|
Name |
Accession |
Description |
Interval |
E-value |
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
44-353 |
9.31e-146 |
|
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: 437.53 E-value: 9.31e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 44 LYDSQDWVIsPICSPEEEPCPTSISPMLAEETFTYMtylsldpssyshpgsrVLSADRVEQMTKTYNDIEVVTHLLAERD 123
Cdd:pfam04849 17 GYANQDWKI-PSPAGRPPEVSLPLSPEQIRETLNYF----------------LLCSDRVSQMTKTYNDIEAVTRLLEEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 124 RDLELAARIGQSLLQRNHLLQERNESVEEQLAQALDQVHQLQHELGKKDELLRMVASASEESETDSSCSTPLHPRQPLAP 203
Cdd:pfam04849 80 RDLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEILQLRHELSKKDDLLQIYSNDAEESETESSCSTPLRRNESFSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 204 AVALSQLEALQGKMSDLEEENLALRSEARHLKTETITYEEKEQQLVSDCVKELRESNSQMVNLTEELSHKNEEVMRHQEE 283
Cdd:pfam04849 160 LHGCVQLDALQEKLRGLEEENLKLRSEASHLKTETDTYEEKEQQLMSDCVEQLSEANQQMAELSEELARKMEENLRQQEE 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 284 ISQLLSQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADRNVECVGMLHESQEEIKELRSK 353
Cdd:pfam04849 240 ITSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLGMLHEAQEELKELRKK 309
|
|
| Milton |
pfam12448 |
Kinesin associated protein; This domain family is found in eukaryotes, and is typically ... |
417-557 |
9.82e-23 |
|
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: 96.20 E-value: 9.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 417 RAAAMATP--PIPGSGGSCLVMTAQPF----LSAQGIDQSHCGAKEevpLGKPGAPGGNDLVSALHRLSLRRQNFLCERQ 490
Cdd:pfam12448 25 RSSSSSTPrsSYYGGDGSSISLDNRTNsilsETSSSQDSGYDRPKK---PGTPGTPGARDLEAALRRLSLRRQNYLSERR 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 491 FFQAERDKKLEALAGGVESD-VEGSGYSSPMSSVMSSFTNLSEFSVSSSCFKT--FLPEKLQIVKPMEGS 557
Cdd:pfam12448 102 FFEEERERKLLALAGTYNYDeGEHGGSLTPNDSIMSLGSNHSGSSSHSSGFSSrsYLPEKLQIVKPLEGS 171
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-351 |
4.94e-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: 77.02 E-value: 4.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 101 RVEQMTKTYNDIE----VVTHLLAERDRDLELAARIGQSLLQRNHLLQERNESVEEQLAQALDQVHQLQHELGKKDELLR 176
Cdd:TIGR02168 685 KIEELEEKIAELEkalaELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 177 MVASASEESETdsscstplhprqplAPAVALSQLEALQGKMSDLEEENLALRSEARHLKTETITYEEKEQQLVS---DCV 253
Cdd:TIGR02168 765 ELEERLEEAEE--------------ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRErleSLE 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 254 KELRESNSQMVNLTEELSHKNEEVMRHQEEISQLLSQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADRN 333
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
|
250
....*....|....*...
gi 1696052192 334 VECVGMLHESQEEIKELR 351
Cdd:TIGR02168 911 SELRRELEELREKLAQLE 928
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
95-392 |
4.56e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.01 E-value: 4.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 95 RVLSADRVEQMTKtyNDIEVVTHLLAERDRdLElaarigqSLLQRNHLLQERNESVEEQLAQALDQVHQLQHELGKKDEL 174
Cdd:PRK03918 153 QILGLDDYENAYK--NLGEVIKEIKRRIER-LE-------KFIKRTENIEELIKEKEKELEEVLREINEISSELPELREE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 175 LRMVASASEESETDSSCSTPLHprqplapavalSQLEALQGKMSDLEEENLALRSEARHLKTETITYEEKEQQLvsdcvK 254
Cdd:PRK03918 223 LEKLEKEVKELEELKEEIEELE-----------KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-----K 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 255 ELRESNSQMVNLTEELSHKNEEVMRHQEEISQLLSQIVELQHRVKELALEKEELrihlqaskdaqRSLTAELNELADRnv 334
Cdd:PRK03918 287 ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL-----------EELKKKLKELEKR-- 353
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1696052192 335 ecVGMLHESQEEIKELRSKNTPSAGMRRHLpyGLFPMDSLAAEIEGTMRRELSVEDEV 392
Cdd:PRK03918 354 --LEELEERHELYEEAKAKKEELERLKKRL--TGLTPEKLEKELEELEKAKEEIEEEI 407
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
111-353 |
3.35e-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: 3.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 111 DIEVVTHLLAERDRDLELA------ARIGQSLLQRNHLLQERNESVEEqLAQALDQVHQLQHELGKkDELLRMVASASEE 184
Cdd:TIGR02169 222 EYEGYELLKEKEALERQKEaierqlASLEEELEKLTEEISELEKRLEE-IEQLLEELNKKIKDLGE-EEQLRVKEKIGEL 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 185 SETDSSCSTPLhprqplapAVALSQLEALQGKMSDLEEENLALRSEARHLKTEtITYEEKEQQLVSDCVKELRESNSQMV 264
Cdd:TIGR02169 300 EAEIASLERSI--------AEKERELEDAEERLAKLEAEIDKLLAEIEELERE-IEEERKRRDKLTEEYAELKEELEDLR 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 265 NLTEELSHKN----EEVMRHQEEISQLLSQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADRnvecvgmL 340
Cdd:TIGR02169 371 AELEEVDKEFaetrDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEE-------K 443
|
250
....*....|...
gi 1696052192 341 HESQEEIKELRSK 353
Cdd:TIGR02169 444 EDKALEIKKQEWK 456
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
121-352 |
4.01e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.19 E-value: 4.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 121 ERDRDLELAARIGQSLLQRNHLLQERNESVEEQLAQALDQVHQLQHELgkkdELLRMVASASEEsetdsscstplhprqp 200
Cdd:COG1196 222 LKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL----EELRLELEELEL---------------- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 201 lapavalsQLEALQGKMSDLEEENLALRSEARHLKTETITYEEKEQQLVsdcvKELRESNSQMVNLTEELSHKNEEVMRH 280
Cdd:COG1196 282 --------ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE----EELAELEEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1696052192 281 QEEISQLLSQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADRNVECVGMLHESQEEIKELRS 352
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
102-352 |
7.46e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.15 E-value: 7.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 102 VEQMTKTYNDIEVVTHLLAE-RDRDLELAARIgQSLLQRNHLLQERNESVEEQLAQALDQVHQLQHELGKKDELLRMVAS 180
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEElRLEVSELEEEI-EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 181 ASEESETDSSCSTPlhprqplapavalsQLEALQGKMSDLEEENLALRSEARHLKTETITYEEKEQQLVSDcVKELRES- 259
Cdd:TIGR02168 331 KLDELAEELAELEE--------------KLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK-VAQLELQi 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 260 ---NSQMVNLTEELSHKNEEVMRHQEEISQLLSQIV-----ELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELAD 331
Cdd:TIGR02168 396 aslNNEIERLEARLERLEDRRERLQQEIEELLKKLEeaelkELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
|
250 260
....*....|....*....|.
gi 1696052192 332 RNVECVGMLHESQEEIKELRS 352
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLER 496
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
116-418 |
2.72e-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: 61.34 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 116 THLLAERDrdlELAARigqsLLQRNHLLQERNESVEEQLAQALDQVHQLQHELGKKDELLRMVASASEESETdsscstpl 195
Cdd:pfam01576 53 TELCAEAE---EMRAR----LAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEA-------- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 196 hPRQPLapavalsQLE--ALQGKMSDLEEENLALRSEARHLKTETITYEEKeqqlVSDCVKELRESNSQMVNLTEeLSHK 273
Cdd:pfam01576 118 -ARQKL-------QLEkvTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER----ISEFTSNLAEEEEKAKSLSK-LKNK 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 274 NEEVMRHQE----------------------EISQLLSQIVELQHRVKELALE---KEElriHLQASKDAQRSLTAELNE 328
Cdd:pfam01576 185 HEAMISDLEerlkkeekgrqelekakrklegESTDLQEQIAELQAQIAELRAQlakKEE---ELQAALARLEEETAQKNN 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 329 LADRNVECVGMLHESQEEIKELRSKNTPSAGMRRHLPYGLFPM--------DSLAAEIEGTMRRELSV-------EDEVA 393
Cdd:pfam01576 262 ALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALkteledtlDTTAAQQELRSKREQEVtelkkalEEETR 341
|
330 340
....*....|....*....|....*..
gi 1696052192 394 FQDQKVSQKRV--FQTVRVVNESVERA 418
Cdd:pfam01576 342 SHEAQLQEMRQkhTQALEELTEQLEQA 368
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
195-354 |
2.91e-09 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 60.30 E-value: 2.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 195 LHPRQPLAPAVALSQLEALQGKMSDLEEENLALRSEARHLKTEtitYEEKEQQL------VSDCVKELRESNSQMVNLTE 268
Cdd:COG4372 18 LRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREE---LEQLEEELeqarseLEQLEEELEELNEQLQAAQA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 269 ELSHKNEEVMRHQEEISQLLSQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADRnvecvgmLHESQEEIK 348
Cdd:COG4372 95 ELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ-------LESLQEELA 167
|
....*.
gi 1696052192 349 ELRSKN 354
Cdd:COG4372 168 ALEQEL 173
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
111-516 |
3.11e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.11 E-value: 3.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 111 DIEVVTHLLAERDRDLELAARIGQSLLQRNHLLQERNESVEEQLAQALDQVHQLQHELGKKDELLRMVASASEESETDSs 190
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 191 cstplhprqplapAVALSQLEALQGKMSDLEEENLALRSEARHLKTETITYEEKEQQL----------VSDCVKELRESN 260
Cdd:COG1196 305 -------------ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAeeeleeaeaeLAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 261 SQMVNLTEELSHKNEEVMRHQEE-------ISQLLSQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADRn 333
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAaaelaaqLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE- 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 334 vecvgmLHESQEEIKELRSKntpsagmrrhlpyglfpmdsLAAEIEGTMRRELSVEDEVAFQDQKVSQkrvfqtvrvvnE 413
Cdd:COG1196 451 ------EAELEEEEEALLEL--------------------LAELLEEAALLEAALAELLEELAEAAAR-----------L 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 414 SVERAAAMATPPIPGSGGSCLVMTAQPFLSAQGIDQSHCGAKEEVPLGKPGAPGGNDLVSALHRLSLRRQNFLCERQ--- 490
Cdd:COG1196 494 LLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKagr 573
|
410 420
....*....|....*....|....*...
gi 1696052192 491 --FFQAERDKKLEALAGGVESDVEGSGY 516
Cdd:COG1196 574 atFLPLDKIRARAALAAALARGAIGAAV 601
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
119-353 |
6.41e-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: 60.47 E-value: 6.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 119 LAERDRDLELAARIGQSLLQRNHLLQERN--ESVEEQLAQALDQVHQLQHELGKKDELLRMVASAS----EESETD-SSC 191
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRriENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLkerlEELEEDlSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 192 STPLhprqplapAVALSQLEALQGKMSDLEEENLALRSE----ARHLKTETItyEEKEQQLvSDCVKELRESNSQMVNLT 267
Cdd:TIGR02169 750 EQEI--------ENVKSELKELEARIEELEEDLHKLEEAlndlEARLSHSRI--PEIQAEL-SKLEEEVSRIEARLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 268 EELSHKNEEVMRHQEEISQLLSQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADRNVECVGMLHESQEEI 347
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL 898
|
....*.
gi 1696052192 348 KELRSK 353
Cdd:TIGR02169 899 RELERK 904
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
102-332 |
8.92e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 8.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 102 VEQMTKTYNDIEVVTHLLAERDRDLELAARIGQSLLQRNHLLQERNESVEEQLAQALDQVHQLQHELGKKDELLRMVASA 181
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 182 SEESETDSScstplhprqplapAVALSQLEALQGKMSDLEEENLALRSEARHLKTETITYEEKEQQLvsdcvKELRESNS 261
Cdd:COG1196 374 LAEAEEELE-------------ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE-----EALAELEE 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1696052192 262 QMVNLTEELSHKNEEVMRHQEEISQLLSQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADR 332
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
150-353 |
9.50e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.69 E-value: 9.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 150 VEEQLAQALDQVHQLQHELG---KKDELLR---MVASASEESEtdsscSTPLHPRQPLAPAVAlsQLEALQGKMSDLEEE 223
Cdd:TIGR02168 627 VVDDLDNALELAKKLRPGYRivtLDGDLVRpggVITGGSAKTN-----SSILERRREIEELEE--KIEELEEKIAELEKA 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 224 NLALRSEARHLKTEtityeekeqqlVSDCVKELRESNSQMVNLTEELSHKNEEVMRHQEEISQLLSQIVELQHRVKELAL 303
Cdd:TIGR02168 700 LAELRKELEELEEE-----------LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE 768
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1696052192 304 EKEELRIHLQASKDAQRSLTAELNELADRNVECVGMLHESQEEIKELRSK 353
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEE 818
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
143-419 |
3.22e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 143 LQERNESVEEQLAQA---LDQVHQLQHELGKKDELLRMVASA--------SEESETDSscstplhprqplapAVALSQLE 211
Cdd:TIGR02168 170 YKERRKETERKLERTrenLDRLEDILNELERQLKSLERQAEKaerykelkAELRELEL--------------ALLVLRLE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 212 ALQGKMSDLEEENLALRSEARHLKTETITYEEKEQQL---VSDCVKELRESNSQMVNLTEELSHKNEEVMRHQEEISQLL 288
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELrleVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 289 SQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADRNVECVGML-------HESQEEIKELRSKntpSAGMR 361
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELeelesrlEELEEQLETLRSK---VAQLE 392
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1696052192 362 RHLpyglfpmDSLAAEIEgTMRRELsvedevafQDQKVSQKRVFQTVRVVNESVERAA 419
Cdd:TIGR02168 393 LQI-------ASLNNEIE-RLEARL--------ERLEDRRERLQQEIEELLKKLEEAE 434
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
143-335 |
1.03e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 55.29 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 143 LQERNESVEEQLAQALDQVHQLQHELGK-KDELLRMVASASEESETDSSCSTPLhprqplapAVALSQLEALQGKMSDLE 221
Cdd:COG4372 43 LQEELEQLREELEQAREELEQLEEELEQaRSELEQLEEELEELNEQLQAAQAEL--------AQAQEELESLQEEAEELQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 222 EENLALRSEARHLKTETITYEEKEQQLVSdcvkELRESNSQMVNLTEELSHKNEEVMRHQEEISQLLSQivELQHRVKEL 301
Cdd:COG4372 115 EELEELQKERQDLEQQRKQLEAQIAELQS----EIAEREEELKELEEQLESLQEELAALEQELQALSEA--EAEQALDEL 188
|
170 180 190
....*....|....*....|....*....|....
gi 1696052192 302 ALEKEELRIHLQASKDAQRSLTAELNELADRNVE 335
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLE 222
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
126-422 |
1.53e-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: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 126 LELAARIGQSLLQRNH--------LLQERNESVEEQLAQALD---QVHQLQHELGKKDELL---RMVASASEESETDSSC 191
Cdd:pfam05483 361 LEELLRTEQQRLEKNEdqlkiitmELQKKSSELEEMTKFKNNkevELEELKKILAEDEKLLdekKQFEKIAEELKGKEQE 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 192 STPLhprqplapavalsqLEALQGKMSDLEEENLALRSEARH-------LKTETITYEEKEQQLVSDCVKELRESNSqmv 264
Cdd:pfam05483 441 LIFL--------------LQAREKEIHDLEIQLTAIKTSEEHylkevedLKTELEKEKLKNIELTAHCDKLLLENKE--- 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 265 nLTEELSHKNEEVMRHQEEI-------SQLLSQIV-----------ELQHRVKELALEKEELRIHLQASKDAQRSLTAEL 326
Cdd:pfam05483 504 -LTQEASDMTLELKKHQEDIinckkqeERMLKQIEnleekemnlrdELESVREEFIQKGDEVKCKLDKSEENARSIEYEV 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 327 ----NELADRNVECVGM----------LHESQEEIKELRSKNTPSAgmrRHLPYGLFPMDSLAAEIEGTMRR--ELSVED 390
Cdd:pfam05483 583 lkkeKQMKILENKCNNLkkqienknknIEELHQENKALKKKGSAEN---KQLNAYEIKVNKLELELASAKQKfeEIIDNY 659
|
330 340 350
....*....|....*....|....*....|..
gi 1696052192 391 EVAFQDQKVSQKRVFqtvrvvnESVERAAAMA 422
Cdd:pfam05483 660 QKEIEDKKISEEKLL-------EEVEKAKAIA 684
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
122-335 |
1.89e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.41 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 122 RDRDLELAARIGQSLLQ--RNHLLQERNESVEEQLAQALDQVHQLQHELGKKDELLR------MVASASEESEtdsscst 193
Cdd:COG3206 143 TSPDPELAAAVANALAEayLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEefrqknGLVDLSEEAK------- 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 194 plhprqplapaVALSQLEALQGKMSDLEEENLALRSEARHLKTETITYEEKEQQLVSDCV-----KELRESNSQMVNLTE 268
Cdd:COG3206 216 -----------LLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPViqqlrAQLAELEAELAELSA 284
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1696052192 269 ELSHKNEEVMRHQEEISQLLSQI-VELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADRNVE 335
Cdd:COG3206 285 RYTPNHPDVIALRAQIAALRAQLqQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAE 352
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
173-353 |
2.28e-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: 53.56 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 173 ELLRMVASASEESETDSSCSTPLHPRQP-LAPAVALSQLEALQGKMSDLEEENLALRSEARHLKTE-TITYEEKEQ--QL 248
Cdd:pfam15294 90 ELLEQIAEFEEREFTSSNKKPNFELNKPkLEPLNEGGGSALLHMEIERLKEENEKLKERLKTLESQaTQALDEKSKleKA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 249 VSDCVKELRESNSQMVNlTEELShKNEEVMRH-QEEISQLLSQIVELQHRVKE-LALEKEE-LRIHLQASKdAQRSLTAE 325
Cdd:pfam15294 170 LKDLQKEQGAKKDVKSN-LKEIS-DLEEKMAAlKSDLEKTLNASTALQKSLEEdLASTKHElLKVQEQLEM-AEKELEKK 246
|
170 180
....*....|....*....|....*....
gi 1696052192 326 LNELAD-RNVEcvGMLHESQEEIKELRSK 353
Cdd:pfam15294 247 FQQTAAyRNMK--EMLTKKNEQIKELRKR 273
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
119-350 |
2.30e-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: 55.06 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 119 LAERDRDLELAARIGQSLLQRNHLLQERNESVEEQLAQALDQVHQLQHELGKKDELLRMVASASEESETdsscstplhpr 198
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE----------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 199 qplapavalsQLEALQGKMSDLEEENLALRSEARHLKtetityEEKEQQlvsdcvkELRESNSQMVNLTEELSHKNEEVM 278
Cdd:TIGR02168 380 ----------QLETLRSKVAQLELQIASLNNEIERLE------ARLERL-------EDRRERLQQEIEELLKKLEEAELK 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1696052192 279 RHQEEISQLLSQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADRNVECVGML--HES-QEEIKEL 350
Cdd:TIGR02168 437 ELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQenLEGfSEGVKAL 511
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
101-330 |
2.40e-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: 54.97 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 101 RVEQMTKTYN----DIEVVTH-LLAERDRDLELAARIgQSLLQRNHLLQERNESVEEQLAQALDQVHQLQHELGKKDELL 175
Cdd:TIGR00618 529 RMQRGEQTYAqletSEEDVYHqLTSERKQRASLKEQM-QEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAE 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 176 RMVASASEESETDsscstplhprqpLAPAVALSQLEALQGKMsdleEENLALRSEARHLKTETITYEEKEQQLVSDCVKE 255
Cdd:TIGR00618 608 DMLACEQHALLRK------------LQPEQDLQDVRLHLQQC----SQELALKLTALHALQLTLTQERVREHALSIRVLP 671
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1696052192 256 LReSNSQMVNLTEELSHKNEEVMRHQEEISQLLSQIVELQHRVKELALEKEELRihlQASKDAQRSLTAELNELA 330
Cdd:TIGR00618 672 KE-LLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIE---NASSSLGSDLAAREDALN 742
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
118-303 |
3.13e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 118 LLAERDRDLELAARIGQSLLQRNHLLQERNESVEEQLAQALDQVHQLQHELGKKDELLRMVASASEESETDSScstpLHP 197
Cdd:COG4717 68 LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAE----LAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 198 RQPLAPAvALSQLEALQGKMSDLEEENLALRSEARHLKTETITYEEKEQQLVSDCVKELRESNSQMVNLTEELSHKNEEV 277
Cdd:COG4717 144 LPERLEE-LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL 222
|
170 180
....*....|....*....|....*...
gi 1696052192 278 MRHQEEISQLLSQIV--ELQHRVKELAL 303
Cdd:COG4717 223 EELEEELEQLENELEaaALEERLKEARL 250
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
105-354 |
3.18e-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: 3.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 105 MTKTYNDIEVVTHLLAERDRDLELAarigqslLQRNHLLQERNESVEEQLA-QALDQVHQLQHELGKKDELLRMvaSASE 183
Cdd:pfam02463 179 IEETENLAELIIDLEELKLQELKLK-------EQAKKALEYYQLKEKLELEeEYLLYLDYLKLNEERIDLLQEL--LRDE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 184 ESETDSscstplhprqplapavalsqlealQGKMSDLEEENLALRSEARHLKTETITYEEKEQQLVSdcvKELRESNSQM 263
Cdd:pfam02463 250 QEEIES------------------------SKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLA---KEEEELKSEL 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 264 VNLTEELSHKNEEVMRHQEEISQLLSQIVELQHRVKELALEKEEL---RIHLQASKDAQRSLTAELNELADRNVECVGML 340
Cdd:pfam02463 303 LKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELeikREAEEEEEEELEKLQEKLEQLEEELLAKKKLE 382
|
250
....*....|....
gi 1696052192 341 HESQEEIKELRSKN 354
Cdd:pfam02463 383 SERLSSAAKLKEEE 396
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
213-353 |
5.73e-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: 5.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 213 LQGKMSDLEEENLALRSEARHLKtetityeeKEQQLVSDCVKELRE----SNSQMVNLTEELSHKNE----EVMRHQEEI 284
Cdd:smart00787 142 LEGLKEGLDENLEGLKEDYKLLM--------KELELLNSIKPKLRDrkdaLEEELRQLKQLEDELEDcdptELDRAKEKL 213
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1696052192 285 SQLLSQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADRNVECVGMlheSQEEIKELRSK 353
Cdd:smart00787 214 KKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGF---TFKEIEKLKEQ 279
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
139-353 |
1.21e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 139 RNHLLQERN---------------ESVEEQLAQALDQVHQLQHELGKKDELLRMVASASEESETdsscstplhpRQPLAP 203
Cdd:COG4913 214 REYMLEEPDtfeaadalvehfddlERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYL----------RAALRL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 204 AVALSQLEALQGKMSDLEEENLALRSEARHLKTETITYEEKEQQLvsdcvKELRESNS--QMVNLTEELSHKNEEVMRHQ 281
Cdd:COG4913 284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDEL-----EAQIRGNGgdRLEQLEREIERLERELEERE 358
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1696052192 282 EEISQLLSQIVELQHRV----KELALEKEELRIHLQASKDAQRSLTAELNELADRNVECVGMLHESQEEIKELRSK 353
Cdd:COG4913 359 RRRARLEALLAALGLPLpasaEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
143-352 |
4.39e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 4.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 143 LQERNESVEEQLAQALDQVHQLQHELGKKDELLRMVASASEESETdssCSTPL--HPRQPLAPAVALsQLEALQGKMSDL 220
Cdd:PRK03918 396 LEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPV---CGRELteEHRKELLEEYTA-ELKRIEKELKEI 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 221 EEENLALRSEARhlKTETITYEEKE---QQLVSDCVKELRESNSQmVNLtEELSHKNEEVMRHQEEISQLLSQIVELQHR 297
Cdd:PRK03918 472 EEKERKLRKELR--ELEKVLKKESElikLKELAEQLKELEEKLKK-YNL-EELEKKAEEYEKLKEKLIKLKGEIKSLKKE 547
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1696052192 298 VKELALEKEELRIHLQASKDAQRSLTAELNELADRNVECVgmlHESQEEIKELRS 352
Cdd:PRK03918 548 LEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESV---EELEERLKELEP 599
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
235-354 |
4.63e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.29 E-value: 4.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 235 KTETITYEEKEQQLVSDCVKELRESNSQMVNLTEELSHKNEEVMRHQEEISQLLSQIVELQHRVKELALEKEELRIHLQA 314
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA 91
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1696052192 315 SKDAQRSLTAELNELADRNVECVGMLHESQEEIKELRSKN 354
Cdd:COG4372 92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQR 131
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
211-331 |
4.86e-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: 47.29 E-value: 4.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 211 EALQGKMSDLEEENLALRSEARHLKTETITYEEKEQQLVsdcvKELRESNSQMVNLTEELSHKNEEVMRHQEEISQLLSQ 290
Cdd:pfam10473 27 ENLERELEMSEENQELAILEAENSKAEVETLKAEIEEMA----QNLRDLELDLVTLRSEKENLTKELQKKQERVSELESL 102
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1696052192 291 IVELQHRVKElaLEKEELRIHlQASKDAQRSLTAELNELAD 331
Cdd:pfam10473 103 NSSLENLLEE--KEQEKVQMK-EESKTAVEMLQTQLKELNE 140
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
209-353 |
6.84e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 6.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 209 QLEALQGKMSDLEEENLALRSEARHLKTEtitYEEKEQQLvSDCVKELRESNSQMVNLTEELSH--KNEEVMRHQEEISQ 286
Cdd:COG1579 25 RLKELPAELAELEDELAALEARLEAAKTE---LEDLEKEI-KRLELEIEEVEARIKKYEEQLGNvrNNKEYEALQKEIES 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1696052192 287 LLSQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNEL-ADRNVEcvgmLHESQEEIKELRSK 353
Cdd:COG1579 101 LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKkAELDEE----LAELEAELEELEAE 164
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
119-355 |
6.90e-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: 6.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 119 LAERDRDLELAARIGQSLLQRNHLLQERNESVE------EQLAQALD-QVHQLQHELGKKDELLRMVASASEESEtdssc 191
Cdd:TIGR04523 365 LEEKQNEIEKLKKENQSYKQEIKNLESQINDLEskiqnqEKLNQQKDeQIKKLQQEKELLEKEIERLKETIIKNN----- 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 192 stplhprqplapavalSQLEALQGKMSDLEE--ENLALRSEARHLKTETITYE-EKEQQLVSDCVKELRESNSQMVNLTE 268
Cdd:TIGR04523 440 ----------------SEIKDLTNQDSVKELiiKNLDNTRESLETQLKVLSRSiNKIKQNLEQKQKELKSKEKELKKLNE 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 269 ELSHKNEEVMRHQEEISQLLSqivelqhrvKELALEKEELRIHLQASkdaqrSLTAELNELADR----NVECVgmLHESQ 344
Cdd:TIGR04523 504 EKKELEEKVKDLTKKISSLKE---------KIEKLESEKKEKESKIS-----DLEDELNKDDFElkkeNLEKE--IDEKN 567
|
250
....*....|.
gi 1696052192 345 EEIKELRSKNT 355
Cdd:TIGR04523 568 KEIEELKQTQK 578
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
208-350 |
9.62e-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: 9.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 208 SQLEALQGKMSDLEEENLALRSEARHLKTE----TITYEEKEQQLvSDCVKELRESNSQM--VNLTEELSHKNEEVMRHQ 281
Cdd:TIGR04523 496 KELKKLNEEKKELEEKVKDLTKKISSLKEKieklESEKKEKESKI-SDLEDELNKDDFELkkENLEKEIDEKNKEIEELK 574
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1696052192 282 EEISQLLSQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADRNVECVGM---LHESQEEIKEL 350
Cdd:TIGR04523 575 QTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIiknIKSKKNKLKQE 646
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
101-353 |
1.08e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 101 RVEQMTKTYNDIEVVTHLLAERDRDLE-LAARIGQsllqrnhlLQERNESVEEQLAQALDQVHQLQHELGKKDELLRMVA 179
Cdd:PRK03918 229 EVKELEELKEEIEELEKELESLEGSKRkLEEKIRE--------LEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 180 SASEESETDSSCSTPLHPRQPLAPAVA--LSQLEALQGKMSDLEEENLALRSEARHLKTETITYEEKEQQLvsdcvKELR 257
Cdd:PRK03918 301 FYEEYLDELREIEKRLSRLEEEINGIEerIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKK-----EELE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 258 ESNSQMVNLT-EELSHKNEEVMRH----QEEISQLLSQIVELQHRVKELALEKEELR------------IHLQASKDAQR 320
Cdd:PRK03918 376 RLKKRLTGLTpEKLEKELEELEKAkeeiEEEISKITARIGELKKEIKELKKAIEELKkakgkcpvcgreLTEEHRKELLE 455
|
250 260 270
....*....|....*....|....*....|...
gi 1696052192 321 SLTAELNELADRNVECVGMLHESQEEIKELRSK 353
Cdd:PRK03918 456 EYTAELKRIEKELKEIEEKERKLRKELRELEKV 488
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
210-353 |
1.36e-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: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 210 LEALQGKMSDLEEENLALRSEARHLKTETITYEE--KEQQLVSDCVKELRESNSQMVNLTEELSHKNEEVMRHQEEISQL 287
Cdd:pfam15905 193 LEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEyiTELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQE 272
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1696052192 288 LS-QIVELQHRVKELALEKEELrihLQASKDAQRSLTAELNELADRnvecvgmLHESQEEIKELRSK 353
Cdd:pfam15905 273 LSkQIKDLNEKCKLLESEKEEL---LREYEEKEQTLNAELEELKEK-------LTLEEQEHQKLQQK 329
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
103-355 |
1.59e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.20 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 103 EQMTKTYND-IEVVTHLLAERdRDLELAARIGQSLLQRNHLLQERNESVEEQLAQALDQVHQLQHELG------KKDELL 175
Cdd:TIGR00618 211 PCMPDTYHErKQVLEKELKHL-REALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAvleetqERINRA 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 176 RMVASASEESETDSSCstplhpRQPlapavALSQLEALQGKMSDLEEEnLALRSEARHLKTETITYEEKEQQLVSDCV-- 253
Cdd:TIGR00618 290 RKAAPLAAHIKAVTQI------EQQ-----AQRIHTELQSKMRSRAKL-LMKRAAHVKQQSSIEEQRRLLQTLHSQEIhi 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 254 -------KELRESNSQMVNLTEELsHKNEEVMRHQEEISQLLSQIVE----LQHRVKELALEKEELRIHLQASKDAQR-- 320
Cdd:TIGR00618 358 rdahevaTSIREISCQQHTLTQHI-HTLQQQKTTLTQKLQSLCKELDilqrEQATIDTRTSAFRDLQGQLAHAKKQQElq 436
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1696052192 321 ---------SLTAELNELADRNVECVGMLHESQEEIKELRSKNT 355
Cdd:TIGR00618 437 qryaelcaaAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQ 480
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
226-355 |
1.76e-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: 45.32 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 226 ALRSEARHLKTETITYEEKEQQLVSDCVKELRESNSQMVNLTEELSHKNEEVmrhqEEISQLLSQIVELQHRVKELALEK 305
Cdd:pfam07926 5 SLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERELVLHAEDI----KALQALREELNELKAEIAELKAEA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1696052192 306 EELRIHLQASKDA----QRSLTAELNELADRnvecvgmlhesqeeIKELRSKNT 355
Cdd:pfam07926 81 ESAKAELEESEESweeqKKELEKELSELEKR--------------IEDLNEQNK 120
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
203-353 |
2.30e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 203 PAVALSQLEALQGKMSDLEEENLALRSEARHLKTETITYEEKEQQLVS--------DCVKELRESNSQMVNLTEELSHKN 274
Cdd:COG4717 66 PELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEElreeleklEKLLQLLPLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 275 ---EEVMRHQEEISQLLSQIVELQHRVKELALEKEELRIHLQASKDAQ-RSLTAELNELADRNVECVGMLHESQEEIKEL 350
Cdd:COG4717 146 erlEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
...
gi 1696052192 351 RSK 353
Cdd:COG4717 226 EEE 228
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
127-351 |
3.67e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.83 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 127 ELAARIGQSLLQRNHLLQERNESVEE--QLAQALD----QVHQLQHELG----KKDELLRMVASASEE-SETDSSCSTpl 195
Cdd:COG1340 12 ELEEKIEELREEIEELKEKRDELNEElkELAEKRDelnaQVKELREEAQelreKRDELNEKVKELKEErDELNEKLNE-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 196 hprqplapavALSQLEALQGKMSDLEEENL---ALRSEARHL----KTETITyEEKEQQLVSDcVKELREsnsqMVNLTE 268
Cdd:COG1340 90 ----------LREELDELRKELAELNKAGGsidKLRKEIERLewrqQTEVLS-PEEEKELVEK-IKELEK----ELEKAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 269 ELSHKNEEVMRHQEEISQLLSQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADRNVEC---VGMLH---- 341
Cdd:COG1340 154 KALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAqekADELHeeii 233
|
250
....*....|
gi 1696052192 342 ESQEEIKELR 351
Cdd:COG1340 234 ELQKELRELR 243
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
127-365 |
3.88e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.07 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 127 ELAARIGQSLLQRNHLLQERnESVEEQLAQALDQVHQLQHELGKKDELLRMVASASEESETDSScstplHPRQPLApava 206
Cdd:COG4942 38 ELEKELAALKKEEKALLKQL-AALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE-----AQKEELA---- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 207 lSQLEALQgKMSDLEEENLALRSEarhlkteTITYEEKEQQLVSDCVKELRESNSQMVNLTEELSHKNEEVMRHQEEISQ 286
Cdd:COG4942 108 -ELLRALY-RLGRQPPLALLLSPE-------DFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1696052192 287 LLSQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADRNVECVGMLhESQEEIKELRSKNTPSAGMRRHLP 365
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 ... |
134-313 |
5.29e-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: 45.17 E-value: 5.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 134 QSLLQRNHLLQERNESVEEQLA-----------QALDQVHQLQHE--LGKKDELLRMVASASEESETdsscSTPLHPRQP 200
Cdd:pfam14662 18 QKLLQENSKLKATVETREETNAklleenlnlrkQAKSQQQAVQKEklLEEELEDLKLIVNSLEEARR----SLLAQNKQL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 201 LAPAVALSQlealqgKMSDLEEENLALRSEARHLKTETityeeKEQQLVSDCVKELRESNSQMVNLTEELShknEEVMRH 280
Cdd:pfam14662 94 EKENQSLLQ------EIESLQEENKKNQAERDKLQKKK-----KELLKSKACLKEQLHSCEDLACNRETIL---IEKTTQ 159
|
170 180 190
....*....|....*....|....*....|...
gi 1696052192 281 QEEisqLLSQIVELQHRVKELALEKEELRIHLQ 313
Cdd:pfam14662 160 IEE---LKSTVEEYSSIEEELRAEKSRLESQLP 189
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
254-418 |
5.65e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 5.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 254 KELRESNSQMvnltEELSHKNEEVMRHQEEISQLLSQIVELQHRVKELALEKEELRIHLQASKDAQR--SLTAELNELAD 331
Cdd:COG4717 71 KELKELEEEL----KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQEleALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 332 RnvecvgmLHESQEEIKELRSKNTPSAGMRRHLpyglfpmDSLAAEIEgTMRRELSVEDEVAFQDQKVSQKRVFQTVRVV 411
Cdd:COG4717 147 R-------LEELEERLEELRELEEELEELEAEL-------AELQEELE-ELLEQLSLATEEELQDLAEELEELQQRLAEL 211
|
....*..
gi 1696052192 412 NESVERA 418
Cdd:COG4717 212 EEELEEA 218
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
147-393 |
6.32e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 46.07 E-value: 6.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 147 NESVEEQ-----LAQALDQVHQLQHE---LGKKDELLRMVASAsEESETDSSCSTPLhprqplapAVALSQLEALQGKMS 218
Cdd:pfam00038 1 NEKEQLQelndrLASYIDKVRFLEQQnklLETKISELRQKKGA-EPSRLYSLYEKEI--------EDLRRQLDTLTVERA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 219 DLEEENLALRSEARHLKTEtitYEEK--EQQLVSDCVKELR-----------ESNSQMVNLTEELshkneEVMR--HQEE 283
Cdd:pfam00038 72 RLQLELDNLRLAAEDFRQK---YEDElnLRTSAENDLVGLRkdldeatlarvDLEAKIESLKEEL-----AFLKknHEEE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 284 ISQLLSQIVElQHRV--------KELALEKEELRIHL--QASKDAQ------RSLTAELNELADRNVEcvgMLHESQEEI 347
Cdd:pfam00038 144 VRELQAQVSD-TQVNvemdaarkLDLTSALAEIRAQYeeIAAKNREeaeewyQSKLEELQQAAARNGD---ALRSAKEEI 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1696052192 348 KELRskntpsagmRRhlpyglfpMDSLAAEIEGTMRRELSVEDEVA 393
Cdd:pfam00038 220 TELR---------RT--------IQSLEIELQSLKKQKASLERQLA 248
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
97-332 |
6.92e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 6.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 97 LSADRVEQMTKTYndiEVVTHLLAERDRdlELAARIGQSLLQRnhLLQERNESveEQLAQALDQVHQLQHELGKKDELLR 176
Cdd:PRK04863 467 VAQAAHSQFEQAY---QLVRKIAGEVSR--SEAWDVARELLRR--LREQRHLA--EQLQQLRMRLSELEQRLRQQQRAER 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 177 MVASASEEsetdsscstplHPRQPLAPAVA---LSQLEALQGKMSDLEEENLALRSEARHlktetityeeKEQQLVSDcV 253
Cdd:PRK04863 538 LLAEFCKR-----------LGKNLDDEDELeqlQEELEARLESLSESVSEARERRMALRQ----------QLEQLQAR-I 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 254 KELRESNSQMVNLTEELSHKNEEVMRHQEEISQLLSQIVELQHRVKELALEKEEL-----RIHLQASKDAQR--SLTAEL 326
Cdd:PRK04863 596 QRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELaarkqALDEEIERLSQPggSEDPRL 675
|
....*.
gi 1696052192 327 NELADR 332
Cdd:PRK04863 676 NALAER 681
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
134-355 |
8.36e-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: 8.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 134 QSLLQRNHLLQERNESVEEQLAQALDQVHQLQHELGKKDELLRMVAS----ASEESETDSscsTPLHPRQplapavalSQ 209
Cdd:TIGR04523 207 KKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTqlnqLKDEQNKIK---KQLSEKQ--------KE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 210 LEALQGKMSDLEEENLALRSEARHLKtetityEEKEQQLVSDCVKELRESNSQMVNLTEELSHKNEEVMRHQEEISQLLS 289
Cdd:TIGR04523 276 LEQNNKKIKELEKQLNQLKSEISDLN------NQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKK 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 290 QI-----------VELQHRVKELALEKEELRIHLQASKDAQRSLTA---------ELNELADRNVECVGMLHES-QEEIK 348
Cdd:TIGR04523 350 ELtnsesensekqRELEEKQNEIEKLKKENQSYKQEIKNLESQINDleskiqnqeKLNQQKDEQIKKLQQEKELlEKEIE 429
|
....*..
gi 1696052192 349 ELRSKNT 355
Cdd:TIGR04523 430 RLKETII 436
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
148-353 |
8.88e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 8.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 148 ESVEEQLAQALDQVHQLQHELGKKDELLRMVASASEESETDSSCSTPLHPRQplapaVALSQLEALQGKMSDLEE--ENL 225
Cdd:PRK02224 179 ERVLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQRE-----QARETRDEADEVLEEHEErrEEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 226 A-LRSEARHLkTETITYEEKEQQLVSDCVKELREsnsQMVNLTEELSHKNEEVMRHQEEISQLLSQIVELQHRVKELALE 304
Cdd:PRK02224 254 EtLEAEIEDL-RETIAETEREREELAEEVRDLRE---RLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDR 329
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1696052192 305 KEELRIHLQASKDAQRSLTAELNELADRNvecvgmlHESQEEIKELRSK 353
Cdd:PRK02224 330 LEECRVAAQAHNEEAESLREDADDLEERA-------EELREEAAELESE 371
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
53-353 |
1.15e-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: 46.17 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 53 SPICSPEEEPCPTSISPMLAEETFTYMTYLSLDPSSYSHPGSRVLSADRVEQMTKTYNDIEVVTHLLAERDRDLELAARI 132
Cdd:pfam05667 165 QTLVLPGRKGKTLKNSKELKEFYSEYLPPVTAQPSSRASVVPSLLERNAAELAAAQEWEEEWNSQGLASRLTPEEYRKRK 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 133 GQSLLQRnhllqernesVEEQLAQALDQVHQL-QHELGKKDELLRMVASASEESETDSSCS-------------TPLHPR 198
Cdd:pfam05667 245 RTKLLKR----------IAEQLRSAALAGTEAtSGASRSAQDLAELLSSFSGSSTTDTGLTkgsrfthteklqfTNEAPA 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 199 QPLAPAVALSQLEALQGKMsdlEEENLALRSEARHLktetityEEKEQQLVSDcVKELRESNSQMVNLTEELSHKNEE-- 276
Cdd:pfam05667 315 ATSSPPTKVETEEELQQQR---EEELEELQEQLEDL-------ESSIQELEKE-IKKLESSIKQVEEELEELKEQNEEle 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 277 ----VMRH--------QEEISQLLSQIVELQHRVKELALEKEELRIhlqaskdaqrSLTAELNELADrnvECVGMLHESQ 344
Cdd:pfam05667 384 kqykVKKKtldllpdaEENIAKLQALVDASAQRLVELAGQWEKHRV----------PLIEEYRALKE---AKSNKEDESQ 450
|
330
....*....|..
gi 1696052192 345 ---EEIKELRSK 353
Cdd:pfam05667 451 rklEEIKELREK 462
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
120-332 |
1.21e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 120 AERDRDlELAARIGQSLLQRNHLLQERNESVEEQLAQALDQ--VHQLQHELGKKDELLRmvaSASEESETDSScstplhp 197
Cdd:PRK02224 270 TERERE-ELAEEVRDLRERLEELEEERDDLLAEAGLDDADAeaVEARREELEDRDEELR---DRLEECRVAAQ------- 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 198 rqplapaVALSQLEALQGKMSDLEEENLALRSEARHLKTEtityeekeqqlVSDCVKELRESNSQMVNLTEELshknEEV 277
Cdd:PRK02224 339 -------AHNEEAESLREDADDLEERAEELREEAAELESE-----------LEEAREAVEDRREEIEELEEEI----EEL 396
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1696052192 278 MrhqEEISQLLSQIVELQHRVKELALEKEELRIHLqaskdaqRSLTAELNELADR 332
Cdd:PRK02224 397 R---ERFGDAPVDLGNAEDFLEELREERDELRERE-------AELEATLRTARER 441
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
159-402 |
1.68e-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: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 159 DQVHQLQHELGK-KDELLRMVASASEESETDSSCSTPLHPRQPLAPAVALSQLEALQGKMSDLEEENLALRSEARHLKTE 237
Cdd:TIGR00606 684 QRVFQTEAELQEfISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRL 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 238 TITYEEKEQQLVSDCVKELRESNSQM-VNLTEELSHKNEEVMRHQEE-------------ISQLLSQIVELQHRVKELAL 303
Cdd:TIGR00606 764 KNDIEEQETLLGTIMPEEESAKVCLTdVTIMERFQMELKDVERKIAQqaaklqgsdldrtVQQVNQEKQEKQHELDTVVS 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 304 EKEELRIHLQASKDAQRSLTAELNELADRNVECV-------GMLHESQEEIKELRSKNTPSAGMRRH-LPYGLFPMDSLA 375
Cdd:TIGR00606 844 KIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGtnlqrrqQFEEQLVELSTEVQSLIREIKDAKEQdSPLETFLEKDQQ 923
|
250 260 270
....*....|....*....|....*....|
gi 1696052192 376 AEIEGTMRRELS---VEDEVAFQDQKVSQK 402
Cdd:TIGR00606 924 EKEELISSKETSnkkAQDKVNDIKEKVKNI 953
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
204-384 |
1.95e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 204 AVALSQLEALQGKMSDLEEENLALRSEARHLKTE------TITYEEKEQQLvsdcvKELRESNSQMVNLTEELSHKNEEV 277
Cdd:COG4913 627 AEAEERLEALEAELDALQERREALQRLAEYSWDEidvasaEREIAELEAEL-----ERLDASSDDLAALEEQLEELEAEL 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 278 MRHQEEISQLLSQIVELQHRVKELALEKEELRIHLQASKDAQRS-----LTAELNELADRNVEcVGMLHESQEEIKELRS 352
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLelralLEERFAAALGDAVE-RELRENLEERIDALRA 780
|
170 180 190
....*....|....*....|....*....|..
gi 1696052192 353 KntpsagmrrhlpyglfpMDSLAAEIEGTMRR 384
Cdd:COG4913 781 R-----------------LNRAEEELERAMRA 795
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
200-330 |
2.03e-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: 44.15 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 200 PLAPAVALSQLEALQGKMSDLEEENLALRSEARHLKTETITYEEK----EQQL--VSDcVKELRESNSQMVNLTEELSHK 273
Cdd:COG1579 30 PAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARikkyEEQLgnVRN-NKEYEALQKEIESLKRRISDL 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1696052192 274 NEEVMRHQEEISQLLSQIVELQHRVK----ELALEKEELRIHLQASKDAQRSLTAELNELA 330
Cdd:COG1579 109 EDEILELMERIEELEEELAELEAELAeleaELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
132-332 |
2.16e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 132 IGQSLLQRNHLLQERNESVEEQLAQA---LDQVHQLQHELGKKDELLRMVASASEEsETDSscstplhprqplapAVALS 208
Cdd:COG4913 604 LGFDNRAKLAALEAELAELEEELAEAeerLEALEAELDALQERREALQRLAEYSWD-EIDV--------------ASAER 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 209 QLEALQGKMSDLEEENLALRSEARHLKTETITYEEKEQQLvSDCVKELRESNSQMVNLTEELSHKNEEVMRHQEEISQLL 288
Cdd:COG4913 669 EIAELEAELERLDASSDDLAALEEQLEELEAELEELEEEL-DELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL 747
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1696052192 289 SQivELQHRVKELALEKEELRIHLQASKDaQRSLTAELNELADR 332
Cdd:COG4913 748 RA--LLEERFAAALGDAVERELRENLEER-IDALRARLNRAEEE 788
|
|
| NIP100 |
COG5244 |
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ... |
122-424 |
2.22e-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: 45.06 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 122 RDRDLELAARIGQSLLQRNHLLQE-RNESV-EEQLAQALDQVHQLQHELgkkdellrmvASASEESETDSSCSTPlhprq 199
Cdd:COG5244 57 KKRHGIFIRPDDDSLLNGNAAYEKiKGGLVcESKGMDKDGEIKQENHED----------RIHFEESKIRRLEETI----- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 200 plapaVALSQLEalqgkmsdlEEENLALRSEARHLKTETITYEEK----EQQLVSDCVKELRESNSQMVnlteelshknE 275
Cdd:COG5244 122 -----EALKSTE---------KEEIVELRRENEELDKINLSLRERisseEPELNKDGSKLSYDELKEFV----------E 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 276 EVMRHQEEISQLLSQIVELQHRVKELALE--KEELRihlqaskdaqrslTAELNELADRNVECVGMLHESQEEIKELRSK 353
Cdd:COG5244 178 ESRVQVYDMVELVSDISETLNRNGSIQRSsvRECER-------------SNIHDVLFLVNGILDGVIDELNGELERLRRQ 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1696052192 354 NTpsagmrrhlpyglFPMDSLAAEIEGTMRRELSVEDEVAFQDQ-KVSQKRVFQTVRVVN-ESVERAAAMATP 424
Cdd:COG5244 245 LV-------------SLMSSHGIEVEENSRLKATLEKFQSLELKvNTLQEELYQNKLLKKfYQIYEPFAQAAL 304
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
208-350 |
2.32e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.52 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 208 SQLEALQGKMSDLEEENLALRSEARHLKtetityeekeqqlvsdcvKELRESNSQMVNLTEELSHKNEEVMRHQEEISQL 287
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELK------------------EKRDELNEELKELAEKRDELNAQVKELREEAQEL 62
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1696052192 288 LSQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADRNVEcvgmLHESQEEIKEL 350
Cdd:COG1340 63 REKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGS----IDKLRKEIERL 121
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
208-308 |
2.33e-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: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 208 SQLEALQGKMSDLEEENLALRSEARHLKTETityeEKEQQLVSdcvkELRESNSQMVNLTEELshknEEVMRHQEEisql 287
Cdd:pfam10473 59 AEIEEMAQNLRDLELDLVTLRSEKENLTKEL----QKKQERVS----ELESLNSSLENLLEEK----EQEKVQMKE---- 122
|
90 100
....*....|....*....|.
gi 1696052192 288 lsqivELQHRVKELALEKEEL 308
Cdd:pfam10473 123 -----ESKTAVEMLQTQLKEL 138
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
97-317 |
2.84e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 97 LSADRVEQMTKTYNDI---------EVVTHLLAERDRDLELAARIGQSLLQRNHLLQERNESVEEQlAQALDQVHQLQHE 167
Cdd:PHA02562 188 MKIDHIQQQIKTYNKNieeqrkkngENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDP-SAALNKLNTAAAK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 168 LGKKDELLRMVASASEESETDSSCSTPLHPRQPLAPAVALS------QLEALQGKMSDLEE---ENLALRSEARHLKTEt 238
Cdd:PHA02562 267 IKSKIEQFQKVIKMYEKGGVCPTCTQQISEGPDRITKIKDKlkelqhSLEKLDTAIDELEEimdEFNEQSKKLLELKNK- 345
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1696052192 239 itYEEKEQQLVSdCVKELRESNSQMVNLTEElsHKNEEvmrhqEEISQLLSQIVELQHRVKELALEKEELRIHLQASKD 317
Cdd:PHA02562 346 --ISTNKQSLIT-LVDKAKKVKAAIEELQAE--FVDNA-----EELAKLQDELDKIVKTKSELVKEKYHRGIVTDLLKD 414
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
178-351 |
2.89e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.85 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 178 VASASEESETDSScsTPLHPRQPLAPAVALSQLEALQGKMSDLEEENLALRSEARHLKTETityEEKEQQLvSDCVKELR 257
Cdd:COG2433 378 IEEALEELIEKEL--PEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAEL---EEKDERI-ERLERELS 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 258 ESNSQMvnltEELSHKNEEVMRHQEEISQLLSQIVELQHRVKELALEKEELRIHL---------------QASKDAQRSL 322
Cdd:COG2433 452 EARSEE----RREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWklehsgelvpvkvveKFTKEAIRRL 527
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1696052192 323 TAEL---------------------NELADRNVECV----GMLHESQEEIKELR 351
Cdd:COG2433 528 EEEYglkegdvvylrdasgagrstaELLAEAGPRAVivpgELSEAADEVLFEEG 581
|
|
| Kre28 |
pfam17097 |
Spindle pole body component; In Saccharomyces cerevisae Kre28 and Spc105 form a kinetochore ... |
149-364 |
2.95e-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: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 149 SVEEQLAQALDQV--HQLQHELGKKDELLRMVASASEESE--TDSSCSTPLH--PRQPlapAVALSQLEAL--QGKMSDL 220
Cdd:pfam17097 15 ELEEQTAHSSEQVltEQDKRLLGALRELTQSVIQLIEENSlvTVSGDAANLLidPSGI---EVKIRQLDQLveLLKVTHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 221 EEENLA--LR---SEARHLKTETITyEEKEQQLvSDCVKELREsnsqmvnltEELSHKNEEVMRHQEEISQLLSQIVELQ 295
Cdd:pfam17097 92 EQETLDnfLRytiSSTDLLQLESVS-DPKYASL-EDEVSQLED---------DTLTVLNQEIDQIKGDILQVAQEIADKQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1696052192 296 HRVKELALEK----EELRIHLQASKDAQRSLTAELNELADRNVECVGMLHESQEEIKELRSKNTPSAGMRRHL 364
Cdd:pfam17097 161 DQVNELCLETsnelDECWELLNELERLRDQRITVEEQTSNEKDTELDPVEETYEEWKSLQESLQQLEHLKEEL 233
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
119-348 |
3.49e-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: 44.78 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 119 LAERDRDLELAARIGQSLLQRnhLLQERNESVE---EQLAQA------LDQVHQ-LQHELGKKDELLRMVASASEESEtd 188
Cdd:pfam01576 329 VTELKKALEEETRSHEAQLQE--MRQKHTQALEeltEQLEQAkrnkanLEKAKQaLESENAELQAELRTLQQAKQDSE-- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 189 sscstplHPRQPLApavalSQLEALQGKMSDLEEENLALRSEARHLKTE----TITYEEKEQQLVSdCVKELRESNSQMV 264
Cdd:pfam01576 405 -------HKRKKLE-----GQLQELQARLSESERQRAELAEKLSKLQSElesvSSLLNEAEGKNIK-LSKDVSSLESQLQ 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 265 NLTEELshkneevmrhQEEISQLLSqiveLQHRVKELALEKEELRIHLQASKDAQRSLTAELN----ELAD--RNVECVG 338
Cdd:pfam01576 472 DTQELL----------QEETRQKLN----LSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLStlqaQLSDmkKKLEEDA 537
|
250
....*....|
gi 1696052192 339 MLHESQEEIK 348
Cdd:pfam01576 538 GTLEALEEGK 547
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
148-331 |
3.63e-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: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 148 ESVEEQLAQALDQVHQLQHELGK--------KDELLRMVASASEESETDSSCSTPLHprqplapavALSQLEA-LQGKMS 218
Cdd:pfam04108 115 EILRDALKELIDELQAAQESLDSdlkrfdddLRDLQKELESLSSPSESISLIPTLLK---------ELESLEEeMASLLE 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 219 DLEEE----NLALRSEARHLKtETITYEEKEQQLVSDCVKELRESNSQMVNLTEELSHKNEEVMRHQEEISQLLSQIVEL 294
Cdd:pfam04108 186 SLTNHydqcVTAVKLTEGGRA-EMLEVLENDARELDDVVPELQDRLDEMENNYERLQKLLEQKNSLIDELLSALQLIAEI 264
|
170 180 190
....*....|....*....|....*....|....*..
gi 1696052192 295 QHRVKELALEKEELRIHLQASKDAQRSLTAELNELAD 331
Cdd:pfam04108 265 QSRLPEYLAALKEFEERWEEEKETIEDYLSELEDLRE 301
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
118-330 |
4.05e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 44.30 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 118 LLAERDRdLELAARIGQSLLQRNHLLQERNESVEEQLAQALDQVHQLQHELGKKDELLRMVASASEESEtDsscstplhp 197
Cdd:COG0497 211 LEEERRR-LSNAEKLREALQEALEALSGGEGGALDLLGQALRALERLAEYDPSLAELAERLESALIELE-E--------- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 198 rqplapavALSQLEALQGKMsDLEEENLAL----RSEARHLKtetityeekeqqlvsdcvKELRESNSQMVNLTEELSHK 273
Cdd:COG0497 280 --------AASELRRYLDSL-EFDPERLEEveerLALLRRLA------------------RKYGVTVEELLAYAEELRAE 332
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1696052192 274 NEEVMRHQEEISQLLSQIVELQHRVKELALEKEELRIhlQASKDAQRSLTAELNELA 330
Cdd:COG0497 333 LAELENSDERLEELEAELAEAEAELLEAAEKLSAARK--KAAKKLEKAVTAELADLG 387
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
199-353 |
4.32e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 4.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 199 QPLAPAVALSQLEALQGKMSDLEEENLALRSEARHLKtetityeekeqqlvsdcvKELRESNSQMVNLTEELSHKNEEVM 278
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALL------------------KQLAALERRIAALARRIRALEQELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 279 RHQEEISQLLSQIVELQhrvKELALEKEELRIHLQA------------------SKDAQRSLTAeLNELADRNVECVGML 340
Cdd:COG4942 80 ALEAELAELEKEIAELR---AELEAQKEELAELLRAlyrlgrqpplalllspedFLDAVRRLQY-LKYLAPARREQAEEL 155
|
170
....*....|...
gi 1696052192 341 HESQEEIKELRSK 353
Cdd:COG4942 156 RADLAELAALRAE 168
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
138-309 |
4.40e-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: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 138 QRNHLLQERNESVEEQLAQALDQVHQLQHELGKKDELLRMVASASEESETDsscstplhprqplapavalsQLEALQGKM 217
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGD--------------------RLEQLEREI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 218 SDLEEEnLALRSEARHlktetiTYEEKEQQL---VSDCVKELRESNSQMVNLTEELShknEEVMRHQEEISQLLSQIVEL 294
Cdd:COG4913 348 ERLERE-LEERERRRA------RLEALLAALglpLPASAEEFAALRAEAAALLEALE---EELEALEEALAEAEAALRDL 417
|
170
....*....|....*
gi 1696052192 295 QHRVKELALEKEELR 309
Cdd:COG4913 418 RRELRELEAEIASLE 432
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
144-353 |
6.85e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 6.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 144 QERNESVEEQLAQALDQVHQLQHELgkKDELLRMVASASEesetdsscstplhprqplaPAVALSQLEALQGKMSDleee 223
Cdd:PHA02562 215 IARKQNKYDELVEEAKTIKAEIEEL--TDELLNLVMDIED-------------------PSAALNKLNTAAAKIKS---- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 224 nlalrsearhlKTETITYEEK---EQQLVSDCVKELRESNSQMVNLTE---ELSHKNEEVMRHQEEISQLLSQIVELQHR 297
Cdd:PHA02562 270 -----------KIEQFQKVIKmyeKGGVCPTCTQQISEGPDRITKIKDklkELQHSLEKLDTAIDELEEIMDEFNEQSKK 338
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1696052192 298 VKELALEKEELRIHLQASKDAQRSLTAELNELADRNVECVGMLHESQEEIKELRSK 353
Cdd:PHA02562 339 LLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKT 394
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
214-353 |
9.28e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.35 E-value: 9.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 214 QGKMSDLEEENLALRSEarhLKTETITYE--EKEQQLVSDCVKELRESNSQMVNLTEELSHKNEEVmrhqEEISQllsQI 291
Cdd:PRK01156 137 QGEMDSLISGDPAQRKK---ILDEILEINslERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLEL----ENIKK---QI 206
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1696052192 292 VELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADRNvecvGMLHESQEEIKELRSK 353
Cdd:PRK01156 207 ADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLE----DMKNRYESEIKTAESD 264
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
119-332 |
9.60e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 9.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 119 LAERDRDLELAARIGQSLLQRNHLLQERNESVEEQLAQALDQVHQLQHELGKKDELLRMVASASEESETDSscstplhpr 198
Cdd:COG4717 352 LLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELL--------- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 199 QPLAPAVALSQLEALQGKMSDLEEENLALRSEARHLKTEtityeekeqqlvsdcVKELRESnsqmvnltEELSHKneevm 278
Cdd:COG4717 423 EALDEEELEEELEELEEELEELEEELEELREELAELEAE---------------LEQLEED--------GELAEL----- 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1696052192 279 rhQEEISQLLSQIVELQHRVKELALEKEELRihlQASKDAQRSLTAELNELADR 332
Cdd:COG4717 475 --LQELEELKAELRELAEEWAALKLALELLE---EAREEYREERLPPVLERASE 523
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
143-329 |
1.10e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.24 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 143 LQERNESVEEQLAQALDQVHQLQHELGKKDELLRMVASASEESETD-SSCSTPLH---------PRQPLAPAVALSQLEA 212
Cdd:pfam01576 417 LQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDvSSLESQLQdtqellqeeTRQKLNLSTRLRQLED 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 213 LQ-GKMSDLEEENLALRSEARHLKTETITYEE--KEQQLVSDCVKELRESNSQMVNLTEELSHKNEEVM----------- 278
Cdd:pfam01576 497 ERnSLQEQLEEEEEAKRNVERQLSTLQAQLSDmkKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAaaydklektkn 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 279 RHQEEISQLL------SQIV-------------------------------ELQHRVKE-----LALEKEELRIHLQASK 316
Cdd:pfam01576 577 RLQQELDDLLvdldhqRQLVsnlekkqkkfdqmlaeekaisaryaeerdraEAEAREKEtralsLARALEEALEAKEELE 656
|
250
....*....|...
gi 1696052192 317 DAQRSLTAELNEL 329
Cdd:pfam01576 657 RTNKQLRAEMEDL 669
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
258-332 |
1.50e-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: 38.70 E-value: 1.50e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1696052192 258 ESNSQMVNLTEELSHKNEEVMRHQEEISQLLSQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADR 332
Cdd:cd22887 1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVER 75
|
|
| DUF4456 |
pfam14644 |
Domain of unknown function (DUF4456); This domain family is found in bacteria and eukaryotes, ... |
241-353 |
1.54e-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: 41.12 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 241 YEEKEQQLVSDCVKELREsnsQMVNLTEELSHKNEEVM-----RHQEEISQLLSQIV-ELQHRVKELALEKE----ELRI 310
Cdd:pfam14644 41 YQEQADEYHNSCLQELRN---QVERLEELLPSVPELIFesllkRHLQKLERAMKNIAaEFSQKQKQLEQLKQqheqQLRP 117
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1696052192 311 HLQaskDAQRSltAELNEL----ADRNVECVGMLHESQEEIKELRSK 353
Cdd:pfam14644 118 TLG---HPQNA--QELEQLcdreEDRQKEHIELIQAHREALLEAVDK 159
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
209-350 |
1.71e-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: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 209 QLEALQgkmsDLEEENLALRSEARHLKTEtitYEE---KEQQLVSDCVKELRESNSQMVNLTEelshkNEEVMRhqEEIS 285
Cdd:pfam10168 573 QLQELQ----SLEEERKSLSERAEKLAEK---YEEikdKQEKLMRRCKKVLQRLNSQLPVLSD-----AEREMK--KELE 638
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1696052192 286 QLLSQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADRNVEcvGMLHESQEEIKEL 350
Cdd:pfam10168 639 TINEQLKHLANAIKQAKKKMNYQRYQIAKSQSIRKKSSLSLSEKQRKTIK--EILKQLGSEIDEL 701
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
124-348 |
1.98e-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: 41.97 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 124 RDLELAARIGQSLLQRNHLLQ-----ERNESVEEQ-----LAQALDQVHQLQHE---LGKKDELLRMVASASE-ESETDS 189
Cdd:pfam15742 93 RELELEVLKQAQSIKSQNSLQeklaqEKSRVADAEekileLQQKLEHAHKVCLTdtcILEKKQLEERIKEASEnEAKLKQ 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 190 SCSTPLHPRQPLAPAVA--LSQLEALQGKMSDLEEENLALRS-----EAR--HLKTETITYEE--------KEQQLVSDC 252
Cdd:pfam15742 173 QYQEEQQKRKLLDQNVNelQQQVRSLQDKEAQLEMTNSQQQLriqqqEAQlkQLENEKRKSDEhlksnqelSEKLSSLQQ 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 253 VKE-LRESNSQMVN-LTEELSHKNEEVMRHQEEIS---QLLSQIVELQ-HRVKELALEKEELRIHLQASKDAQRSLTAEL 326
Cdd:pfam15742 253 EKEaLQEELQQVLKqLDVHVRKYNEKHHHHKAKLRrakDRLVHEVEQRdERIKQLENEIGILQQQSEKEKAFQKQVTAQN 332
|
250 260
....*....|....*....|..
gi 1696052192 327 NELADRNVECVGMLHESQEEIK 348
Cdd:pfam15742 333 EILLLEKRKLLEQLTEQEELIK 354
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
100-354 |
1.99e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 100 DRVEQMTKTYNDIEVVTHLLAER-DR--DL-ELAARIgQSLLQRNHLLQERNESVEEQLAQALDQVHQLQHElgkKDELl 175
Cdd:PRK02224 475 ERVEELEAELEDLEEEVEEVEERlERaeDLvEAEDRI-ERLEERREDLEELIAERRETIEEKRERAEELRER---AAEL- 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 176 rmvASASEESETDSScstplhpRQPLAPAVALSQLEALQGKMSDLEEENLALRSearhLKTETITYEEKEQQLVsdcvkE 255
Cdd:PRK02224 550 ---EAEAEEKREAAA-------EAEEEAEEAREEVAELNSKLAELKERIESLER----IRTLLAAIADAEDEIE-----R 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 256 LRESNSQMVNLTEE----LSHKNEevmRHQ-----------EEISQLLSQIVELQHRVKELALEKEELRIHLQASKDAQR 320
Cdd:PRK02224 611 LREKREALAELNDErrerLAEKRE---RKReleaefdeariEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVE 687
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1696052192 321 SLTAELNELADR------NVECVGMLHESQEEIK--------ELRSKN 354
Cdd:PRK02224 688 NELEELEELRERrealenRVEALEALYDEAEELEsmygdlraELRQRN 735
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
163-355 |
2.28e-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: 41.80 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 163 QLQHELGKKDELLRMVASASEESETDSSCSTPLHprqplapavalsqlEALQGKMSDLEEENLALRSEARHLKTETITYE 242
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDR--------------EQWERQRRELESRVAELKEELRQSREKHEELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 243 E--KEQQLVSDCVKE---------------LRESNSQMVNLTEELSHKNEEVMRHQEEISQLLSQIvelqhrvKELALEK 305
Cdd:pfam07888 101 EkyKELSASSEELSEekdallaqraahearIRELEEDIKTLTQRVLERETELERMKERAKKAGAQR-------KEEEAER 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1696052192 306 EELRIHLQASKDAQRSLTAELNELADRNVECVGMLHESQEEIKELRSKNT 355
Cdd:pfam07888 174 KQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLT 223
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
143-359 |
2.52e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 143 LQERNESVEEQLAQALDQVHQLQHELGKKDELLRMVASASEESETDSscstplhprqplapAVALSQLEALQGKMSDLEE 222
Cdd:COG3883 21 KQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI--------------DKLQAEIAEAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 223 EnlaLRSEARHLKTE--TITYEEkeqQLVS-----------DCVKELRESNSQMVnltEELSHKNEEVMRHQEEISQLLS 289
Cdd:COG3883 87 E---LGERARALYRSggSVSYLD---VLLGsesfsdfldrlSALSKIADADADLL---EELKADKAELEAKKAELEAKLA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 290 QIVELQhrvKELALEKEELRIHLQASKDAQRSLTAELNELADRNVECVGMLHESQEEIKELRSKNTPSAG 359
Cdd:COG3883 158 ELEALK---AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
113-328 |
3.32e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 41.21 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 113 EVVTHLLAERDRDLELAARIGQSLLQRNHLlqeRNE--SVEEQLAQALDQVHQLQHELGKKDELLRMVASASEEsetdss 190
Cdd:pfam19220 38 AILRELPQAKSRLLELEALLAQERAAYGKL---RRElaGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEE------ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 191 cstplhprQPLAPAVALSQLEALQGKMSD-------LEEENLALRSEArhlktetityEEKEQQLVsdcvkelrESNSQM 263
Cdd:pfam19220 109 --------LRIELRDKTAQAEALERQLAAeteqnraLEEENKALREEA----------QAAEKALQ--------RAEGEL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1696052192 264 VNLTEELSHKNEEVMRHQEEISQLLSQIVELQHRVKELAlekEELRIHLQASKDAQRSLTAELNE 328
Cdd:pfam19220 163 ATARERLALLEQENRRLQALSEEQAAELAELTRRLAELE---TQLDATRARLRALEGQLAAEQAE 224
|
|
| HAUS5 |
pfam14817 |
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. ... |
120-190 |
3.72e-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: 41.18 E-value: 3.72e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1696052192 120 AERDRDLELAARIGQSLLQRNHLLQERNESVEE---QLAQALDQVHQLQHEL-GKKDELLRMVASASEESETDSS 190
Cdd:pfam14817 285 YESNHLLDVSSDESSDLPSVRQLLERQWAHVQQflnELAETRSRCQQLQARLqGLKDEAELESLGIGDTSQNDSL 359
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
208-364 |
4.30e-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: 41.03 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 208 SQLEALQGKMSDL----EEENLALRSEARHLKTETITYEEKEQQLVSDcVKELRESNSQMVNLTEELSHKNEEVMRHQEE 283
Cdd:pfam07888 34 NRLEECLQERAELlqaqEAANRQREKEKERYKRDREQWERQRRELESR-VAELKEELRQSREKHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 284 ISQ----LLSQIVELQHRVKELalekeELRIHLQASKDAQRSltAELNELADRNVECVGMLHESQEEIKELRSKNTPSAG 359
Cdd:pfam07888 113 LSEekdaLLAQRAAHEARIREL-----EEDIKTLTQRVLERE--TELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEE 185
|
....*
gi 1696052192 360 MRRHL 364
Cdd:pfam07888 186 ELRSL 190
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
95-332 |
4.48e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.19 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 95 RVLSADRVEQMTKTYNDIEVVT-----HLLAERDRDLEL-----AARIGQSLLQRN-HLLQERNESVEEQ-----LAQAL 158
Cdd:PRK10929 60 RKGSLERAKQYQQVIDNFPKLSaelrqQLNNERDEPRSVppnmsTDALEQEILQVSsQLLEKSRQAQQEQdrareISDSL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 159 DQVHQLQhelgkkDELLRMVASASEESETDSSCSTPLhprqplapavALSQLEALQGKmsdleeenlalrSEARHLKTET 238
Cdd:PRK10929 140 SQLPQQQ------TEARRQLNEIERRLQTLGTPNTPL----------AQAQLTALQAE------------SAALKALVDE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 239 ItyeEKEQqlvsdcvkeLRESNSQmvnlteELSHKNEEVM--RHQE---EISQLLSQIVELQHRVKELALEKEELRIH-- 311
Cdd:PRK10929 192 L---ELAQ---------LSANNRQ------ELARLRSELAkkRSQQldaYLQALRNQLNSQRQREAERALESTELLAEqs 253
|
250 260
....*....|....*....|....*..
gi 1696052192 312 --LQASKDAQ----RSLTAELNELADR 332
Cdd:PRK10929 254 gdLPKSIVAQfkinRELSQALNQQAQR 280
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
206-309 |
4.54e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 206 ALSQLEALQGKMSDLEEENLALRSEARHLKTETITYEEKEQQL---VSDCVKELRESNSQMVNLTEELSHKNEEVMRHQE 282
Cdd:COG1340 151 KAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELheeMIELYKEADELRKEADELHKEIVEAQEKADELHE 230
|
90 100
....*....|....*....|....*..
gi 1696052192 283 EISQLLSQIVELQHRVKELALEKEELR 309
Cdd:COG1340 231 EIIELQKELRELRKELKKLRKKQRALK 257
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
145-353 |
4.56e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 145 ERNESVEEQLAQALDQVHQLQHELGKKDELLRMVASASEESETDSscstplhprqplapAVALSQLEALQGKMSDLEEEN 224
Cdd:PRK02224 223 ERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETI--------------AETEREREELAEEVRDLRERL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 225 LALRSEARHLKTETiTYEEKEQQLVSDCVKELRESNSQmvnLTEELSHKNEEVMRHQEEISQLLSQIVELQHRVKELALE 304
Cdd:PRK02224 289 EELEEERDDLLAEA-GLDDADAEAVEARREELEDRDEE---LRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREE 364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 305 KEELRIHLQASKDAQRSLTAELNEL---------------------ADRNVECVGMLHESQEEIKELRSK 353
Cdd:PRK02224 365 AAELESELEEAREAVEDRREEIEELeeeieelrerfgdapvdlgnaEDFLEELREERDELREREAELEAT 434
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
120-353 |
5.42e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 120 AERDRDLELAARIGQSLLQRNHLLQERnESVEEQLAQALDQVHQLQHELG-------------KKDELLRMVASASEESE 186
Cdd:COG4717 182 LLEQLSLATEEELQDLAEELEELQQRL-AELEEELEEAQEELEELEEELEqleneleaaaleeRLKEARLLLLIAAALLA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 187 TDSSCSTPLHPRQPLAPAVAL--------------------SQLEALQG--KMSDLEEENLALRSEARHLKTEtitYEEK 244
Cdd:COG4717 261 LLGLGGSLLSLILTIAGVLFLvlgllallflllarekaslgKEAEELQAlpALEELEEEELEELLAALGLPPD---LSPE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 245 EQQLVSDCVKELRESNSQMVNLTEELshkneEVMRHQEEISQLLS-----------QIVELQHRVKELALEKEELRIHLQ 313
Cdd:COG4717 338 ELLELLDRIEELQELLREAEELEEEL-----QLEELEQEIAALLAeagvedeeelrAALEQAEEYQELKEELEELEEQLE 412
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1696052192 314 ASKDAQRSLTAELN--ELADRNVECVGMLHESQEEIKELRSK 353
Cdd:COG4717 413 ELLGELEELLEALDeeELEEELEELEEELEELEEELEELREE 454
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
218-348 |
5.83e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 39.12 E-value: 5.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 218 SDLEEENLALRseaRHLKTETITYEEKEQQlvsdCVKELRESNSQMVNLTEELSHKNEEVMRHQEEISQLLSQIVELQH- 296
Cdd:pfam13851 18 NDITRNNLELI---KSLKEEIAELKKKEER----NEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLKNl 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1696052192 297 --RVKELALEKEELRIHLQASKDAQRSLTAELNELADRNVECVgmlHESQEEIK 348
Cdd:pfam13851 91 kaRLKVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAAI---QDVQQKTG 141
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
275-353 |
6.43e-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: 39.52 E-value: 6.43e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1696052192 275 EEVMRHQEEISQLLSQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADRnvecvgmLHESQEEIKELRSK 353
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 ... |
268-349 |
8.16e-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: 40.16 E-value: 8.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 268 EELSHKNEEVMRHQEEISQLLSQIVELQHRVKELALEKEELRIHLQASKDaqrsLTAELNE----LADRNVECVGMLHES 343
Cdd:pfam01576 5 EEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETE----LCAEAEEmrarLAARKQELEEILHEL 80
|
....*.
gi 1696052192 344 QEEIKE 349
Cdd:pfam01576 81 ESRLEE 86
|
|
| KASH_CCD |
pfam14662 |
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of ... |
133-352 |
8.28e-03 |
|
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: 38.62 E-value: 8.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 133 GQSLLQRNHLLQERNESVEEQLAQALDQVHQLQHELGKKDELLRMVASASEesetdsscstplhprqplapavalsqlea 212
Cdd:pfam14662 10 VEDLQANNQKLLQENSKLKATVETREETNAKLLEENLNLRKQAKSQQQAVQ----------------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 213 lqgKMSDLEEENLALRSEARHLktetityEEKEQQLVsdcvkelrESNSQMvnlTEELSHKNEEVMRHQEEISQLLSQIV 292
Cdd:pfam14662 61 ---KEKLLEEELEDLKLIVNSL-------EEARRSLL--------AQNKQL---EKENQSLLQEIESLQEENKKNQAERD 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1696052192 293 ELQHRVKELALEKEELRI------HLQASKDAQRSL-TAELNELADRNVECVGMLHESQEEIKELRS 352
Cdd:pfam14662 120 KLQKKKKELLKSKACLKEqlhsceDLACNRETILIEkTTQIEELKSTVEEYSSIEEELRAEKSRLES 186
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
273-350 |
8.45e-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: 36.77 E-value: 8.45e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1696052192 273 KNEEVMRHQEEISQLLSQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADRNVECvgmlhesQEEIKEL 350
Cdd:cd22887 2 LESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKL-------QEENDEL 72
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
132-293 |
8.63e-03 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 38.07 E-value: 8.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 132 IGQSLLQRNHLLQERN----ESVEEQLAQALDQVHQLqheLGKKDELLRMVASASEESETDSSCSTPLHprqplapaval 207
Cdd:pfam11559 7 INQTLLSRGFLRSGLLfdtaEGVEENIARIINVIYEL---LQQRDRDLEFRESLNETIRTLEAEIERLQ----------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 208 SQLEALQGKMSDLEEENLALRSEARHLktetityeEKEQQLVSDCVKELRESNSQMVNLTEELSHK-NEEVMRHQEEISQ 286
Cdd:pfam11559 73 SKIERLKTQLEDLERELALLQAKERQL--------EKKLKTLEQKLKNEKEELQRLKNALQQIKTQfAHEVKKRDREIEK 144
|
....*..
gi 1696052192 287 LLSQIVE 293
Cdd:pfam11559 145 LKERLAQ 151
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
118-353 |
9.83e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.16 E-value: 9.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 118 LLAERDRDLElaARIGQsLLQRNHLLQERNESVEEQLAQALDQVHQLQHELGKKDELLRMVASASEESEtdsscstplhp 197
Cdd:pfam01576 879 ALQDEKRRLE--ARIAQ-LEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLE----------- 944
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 198 RQPLAPAVALSQLE------------ALQGKMSDLEEEnlaLRSEARhlktetityeEKEQ--QLVSDCVKELRESNSQM 263
Cdd:pfam01576 945 RQNKELKAKLQEMEgtvkskfkssiaALEAKIAQLEEQ---LEQESR----------ERQAanKLVRRTEKKLKEVLLQV 1011
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696052192 264 vnlteelshknEEVMRHQEeisQLLSQIVELQHRVKELALEKEELRIHLQASKDAQRSLTAELNELADRNvECVGmlhes 343
Cdd:pfam01576 1012 -----------EDERRHAD---QYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESN-ESMN----- 1071
|
250
....*....|
gi 1696052192 344 qEEIKELRSK 353
Cdd:pfam01576 1072 -REVSTLKSK 1080
|
|
| |
