRISDLEDEILE 114
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
206-326 |
4.60e-03 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 38.43 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 206 EALQSKLQDLEEENLTLRSEACHLKKETITYEEKEQQLVndcvKELRESNSQMVSLTDElsqkNEDLMRhqeeiaqllsQ 285
Cdd:pfam10473 27 ENLERELEMSEENQELAILEAENSKAEVETLKAEIEEMA----QNLRDLELDLVTLRSE----KENLTK----------E 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 326668399 286 IVELQHRVKELA------------LEKEELRIHlQASKEAQRQLTNELKELSD 326
Cdd:pfam10473 89 LQKKQERVSELEslnsslenlleeKEQEKVQMK-EESKTAVEMLQTQLKELNE 140
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
203-303 |
5.01e-03 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 38.43 E-value: 5.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 203 SQLEALQSKLQDLEEENLTLRSEachlkKETITyeeKEQQLVNDCVKELRESNSQMVSLTDELsqknEDLMRHQEEiaql 282
Cdd:pfam10473 59 AEIEEMAQNLRDLELDLVTLRSE-----KENLT---KELQKKQERVSELESLNSSLENLLEEK----EQEKVQMKE---- 122
|
90 100
....*....|....*....|.
gi 326668399 283 lsqivELQHRVKELALEKEEL 303
Cdd:pfam10473 123 -----ESKTAVEMLQTQLKEL 138
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
113-328 |
5.10e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.93 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 113 LLSERDRDLElaARIGQsLLQRNHVLQERNESLEEQLAQALDQVHQLQHELAKKDELLRMVASASEESE-TDSSCSTPLR 191
Cdd:pfam01576 879 ALQDEKRRLE--ARIAQ-LEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLErQNKELKAKLQ 955
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 192 HPVPAGAALALSQLEALQSKLQDLEEEnltlrseachlkketITYEEKEQQLVNDCV----KELRESNSQMvsltdelsq 267
Cdd:pfam01576 956 EMEGTVKSKFKSSIAALEAKIAQLEEQ---------------LEQESRERQAANKLVrrteKKLKEVLLQV--------- 1011
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 326668399 268 knEDLMRHQEeiaQLLSQIVELQHRVKELALEKEELRIHLQASKEAQRQLTNELKELSDRN 328
Cdd:pfam01576 1012 --EDERRHAD---QYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESN 1067
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
201-356 |
5.30e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 39.28 E-value: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 201 ALSQLEALQSKLQDlEEENLTLRSEAchlkketitYEEKEQQLVNDCVKEL-RESNSQMVSLTDELSQKNEDLMRHQEEI 279
Cdd:pfam04012 44 ALAQTIARQKQLER-RLEQQTEQAKK---------LEEKAQAALTKGNEELaREALAEKKSLEKQAEALETQLAQQRSAV 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 326668399 280 AQLLSQIVELQHRVKELALEKEELRIHLQASKeAQRQLTNELKELSdrNAECVGMLHESQEEIKDLRSKNTPSAGLR 356
Cdd:pfam04012 114 EQLRKQLAALETKIQQLKAKKNLLKARLKAAK-AQEAVQTSLGSLS--TSSATDSFERIEEKIEEREARADAAAELA 187
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
143-324 |
5.46e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.93 E-value: 5.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 143 ESLEEQLAQA------LDQVHQ-LQHELAKKDELLRMVASASEESETdsscstplrhpvpaGAALALSQLEALQSKLQDL 215
Cdd:pfam01576 359 EELTEQLEQAkrnkanLEKAKQaLESENAELQAELRTLQQAKQDSEH--------------KRKKLEGQLQELQARLSES 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 216 EEENLTLRSEACHLKKEtityeekeqqlVNDCVKELRESNSQMVSLTDELSQKNEDLMRHQEEIAQLLSQIVELQHRVKE 295
Cdd:pfam01576 425 ERQRAELAEKLSKLQSE-----------LESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQ 493
|
170 180
....*....|....*....|....*....
gi 326668399 296 LALEKEELRIHLQASKEAQRQLTNELKEL 324
Cdd:pfam01576 494 LEDERNSLQEQLEEEEEAKRNVERQLSTL 522
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
264-348 |
5.60e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.61 E-value: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 264 ELSQKNEDLMRHQEEIAQLLSQIVELQHRVKEL--ALEKEELRIHLqASKEAQRQL--TNELKELSDRNAECVGMLHESQ 339
Cdd:COG2433 407 ELTEEEEEIRRLEEQVERLEAEVEELEAELEEKdeRIERLERELSE-ARSEERREIrkDREISRLDREIERLERELEEER 485
|
....*....
gi 326668399 340 EEIKDLRSK 348
Cdd:COG2433 486 ERIEELKRK 494
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
138-326 |
6.99e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.32 E-value: 6.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 138 LQERNESLEEQLAQALDQVHQLQHELAKKD----------ELLRMVASASEESETDSSCSTPLRHpVPAGAALAlSQLEA 207
Cdd:COG3096 439 AEDYLAAFRAKEQQATEEVLELEQKLSVADaarrqfekayELVCKIAGEVERSQAWQTARELLRR-YRSQQALA-QRLQQ 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 208 LQSKLQDLEEEnltLRSEachlkketityeEKEQQLVNDCVKELRESNSQMVSLTDELSQKNEDLMRHQEEIAQLLSQIV 287
Cdd:COG3096 517 LRAQLAELEQR---LRQQ------------QNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRS 581
|
170 180 190
....*....|....*....|....*....|....*....
gi 326668399 288 ELQHRVKELALEKEELRIHLQASKEAQRQLtNELKELSD 326
Cdd:COG3096 582 ELRQQLEQLRARIKELAARAPAWLAAQDAL-ERLREQSG 619
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
205-344 |
7.86e-03 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 38.95 E-value: 7.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 205 LEALQSKLQDLEEENLTLRSEACHLKKETITYEEKEQQLVnDCVKELRESNSQMVSLtdelsqknedLMRHQEEIAQLLS 284
Cdd:pfam17078 5 IESLHDQIDALTKTNLQLTVQSQNLLSKLEIAQQKESKFL-ENLASLKHENDNLSSM----------LNRKERRLKDLED 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 326668399 285 QIVELQHRVKELALEKEELRIHLQASKEAQRQLTNELKELSDR-NAecvgmLHESQEEIKD 344
Cdd:pfam17078 74 QLSELKNSYEELTESNKQLKKRLENSSASETTLEAELERLQIQyDA-----LVDSQNEYKD 129
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
116-345 |
8.59e-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: 8.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 116 ERDRDLELAARIGQSLLQRNHVLQERNESLEEQLAQALDQVHQLQhelAKKDELLRMVASASEESETDSScstplrhpVP 195
Cdd:pfam07888 56 QREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELE---EKYKELSASSEELSEEKDALLA--------QR 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 196 AGAALALSQLE----ALQSKLQDLEEENLTLRSEACHL---KKETITYEEKEQQLVNDCVKELRESNSQMVSLTDELSQK 268
Cdd:pfam07888 125 AAHEARIRELEedikTLTQRVLERETELERMKERAKKAgaqRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQR 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326668399 269 NEDLMRHQEEIAQLLSQIVELQHRVKELALEKEELRI---HLQASKEAQRQLTNELKELSDRNAECVGMLHESQEEIKDL 345
Cdd:pfam07888 205 DTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSlqeRLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQL 284
|
|
| |
