|
Name |
Accession |
Description |
Interval |
E-value |
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
1-249 |
2.44e-134 |
|
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: 405.18 E-value: 2.44e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 1 MTKTYNDIEVVTHLLAERDRDLELAARIGQSLLQRNHLLQERNESVEEQLAQALDQVHQLQHELGKKDELLRMVASASEE 80
Cdd:pfam04849 61 MTKTYNDIEAVTRLLEEKERDLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEILQLRHELSKKDDLLQIYSNDAEE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 81 SETDSSCSTPLHPRQPLAPAVALSQLEALQGKMSDLEEENLALRSEARHLKTETITYEEKEQQLVSDCVKELRESNSQMV 160
Cdd:pfam04849 141 SETESSCSTPLRRNESFSSLHGCVQLDALQEKLRGLEEENLKLRSEASHLKTETDTYEEKEQQLMSDCVEQLSEANQQMA 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 161 NLTEELSHKNEEVMRHQEEISQLLSQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADRNVECVGMLHESQ 240
Cdd:pfam04849 221 ELSEELARKMEENLRQQEEITSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLGMLHEAQ 300
|
....*....
gi 1696052198 241 EEIKELRSK 249
Cdd:pfam04849 301 EELKELRKK 309
|
|
| Milton |
pfam12448 |
Kinesin associated protein; This domain family is found in eukaryotes, and is typically ... |
313-454 |
3.52e-24 |
|
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: 100.05 E-value: 3.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 313 RAAAMATP--PIPGSGGSCLVMTAQPFLSAQGIDQSHCGANREEVPLGKPGAPGGNDLVSALHRLSLRRQNFLCERQFFQ 390
Cdd:pfam12448 25 RSSSSSTPrsSYYGGDGSSISLDNRTNSILSETSSSQDSGYDRPKKPGTPGTPGARDLEAALRRLSLRRQNYLSERRFFE 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1696052198 391 AERDKKLEALAGGVESD-VEGSGYSSPMSSVMSSFTNLSEFSVSSSCFKT--FLPEKLQIVKPMEGS 454
Cdd:pfam12448 105 EERERKLLALAGTYNYDeGEHGGSLTPNDSIMSLGSNHSGSSSHSSGFSSrsYLPEKLQIVKPLEGS 171
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
8-247 |
9.19e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.86 E-value: 9.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 8 IEVVTHLLAERDRDLELAARIGQSLLQRNHLLQERNESVEEQLAQALDQVHQLQHELGKKDELLRMVASASEESETdssc 87
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE---- 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 88 stplhprqplAPAVALSQLEALQGKMSDLEEENLALRSEARHLKTETITYEEKEQQLVS---DCVKELRESNSQMVNLTE 164
Cdd:TIGR02168 776 ----------ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRErleSLERRIAATERRLEDLEE 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 165 ELSHKNEEVMRHQEEISQLLSQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADRNVECVGMLHESQEEIK 244
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925
|
...
gi 1696052198 245 ELR 247
Cdd:TIGR02168 926 QLE 928
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
11-314 |
7.04e-11 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 66.30 E-value: 7.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 11 VTHLLAERDRDLE-LAARIGQSLLQRNHLLQERNESVEEQLAQALDQVHQL--QHELgkkdELLRMVASASEESETDSSC 87
Cdd:pfam15921 222 ISKILRELDTEISyLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLisEHEV----EITGLTEKASSARSQANSI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 88 STPLHPRQplapAVALSQLEALQGKMSDLEEENLALRSEARHLKTetiTYEEKEQQLVsdcvKELRESNSQMVNLTEELS 167
Cdd:pfam15921 298 QSQLEIIQ----EQARNQNSMYMRQLSDLESTVSQLRSELREAKR---MYEDKIEELE----KQLVLANSELTEARTERD 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 168 HKNEEVMRHQEEISQLLSqivELQHRVKELALEKEELRihLQASKDAQRSLTAE--LNELADRNVEcvgmLHESQEEIKE 245
Cdd:pfam15921 367 QFSQESGNLDDQLQKLLA---DLHKREKELSLEKEQNK--RLWDRDTGNSITIDhlRRELDDRNME----VQRLEALLKA 437
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1696052198 246 LRSKNtpSAGMRRHLPY------GLFPMDSLAAEIEGT--MRRELsVEDEVAFQDQKVSQKRVFQTVRVVNESVERA 314
Cdd:pfam15921 438 MKSEC--QGQMERQMAAiqgkneSLEKVSSLTAQLESTkeMLRKV-VEELTAKKMTLESSERTVSDLTASLQEKERA 511
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
9-288 |
2.98e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.31 E-value: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 9 EVVTHLLAERDRdLElaarigqSLLQRNHLLQERNESVEEQLAQALDQVHQLQHELGKKDELLRMVASASEESETDSSCS 88
Cdd:PRK03918 169 EVIKEIKRRIER-LE-------KFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 89 TPLHprqplapavalSQLEALQGKMSDLEEENLALRSEARHLKTETITYEEKEQQLvsdcvKELRESNSQMVNLTEELSH 168
Cdd:PRK03918 241 EELE-----------KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-----KELKEKAEEYIKLSEFYEE 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 169 KNEEVMRHQEEISQLLSQIVELQHRVKELALEKEELrihlqaskdaqRSLTAELNELADRnvecVGMLHESQEEIKELRS 248
Cdd:PRK03918 305 YLDELREIEKRLSRLEEEINGIEERIKELEEKEERL-----------EELKKKLKELEKR----LEELEERHELYEEAKA 369
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1696052198 249 KNTPSAGMRRHLpyGLFPMDSLAAEIEGTMRRELSVEDEV 288
Cdd:PRK03918 370 KKEELERLKKRL--TGLTPEKLEKELEELEKAKEEIEEEI 407
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
7-249 |
3.48e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 64.32 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 7 DIEVVTHLLAERDRDLELA------ARIGQSLLQRNHLLQERNESVEEqLAQALDQVHQLQHELGKkDELLRMVASASEE 80
Cdd:TIGR02169 222 EYEGYELLKEKEALERQKEaierqlASLEEELEKLTEEISELEKRLEE-IEQLLEELNKKIKDLGE-EEQLRVKEKIGEL 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 81 SETDSSCSTPLhprqplapAVALSQLEALQGKMSDLEEENLALRSEARHLKTEtITYEEKEQQLVSDCVKELRESNSQMV 160
Cdd:TIGR02169 300 EAEIASLERSI--------AEKERELEDAEERLAKLEAEIDKLLAEIEELERE-IEEERKRRDKLTEEYAELKEELEDLR 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 161 NLTEELSHKN----EEVMRHQEEISQLLSQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADRnvecvgmL 236
Cdd:TIGR02169 371 AELEEVDKEFaetrDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEE-------K 443
|
250
....*....|...
gi 1696052198 237 HESQEEIKELRSK 249
Cdd:TIGR02169 444 EDKALEIKKQEWK 456
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
102-247 |
6.55e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.42 E-value: 6.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 102 ALSQLEALQGKMSDLEEENLALRSEARHLKTETITYEEK---EQQLVSDCVKELRESNSQMVNLTEELSHKNEEVMRHQE 178
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLEleeLELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1696052198 179 EISQLLSQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADRNVECVGMLHESQEEIKELR 247
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
17-248 |
7.01e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 7.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 17 ERDRDLELAARIGQSLLQRNHLLQERNESVEEQLAQALDQVHQLQHELgkkdELLRMVASASEEsetdsscstplhprqp 96
Cdd:COG1196 222 LKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL----EELRLELEELEL---------------- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 97 lapavalsQLEALQGKMSDLEEENLALRSEARHLKTETITYEEKEQQLVsdcvKELRESNSQMVNLTEELSHKNEEVMRH 176
Cdd:COG1196 282 --------ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE----EELAELEEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1696052198 177 QEEISQLLSQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADRNVECVGMLHESQEEIKELRS 248
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
18-248 |
1.38e-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: 62.38 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 18 RDRDLELAARIgQSLLQRNHLLQERNESVEEQLAQALDQVHQLQHELGKKDELLRMVASASEESETDSSCSTPlhprqpl 97
Cdd:TIGR02168 273 RLEVSELEEEI-EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEE------- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 98 apavalsQLEALQGKMSDLEEENLALRSEARHLKTETITYEEKEQQLVSDcVKELRES----NSQMVNLTEELSHKNEEV 173
Cdd:TIGR02168 345 -------KLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK-VAQLELQiaslNNEIERLEARLERLEDRR 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 174 MRHQEEISQLLSQIV-----ELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADRNVECVGMLHESQEEIKELRS 248
Cdd:TIGR02168 417 ERLQQEIEELLKKLEeaelkELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
12-314 |
4.41e-09 |
|
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: 60.57 E-value: 4.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 12 THLLAERDrdlELAARigqsLLQRNHLLQERNESVEEQLAQALDQVHQLQHELGKKDELLRMVASASEESETdsscstpl 91
Cdd:pfam01576 53 TELCAEAE---EMRAR----LAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEA-------- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 92 hPRQPLapavalsQLE--ALQGKMSDLEEENLALRSEARHLKTETITYEEKeqqlVSDCVKELRESNSQMVNLTEeLSHK 169
Cdd:pfam01576 118 -ARQKL-------QLEkvTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER----ISEFTSNLAEEEEKAKSLSK-LKNK 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 170 NEEVMRHQE----------------------EISQLLSQIVELQHRVKELALE---KEElriHLQASKDAQRSLTAELNE 224
Cdd:pfam01576 185 HEAMISDLEerlkkeekgrqelekakrklegESTDLQEQIAELQAQIAELRAQlakKEE---ELQAALARLEEETAQKNN 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 225 LADRNVECVGMLHESQEEIKELRSKNTPSAGMRRHLPYGLFPM--------DSLAAEIEGTMRRELSV-------EDEVA 289
Cdd:pfam01576 262 ALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALkteledtlDTTAAQQELRSKREQEVtelkkalEEETR 341
|
330 340
....*....|....*....|....*..
gi 1696052198 290 FQDQKVSQKRV--FQTVRVVNESVERA 314
Cdd:pfam01576 342 SHEAQLQEMRQkhTQALEELTEQLEQA 368
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
7-249 |
5.73e-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: 5.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 7 DIEVVTHLLAERDRDLELAARIGQSLLQRNHLLQERNESVEEQLAQALDQVHQLQHELGKKDELLRMVASASEESETDSs 86
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 87 cstplhprqplapAVALSQLEALQGKMSDLEEENLALRSEARHLKTETITYEEKEQQL----------VSDCVKELRESN 156
Cdd:COG1196 305 -------------ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAeeeleeaeaeLAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 157 SQMVNLTEELSHKNEEVMRHQEE-------ISQLLSQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADRn 229
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAaaelaaqLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE- 450
|
250 260
....*....|....*....|
gi 1696052198 230 vecvgmLHESQEEIKELRSK 249
Cdd:COG1196 451 ------EAELEEEEEALLEL 464
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
15-249 |
6.47e-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: 60.08 E-value: 6.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 15 LAERDRDLELAARIGQSLLQRNHLLQERN--ESVEEQLAQALDQVHQLQHELGKKDELLRMVASAS----EESETD-SSC 87
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRriENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLkerlEELEEDlSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 88 STPLhprqplapAVALSQLEALQGKMSDLEEENLALRSE----ARHLKTETItyEEKEQQLvSDCVKELRESNSQMVNLT 163
Cdd:TIGR02169 750 EQEI--------ENVKSELKELEARIEELEEDLHKLEEAlndlEARLSHSRI--PEIQAEL-SKLEEEVSRIEARLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 164 EELSHKNEEVMRHQEEISQLLSQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADRNVECVGMLHESQEEI 243
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL 898
|
....*.
gi 1696052198 244 KELRSK 249
Cdd:TIGR02169 899 RELERK 904
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
91-250 |
7.33e-09 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 58.76 E-value: 7.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 91 LHPRQPLAPAVALSQLEALQGKMSDLEEENLALRSEARHLKTEtitYEEKEQQL------VSDCVKELRESNSQMVNLTE 164
Cdd:COG4372 18 LRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREE---LEQLEEELeqarseLEQLEEELEELNEQLQAAQA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 165 ELSHKNEEVMRHQEEISQLLSQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADRnvecvgmLHESQEEIK 244
Cdd:COG4372 95 ELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ-------LESLQEELA 167
|
....*.
gi 1696052198 245 ELRSKN 250
Cdd:COG4372 168 ALEQEL 173
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
46-249 |
1.50e-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: 58.91 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 46 VEEQLAQALDQVHQLQHELG---KKDELLR---MVASASEESEtdsscSTPLHPRQPLAPAVAlsQLEALQGKMSDLEEE 119
Cdd:TIGR02168 627 VVDDLDNALELAKKLRPGYRivtLDGDLVRpggVITGGSAKTN-----SSILERRREIEELEE--KIEELEEKIAELEKA 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 120 NLALRSEARHLKTEtityeekeqqlVSDCVKELRESNSQMVNLTEELSHKNEEVMRHQEEISQLLSQIVELQHRVKELAL 199
Cdd:TIGR02168 700 LAELRKELEELEEE-----------LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE 768
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1696052198 200 EKEELRIHLQASKDAQRSLTAELNELADRNVECVGMLHESQEEIKELRSK 249
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEE 818
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
6-228 |
1.76e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 6 NDIEVVTHLLAERDRDLELAARIGQSLLQRNHLLQERNESVEEQLAQALDQVHQLQHELGKKDELLRMVASASEESETDS 85
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 86 ScstplhprqplapAVALSQLEALQGKMSDLEEENLALRSEARHLKTETITYEEKEQQLvsdcvKELRESNSQMVNLTEE 165
Cdd:COG1196 382 E-------------ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE-----EALAELEEEEEEEEEA 443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1696052198 166 LSHKNEEVMRHQEEISQLLSQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADR 228
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
39-315 |
6.04e-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: 56.99 E-value: 6.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 39 LQERNESVEEQLAQA---LDQVHQLQHELGKKDELLRMVASA--------SEESETDSscstplhprqplapAVALSQLE 107
Cdd:TIGR02168 170 YKERRKETERKLERTrenLDRLEDILNELERQLKSLERQAEKaerykelkAELRELEL--------------ALLVLRLE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 108 ALQGKMSDLEEENLALRSEARHLKTETITYEEKEQQL---VSDCVKELRESNSQMVNLTEELSHKNEEVMRHQEEISQLL 184
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELrleVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 185 SQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADRNVECVGML-------HESQEEIKELRSKntpSAGMR 257
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELeelesrlEELEEQLETLRSK---VAQLE 392
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1696052198 258 RHLpyglfpmDSLAAEIEgTMRRELsvedevafQDQKVSQKRVFQTVRVVNESVERAA 315
Cdd:TIGR02168 393 LQI-------ASLNNEIE-RLEARL--------ERLEDRRERLQQEIEELLKKLEEAE 434
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
22-318 |
1.34e-07 |
|
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: 55.50 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 22 LELAARIGQSLLQRNH--------LLQERNESVEEQLAQALD---QVHQLQHELGKKDELL---RMVASASEESETDSSC 87
Cdd:pfam05483 361 LEELLRTEQQRLEKNEdqlkiitmELQKKSSELEEMTKFKNNkevELEELKKILAEDEKLLdekKQFEKIAEELKGKEQE 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 88 STPLhprqplapavalsqLEALQGKMSDLEEENLALRSEARH-------LKTETITYEEKEQQLVSDCVKELRESNSqmv 160
Cdd:pfam05483 441 LIFL--------------LQAREKEIHDLEIQLTAIKTSEEHylkevedLKTELEKEKLKNIELTAHCDKLLLENKE--- 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 161 nLTEELSHKNEEVMRHQEEI-------SQLLSQIV-----------ELQHRVKELALEKEELRIHLQASKDAQRSLTAEL 222
Cdd:pfam05483 504 -LTQEASDMTLELKKHQEDIinckkqeERMLKQIEnleekemnlrdELESVREEFIQKGDEVKCKLDKSEENARSIEYEV 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 223 ----NELADRNVECVGM----------LHESQEEIKELRSKNTPSAgmrRHLPYGLFPMDSLAAEIEGTMRR--ELSVED 286
Cdd:pfam05483 583 lkkeKQMKILENKCNNLkkqienknknIEELHQENKALKKKGSAEN---KQLNAYEIKVNKLELELASAKQKfeEIIDNY 659
|
330 340 350
....*....|....*....|....*....|..
gi 1696052198 287 EVAFQDQKVSQKRVFqtvrvvnESVERAAAMA 318
Cdd:pfam05483 660 QKEIEDKKISEEKLL-------EEVEKAKAIA 684
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
69-249 |
2.32e-07 |
|
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: 53.17 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 69 ELLRMVASASEESETDSSCSTPLHPRQP-LAPAVALSQLEALQGKMSDLEEENLALRSEARHLKTE-TITYEEKEQ--QL 144
Cdd:pfam15294 90 ELLEQIAEFEEREFTSSNKKPNFELNKPkLEPLNEGGGSALLHMEIERLKEENEKLKERLKTLESQaTQALDEKSKleKA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 145 VSDCVKELRESNSQMVNlTEELShKNEEVMRH-QEEISQLLSQIVELQHRVKE-LALEKEE-LRIHLQASKdAQRSLTAE 221
Cdd:pfam15294 170 LKDLQKEQGAKKDVKSN-LKEIS-DLEEKMAAlKSDLEKTLNASTALQKSLEEdLASTKHElLKVQEQLEM-AEKELEKK 246
|
170 180
....*....|....*....|....*....
gi 1696052198 222 LNELAD-RNVEcvGMLHESQEEIKELRSK 249
Cdd:pfam15294 247 FQQTAAyRNMK--EMLTKKNEQIKELRKR 273
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
39-231 |
2.50e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.14 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 39 LQERNESVEEQLAQALDQVHQLQHELGK-KDELLRMVASASEESETDSSCSTPLhprqplapAVALSQLEALQGKMSDLE 117
Cdd:COG4372 43 LQEELEQLREELEQAREELEQLEEELEQaRSELEQLEEELEELNEQLQAAQAEL--------AQAQEELESLQEEAEELQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 118 EENLALRSEARHLKTETITYEEKEQQLVSdcvkELRESNSQMVNLTEELSHKNEEVMRHQEEISQLLSQivELQHRVKEL 197
Cdd:COG4372 115 EELEELQKERQDLEQQRKQLEAQIAELQS----EIAEREEELKELEEQLESLQEELAALEQELQALSEA--EAEQALDEL 188
|
170 180 190
....*....|....*....|....*....|....
gi 1696052198 198 ALEKEELRIHLQASKDAQRSLTAELNELADRNVE 231
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLE 222
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1-250 |
2.83e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 54.59 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 1 MTKTYNDIEVVTHLLAERDRDLELAarigqslLQRNHLLQERNESVEEQLA-QALDQVHQLQHELGKKDELLRMvaSASE 79
Cdd:pfam02463 179 IEETENLAELIIDLEELKLQELKLK-------EQAKKALEYYQLKEKLELEeEYLLYLDYLKLNEERIDLLQEL--LRDE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 80 ESETDSscstplhprqplapavalsqlealQGKMSDLEEENLALRSEARHLKTETITYEEKEQQLVSdcvKELRESNSQM 159
Cdd:pfam02463 250 QEEIES------------------------SKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLA---KEEEELKSEL 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 160 VNLTEELSHKNEEVMRHQEEISQLLSQIVELQHRVKELALEKEEL---RIHLQASKDAQRSLTAELNELADRNVECVGML 236
Cdd:pfam02463 303 LKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELeikREAEEEEEEELEKLQEKLEQLEEELLAKKKLE 382
|
250
....*....|....
gi 1696052198 237 HESQEEIKELRSKN 250
Cdd:pfam02463 383 SERLSSAAKLKEEE 396
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
15-246 |
3.24e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 15 LAERDRDLELAARIGQSLLQRNHLLQERNESVEEQLAQALDQVHQLQHELGKKDELLRMVASASEESETdsscstplhpr 94
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE----------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 95 qplapavalsQLEALQGKMSDLEEENLALRSEARHLKtetityEEKEQQlvsdcvkELRESNSQMVNLTEELSHKNEEVM 174
Cdd:TIGR02168 380 ----------QLETLRSKVAQLELQIASLNNEIERLE------ARLERL-------EDRRERLQQEIEELLKKLEEAELK 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1696052198 175 RHQEEISQLLSQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADRNVECVGML--HES-QEEIKEL 246
Cdd:TIGR02168 437 ELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQenLEGfSEGVKAL 511
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
8-226 |
4.41e-07 |
|
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: 54.20 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 8 IEVVTH-LLAERDRDLELAARIgQSLLQRNHLLQERNESVEEQLAQALDQVHQLQHELGKKDELLRMVASASEESETDss 86
Cdd:TIGR00618 544 EEDVYHqLTSERKQRASLKEQM-QEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRK-- 620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 87 cstplhprqpLAPAVALSQLEALQGKMsdleEENLALRSEARHLKTETITYEEKEQQLVSDCVKELReSNSQMVNLTEEL 166
Cdd:TIGR00618 621 ----------LQPEQDLQDVRLHLQQC----SQELALKLTALHALQLTLTQERVREHALSIRVLPKE-LLASRQLALQKM 685
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 167 SHKNEEVMRHQEEISQLLSQIVELQHRVKELALEKEELRihlQASKDAQRSLTAELNELA 226
Cdd:TIGR00618 686 QSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIE---NASSSLGSDLAAREDALN 742
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
18-231 |
4.66e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.87 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 18 RDRDLELAARIGQSLLQ--RNHLLQERNESVEEQLAQALDQVHQLQHELGKKDELLR------MVASASEESEtdsscst 89
Cdd:COG3206 143 TSPDPELAAAVANALAEayLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEefrqknGLVDLSEEAK------- 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 90 plhprqplapaVALSQLEALQGKMSDLEEENLALRSEARHLKTETITYEEKEQQLVSDCV-----KELRESNSQMVNLTE 164
Cdd:COG3206 216 -----------LLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPViqqlrAQLAELEAELAELSA 284
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1696052198 165 ELSHKNEEVMRHQEEISQLLSQI-VELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADRNVE 231
Cdd:COG3206 285 RYTPNHPDVIALRAQIAALRAQLqQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAE 352
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
109-249 |
5.06e-07 |
|
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: 52.71 E-value: 5.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 109 LQGKMSDLEEENLALRSEARHLKtetityeeKEQQLVSDCVKELRE----SNSQMVNLTEELSHKNE----EVMRHQEEI 180
Cdd:smart00787 142 LEGLKEGLDENLEGLKEDYKLLM--------KELELLNSIKPKLRDrkdaLEEELRQLKQLEDELEDcdptELDRAKEKL 213
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1696052198 181 SQLLSQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADRNVECVGMlheSQEEIKELRSK 249
Cdd:smart00787 214 KKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGF---TFKEIEKLKEQ 279
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
14-199 |
5.18e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 5.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 14 LLAERDRDLELAARIGQSLLQRNHLLQERNESVEEQLAQALDQVHQLQHELGKKDELLRMVASASEESETDSScstpLHP 93
Cdd:COG4717 68 LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAE----LAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 94 RQPLAPAvALSQLEALQGKMSDLEEENLALRSEARHLKTETITYEEKEQQLVSDCVKELRESNSQMVNLTEELSHKNEEV 173
Cdd:COG4717 144 LPERLEE-LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL 222
|
170 180
....*....|....*....|....*...
gi 1696052198 174 MRHQEEISQLLSQIV--ELQHRVKELAL 199
Cdd:COG4717 223 EELEEELEQLENELEaaALEERLKEARL 250
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
35-249 |
1.98e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 35 RNHLLQERN---------------ESVEEQLAQALDQVHQLQHELGKKDELLRMVASASEESETdsscstplhpRQPLAP 99
Cdd:COG4913 214 REYMLEEPDtfeaadalvehfddlERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYL----------RAALRL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 100 AVALSQLEALQGKMSDLEEENLALRSEARHLKTETITYEEKEQQLvsdcvKELRESNS--QMVNLTEELSHKNEEVMRHQ 177
Cdd:COG4913 284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDEL-----EAQIRGNGgdRLEQLEREIERLERELEERE 358
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1696052198 178 EEISQLLSQIVELQHRV----KELALEKEELRIHLQASKDAQRSLTAELNELADRNVECVGMLHESQEEIKELRSK 249
Cdd:COG4913 359 RRRARLEALLAALGLPLpasaEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
39-248 |
3.99e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 3.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 39 LQERNESVEEQLAQALDQVHQLQHELGKKDELLRMVASASEESETdssCSTPL--HPRQPLAPAVALsQLEALQGKMSDL 116
Cdd:PRK03918 396 LEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPV---CGRELteEHRKELLEEYTA-ELKRIEKELKEI 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 117 EEENLALRSEARhlKTETITYEEKE---QQLVSDCVKELRESNSQmVNLtEELSHKNEEVMRHQEEISQLLSQIVELQHR 193
Cdd:PRK03918 472 EEKERKLRKELR--ELEKVLKKESElikLKELAEQLKELEEKLKK-YNL-EELEKKAEEYEKLKEKLIKLKGEIKSLKKE 547
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1696052198 194 VKELALEKEELRIHLQASKDAQRSLTAELNELADRNVECVgmlHESQEEIKELRS 248
Cdd:PRK03918 548 LEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESV---EELEERLKELEP 599
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
107-227 |
5.02e-06 |
|
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: 46.91 E-value: 5.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 107 EALQGKMSDLEEENLALRSEARHLKTETITYEEKEQQLVsdcvKELRESNSQMVNLTEELSHKNEEVMRHQEEISQLLSQ 186
Cdd:pfam10473 27 ENLERELEMSEENQELAILEAENSKAEVETLKAEIEEMA----QNLRDLELDLVTLRSEKENLTKELQKKQERVSELESL 102
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1696052198 187 IVELQHRVKElaLEKEELRIHlQASKDAQRSLTAELNELAD 227
Cdd:pfam10473 103 NSSLENLLEE--KEQEKVQMK-EESKTAVEMLQTQLKELNE 140
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
15-251 |
6.07e-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: 6.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 15 LAERDRDLELAARIGQSLLQRNHLLQERNESVE------EQLAQALD-QVHQLQHELGKKDELLRMVASASEESEtdssc 87
Cdd:TIGR04523 365 LEEKQNEIEKLKKENQSYKQEIKNLESQINDLEskiqnqEKLNQQKDeQIKKLQQEKELLEKEIERLKETIIKNN----- 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 88 stplhprqplapavalSQLEALQGKMSDLEE--ENLALRSEARHLKTETITYE-EKEQQLVSDCVKELRESNSQMVNLTE 164
Cdd:TIGR04523 440 ----------------SEIKDLTNQDSVKELiiKNLDNTRESLETQLKVLSRSiNKIKQNLEQKQKELKSKEKELKKLNE 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 165 ELSHKNEEVMRHQEEISQLLSqivelqhrvKELALEKEELRIHLQASkdaqrSLTAELNELADR----NVECVgmLHESQ 240
Cdd:TIGR04523 504 EKKELEEKVKDLTKKISSLKE---------KIEKLESEKKEKESKIS-----DLEDELNKDDFElkkeNLEKE--IDEKN 567
|
250
....*....|.
gi 1696052198 241 EEIKELRSKNT 251
Cdd:TIGR04523 568 KEIEELKQTQK 578
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
131-250 |
8.45e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 8.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 131 KTETITYEEKEQQLVSDCVKELRESNSQMVNLTEELSHKNEEVMRHQEEISQLLSQIVELQHRVKELALEKEELRIHLQA 210
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA 91
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1696052198 211 SKDAQRSLTAELNELADRNVECVGMLHESQEEIKELRSKN 250
Cdd:COG4372 92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQR 131
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
104-246 |
8.47e-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: 49.63 E-value: 8.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 104 SQLEALQGKMSDLEEENLALRSEARHLKTE----TITYEEKEQQLvSDCVKELRESNSQM--VNLTEELSHKNEEVMRHQ 177
Cdd:TIGR04523 496 KELKKLNEEKKELEEKVKDLTKKISSLKEKieklESEKKEKESKI-SDLEDELNKDDFELkkENLEKEIDEKNKEIEELK 574
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1696052198 178 EEISQLLSQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADRNVECVGM---LHESQEEIKEL 246
Cdd:TIGR04523 575 QTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIiknIKSKKNKLKQE 646
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
105-249 |
1.06e-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: 48.00 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 105 QLEALQGKMSDLEEENLALRSEARHLKTEtitYEEKEQQLvSDCVKELRESNSQMVNLTEELSH--KNEEVMRHQEEISQ 182
Cdd:COG1579 25 RLKELPAELAELEDELAALEARLEAAKTE---LEDLEKEI-KRLELEIEEVEARIKKYEEQLGNvrNNKEYEALQKEIES 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1696052198 183 LLSQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNEL-ADRNVEcvgmLHESQEEIKELRSK 249
Cdd:COG1579 101 LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKkAELDEE----LAELEAELEELEAE 164
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
106-249 |
1.22e-05 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 48.27 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 106 LEALQGKMSDLEEENLALRSEARHLKTETITYEE--KEQQLVSDCVKELRESNSQMVNLTEELSHKNEEVMRHQEEISQL 183
Cdd:pfam15905 193 LEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEyiTELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQE 272
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1696052198 184 LS-QIVELQHRVKELALEKEELrihLQASKDAQRSLTAELNELADRnvecvgmLHESQEEIKELRSK 249
Cdd:pfam15905 273 LSkQIKDLNEKCKLLESEKEEL---LREYEEKEQTLNAELEELKEK-------LTLEEQEHQKLQQK 329
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
122-231 |
2.60e-05 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 44.55 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 122 ALRSEARHLKTETITYEEKEQQLVSDCVKELRESNSQMVNLTEELSHKNEEVmrhqEEISQLLSQIVELQHRVKELALEK 201
Cdd:pfam07926 5 SLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERELVLHAEDI----KALQALREELNELKAEIAELKAEA 80
|
90 100 110
....*....|....*....|....*....|....
gi 1696052198 202 EELRIHLQASKDA----QRSLTAELNELADRNVE 231
Cdd:pfam07926 81 ESAKAELEESEESweeqKKELEKELSELEKRIED 114
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
99-249 |
3.66e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 99 PAVALSQLEALQGKMSDLEEENLALRSEARHLKTETITYEEKEQQLVS--------DCVKELRESNSQMVNLTEELSHKN 170
Cdd:COG4717 66 PELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEElreeleklEKLLQLLPLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 171 ---EEVMRHQEEISQLLSQIVELQHRVKELALEKEELRIHLQASKDAQ-RSLTAELNELADRNVECVGMLHESQEEIKEL 246
Cdd:COG4717 146 erlEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
...
gi 1696052198 247 RSK 249
Cdd:COG4717 226 EEE 228
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
23-247 |
5.69e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.06 E-value: 5.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 23 ELAARIGQSLLQRNHLLQERNESVEE--QLAQALD----QVHQLQHELG----KKDELLRMVASASEE-SETDSSCSTpl 91
Cdd:COG1340 12 ELEEKIEELREEIEELKEKRDELNEElkELAEKRDelnaQVKELREEAQelreKRDELNEKVKELKEErDELNEKLNE-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 92 hprqplapavALSQLEALQGKMSDLEEENL---ALRSEARHL----KTETITyEEKEQQLVSDcVKELREsnsqMVNLTE 164
Cdd:COG1340 90 ----------LREELDELRKELAELNKAGGsidKLRKEIERLewrqQTEVLS-PEEEKELVEK-IKELEK----ELEKAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 165 ELSHKNEEVMRHQEEISQLLSQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADRNVEC---VGMLH---- 237
Cdd:COG1340 154 KALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAqekADELHeeii 233
|
250
....*....|
gi 1696052198 238 ESQEEIKELR 247
Cdd:COG1340 234 ELQKELRELR 243
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
23-261 |
7.20e-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: 7.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 23 ELAARIGQSLLQRNHLLQERnESVEEQLAQALDQVHQLQHELGKKDELLRMVASASEESETDSScstplHPRQPLApava 102
Cdd:COG4942 38 ELEKELAALKKEEKALLKQL-AALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE-----AQKEELA---- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 103 lSQLEALQgKMSDLEEENLALRSEarhlkteTITYEEKEQQLVSDCVKELRESNSQMVNLTEELSHKNEEVMRHQEEISQ 182
Cdd:COG4942 108 -ELLRALY-RLGRQPPLALLLSPE-------DFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1696052198 183 LLSQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADRNVECVGMLhESQEEIKELRSKNTPSAGMRRHLP 261
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL-EAEAAAAAERTPAAGFAALKGKLP 256
|
|
| KASH_CCD |
pfam14662 |
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of ... |
30-209 |
7.24e-05 |
|
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of KASH or Klarsicht/ANC-1/Syne/homology proteins. KASH are a meiosis-specific proteins that localize at telomeres and interact with SUN1, thus being implicated in meiotic chromosome dynamics and homolog pairing.
Pssm-ID: 405365 [Multi-domain] Cd Length: 191 Bit Score: 44.79 E-value: 7.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 30 QSLLQRNHLLQERNESVEEQLA-----------QALDQVHQLQHE--LGKKDELLRMVASASEESETdsscSTPLHPRQP 96
Cdd:pfam14662 18 QKLLQENSKLKATVETREETNAklleenlnlrkQAKSQQQAVQKEklLEEELEDLKLIVNSLEEARR----SLLAQNKQL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 97 LAPAVALSQlealqgKMSDLEEENLALRSEARHLKTETityeeKEQQLVSDCVKELRESNSQMVNLTEELShknEEVMRH 176
Cdd:pfam14662 94 EKENQSLLQ------EIESLQEENKKNQAERDKLQKKK-----KELLKSKACLKEQLHSCEDLACNRETIL---IEKTTQ 159
|
170 180 190
....*....|....*....|....*....|...
gi 1696052198 177 QEEisqLLSQIVELQHRVKELALEKEELRIHLQ 209
Cdd:pfam14662 160 IEE---LKSTVEEYSSIEEELRAEKSRLESQLP 189
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
30-251 |
7.38e-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: 46.55 E-value: 7.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 30 QSLLQRNHLLQERNESVEEQLAQALDQVHQLQHELGKKDELLRMVAS----ASEESETDSscsTPLHPRQplapavalSQ 105
Cdd:TIGR04523 207 KKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTqlnqLKDEQNKIK---KQLSEKQ--------KE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 106 LEALQGKMSDLEEENLALRSEARHLKtetityEEKEQQLVSDCVKELRESNSQMVNLTEELSHKNEEVMRHQEEISQLLS 185
Cdd:TIGR04523 276 LEQNNKKIKELEKQLNQLKSEISDLN------NQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKK 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 186 QI-----------VELQHRVKELALEKEELRIHLQASKDAQRSLTA---------ELNELADRNVECVGMLHES-QEEIK 244
Cdd:TIGR04523 350 ELtnsesensekqRELEEKQNEIEKLKKENQSYKQEIKNLESQINDleskiqnqeKLNQQKDEQIKKLQQEKELlEKEIE 429
|
....*..
gi 1696052198 245 ELRSKNT 251
Cdd:TIGR04523 430 RLKETII 436
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
150-314 |
1.02e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 150 KELRESNSQMvnltEELSHKNEEVMRHQEEISQLLSQIVELQHRVKELALEKEELRIHLQASKDAQR--SLTAELNELAD 227
Cdd:COG4717 71 KELKELEEEL----KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQEleALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 228 RnvecvgmLHESQEEIKELRSKNTPSAGMRRHLpyglfpmDSLAAEIEgTMRRELSVEDEVAFQDQKVSQKRVFQTVRVV 307
Cdd:COG4717 147 R-------LEELEERLEELRELEEELEELEAEL-------AELQEELE-ELLEQLSLATEEELQDLAEELEELQQRLAEL 211
|
....*..
gi 1696052198 308 NESVERA 314
Cdd:COG4717 212 EEELEEA 218
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
44-249 |
1.05e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 44 ESVEEQLAQALDQVHQLQHELGKKDELLRMVASASEESETDSSCSTPLHPRQplapaVALSQLEALQGKMSDLEE--ENL 121
Cdd:PRK02224 179 ERVLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQRE-----QARETRDEADEVLEEHEErrEEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 122 A-LRSEARHLkTETITYEEKEQQLVSDCVKELREsnsQMVNLTEELSHKNEEVMRHQEEISQLLSQIVELQHRVKELALE 200
Cdd:PRK02224 254 EtLEAEIEDL-RETIAETEREREELAEEVRDLRE---RLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDR 329
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1696052198 201 KEELRIHLQASKDAQRSLTAELNELADRNvecvgmlHESQEEIKELRSK 249
Cdd:PRK02224 330 LEECRVAAQAHNEEAESLREDADDLEERA-------EELREEAAELESE 371
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
43-289 |
1.24e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 45.30 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 43 NESVEEQ-----LAQALDQVHQLQHE---LGKKDELLRMVASAsEESETDSSCSTPLhprqplapAVALSQLEALQGKMS 114
Cdd:pfam00038 1 NEKEQLQelndrLASYIDKVRFLEQQnklLETKISELRQKKGA-EPSRLYSLYEKEI--------EDLRRQLDTLTVERA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 115 DLEEENLALRSEARHLKTEtitYEEK--EQQLVSDCVKELR-----------ESNSQMVNLTEELshkneEVMR--HQEE 179
Cdd:pfam00038 72 RLQLELDNLRLAAEDFRQK---YEDElnLRTSAENDLVGLRkdldeatlarvDLEAKIESLKEEL-----AFLKknHEEE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 180 ISQLLSQIVElQHRV--------KELALEKEELRIHL--QASKDAQ------RSLTAELNELADRNVEcvgMLHESQEEI 243
Cdd:pfam00038 144 VRELQAQVSD-TQVNvemdaarkLDLTSALAEIRAQYeeIAAKNREeaeewyQSKLEELQQAAARNGD---ALRSAKEEI 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1696052198 244 KELRskntpsagmRRhlpyglfpMDSLAAEIEGTMRRELSVEDEVA 289
Cdd:pfam00038 220 TELR---------RT--------IQSLEIELQSLKKQKASLERQLA 248
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
16-228 |
1.51e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 16 AERDRDlELAARIGQSLLQRNHLLQERNESVEEQLAQALDQ--VHQLQHELGKKDELLRmvaSASEESETDSScstplhp 93
Cdd:PRK02224 270 TERERE-ELAEEVRDLRERLEELEEERDDLLAEAGLDDADAeaVEARREELEDRDEELR---DRLEECRVAAQ------- 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 94 rqplapaVALSQLEALQGKMSDLEEENLALRSEARHLKTEtityeekeqqlVSDCVKELRESNSQMVNLTEELshknEEV 173
Cdd:PRK02224 339 -------AHNEEAESLREDADDLEERAEELREEAAELESE-----------LEEAREAVEDRREEIEELEEEI----EEL 396
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1696052198 174 MrhqEEISQLLSQIVELQHRVKELALEKEELRIHLqaskdaqRSLTAELNELADR 228
Cdd:PRK02224 397 R---ERFGDAPVDLGNAEDFLEELREERDELRERE-------AELEATLRTARER 441
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
55-298 |
1.54e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.81 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 55 DQVHQLQHELGK-KDELLRMVASASEESETDSSCSTPLHPRQPLAPAVALSQLEALQGKMSDLEEENLALRSEARHLKTE 133
Cdd:TIGR00606 684 QRVFQTEAELQEfISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRL 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 134 TITYEEKEQQLVSDCVKELRESNSQM-VNLTEELSHKNEEVMRHQEE-------------ISQLLSQIVELQHRVKELAL 199
Cdd:TIGR00606 764 KNDIEEQETLLGTIMPEEESAKVCLTdVTIMERFQMELKDVERKIAQqaaklqgsdldrtVQQVNQEKQEKQHELDTVVS 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 200 EKEELRIHLQASKDAQRSLTAELNELADRNVECV-------GMLHESQEEIKELRSKNTPSAGMRRH-LPYGLFPMDSLA 271
Cdd:TIGR00606 844 KIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGtnlqrrqQFEEQLVELSTEVQSLIREIKDAKEQdSPLETFLEKDQQ 923
|
250 260 270
....*....|....*....|....*....|
gi 1696052198 272 AEIEGTMRRELS---VEDEVAFQDQKVSQK 298
Cdd:TIGR00606 924 EKEELISSKETSnkkAQDKVNDIKEKVKNI 953
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1-251 |
1.64e-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: 45.73 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 1 MTKTYND-IEVVTHLLAERdRDLELAARIGQSLLQRNHLLQERNESVEEQLAQALDQVHQLQHELG------KKDELLRM 73
Cdd:TIGR00618 213 MPDTYHErKQVLEKELKHL-REALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAvleetqERINRARK 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 74 VASASEESETDSSCstplhpRQPlapavALSQLEALQGKMSDLEEEnLALRSEARHLKTETITYEEKEQQLVSDCV---- 149
Cdd:TIGR00618 292 AAPLAAHIKAVTQI------EQQ-----AQRIHTELQSKMRSRAKL-LMKRAAHVKQQSSIEEQRRLLQTLHSQEIhird 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 150 -----KELRESNSQMVNLTEELsHKNEEVMRHQEEISQLLSQIVE----LQHRVKELALEKEELRIHLQASKDAQR---- 216
Cdd:TIGR00618 360 ahevaTSIREISCQQHTLTQHI-HTLQQQKTTLTQKLQSLCKELDilqrEQATIDTRTSAFRDLQGQLAHAKKQQElqqr 438
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1696052198 217 -------SLTAELNELADRNVECVGMLHESQEEIKELRSKNT 251
Cdd:TIGR00618 439 yaelcaaAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQ 480
|
|
| NIP100 |
COG5244 |
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ... |
18-320 |
1.71e-04 |
|
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: 45.45 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 18 RDRDLELAARIGQSLLQRNHLLQE-RNESV-EEQLAQALDQVHQLQHELgkkdellrmvASASEESETDSSCSTPlhprq 95
Cdd:COG5244 57 KKRHGIFIRPDDDSLLNGNAAYEKiKGGLVcESKGMDKDGEIKQENHED----------RIHFEESKIRRLEETI----- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 96 plapaVALSQLEalqgkmsdlEEENLALRSEARHLKTETITYEEK----EQQLVSDCVKELRESNSQMVnlteelshknE 171
Cdd:COG5244 122 -----EALKSTE---------KEEIVELRRENEELDKINLSLRERisseEPELNKDGSKLSYDELKEFV----------E 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 172 EVMRHQEEISQLLSQIVELQHRVKELALE--KEELRihlqaskdaqrslTAELNELADRNVECVGMLHESQEEIKELRSK 249
Cdd:COG5244 178 ESRVQVYDMVELVSDISETLNRNGSIQRSsvRECER-------------SNIHDVLFLVNGILDGVIDELNGELERLRRQ 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1696052198 250 NTpsagmrrhlpyglFPMDSLAAEIEGTMRRELSVEDEVAFQDQ-KVSQKRVFQTVRVVN-ESVERAAAMATP 320
Cdd:COG5244 245 LV-------------SLMSSHGIEVEENSRLKATLEKFQSLELKvNTLQEELYQNKLLKKfYQIYEPFAQAAL 304
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-249 |
2.12e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 1 MTKTYNDIEVVTHLLAERDRDLE-LAARIGQsllqrnhlLQERNESVEEQLAQALDQVHQLQHELGKKDELLRMVASASE 79
Cdd:PRK03918 233 LEELKEEIEELEKELESLEGSKRkLEEKIRE--------LEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEE 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 80 ESETDSSCSTPLHPRQPLAPAVA--LSQLEALQGKMSDLEEENLALRSEARHLKTETITYEEKEQQLvsdcvKELRESNS 157
Cdd:PRK03918 305 YLDELREIEKRLSRLEEEINGIEerIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKK-----EELERLKK 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 158 QMVNLT-EELSHKNEEVMRH----QEEISQLLSQIVELQHRVKELALEKEELR------------IHLQASKDAQRSLTA 220
Cdd:PRK03918 380 RLTGLTpEKLEKELEELEKAkeeiEEEISKITARIGELKKEIKELKKAIEELKkakgkcpvcgreLTEEHRKELLEEYTA 459
|
250 260
....*....|....*....|....*....
gi 1696052198 221 ELNELADRNVECVGMLHESQEEIKELRSK 249
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKV 488
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
104-204 |
2.26e-04 |
|
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: 42.28 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 104 SQLEALQGKMSDLEEENLALRSEARHLKTETityeEKEQQLVSdcvkELRESNSQMVNLTEELshknEEVMRHQEEisql 183
Cdd:pfam10473 59 AEIEEMAQNLRDLELDLVTLRSEKENLTKEL----QKKQERVS----ELESLNSSLENLLEEK----EQEKVQMKE---- 122
|
90 100
....*....|....*....|.
gi 1696052198 184 lsqivELQHRVKELALEKEEL 204
Cdd:pfam10473 123 -----ESKTAVEMLQTQLKEL 138
|
|
| Kre28 |
pfam17097 |
Spindle pole body component; In Saccharomyces cerevisae Kre28 and Spc105 form a kinetochore ... |
45-260 |
2.37e-04 |
|
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: 44.41 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 45 SVEEQLAQALDQV--HQLQHELGKKDELLRMVASASEESE--TDSSCSTPLH--PRQPlapAVALSQLEAL--QGKMSDL 116
Cdd:pfam17097 15 ELEEQTAHSSEQVltEQDKRLLGALRELTQSVIQLIEENSlvTVSGDAANLLidPSGI---EVKIRQLDQLveLLKVTHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 117 EEENLA--LR---SEARHLKTETITyEEKEQQLvSDCVKELREsnsqmvnltEELSHKNEEVMRHQEEISQLLSQIVELQ 191
Cdd:pfam17097 92 EQETLDnfLRytiSSTDLLQLESVS-DPKYASL-EDEVSQLED---------DTLTVLNQEIDQIKGDILQVAQEIADKQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1696052198 192 HRVKELALEK----EELRIHLQASKDAQRSLTAELNELADRNVECVGMLHESQEEIKELRSKNTPSAGMRRHL 260
Cdd:pfam17097 161 DQVNELCLETsnelDECWELLNELERLRDQRITVEEQTSNEKDTELDPVEETYEEWKSLQESLQQLEHLKEEL 233
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
104-246 |
2.71e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 104 SQLEALQGKMSDLEEENLALRSEARHLKtetityeekeqqlvsdcvKELRESNSQMVNLTEELSHKNEEVMRHQEEISQL 183
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELK------------------EKRDELNEELKELAEKRDELNAQVKELREEAQEL 62
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1696052198 184 LSQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADRNVEcvgmLHESQEEIKEL 246
Cdd:COG1340 63 REKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGS----IDKLRKEIERL 121
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
96-226 |
2.95e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 96 PLAPAVALSQLEALQGKMSDLEEENLALRSEARHLKTETITYEEK----EQQL--VSDcVKELRESNSQMVNLTEELSHK 169
Cdd:COG1579 30 PAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARikkyEEQLgnVRN-NKEYEALQKEIESLKRRISDL 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1696052198 170 NEEVMRHQEEISQLLSQIVELQHRVK----ELALEKEELRIHLQASKDAQRSLTAELNELA 226
Cdd:COG1579 109 EDEILELMERIEELEEELAELEAELAeleaELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
100-280 |
3.07e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 100 AVALSQLEALQGKMSDLEEENLALRSEARHLKTE------TITYEEKEQQLvsdcvKELRESNSQMVNLTEELSHKNEEV 173
Cdd:COG4913 627 AEAEERLEALEAELDALQERREALQRLAEYSWDEidvasaEREIAELEAEL-----ERLDASSDDLAALEEQLEELEAEL 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 174 MRHQEEISQLLSQIVELQHRVKELALEKEELRIHLQASKDAQRS-----LTAELNELADRNVEcVGMLHESQEEIKELRS 248
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLelralLEERFAAALGDAVE-RELRENLEERIDALRA 780
|
170 180 190
....*....|....*....|....*....|..
gi 1696052198 249 KntpsagmrrhlpyglfpMDSLAAEIEGTMRR 280
Cdd:COG4913 781 R-----------------LNRAEEELERAMRA 795
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
74-205 |
3.13e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.46 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 74 VASASEESETDSScsTPLHPRQPLAPAVALSQLEALQGKMSDLEEENLALRSEARHLKTETityEEKEQQLvSDCVKELR 153
Cdd:COG2433 378 IEEALEELIEKEL--PEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAEL---EEKDERI-ERLERELS 451
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1696052198 154 ESNSQMvnltEELSHKNEEVMRHQEEISQLLSQIVELQHRVKELALEKEELR 205
Cdd:COG2433 452 EARSEE----RREIRKDREISRLDREIERLERELEEERERIEELKRKLERLK 499
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
28-228 |
3.31e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 28 IGQSLLQRNHLLQERNESVEEQLAQA---LDQVHQLQHELGKKDELLRMVASASEEsETDSscstplhprqplapAVALS 104
Cdd:COG4913 604 LGFDNRAKLAALEAELAELEEELAEAeerLEALEAELDALQERREALQRLAEYSWD-EIDV--------------ASAER 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 105 QLEALQGKMSDLEEENLALRSEARHLKTETITYEEKEQQLvSDCVKELRESNSQMVNLTEELSHKNEEVMRHQEEISQLL 184
Cdd:COG4913 669 EIAELEAELERLDASSDDLAALEEQLEELEAELEELEEEL-DELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL 747
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1696052198 185 SQivELQHRVKELALEKEELRIHLQASKDaQRSLTAELNELADR 228
Cdd:COG4913 748 RA--LLEERFAAALGDAVERELRENLEER-IDALRARLNRAEEE 788
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
44-227 |
3.73e-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: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 44 ESVEEQLAQALDQVHQLQHELGK--------KDELLRMVASASEESETDSSCSTPLHprqplapavALSQLEA-LQGKMS 114
Cdd:pfam04108 115 EILRDALKELIDELQAAQESLDSdlkrfdddLRDLQKELESLSSPSESISLIPTLLK---------ELESLEEeMASLLE 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 115 DLEEE----NLALRSEARHLKtETITYEEKEQQLVSDCVKELRESNSQMVNLTEELSHKNEEVMRHQEEISQLLSQIVEL 190
Cdd:pfam04108 186 SLTNHydqcVTAVKLTEGGRA-EMLEVLENDARELDDVVPELQDRLDEMENNYERLQKLLEQKNSLIDELLSALQLIAEI 264
|
170 180 190
....*....|....*....|....*....|....*..
gi 1696052198 191 QHRVKELALEKEELRIHLQASKDAQRSLTAELNELAD 227
Cdd:pfam04108 265 QSRLPEYLAALKEFEERWEEEKETIEDYLSELEDLRE 301
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
9-228 |
3.93e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 9 EVVTHLLAERDRdlELAARIGQSLLQRnhLLQERNESveEQLAQALDQVHQLQHELGKKDELLRMVASASEEsetdsscs 88
Cdd:PRK04863 480 QLVRKIAGEVSR--SEAWDVARELLRR--LREQRHLA--EQLQQLRMRLSELEQRLRQQQRAERLLAEFCKR-------- 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 89 tplHPRQPLAPAVA---LSQLEALQGKMSDLEEENLALRSEARHlktetityeeKEQQLVSDcVKELRESNSQMVNLTEE 165
Cdd:PRK04863 546 ---LGKNLDDEDELeqlQEELEARLESLSESVSEARERRMALRQ----------QLEQLQAR-IQRLAARAPAWLAAQDA 611
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 166 LSHKNEEVMRHQEEISQLLSQIVELQHRVKELALEKEEL-----RIHLQASKDAQR--SLTAELNELADR 228
Cdd:PRK04863 612 LARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELaarkqALDEEIERLSQPggSEDPRLNALAER 681
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
15-244 |
4.87e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.01 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 15 LAERDRDLELAARIGQSLLQrnHLLQERNESVE---EQLAQA------LDQVHQ-LQHELGKKDELLRMVASASEESEtd 84
Cdd:pfam01576 329 VTELKKALEEETRSHEAQLQ--EMRQKHTQALEeltEQLEQAkrnkanLEKAKQaLESENAELQAELRTLQQAKQDSE-- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 85 sscstplHPRQPLApavalSQLEALQGKMSDLEEENLALRSEARHLKTE----TITYEEKEQQLVSdCVKELRESNSQMV 160
Cdd:pfam01576 405 -------HKRKKLE-----GQLQELQARLSESERQRAELAEKLSKLQSElesvSSLLNEAEGKNIK-LSKDVSSLESQLQ 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 161 NLTEELshkneevmrhQEEISQLLSqiveLQHRVKELALEKEELRIHLQASKDAQRSLTAELN----ELAD--RNVECVG 234
Cdd:pfam01576 472 DTQELL----------QEETRQKLN----LSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLStlqaQLSDmkKKLEEDA 537
|
250
....*....|
gi 1696052198 235 MLHESQEEIK 244
Cdd:pfam01576 538 GTLEALEEGK 547
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
14-249 |
5.28e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 43.86 E-value: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 14 LLAERDRDLELAARIGQSLLQRNHLLQERNESVEEQLAQALDQVHQ-----LQHELGKKDELLRMVASASEESETDSSCS 88
Cdd:pfam05667 216 LAAAQEWEEEWNSQGLASRLTPEEYRKRKRTKLLKRIAEQLRSAALagteaTSGASRSAQDLAELLSSFSGSSTTDTGLT 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 89 -------------TPLHPRQPLAPAVALSQLEALQGKMsdlEEENLALRSEARHLktetityEEKEQQLVSDcVKELRES 155
Cdd:pfam05667 296 kgsrfthteklqfTNEAPAATSSPPTKVETEEELQQQR---EEELEELQEQLEDL-------ESSIQELEKE-IKKLESS 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 156 NSQMVNLTEELSHKNEE------VMRH--------QEEISQLLSQIVELQHRVKELALEKEELRIhlqaskdaqrSLTAE 221
Cdd:pfam05667 365 IKQVEEELEELKEQNEElekqykVKKKtldllpdaEENIAKLQALVDASAQRLVELAGQWEKHRV----------PLIEE 434
|
250 260 270
....*....|....*....|....*....|.
gi 1696052198 222 LNELADrnvECVGMLHESQ---EEIKELRSK 249
Cdd:pfam05667 435 YRALKE---AKSNKEDESQrklEEIKELREK 462
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
40-249 |
6.06e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 6.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 40 QERNESVEEQLAQALDQVHQLQHELgkKDELLRMVASASEesetdsscstplhprqplaPAVALSQLEALQGKMSDleee 119
Cdd:PHA02562 215 IARKQNKYDELVEEAKTIKAEIEEL--TDELLNLVMDIED-------------------PSAALNKLNTAAAKIKS---- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 120 nlalrsearhlKTETITYEEK---EQQLVSDCVKELRESNSQMVNLTE---ELSHKNEEVMRHQEEISQLLSQIVELQHR 193
Cdd:PHA02562 270 -----------KIEQFQKVIKmyeKGGVCPTCTQQISEGPDRITKIKDklkELQHSLEKLDTAIDELEEIMDEFNEQSKK 338
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1696052198 194 VKELALEKEELRIHLQASKDAQRSLTAELNELADRNVECVGMLHESQEEIKELRSK 249
Cdd:PHA02562 339 LLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKT 394
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
14-226 |
6.20e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.53 E-value: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 14 LLAERDRdLELAARIGQSLLQRNHLLQERNESVEEQLAQALDQVHQLQHELGKKDELLRMVASASEESEtDsscstplhp 93
Cdd:COG0497 211 LEEERRR-LSNAEKLREALQEALEALSGGEGGALDLLGQALRALERLAEYDPSLAELAERLESALIELE-E--------- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 94 rqplapavALSQLEALQGKMsDLEEENLAL----RSEARHLKtetityeekeqqlvsdcvKELRESNSQMVNLTEELSHK 169
Cdd:COG0497 280 --------AASELRRYLDSL-EFDPERLEEveerLALLRRLA------------------RKYGVTVEELLAYAEELRAE 332
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1696052198 170 NEEVMRHQEEISQLLSQIVELQHRVKELALEKEELRIhlQASKDAQRSLTAELNELA 226
Cdd:COG0497 333 LAELENSDERLEELEAELAEAEAELLEAAEKLSAARK--KAAKKLEKAVTAELADLG 387
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
34-205 |
6.63e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 6.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 34 QRNHLLQERNESVEEQLAQALDQVHQLQHELGKKDELLRMVASASEESETDsscstplhprqplapavalsQLEALQGKM 113
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGD--------------------RLEQLEREI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 114 SDLEEEnLALRSEARHlktetiTYEEKEQQL---VSDCVKELRESNSQMVNLTEELShknEEVMRHQEEISQLLSQIVEL 190
Cdd:COG4913 348 ERLERE-LEERERRRA------RLEALLAALglpLPASAEEFAALRAEAAALLEALE---EELEALEEALAEAEAALRDL 417
|
170
....*....|....*
gi 1696052198 191 QHRVKELALEKEELR 205
Cdd:COG4913 418 RRELRELEAEIASLE 432
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
31-249 |
7.17e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.42 E-value: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 31 SLLQRNHLLQERNESVEEQLAQALDQVHQLQHELGKKD-ELLRMVASASEESETDSSCSTPLHPRQPLAPAVAlSQLEAL 109
Cdd:TIGR00618 376 TLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDtRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAIT-CTAQCE 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 110 QGKMSDLEEENLALRSEARHLKT-ETITYEEKEQQLVSDCVKELRESNSQMvnLTEELSHKN------------------ 170
Cdd:TIGR00618 455 KLEKIHLQESAQSLKEREQQLQTkEQIHLQETRKKAVVLARLLELQEEPCP--LCGSCIHPNparqdidnpgpltrrmqr 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 171 --EEVMRHQEEISQLLSQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELadRNVEcVGMLHESQEEIKELRS 248
Cdd:TIGR00618 533 geQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNL--QNIT-VRLQDLTEKLSEAEDM 609
|
.
gi 1696052198 249 K 249
Cdd:TIGR00618 610 L 610
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
95-249 |
7.86e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 7.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 95 QPLAPAVALSQLEALQGKMSDLEEENLALRSEARHLKtetityeekeqqlvsdcvKELRESNSQMVNLTEELSHKNEEVM 174
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALL------------------KQLAALERRIAALARRIRALEQELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 175 RHQEEISQLLSQIVELQhrvKELALEKEELRIHLQA------------------SKDAQRSLTAeLNELADRNVECVGML 236
Cdd:COG4942 80 ALEAELAELEKEIAELR---AELEAQKEELAELLRAlyrlgrqpplalllspedFLDAVRRLQY-LKYLAPARREQAEEL 155
|
170
....*....|...
gi 1696052198 237 HESQEEIKELRSK 249
Cdd:COG4942 156 RADLAELAALRAE 168
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
110-249 |
8.21e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.35 E-value: 8.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 110 QGKMSDLEEENLALRSEarhLKTETITYE--EKEQQLVSDCVKELRESNSQMVNLTEELSHKNEEVmrhqEEISQllsQI 187
Cdd:PRK01156 137 QGEMDSLISGDPAQRKK---ILDEILEINslERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLEL----ENIKK---QI 206
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1696052198 188 VELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADRNvecvGMLHESQEEIKELRSK 249
Cdd:PRK01156 207 ADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLE----DMKNRYESEIKTAESD 264
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
105-246 |
1.40e-03 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 42.34 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 105 QLEALQgkmsDLEEENLALRSEARHLKTEtitYEE---KEQQLVSDCVKELRESNSQMVNLTEelshkNEEVMRhqEEIS 181
Cdd:pfam10168 573 QLQELQ----SLEEERKSLSERAEKLAEK---YEEikdKQEKLMRRCKKVLQRLNSQLPVLSD-----AEREMK--KELE 638
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1696052198 182 QLLSQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADRNVEcvGMLHESQEEIKEL 246
Cdd:pfam10168 639 TINEQLKHLANAIKQAKKKMNYQRYQIAKSQSIRKKSSLSLSEKQRKTIK--EILKQLGSEIDEL 701
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
19-213 |
1.91e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 19 DRDLELAARIGQSLLQRNHLLQERNESVEEQlAQALDQVHQLQHELGKKDELLRMVASASEESETDSSCSTPLHPRQPLA 98
Cdd:PHA02562 223 DELVEEAKTIKAEIEELTDELLNLVMDIEDP-SAALNKLNTAAAKIKSKIEQFQKVIKMYEKGGVCPTCTQQISEGPDRI 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 99 PAVALS------QLEALQGKMSDLEE---ENLALRSEARHLKTEtitYEEKEQQLVSdCVKELRESNSQMVNLTEElsHK 169
Cdd:PHA02562 302 TKIKDKlkelqhSLEKLDTAIDELEEimdEFNEQSKKLLELKNK---ISTNKQSLIT-LVDKAKKVKAAIEELQAE--FV 375
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1696052198 170 NEEvmrhqEEISQLLSQIVELQHRVKELALEKEELRIHLQASKD 213
Cdd:PHA02562 376 DNA-----EELAKLQDELDKIVKTKSELVKEKYHRGIVTDLLKD 414
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
15-228 |
1.91e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 15 LAERDRDLELAARIGQSLLQRNHLLQERNESVEEQLAQALDQVHQLQHELGKKDELLRMVASASEESETDSscstplhpr 94
Cdd:COG4717 352 LLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELL--------- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 95 QPLAPAVALSQLEALQGKMSDLEEENLALRSEARHLKTEtityeekeqqlvsdcVKELRESnsqmvnltEELSHKneevm 174
Cdd:COG4717 423 EALDEEELEEELEELEEELEELEEELEELREELAELEAE---------------LEQLEED--------GELAEL----- 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1696052198 175 rhQEEISQLLSQIVELQHRVKELALEKEELRihlQASKDAQRSLTAELNELADR 228
Cdd:COG4717 475 --LQELEELKAELRELAEEWAALKLALELLE---EAREEYREERLPPVLERASE 523
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
154-228 |
1.99e-03 |
|
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.
Pssm-ID: 439196 [Multi-domain] Cd Length: 91 Bit Score: 38.32 E-value: 1.99e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1696052198 154 ESNSQMVNLTEELSHKNEEVMRHQEEISQLLSQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADR 228
Cdd:cd22887 1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVER 75
|
|
| DUF4456 |
pfam14644 |
Domain of unknown function (DUF4456); This domain family is found in bacteria and eukaryotes, ... |
137-249 |
2.22e-03 |
|
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: 40.35 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 137 YEEKEQQLVSDCVKELREsnsQMVNLTEELSHKNEEVM-----RHQEEISQLLSQIV-ELQHRVKELALEKE----ELRI 206
Cdd:pfam14644 41 YQEQADEYHNSCLQELRN---QVERLEELLPSVPELIFesllkRHLQKLERAMKNIAaEFSQKQKQLEQLKQqheqQLRP 117
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1696052198 207 HLQaskDAQRSltAELNEL----ADRNVECVGMLHESQEEIKELRSK 249
Cdd:pfam14644 118 TLG---HPQNA--QELEQLcdreEDRQKEHIELIQAHREALLEAVDK 159
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
59-251 |
2.77e-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: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 59 QLQHELGKKDELLRMVASASEESETDSSCSTPLHprqplapavalsqlEALQGKMSDLEEENLALRSEARHLKTETITYE 138
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDR--------------EQWERQRRELESRVAELKEELRQSREKHEELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 139 E--KEQQLVSDCVKE---------------LRESNSQMVNLTEELSHKNEEVMRHQEEISQLLSQIvelqhrvKELALEK 201
Cdd:pfam07888 101 EkyKELSASSEELSEekdallaqraahearIRELEEDIKTLTQRVLERETELERMKERAKKAGAQR-------KEEEAER 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1696052198 202 EELRIHLQASKDAQRSLTAELNELADRNVECVGMLHESQEEIKELRSKNT 251
Cdd:pfam07888 174 KQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLT 223
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
20-244 |
3.51e-03 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 40.82 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 20 RDLELAARIGQSLLQRNHLLQ-----ERNESVEEQ-----LAQALDQVHQLQHE---LGKKDELLRMVASASE-ESETDS 85
Cdd:pfam15742 93 RELELEVLKQAQSIKSQNSLQeklaqEKSRVADAEekileLQQKLEHAHKVCLTdtcILEKKQLEERIKEASEnEAKLKQ 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 86 SCSTPLHPRQPLAPAVA--LSQLEALQGKMSDLEEENLALRS-----EAR--HLKTETITYEE--------KEQQLVSDC 148
Cdd:pfam15742 173 QYQEEQQKRKLLDQNVNelQQQVRSLQDKEAQLEMTNSQQQLriqqqEAQlkQLENEKRKSDEhlksnqelSEKLSSLQQ 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 149 VKE-LRESNSQMVN-LTEELSHKNEEVMRHQEEIS---QLLSQIVELQ-HRVKELALEKEELRIHLQASKDAQRSLTAEL 222
Cdd:pfam15742 253 EKEaLQEELQQVLKqLDVHVRKYNEKHHHHKAKLRrakDRLVHEVEQRdERIKQLENEIGILQQQSEKEKAFQKQVTAQN 332
|
250 260
....*....|....*....|..
gi 1696052198 223 NELADRNVECVGMLHESQEEIK 244
Cdd:pfam15742 333 EILLLEKRKLLEQLTEQEELIK 354
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
39-255 |
3.93e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 39 LQERNESVEEQLAQALDQVHQLQHELGKKDELLRMVASASEESETDSscstplhprqplapAVALSQLEALQGKMSDLEE 118
Cdd:COG3883 21 KQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI--------------DKLQAEIAEAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 119 EnlaLRSEARHLKTE--TITYEEkeqQLVS-----------DCVKELRESNSQMVnltEELSHKNEEVMRHQEEISQLLS 185
Cdd:COG3883 87 E---LGERARALYRSggSVSYLD---VLLGsesfsdfldrlSALSKIADADADLL---EELKADKAELEAKKAELEAKLA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 186 QIVELQhrvKELALEKEELRIHLQASKDAQRSLTAELNELADRNVECVGMLHESQEEIKELRSKNTPSAG 255
Cdd:COG3883 158 ELEALK---AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| HAUS5 |
pfam14817 |
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. ... |
16-86 |
4.60e-03 |
|
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. The HAUS augmin-like complex contributes to mitotic spindle assembly, maintenance of chromosome integrity and completion of cytokinesis.
Pssm-ID: 464332 [Multi-domain] Cd Length: 643 Bit Score: 40.80 E-value: 4.60e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1696052198 16 AERDRDLELAARIGQSLLQRNHLLQERNESVEE---QLAQALDQVHQLQHEL-GKKDELLRMVASASEESETDSS 86
Cdd:pfam14817 285 YESNHLLDVSSDESSDLPSVRQLLERQWAHVQQflnELAETRSRCQQLQARLqGLKDEAELESLGIGDTSQNDSL 359
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
102-205 |
4.69e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 102 ALSQLEALQGKMSDLEEENLALRSEARHLKTETITYEEKEQQL---VSDCVKELRESNSQMVNLTEELSHKNEEVMRHQE 178
Cdd:COG1340 151 KAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELheeMIELYKEADELRKEADELHKEIVEAQEKADELHE 230
|
90 100
....*....|....*....|....*..
gi 1696052198 179 EISQLLSQIVELQHRVKELALEKEELR 205
Cdd:COG1340 231 EIIELQKELRELRKELKKLRKKQRALK 257
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
104-260 |
4.97e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 40.65 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 104 SQLEALQGKMSDL----EEENLALRSEARHLKTETITYEEKEQQLVSDcVKELRESNSQMVNLTEELSHKNEEVMRHQEE 179
Cdd:pfam07888 34 NRLEECLQERAELlqaqEAANRQREKEKERYKRDREQWERQRRELESR-VAELKEELRQSREKHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 180 ISQ----LLSQIVELQHRVKELalekeELRIHLQASKDAQRSltAELNELADRNVECVGMLHESQEEIKELRSKNTPSAG 255
Cdd:pfam07888 113 LSEekdaLLAQRAAHEARIREL-----EEDIKTLTQRVLERE--TELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEE 185
|
....*
gi 1696052198 256 MRRHL 260
Cdd:pfam07888 186 ELRSL 190
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
41-249 |
5.31e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 41 ERNESVEEQLAQALDQVHQLQHELGKKDELLRMVASASEESETDSscstplhprqplapAVALSQLEALQGKMSDLEEEN 120
Cdd:PRK02224 223 ERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETI--------------AETEREREELAEEVRDLRERL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 121 LALRSEARHLKTETiTYEEKEQQLVSDCVKELRESNSQmvnLTEELSHKNEEVMRHQEEISQLLSQIVELQHRVKELALE 200
Cdd:PRK02224 289 EELEEERDDLLAEA-GLDDADAEAVEARREELEDRDEE---LRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREE 364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 201 KEELRIHLQASKDAQRSLTAELNEL---------------------ADRNVECVGMLHESQEEIKELRSK 249
Cdd:PRK02224 365 AAELESELEEAREAVEDRREEIEELeeeieelrerfgdapvdlgnaEDFLEELREERDELREREAELEAT 434
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
17-250 |
6.62e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 6.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 17 ERDRDL-ELAARIgQSLLQRNHLLQERNESVEEQLAQALDQVHQLQHElgkKDELlrmvASASEESETDSScstplhpRQ 95
Cdd:PRK02224 499 ERAEDLvEAEDRI-ERLEERREDLEELIAERRETIEEKRERAEELRER---AAEL----EAEAEEKREAAA-------EA 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 96 PLAPAVALSQLEALQGKMSDLEEENLALRSearhLKTETITYEEKEQQLVsdcvkELRESNSQMVNLTEE----LSHKNE 171
Cdd:PRK02224 564 EEEAEEAREEVAELNSKLAELKERIESLER----IRTLLAAIADAEDEIE-----RLREKREALAELNDErrerLAEKRE 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 172 evmRHQ-----------EEISQLLSQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADR------NVECVG 234
Cdd:PRK02224 635 ---RKReleaefdeariEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERrealenRVEALE 711
|
250 260
....*....|....*....|....
gi 1696052198 235 MLHESQEEIK--------ELRSKN 250
Cdd:PRK02224 712 ALYDEAEELEsmygdlraELRQRN 735
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
114-244 |
7.30e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 38.73 E-value: 7.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 114 SDLEEENLALRseaRHLKTETITYEEKEQQlvsdCVKELRESNSQMVNLTEELSHKNEEVMRHQEEISQLLSQIVELQH- 192
Cdd:pfam13851 18 NDITRNNLELI---KSLKEEIAELKKKEER----NEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLKNl 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1696052198 193 --RVKELALEKEELRIHLQASKDAQRSLTAELNELADRNVECVgmlHESQEEIK 244
Cdd:pfam13851 91 kaRLKVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAAI---QDVQQKTG 141
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
171-249 |
7.91e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.14 E-value: 7.91e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1696052198 171 EEVMRHQEEISQLLSQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADRnvecvgmLHESQEEIKELRSK 249
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKE-------IKRLELEIEEVEAR 74
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
164-245 |
9.16e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.77 E-value: 9.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 164 EELSHKNEEVMRHQEEISQLLSQIVELQHRVKELALEKEELRIHLQASKDaqrsLTAELNE----LADRNVECVGMLHES 239
Cdd:pfam01576 5 EEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETE----LCAEAEEmrarLAARKQELEEILHEL 80
|
....*.
gi 1696052198 240 QEEIKE 245
Cdd:pfam01576 81 ESRLEE 86
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
9-224 |
9.38e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 39.67 E-value: 9.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 9 EVVTHLLAERDRDLELAARIGQSLLQRNHLlqeRNE--SVEEQLAQALDQVHQLQHELGKKDELLRMVASASEEsetdss 86
Cdd:pfam19220 38 AILRELPQAKSRLLELEALLAQERAAYGKL---RRElaGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEE------ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 87 cstplhprQPLAPAVALSQLEALQGKMSD-------LEEENLALRSEArhlktetityEEKEQQLVsdcvkelrESNSQM 159
Cdd:pfam19220 109 --------LRIELRDKTAQAEALERQLAAeteqnraLEEENKALREEA----------QAAEKALQ--------RAEGEL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1696052198 160 VNLTEELSHKNEEVMRHQEEISQLLSQIVELQHRVKELAlekEELRIHLQASKDAQRSLTAELNE 224
Cdd:pfam19220 163 ATARERLALLEQENRRLQALSEEQAAELAELTRRLAELE---TQLDATRARLRALEGQLAAEQAE 224
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
51-203 |
9.71e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 39.89 E-value: 9.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 51 AQALDQVHQLQHE---LGKKDELL---------RMVASASEESETDSSCSTPLHPRQPLAPAVAL--SQLEALQGKMSDL 116
Cdd:PLN02939 152 LQALEDLEKILTEkeaLQGKINILemrlsetdaRIKLAAQEKIHVEILEEQLEKLRNELLIRGATegLCVHSLSKELDVL 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052198 117 EEENLALRSEARHLKTETITYE---------EKEQQLVSDCVKEL-------RESNSQMVNL--------TEELSHKNEE 172
Cdd:PLN02939 232 KEENMLLKDDIQFLKAELIEVAeteervfklEKERSLLDASLRELeskfivaQEDVSKLSPLqydcwwekVENLQDLLDR 311
|
170 180 190
....*....|....*....|....*....|.
gi 1696052198 173 VMRHQEEISQLLSQIVELQHRVKELALEKEE 203
Cdd:PLN02939 312 ATNQVEKAALVLDQNQDLRDKVDKLEASLKE 342
|
|
| |
